value: Ubiquitin carboxyl-terminal hydrolase 8

value: Deubiquitinating enzyme 8

value: Ubiquitin isopeptidase Y

value: hUBPy

value: Ubiquitin thioesterase 8

value: UBPY

value: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controls tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation (PubMed:27302062)

name: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

value: Forms a ternary complex with RNF128 and OTUB1. Interacts (via C-terminal UCH catalytic domain) with OTUB1 isoform 1. Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3, EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ (By similarity). Interacts with NBR1, RASGRF1, RNF41 and IST1. Associates with the ESCRT-0 complex and with microtubules (By similarity). Interacts with BIRC6/bruce and KIF23/MKLP1

commentType: SUBUNIT

value: (Microbial infection) Interacts with Zika virus non-structural protein 1

value: Cytoplasm

value: Nucleus

value: Endosome membrane

value: Peripheral membrane protein

value: Cell membrane

value: Upon growth stimulation in starved human fibroblasts. Decreases in response to growth arrest induced by cell-cell contact

value: The MIT domain is required for endosomal localization, CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR degradation

commentType: DOMAIN

value: The rhodanese domain is sufficient for RNF41-binding

value: Phosphorylation of Ser-718 is essential for interaction with YWHAE and for cytosol localization. Undergoes dephosphorylation at Ser-718 in the M phase. Tyrosine-phosphorylated in its N-terminal half in an EGFR-dependent manner

value: Ubiquitinated. Inactive form is mostly monoubiquitinated, but polyubiquitination happens too. Ubiquitination is increased in EGF-stimulated cells. Ubiquitination of active form is undetectable, suggesting a possibility that USP8 deubiquitinates itself, thereby regulating its own function (By similarity)

diseaseId: Pituitary adenoma 4, ACTH-secreting

description: A form of pituitary adenoma, a neoplasm of the pituitary gland and one of the most common neuroendocrine tumors. Pituitary adenomas are clinically classified as functional and non-functional tumors, and manifest with a variety of features, including local invasion of surrounding structures and excessive hormone secretion. Functional pituitary adenomas are further classified by the type of hormone they secrete. PITA4 results in excessive production of adrenocorticotropic hormone. This leads to hypersecretion of cortisol by the adrenal glands and ACTH-dependent Cushing syndrome. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes.

value: The disease is caused by variants affecting the gene represented in this entry

value: Belongs to the peptidase C19 family

sequenceCautionType: Miscellaneous discrepancy

note: Contaminating sequence. Potential poly-A sequence.

description: Ubiquitin carboxyl-terminal hydrolase 8

description: MIT

description: Rhodanese

description: USP

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Basic and acidic residues

description: Basic and acidic residues

description: Basic and acidic residues

description: Basic and acidic residues

description: Basic and acidic residues

description: Polar residues

description: Nucleophile

description: Proton acceptor

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: Phosphothreonine

description: Phosphoserine

description: Phosphoserine

description: Phosphothreonine

description: in isoform 2

description: in isoform 2

description: found in a patient with spastic paraplegia; uncertain significance; dbSNP:rs587777201

description: in dbSNP:rs3743044

description: in PITA4; uncertain significance; somatic mutation

description: in PITA4; uncertain significance; somatic mutation; dbSNP:rs672601308

description: in PITA4; uncertain significance; somatic mutation; localizes to nucleus instead of cytoplasm; dbSNP:rs672601307

description: in PITA4; uncertain significance; somatic mutation; dbSNP:rs672601311

description: in dbSNP:rs11638390

description: in dbSNP:rs1056577

description: Impairs deubiquitination activity and leads to endosome membrane accumulation.

description: in Ref. 3; CAD97662

description: in Ref. 3; CAD97662

description: in Ref. 3; CAD97662

authors:
Nomura N.
Nagase T.
Miyajima N.
Sazuka T.
Tanaka A.
Sato S.
Seki N.
Kawarabayasi Y.
Ishikawa K.
Tabata S.

title: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)

authors:
Ota T.
Suzuki Y.
Nishikawa T.
Otsuki T.
Sugiyama T.
Irie R.
Wakamatsu A.
Hayashi K.
Sato H.
Nagai K.
Kimura K.
Makita H.
Sekine M.
Obayashi M.
Nishi T.
Shibahara T.
Tanaka T.
Ishii S.
Yamamoto J.
Saito K.
Kawai Y.
Isono Y.
Nakamura Y.
Nagahari K.
Murakami K.
Yasuda T.
Iwayanagi T.
Wagatsuma M.
Shiratori A.
Sudo H.
Hosoiri T.
Kaku Y.
Kodaira H.
Kondo H.
Sugawara M.
Takahashi M.
Kanda K.
Yokoi T.
Furuya T.
Kikkawa E.
Omura Y.
Abe K.
Kamihara K.
Katsuta N.
Sato K.
Tanikawa M.
Yamazaki M.
Ninomiya K.
Ishibashi T.
Yamashita H.
Murakawa K.
Fujimori K.
Tanai H.
Kimata M.
Watanabe M.
Hiraoka S.
Chiba Y.
Ishida S.
Ono Y.
Takiguchi S.
Watanabe S.
Yosida M.
Hotuta T.
Kusano J.
Kanehori K.
Takahashi-Fujii A.
Hara H.
Tanase T.-O.
Nomura Y.
Togiya S.
Komai F.
Hara R.
Takeuchi K.
Arita M.
Imose N.
Musashino K.
Yuuki H.
Oshima A.
Sasaki N.
Aotsuka S.
Yoshikawa Y.
Matsunawa H.
Ichihara T.
Shiohata N.
Sano S.
Moriya S.
Momiyama H.
Satoh N.
Takami S.
Terashima Y.
Suzuki O.
Nakagawa S.
Senoh A.
Mizoguchi H.
Goto Y.
Shimizu F.
Wakebe H.
Hishigaki H.
Watanabe T.
Sugiyama A.
Takemoto M.
Kawakami B.
Yamazaki M.
Watanabe K.
Kumagai A.
Itakura S.
Fukuzumi Y.
Fujimori Y.
Komiyama M.
Tashiro H.
Tanigami A.
Fujiwara T.
Ono T.
Yamada K.
Fujii Y.
Ozaki K.
Hirao M.
Ohmori Y.
Kawabata A.
Hikiji T.
Kobatake N.
Inagaki H.
Ikema Y.
Okamoto S.
Okitani R.
Kawakami T.
Noguchi S.
Itoh T.
Shigeta K.
Senba T.
Matsumura K.
Nakajima Y.
Mizuno T.
Morinaga M.
Sasaki M.
Togashi T.
Oyama M.
Hata H.
Watanabe M.
Komatsu T.
Mizushima-Sugano J.
Satoh T.
Shirai Y.
Takahashi Y.
Nakagawa K.
Okumura K.
Nagase T.
Nomura N.
Kikuchi H.
Masuho Y.
Yamashita R.
Nakai K.
Yada T.
Nakamura Y.
Ohara O.
Isogai T.
Sugano S.

title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)

authors:
Bechtel S.
Rosenfelder H.
Duda A.
Schmidt C.P.
Ernst U.
Wellenreuther R.
Mehrle A.
Schuster C.
Bahr A.
Bloecker H.
Heubner D.
Hoerlein A.
Michel G.
Wedler H.
Koehrer K.
Ottenwaelder B.
Poustka A.
Wiemann S.
Schupp I.

title: The full-ORF clone resource of the German cDNA consortium.

authors:
Zody M.C.
Garber M.
Sharpe T.
Young S.K.
Rowen L.
O'Neill K.
Whittaker C.A.
Kamal M.
Chang J.L.
Cuomo C.A.
Dewar K.
FitzGerald M.G.
Kodira C.D.
Madan A.
Qin S.
Yang X.
Abbasi N.
Abouelleil A.
Arachchi H.M.
Baradarani L.
Birditt B.
Bloom S.
Bloom T.
Borowsky M.L.
Burke J.
Butler J.
Cook A.
DeArellano K.
DeCaprio D.
Dorris L. III
Dors M.
Eichler E.E.
Engels R.
Fahey J.
Fleetwood P.
Friedman C.
Gearin G.
Hall J.L.
Hensley G.
Johnson E.
Jones C.
Kamat A.
Kaur A.
Locke D.P.
Madan A.
Munson G.
Jaffe D.B.
Lui A.
Macdonald P.
Mauceli E.
Naylor J.W.
Nesbitt R.
Nicol R.
O'Leary S.B.
Ratcliffe A.
Rounsley S.
She X.
Sneddon K.M.B.
Stewart S.
Sougnez C.
Stone S.M.
Topham K.
Vincent D.
Wang S.
Zimmer A.R.
Birren B.W.
Hood L.
Lander E.S.
Nusbaum C.

title: Analysis of the DNA sequence and duplication history of human chromosome 15.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

authors:
Naviglio S.
Mattecucci C.
Matoskova B.
Nagase T.
Nomura N.
Di Fiore P.P.
Draetta G.F.

title: UBPY: a growth-regulated human ubiquitin isopeptidase.

authors:
Row P.E.
Prior I.A.
McCullough J.
Clague M.J.
Urbe S.

title: The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
MUTAGENESIS OF CYS-786

authors:
Beausoleil S.A.
Villen J.
Gerber S.A.
Rush J.
Gygi S.P.

title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

authors:
Row P.E.
Liu H.
Hayes S.
Welchman R.
Charalabous P.
Hofmann K.
Clague M.J.
Sanderson C.M.
Urbe S.

title: The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation.

referencePositions: INTERACTION WITH CHMP1A; CHMP1B AND CHMP7

title: Final stages of cytokinesis and midbody ring formation are controlled by BRUCE.

referencePositions: INTERACTION WITH BIRC6/BRUCE AND KIF23/MKLP1

authors:
Dephoure N.
Zhou C.
Villen J.
Beausoleil S.A.
Bakalarski C.E.
Elledge S.J.
Gygi S.P.

title: A quantitative atlas of mitotic phosphorylation.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452; SER-718 AND SER-719

authors:
Waters S.
Marchbank K.
Solomon E.
Whitehouse C.
Gautel M.

title: Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover.

referencePositions:
INTERACTION WITH NBR1
SUBCELLULAR LOCATION

authors:
Agromayor M.
Carlton J.G.
Phelan J.P.
Matthews D.R.
Carlin L.M.
Ameer-Beg S.
Bowers K.
Martin-Serrano J.

title: Essential role of hIST1 in cytokinesis.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-718

authors:
Burkard T.R.
Planyavsky M.
Kaupe I.
Breitwieser F.P.
Buerckstuemmer T.
Bennett K.L.
Superti-Furga G.
Colinge J.

title: Initial characterization of the human central proteome.

authors:
Rigbolt K.T.
Prokhorova T.A.
Akimov V.
Henningsen J.
Johansen P.T.
Kratchmarova I.
Kassem M.
Mann M.
Olsen J.V.
Blagoev B.

title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577 AND SER-718

authors:
Zhou H.
Di Palma S.
Preisinger C.
Peng M.
Polat A.N.
Heck A.J.
Mohammed S.

title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-392; SER-400; SER-452; THR-577 AND SER-718

authors:
Bian Y.
Song C.
Cheng K.
Dong M.
Wang F.
Huang J.
Sun D.
Wang L.
Ye M.
Zou H.

title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

title: The Endosome-associated Deubiquitinating Enzyme USP8 Regulates BACE1 Enzyme Ubiquitination and Degradation.

authors:
Zheng Y.
Liu Q.
Wu Y.
Ma L.
Zhang Z.
Liu T.
Jin S.
She Y.
Li Y.P.
Cui J.

title: Zika virus elicits inflammation to evade antiviral response by cleaving cGAS via NS1-caspase-1 axis.

referencePositions: INTERACTION WITH ZIKA VIRUS NON-STRUCTURAL PROTEIN 1 (MICROBIAL INFECTION)

authoringGroup: RIKEN structural genomics initiative (RSGI)

title: Solution structure of the rhodanese-like domain in human ubiquitin specific protease 8 (UBP8).

authors:
Avvakumov G.V.
Walker J.R.
Xue S.
Finerty P.J. Jr.
Mackenzie F.
Newman E.M.
Dhe-Paganon S.

title: Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8).

referencePositions: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-318 IN COMPLEX WITH RNF41

authors:
Novarino G.
Fenstermaker A.G.
Zaki M.S.
Hofree M.
Silhavy J.L.
Heiberg A.D.
Abdellateef M.
Rosti B.
Scott E.
Mansour L.
Masri A.
Kayserili H.
Al-Aama J.Y.
Abdel-Salam G.M.
Karminejad A.
Kara M.
Kara B.
Bozorgmehri B.
Ben-Omran T.
Mojahedi F.
Mahmoud I.G.
Bouslam N.
Bouhouche A.
Benomar A.
Hanein S.
Raymond L.
Forlani S.
Mascaro M.
Selim L.
Shehata N.
Al-Allawi N.
Bindu P.S.
Azam M.
Gunel M.
Caglayan A.
Bilguvar K.
Tolun A.
Issa M.Y.
Schroth J.
Spencer E.G.
Rosti R.O.
Akizu N.
Vaux K.K.
Johansen A.
Koh A.A.
Megahed H.
Durr A.
Brice A.
Stevanin G.
Gabriel S.B.
Ideker T.
Gleeson J.G.

title: Exome sequencing links corticospinal motor neuron disease to common neurodegenerative disorders.

authors:
Faucz F.R.
Tirosh A.
Tatsi C.
Berthon A.
Hernandez-Ramirez L.C.
Settas N.
Angelousi A.
Correa R.
Papadakis G.Z.
Chittiboina P.
Quezado M.
Pankratz N.
Lane J.
Dimopoulos A.
Mills J.L.
Lodish M.
Stratakis C.A.

title: Somatic USP8 gene mutations are a common cause of pediatric Cushing disease.

referencePositions: VARIANTS PITA4 718-SER--THR-723 DEL; CYS-718; PRO-718; SER-718 DEL AND ARG-720

referencePositions: CHARACTERIZATION OF VARIANT PITA4 PRO-718

value: Autosomal recessive spastic paraplegia type 59

value: 6 GO annotations based on evolutionary models

value: Expressed in calcaneal tendon and 195 other cell types or tissues

value: P:cellular response to dexamethasone stimulus

value: P:cellular response to nerve growth factor stimulus

value: P:negative regulation of lysosomal protein catabolic process

value: P:positive regulation of amyloid fibril formation

value: P:positive regulation of canonical Wnt signaling pathway

value: P:regulation of protein catabolic process at postsynapse, modulating synaptic transmission

value: Putative ubiquitin carboxyl-terminal hydrolase 8

value: Phosphotransferase system, lactose/cellobiose-type IIA subunit

value: Rhodanese/Cell cycle control phosphatase


entryType: UniProtKB reviewed (Swiss-Prot)

scientificName: Homo sapiens

commonName: Human

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo

proteinExistence: 1: Evidence at protein level

source: PubMed

value: Alpha-AASA dehydrogenase

value: Aldehyde dehydrogenase family 7 member A1

value: Betaine aldehyde dehydrogenase

value: P6c dehydrogenase

flag: Precursor

source: HGNC

value: Aldehyde dehydrogenase enzyme that mediates important protective effects (PubMed:16491085, PubMed:20207735, PubMed:20554659, PubMed:21338592, PubMed:25554827, PubMed:31302938, PubMed:31652343, PubMed:38604394, PubMed:40233740). Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes (PubMed:16491085, PubMed:20207735, PubMed:21338592, PubMed:40233740). Involved in cellular defense against hyperosmotic stress by metabolizing betaine aldehyde to betaine, an important cellular osmolyte and methyl donor (PubMed:20207735)

commentType: FUNCTION

value: Involved in lysine catabolism in the brain by mediating the conversion of L-aminoadipate-semialdehyde ((S)-2-amino-6-oxohexanoate) to L-2-aminoadipate

molecule: Isoform 1

value: Acts as a key inhibitor of ferroptosis both by generating membrane NADH and decreasing the level of reactive aldehydes (PubMed:40233740). Recruited to plasma membrane in response to ferroptotic stress and phosphorylation by AMPK, generating membrane NADH to support AIFM2/FSP1 activity, an essential ferroptosis suppressor protein (PubMed:40233740). Also directly inhibits ferroptosis by decreasing lipid peroxidation via consumption of reactive aldehydes, such as 4-hydroxynonenal (4-HNE) and malonaldehyde (PubMed:40233740). Also acts as a regulator of cellular energy homeostasis in response to cellular energy stress, such as starvation and hypoxia, by inhibiting COPI-mediated intracellular transport, thereby reducing cellular energy consumption (PubMed:31492851)

molecule: Isoform 2

commentType: CATALYTIC ACTIVITY

name: (S)-2-amino-6-oxohexanoate + NAD(+) + H2O = L-2-aminoadipate + NADH + 2 H(+)

database: Rhea

database: ChEBI

directionType: left-to-right

name: nonanal + NAD(+) + H2O = nonanoate + NADH + 2 H(+)

name: betaine aldehyde + NAD(+) + H2O = glycine betaine + NADH + 2 H(+)

name: an aldehyde + NAD(+) + H2O = a carboxylate + NADH + 2 H(+)

name: hexanal + NAD(+) + H2O = hexanoate + NADH + 2 H(+)

name: octanal + NAD(+) + H2O = octanoate + NADH + 2 H(+)

name: (E)-non-2-enal + NAD(+) + H2O = (E)-non-2-enoate + NADH + 2 H(+)

name: (E)-4-hydroxynon-2-enal + NAD(+) + H2O = (E)-4-hydroxynon-2-enoate + NADH + 2 H(+)

name: malonaldehyde + NAD(+) + H2O = 3-oxopropanoate + NADH + 2 H(+)

value: Inhibited by 4-diethylaminobenzaldehyde (DEAB); inhibition is irreversible via formation of a stable covalent acyl-enzyme stalled intermediate

enzyme: enzyme toward L-2-aminoadipate 6-semialdehyde

value: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1

value: Translocates to membranes in response to cellular stress and phosphorylation by AMPK

value: Abundant in hepatoma cells and fetal cochlea, ovary, eye, heart, adrenal gland, liver and kidney. Low levels present in adult peripheral blood leukocytes and fetal brain, thymus, spleen, skeletal muscle, lung and tongue

value: Phosphorylation at Ser-102 by AMPK in response to cellular stress, such as hypoxia or ferroptotic stress, promotes membrane localization and generation of membrane NADH

diseaseId: Epilepsy, early-onset, 4, vitamin B6-dependent

description: An autosomal recessive neurologic disorder ocharacterized by a combination of various seizure types. It usually occurs in the first hours of life and is unresponsive to standard anticonvulsants, responding only to immediate administration of pyridoxine hydrochloride.

value: Belongs to the aldehyde dehydrogenase family

description: Mitochondrion

description: Alpha-aminoadipic semialdehyde dehydrogenase

description: Proton acceptor

description: Nucleophile

description: Transition state stabilizer

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: Phosphoserine; by AMPK

description: in isoform 2

description: in isoform 4

description: in EPEO4

description: in EPEO4; loss of alpha-AASA dehydrogenase activity

description: in EPEO4; abolished aldehyde dehydrogenase activity, abolished homotetramerization; dbSNP:rs758016489

description: in EPEO4; decreased alpha-aminoadipic semialdehyde dehydrogenase efficiency; dbSNP:rs372660425

description: in EPEO4; decreased alpha-aminoadipic semialdehyde dehydrogenase activity; dbSNP:rs779652673

description: in EPEO4; abolished alpha-aminoadipic semialdehyde dehydrogenase activity; dbSNP:rs121912709

description: in EPEO4

description: in EPEO4; decreased alpha-aminoadipic semialdehyde dehydrogenase activity; dbSNP:rs555896752

description: in EPEO4

description: in EPEO4; uncertain significance; dbSNP:rs1181991285

description: in EPEO4; dbSNP:rs1750388815

description: in EPEO4; dbSNP:rs121912711

description: in EPEO4; decreased alpha-aminoadipic semialdehyde dehydrogenase activity; dbSNP:rs148052962

description: in EPEO4; uncertain significance

description: in EPEO4; uncertain significance; dbSNP:rs1389337955

description: in EPEO4; decreased alpha-aminoadipic semialdehyde dehydrogenase activity; dbSNP:rs1168941346

description: in EPEO4; dbSNP:rs754449549

description: in EPEO4

description: in EPEO4

description: in EPEO4

description: in dbSNP:rs2306618

description: in EPEO4; impaired NAD-binding; dbSNP:rs796052271

description: in EPEO4; impaired NAD-binding; dbSNP:rs1311982393

description: in EPEO4; loss of alpha-AASA dehydrogenase activity; impaired NAD-binding; dbSNP:rs121912707

description: in dbSNP:rs12514417

description: in EPEO4; uncertain significance

description: in EPEO4

description: in EPEO4; decreased aldehyde dehydrogenase activity; dbSNP:rs752523070

description: in EPEO4; uncertain significance

description: in EPEO4; uncertain significance; dbSNP:rs556400964

description: Abolished phosphorylation by AMPK and recruitment to membranes.

description: Mimics phosphorylation; promoting plasma membrane recruitment and ability to generate membrane NADH.

description: Does not affect phosphorylation by AMPK and recruitment to membranes.

description: Abolished aldehyde dehydrogenase activity, leading to decreased levels of membrane NADH.

description: in Ref. 2; BAG59812

description: Removed

description: N-acetylserine

authors:
Lee P.
Kuhl W.
Gelbart T.
Kamimura T.
West C.
Beutler E.

title: Homology between a human protein and a protein of the green garden pea.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)
TISSUE SPECIFICITY

authors:
Ota T.
Suzuki Y.
Nishikawa T.
Otsuki T.
Sugiyama T.
Irie R.
Wakamatsu A.
Hayashi K.
Sato H.
Nagai K.
Kimura K.
Makita H.
Sekine M.
Obayashi M.
Nishi T.
Shibahara T.
Tanaka T.
Ishii S.
Yamamoto J.
Saito K.
Kawai Y.
Isono Y.
Nakamura Y.
Nagahari K.
Murakami K.
Yasuda T.
Iwayanagi T.
Wagatsuma M.
Shiratori A.
Sudo H.
Hosoiri T.
Kaku Y.
Kodaira H.
Kondo H.
Sugawara M.
Takahashi M.
Kanda K.
Yokoi T.
Furuya T.
Kikkawa E.
Omura Y.
Abe K.
Kamihara K.
Katsuta N.
Sato K.
Tanikawa M.
Yamazaki M.
Ninomiya K.
Ishibashi T.
Yamashita H.
Murakawa K.
Fujimori K.
Tanai H.
Kimata M.
Watanabe M.
Hiraoka S.
Chiba Y.
Ishida S.
Ono Y.
Takiguchi S.
Watanabe S.
Yosida M.
Hotuta T.
Kusano J.
Kanehori K.
Takahashi-Fujii A.
Hara H.
Tanase T.-O.
Nomura Y.
Togiya S.
Komai F.
Hara R.
Takeuchi K.
Arita M.
Imose N.
Musashino K.
Yuuki H.
Oshima A.
Sasaki N.
Aotsuka S.
Yoshikawa Y.
Matsunawa H.
Ichihara T.
Shiohata N.
Sano S.
Moriya S.
Momiyama H.
Satoh N.
Takami S.
Terashima Y.
Suzuki O.
Nakagawa S.
Senoh A.
Mizoguchi H.
Goto Y.
Shimizu F.
Wakebe H.
Hishigaki H.
Watanabe T.
Sugiyama A.
Takemoto M.
Kawakami B.
Yamazaki M.
Watanabe K.
Kumagai A.
Itakura S.
Fukuzumi Y.
Fujimori Y.
Komiyama M.
Tashiro H.
Tanigami A.
Fujiwara T.
Ono T.
Yamada K.
Fujii Y.
Ozaki K.
Hirao M.
Ohmori Y.
Kawabata A.
Hikiji T.
Kobatake N.
Inagaki H.
Ikema Y.
Okamoto S.
Okitani R.
Kawakami T.
Noguchi S.
Itoh T.
Shigeta K.
Senba T.
Matsumura K.
Nakajima Y.
Mizuno T.
Morinaga M.
Sasaki M.
Togashi T.
Oyama M.
Hata H.
Watanabe M.
Komatsu T.
Mizushima-Sugano J.
Satoh T.
Shirai Y.
Takahashi Y.
Nakagawa K.
Okumura K.
Nagase T.
Nomura N.
Kikuchi H.
Masuho Y.
Yamashita R.
Nakai K.
Yada T.
Nakamura Y.
Ohara O.
Isogai T.
Sugano S.

title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4)

authors:
Schmutz J.
Martin J.
Terry A.
Couronne O.
Grimwood J.
Lowry S.
Gordon L.A.
Scott D.
Xie G.
Huang W.
Hellsten U.
Tran-Gyamfi M.
She X.
Prabhakar S.
Aerts A.
Altherr M.
Bajorek E.
Black S.
Branscomb E.
Caoile C.
Challacombe J.F.
Chan Y.M.
Denys M.
Detter J.C.
Escobar J.
Flowers D.
Fotopulos D.
Glavina T.
Gomez M.
Gonzales E.
Goodstein D.
Grigoriev I.
Groza M.
Hammon N.
Hawkins T.
Haydu L.
Israni S.
Jett J.
Kadner K.
Kimball H.
Kobayashi A.
Lopez F.
Lou Y.
Martinez D.
Medina C.
Morgan J.
Nandkeshwar R.
Noonan J.P.
Pitluck S.
Pollard M.
Predki P.
Priest J.
Ramirez L.
Retterer J.
Rodriguez A.
Rogers S.
Salamov A.
Salazar A.
Thayer N.
Tice H.
Tsai M.
Ustaszewska A.
Vo N.
Wheeler J.
Wu K.
Yang J.
Dickson M.
Cheng J.-F.
Eichler E.E.
Olsen A.
Pennacchio L.A.
Rokhsar D.S.
Richardson P.
Lucas S.M.
Myers R.M.
Rubin E.M.

title: The DNA sequence and comparative analysis of human chromosome 5.

title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

authors:
Skvorak A.B.
Robertson N.G.
Yin Y.
Weremowicz S.
Her H.
Bieber F.R.
Beisel K.W.
Lynch E.D.
Beier D.R.
Morton C.C.

title: An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1).

referencePositions: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-268

authors:
Gauci S.
Helbig A.O.
Slijper M.
Krijgsveld J.
Heck A.J.
Mohammed S.

title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

referencePositions: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2)

referencePositions: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2)

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Brocker C.
Cantore M.
Failli P.
Vasiliou V.

title: Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and oxidative stress induced cytotoxicity.

referencePositions:
FUNCTION
CATALYTIC ACTIVITY
BIOPHYSICOCHEMICAL PROPERTIES

authors:
Bienvenut W.V.
Sumpton D.
Martinez A.
Lilla S.
Espagne C.
Meinnel T.
Giglione C.

title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

authors:
Yang J.S.
Hsu J.W.
Park S.Y.
Lee S.Y.
Li J.
Bai M.
Alves C.
Tseng W.
Michelet X.
Ho I.C.
Hsu V.W.

title: ALDH7A1 inhibits the intracellular transport pathways during hypoxia and starvation to promote cellular energy homeostasis.

referencePositions:
FUNCTION (ISOFORM 2)
SUBCELLULAR LOCATION (ISOFORM 2)
PHOSPHORYLATION AT SER-130
MUTAGENESIS OF SER-130 AND SER-174

authors:
Yang J.S.
Morris A.J.
Kamizaki K.
Chen J.
Stark J.
Oldham W.M.
Nakamura T.
Mishima E.
Loscalzo J.
Minami Y.
Conrad M.
Henry W.S.
Hsu V.W.

title: ALDH7A1 protects against ferroptosis by generating membrane NADH and regulating FSP1.

referencePositions:
FUNCTION (ISOFORM 2)
CATALYTIC ACTIVITY
SUBCELLULAR LOCATION (ISOFORM 2)
PHOSPHORYLATION AT SER-130
MUTAGENESIS OF SER-130 AND GLU-296

authors:
Brocker C.
Lassen N.
Estey T.
Pappa A.
Cantore M.
Orlova V.V.
Chavakis T.
Kavanagh K.L.
Oppermann U.
Vasiliou V.

title: Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 30-526 IN COMPLEX WITH NADH

authors:
Luo M.
Gates K.S.
Henzl M.T.
Tanner J.J.

title: Diethylaminobenzaldehyde is a covalent, irreversible inactivator of ALDH7A1.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-539 IN COMPLEX WITH NAD(+)

title: Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 29-539 IN COMPLEX WITH NAD AND (S)-2-AMINO-6-OXOHEXANOATE

authors:
Laciak A.R.
Korasick D.A.
Wyatt J.W.
Gates K.S.
Tanner J.J.

title: Structural and biochemical consequences of pyridoxine-dependent epilepsy mutations that target the aldehyde binding site of aldehyde dehydrogenase ALDH7A1.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 29-539 OF VARIANTS SER-195; SER-197; VAL-199; VAL-202 AND GLY-203 IN COMPLEX WITH NAD(+)

referencePositions: VARIANTS EPEO4 SER-195; SER-197; VAL-199; VAL-202 AND GLY-203

referencePositions: CHARACTERIZATION OF VARIANTS EPEO4 SER-195; SER-197; VAL-199 AND GLY-203

authors:
Laciak A.R.
Korasick D.A.
Gates K.S.
Tanner J.J.

title: Structural analysis of pathogenic mutations targeting Glu427 of ALDH7A1, the hot spot residue of pyridoxine-dependent epilepsy.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 29-539 OF VARIANTS ASP-427; GLN-427 AND GLY-427 IN COMPLEX WITH NAD(+)

referencePositions: VARIANTS EPEO4 GLN-427; ASP-427 AND GLY-427

referencePositions: CHARACTERIZATION OF VARIANTS EPEO4 GLN-427; ASP-427 AND GLY-427

authors:
Korasick D.A.
Buckley D.P.
Palpacelli A.
Cursio I.
Cesaroni E.
Cheng J.
Tanner J.J.

title: Biochemical, structural, and computational analyses of two new clinically identified missense mutations of ALDH7A1.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 29-539 OF VARIANTS SER-162 AND CYS-429 IN COMPLEX WITH NAD(+)

referencePositions: CHARACTERIZATION OF VARIANTS EPEO4 SER-162 AND CYS-469

authors:
Mills P.B.
Struys E.
Jakobs C.
Plecko B.
Baxter P.
Baumgartner M.
Willemsen M.A.A.P.
Omran H.
Tacke U.
Uhlenberg B.
Weschke B.
Clayton P.T.

title: Mutations in antiquitin in individuals with pyridoxine-dependent seizures.

referencePositions: VARIANTS EPEO4 110-ARG--GLN-539 DEL; VAL-199; 408-TYR--GLN-539 DEL AND GLN-427

referencePositions: CHARACTERIZATION OF VARIANTS EPEO4 110-ARG--GLN-539 DEL; VAL-199 AND GLN-427

authors:
Plecko B.
Paul K.
Paschke E.
Stoeckler-Ipsiroglu S.
Struys E.
Jakobs C.
Hartmann H.
Luecke T.
di Capua M.
Korenke C.
Hikel C.
Reutershahn E.
Freilinger M.
Baumeister F.
Bosch F.
Erwa W.

title: Biochemical and molecular characterization of 18 patients with pyridoxine-dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene.

referencePositions: VARIANTS EPEO4 VAL-202; GLU-291; ILE-301; GLN-335; GLY-395; GLN-427 AND ASN-458

authors:
Bennett C.L.
Chen Y.
Hahn S.
Glass I.A.
Gospe S.M. Jr.

title: Prevalence of ALDH7A1 mutations in 18 North American pyridoxine-dependent seizure (PDS) patients.

authors:
Mills P.B.
Footitt E.J.
Mills K.A.
Tuschl K.
Aylett S.
Varadkar S.
Hemingway C.
Marlow N.
Rennie J.
Baxter P.
Dulac O.
Nabbout R.
Craigen W.J.
Schmitt B.
Feillet F.
Christensen E.
De Lonlay P.
Pike M.G.
Hughes M.I.
Struys E.A.
Jakobs C.
Zuberi S.M.
Clayton P.T.

title: Genotypic and phenotypic spectrum of pyridoxine-dependent epilepsy (ALDH7A1 deficiency).

referencePositions: VARIANTS EPEO4 LEU-106; SER-197; GLY-203; LEU-317; ARG-328 AND LEU-476

referencePositions: CHARACTERIZATION OF VARIANTS EPEO4 LEU-106; SER-197; GLY-203; LEU-317; ARG-328 AND LEU-476

authors:
Tincheva S.
Todorov T.
Todorova A.
Georgieva R.
Stamatov D.
Yordanova I.
Kadiyska T.
Georgieva B.
Bojidarova M.
Tacheva G.
Litvinenko I.
Mitev V.

title: First cases of pyridoxine-dependent epilepsy in Bulgaria: novel mutation in the ALDH7A1 gene.

referencePositions: VARIANTS EPEO4 99-TRP--GLN-539 DEL; 110-ARG--GLN-539 DEL AND SER-195

value: Pyridoxine-dependent-developmental and epileptic encephalopathy

value: 0 GO annotations based on evolutionary models

value: Presynaptic clusters and postsynaptic densities

value: Expressed in right lobe of liver and 173 other cell types or tissues

value: F:aldehyde dehydrogenase (NAD+) activity

value: F:betaine-aldehyde dehydrogenase (NAD+) activity

value: F:L-aminoadipate-semialdehyde dehydrogenase [NAD(P)+] activity

value: F:medium-chain fatty aldehyde dehydrogenase (NAD+) activity

value: F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor

value: P:glycine betaine biosynthetic process from choline

value: P:negative regulation of endosome to plasma membrane protein transport

value: P:negative regulation of Golgi to plasma membrane protein transport

value: Aldehyde Dehydrogenase, Chain A, domain 1

value: Aldehyde Dehydrogenase, Chain A, domain 2


value: C-X-C chemokine receptor type 3

value: G protein-coupled receptor 9

value: Interferon-inducible protein 10 receptor

value: IP-10 receptor

value: Receptor for the C-X-C chemokines CXCL9, CXCL10 and CXCL11, and mediates the proliferation, survival and angiogenic activity of human mesangial cells (HMC) through a heterotrimeric G-protein signaling pathway (PubMed:12782716). Probably promotes cell chemotaxis response. Upon activation by PF4, induces activated T-lymphocyte migration mediated via downstream Ras/extracellular signal-regulated kinase (ERK) signaling

value: Receptor for the C-X-C chemokine CXCL4 and also mediates the inhibitory activities of CXCL9, CXCL10 and CXCL11 on the proliferation, survival and angiogenic activity of human microvascular endothelial cells (HMVEC) through a cAMP-mediated signaling pathway (PubMed:12782716). Does not promote cell chemotaxis response. Interaction with CXCL4 or CXCL10 leads to activation of the p38MAPK pathway and contributes to inhibition of angiogenesis. Overexpression in renal cancer cells down-regulates expression of the anti-apoptotic protein HMOX1 and promotes apoptosis

value: Mediates the activity of CXCL11

molecule: Isoform 3

value: Homomer. Forms heteromers with ACKR4

value: Interacts with PF4/CXCL4

commentType: INTERACTION

commentType: SUBCELLULAR LOCATION

value: Cell membrane

value: Multi-pass membrane protein

commentType: ALTERNATIVE PRODUCTS

isoformSequenceStatus: Displayed

isoformSequenceStatus: Described

value: Isoform 1 and isoform 2 are mainly expressed in heart, kidney, liver and skeletal muscle. Isoform 1 is also expressed in placenta. Isoform 2 is expressed in endothelial cells. Expressed in T-cells (at protein level)

commentType: TISSUE SPECIFICITY

value: Sulfation on Tyr-27 and Tyr-29 is essential for CXCL10 binding and subsequent signal transduction induction

commentType: PTM

value: N-glycosylated

value: Due to exon skipping

commentType: MISCELLANEOUS

source: PROSITE-ProRule

value: Belongs to the G protein-coupled receptor 1 family

commentType: SIMILARITY

value: In contrast to its murine ortholog, human chemokine CCL21 does not bind the CXCR3 chemokine receptor

commentType: CAUTION

commentType: WEB RESOURCE

resourceName: Atlas of Genetics and Cytogenetics in Oncology and Haematology

resourceName: Wikipedia

note: CXC chemokine receptors entry

type: Chain

modifier: EXACT

description: C-X-C chemokine receptor type 3

type: Topological domain

description: Extracellular

type: Transmembrane

description: Helical; Name=1

description: Cytoplasmic

description: Helical; Name=2

description: Extracellular

description: Helical; Name=3

description: Cytoplasmic

description: Helical; Name=4

description: Extracellular

description: Helical; Name=5

description: Cytoplasmic

description: Helical; Name=6

description: Extracellular

description: Helical; Name=7

description: Cytoplasmic

description: Disordered

description: Low complexity

description: Sulfotyrosine

description: Sulfotyrosine

description: N-linked (GlcNAc...) asparagine

description: N-linked (GlcNAc...) asparagine

description: in isoform 2

description: in isoform 3

description: in dbSNP:rs139226823

description: in dbSNP:rs766348940

description: Reduces binding to CXCL10 and CXCL11, and reduces CXCL10- and CXCL11-induced chemotaxis and activation. Does not affect CXCL9-induced chemotaxis and activation.

description: Does not affect binding to CXCL9, CXCL10 and CXCL11 or activation.

description: Reduces slightly CXCL9-, CXCL10- and CXCL11-induced chemotaxis.

description: Reduces sulfation and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to CXCL10. Abolishes sulfation, binding to CXCL11, ligand-induced receptor internalization and CXCL9-, CXCL10- and CXCL11-induced chemotaxis; when associated with F-29.

description: Reduces sulfation, binding to CXCL10 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes sulfation, binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis; when associated with F-27.

description: Abolishes binding to CXCL10 and CXCL11. Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis.

description: Abolishes binding to CXCL10 and CXCL11 and CXCL10- and CXCL11-induced chemotaxis. Reduces CXCL9-induced chemotaxis.

description: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Reduces ligand-induced receptor internalization.

description: Abolishes CXCL10-induced chemotaxis. Reduces CXCL9- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11.

description: Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11 or receptor internalization.

description: Abolishes binding to CXCL10 and CXCL11 and CXCL11-induced chemotaxis. Reduces CXCL9 and CXCL10-induced chemotaxis.

description: Reduces binding to CXCL10 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11.

description: Reduces binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis.

description: Reduces binding to CXCL10 and CXCL9- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11 and CXCL10-induced chemotaxis.

description: in Ref. 4; CAB02143

description: in Ref. 6; BAG36429

authors:
Loetscher M.
Gerber B.
Loetscher P.
Jones S.A.
Piali L.
Clark-Lewis I.
Baggiolini M.
Moser B.

title: Chemokine receptor specific for IP10 and mig: structure, function, and expression in activated T-lymphocytes.

authors:
Lasagni L.
Francalanci M.
Annunziato F.
Lazzeri E.
Giannini S.
Cosmi L.
Sagrinati C.
Mazzinghi B.
Orlando C.
Maggi E.
Marra F.
Romagnani S.
Serio M.
Romagnani P.

title: An alternatively spliced variant of CXCR3 mediates the inhibition of endothelial cell growth induced by IP-10, Mig, and I-TAC, and acts as functional receptor for platelet factor 4.

referencePositions: LACK OF CCL21-BINDING ACTIVITY (ISOFORM 2)

authors:
Petrai I.
Rombouts K.
Lasagni L.
Annunziato F.
Cosmi L.
Romanelli R.G.
Sagrinati C.
Mazzinghi B.
Pinzani M.
Romagnani S.
Romagnani P.
Marra F.

title: Activation of p38(MAPK) mediates the angiostatic effect of the chemokine receptor CXCR3-B.

referencePositions: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2)

authors:
Gutierrez J.
Varona R.
Zaballos A.
Lind P.
Marquez G.

referencePositions: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2)

title: cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org).

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)

authors:
Ota T.
Suzuki Y.
Nishikawa T.
Otsuki T.
Sugiyama T.
Irie R.
Wakamatsu A.
Hayashi K.
Sato H.
Nagai K.
Kimura K.
Makita H.
Sekine M.
Obayashi M.
Nishi T.
Shibahara T.
Tanaka T.
Ishii S.
Yamamoto J.
Saito K.
Kawai Y.
Isono Y.
Nakamura Y.
Nagahari K.
Murakami K.
Yasuda T.
Iwayanagi T.
Wagatsuma M.
Shiratori A.
Sudo H.
Hosoiri T.
Kaku Y.
Kodaira H.
Kondo H.
Sugawara M.
Takahashi M.
Kanda K.
Yokoi T.
Furuya T.
Kikkawa E.
Omura Y.
Abe K.
Kamihara K.
Katsuta N.
Sato K.
Tanikawa M.
Yamazaki M.
Ninomiya K.
Ishibashi T.
Yamashita H.
Murakawa K.
Fujimori K.
Tanai H.
Kimata M.
Watanabe M.
Hiraoka S.
Chiba Y.
Ishida S.
Ono Y.
Takiguchi S.
Watanabe S.
Yosida M.
Hotuta T.
Kusano J.
Kanehori K.
Takahashi-Fujii A.
Hara H.
Tanase T.-O.
Nomura Y.
Togiya S.
Komai F.
Hara R.
Takeuchi K.
Arita M.
Imose N.
Musashino K.
Yuuki H.
Oshima A.
Sasaki N.
Aotsuka S.
Yoshikawa Y.
Matsunawa H.
Ichihara T.
Shiohata N.
Sano S.
Moriya S.
Momiyama H.
Satoh N.
Takami S.
Terashima Y.
Suzuki O.
Nakagawa S.
Senoh A.
Mizoguchi H.
Goto Y.
Shimizu F.
Wakebe H.
Hishigaki H.
Watanabe T.
Sugiyama A.
Takemoto M.
Kawakami B.
Yamazaki M.
Watanabe K.
Kumagai A.
Itakura S.
Fukuzumi Y.
Fujimori Y.
Komiyama M.
Tashiro H.
Tanigami A.
Fujiwara T.
Ono T.
Yamada K.
Fujii Y.
Ozaki K.
Hirao M.
Ohmori Y.
Kawabata A.
Hikiji T.
Kobatake N.
Inagaki H.
Ikema Y.
Okamoto S.
Okitani R.
Kawakami T.
Noguchi S.
Itoh T.
Shigeta K.
Senba T.
Matsumura K.
Nakajima Y.
Mizuno T.
Morinaga M.
Sasaki M.
Togashi T.
Oyama M.
Hata H.
Watanabe M.
Komatsu T.
Mizushima-Sugano J.
Satoh T.
Shirai Y.
Takahashi Y.
Nakagawa K.
Okumura K.
Nagase T.
Nomura N.
Kikuchi H.
Masuho Y.
Yamashita R.
Nakai K.
Yada T.
Nakamura Y.
Ohara O.
Isogai T.
Sugano S.

title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

authors:
Marchese A.
Heiber M.
Nguyen T.
Heng H.H.Q.
Saldivia V.R.
Cheng R.
Murphy P.M.
Tsui L.-C.
Shi X.
Gregor P.
George S.R.
O'Dowd B.F.
Docherty J.M.

title: Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and somatostatin receptors.

referencePositions: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-368

title: Single nucleotide polymorphisms in the coding regions of human CXC-chemokine receptors CXCR1, CXCR2 and CXCR3.

referencePositions: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-368

authors:
Jenh C.H.
Cox M.A.
Kaminski H.
Zhang M.
Byrnes H.
Fine J.
Lundell D.
Chou C.C.
Narula S.K.
Zavodny P.J.

title: Cutting edge: species specificity of the CC chemokine 6Ckine signaling through the CXC chemokine receptor CXCR3: human 6Ckine is not a ligand for the human or mouse CXCR3 receptors.

authors:
Ehlert J.E.
Addison C.A.
Burdick M.D.
Kunkel S.L.
Strieter R.M.

title: Identification and partial characterization of a variant of human CXCR3 generated by posttranscriptional exon skipping.

referencePositions:
ALTERNATIVE SPLICING (ISOFORM 3)
FUNCTION

authors:
Cole K.E.
Strick C.A.
Paradis T.J.
Ogborne K.T.
Loetscher M.
Gladue R.P.
Lin W.
Boyd J.G.
Moser B.
Wood D.E.
Sahagan B.G.
Neote K.

title: Interferon-inducible T cell alpha chemoattractant (I-TAC): a novel non-ELR CXC chemokine with potent activity on activated T cells through selective high affinity binding to CXCR3.

authors:
Colvin R.A.
Campanella G.S.
Manice L.A.
Luster A.D.

title: CXCR3 requires tyrosine sulfation for ligand binding and a second extracellular loop arginine residue for ligand-induced chemotaxis.

authors:
Mueller A.
Meiser A.
McDonagh E.M.
Fox J.M.
Petit S.J.
Xanthou G.
Williams T.J.
Pease J.E.

title: CXCL4-induced migration of activated T lymphocytes is mediated by the chemokine receptor CXCR3.

referencePositions:
FUNCTION (ISOFORM 1)
INTERACTION WITH PF4 (ISOFORM 1 AND 2)

authors:
Gao J.M.
Xiang R.L.
Jiang L.
Li W.H.
Feng Q.P.
Guo Z.J.
Sun Q.
Zeng Z.P.
Fang F.D.

title: Sulfated tyrosines 27 and 29 in the N-terminus of human CXCR3 participate in binding native IP-10.

referencePositions:
SULFATION AT TYR-27 AND TYR-29
MUTAGENESIS OF TYR-27 AND TYR-29

authors:
Datta D.
Banerjee P.
Gasser M.
Waaga-Gasser A.M.
Pal S.

title: CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells by down-regulating the expression of heme oxygenase-1.

authors:
Vinet J.
van Zwam M.
Dijkstra I.M.
Brouwer N.
van Weering H.R.
Watts A.
Meijer M.
Fokkens M.R.
Kannan V.
Verzijl D.
Vischer H.F.
Smit M.J.
Leurs R.
Biber K.
Boddeke H.W.

title: Inhibition of CXCR3-mediated chemotaxis by the human chemokine receptor-like protein CCX-CKR.

authors:
Van Raemdonck K.
Gouwy M.
Lepers S.A.
Van Damme J.
Struyf S.

title: CXCL4L1 and CXCL4 signaling in human lymphatic and microvascular endothelial cells and activated lymphocytes: involvement of mitogen-activated protein (MAP) kinases, Src and p70S6 kinase.

value: Tissue enhanced (bone marrow, intestine, lymphoid tissue)

value: 7 GO annotations based on evolutionary models

value: Differentiation of naive CD4+ T cells to T helper 1 cells (Th1 cells)

value: Expressed in granulocyte and 109 other cell types or tissues

value: P:adenylate cyclase-activating G protein-coupled receptor signaling pathway

value: P:cell surface receptor signaling pathway

value: P:G protein-coupled receptor signaling pathway

value: P:negative regulation of endothelial cell proliferation

value: P:negative regulation of execution phase of apoptosis

value: P:positive regulation of cell population proliferation

value: P:positive regulation of cytosolic calcium ion concentration

value: P:positive regulation of execution phase of apoptosis

value: P:positive regulation of release of sequestered calcium ion into cytosol

value: P:positive regulation of transcription by RNA polymerase II

value: Rhodopsin 7-helix transmembrane proteins

value: Family A G protein-coupled receptor-like


value: Cyclin-dependent kinase 7

value: 39 kDa protein kinase

value: CDK-activating kinase 1

value: Cell division protein kinase 7

value: Serine/threonine-protein kinase 1

value: TFIIH basal transcription factor complex kinase subunit

value: CAK

value: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription (PubMed:9852112, PubMed:19136461, PubMed:26257281, PubMed:28768201). As a cyclin-dependent kinase, CDK7 is activated by the binding to cyclin-H/CCNH and the CDK-activating kinase assembly factor MAT1 (PubMed:41100585). Catalytic subunit of the CDK-activating kinase (CAK) complex, a master regulator of CDK activity by catalyzing the activating threonine phosphorylation of CDKs (PubMed:41100585). CAK activates major mediators of cell cycle control, including CDK1, CDK2, CDK4 and CDK6, and plays a key role in regulating cell cycle progression (PubMed:41100585). CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the CTD of POLR2A, allowing its escape from the promoter and elongation of the transcripts (PubMed:9852112). Initiates transcription by RNA polymerase II by mediating phosphorylation of POLR2A at 'Ser-5' of the repetitive C-terminal domain (CTD) when POLR2A is in complex with DNA, promoting dissociation from DNA and initiation (PubMed:19136461, PubMed:26257281, PubMed:28768201). Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11 (PubMed:9372954, PubMed:9840937, PubMed:19136461, PubMed:26257281, PubMed:28768201, PubMed:41100585, PubMed:41100585). Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition

name: L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)

name: L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)

name: [DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + ADP + H(+)

value: Activated by phosphorylation (PubMed:41100585). Phosphorylated by CDKs, including CDK1 and CDK2, and reciprocally phosphorylating its activating kinase (PubMed:41100585). Repressed by roscovitine (seliciclib, CYC202), R547 (Ro-4584820) and SNS-032 (BMS-387032). The association of p53/TP53 to the CAK complex in response to DNA damage reduces kinase activity toward CDK2 and RNA polymerase II repetitive C-terminal domain (CTD), thus stopping cell cycle progression (PubMed:9840937). The inactivation by roscovitine promotes caspase-mediated apoptosis in leukemic cells (PubMed:19911397). Specifically inactivated by THZ1 (PubMed:26257281)

commentType: ACTIVITY REGULATION

value: Component of the CDK-activating kinase (CAK) complex, consisting of CDK7, cyclin-H/CCNH and MAT1, which is a master regulator of CDK activity (PubMed:41100585). CAK binds to both free CDK2 and cyclin-bound CDK2, with a higher affinity for the cyclin-bound form (PubMed:41100585). CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor (PubMed:9852112). The CAK complex binds to p53/TP53 in response to DNA damage. Interacts with CDK2, SF1/NR5A1, PUF60 and PRKCI. Interacts with HINT1 (PubMed:10958787)

value: Colocalizes with PRKCI in the cytoplasm and nucleus (PubMed:15695176). Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides (PubMed:19071173)

value: Nucleus

value: Cytoplasm

value: Cytoplasm, perinuclear region

value: Phosphorylation of Ser-164 during mitosis inactivates the enzyme. Phosphorylation of Thr-170 is required for activity. Phosphorylated at Ser-164 and Thr-170 by CDK2

value: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily

description: Removed

description: Cyclin-dependent kinase 7

description: Protein kinase

description: Proton acceptor

description: N-acetylalanine

description: Phosphoserine

description: Phosphoserine; by CDK1 and CDK2

description: Phosphothreonine; by CDK2

description: Phosphoserine

description: in dbSNP:rs34584424

description: Total loss of activity.

description: No effect on interaction with HINT1.

description: Enhanced capacity to bind ATP analogs.

description: No mitotic repression of transcriptional activity of the reconstituted TFIIH complex.

description: Total loss of activity. Total loss of transcriptional activity of the reconstituted TFIIH complex.

description: No effect on interaction with HINT1.

description: Impairs phosphorylation of CDK2; when associated with A-217 and A-223.

description: Impairs phosphorylation of CDK2; when associated with A-176 and A-223.

description: Impairs phosphorylation of CDK2.

description: Impairs phosphorylation of CDK2; when associated with A-176 and A-217.

description: in Ref. 7; AAH05298

description: in Ref. 5; CAA73587

description: in Ref. 5; CAA73587

authors:
Tassan J.-P.
Schultz S.J.
Bartek J.
Nigg E.A.

title: Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase).

authors:
Levedakou E.N.
He M.
Baptist E.W.
Craven R.J.
Cance W.G.
Welcsh P.L.
Simmons A.
Naylor S.L.
Leach R.J.
Lewis T.B.
Bowcock A.
Liu E.T.

title: Two novel human serine/threonine kinases with homologies to the cell cycle regulating Xenopus MO15, and NIMA kinases: cloning and characterization of their expression pattern.

authors:
Darbon J.-M.
Devault A.
Taviaux S.
Fesquet D.
Martinez A.-M.
Galas S.
Cavadore J.-C.
Doree M.
Blanchard J.-M.

title: Cloning, expression and subcellular localization of the human homolog of p40MO15 catalytic subunit of cdk-activating kinase.

authors:
Wu L.
Yee A.
Liu L.
Carbonaro-Hall D.
Venkatesan N.
Tolo T.
Hall F.L.

title: Molecular cloning of the human CAK1 gene encoding a cyclin-dependent kinase-activating kinase.

authors:
Kobelt D.
Karn T.
Hock B.
Holtrich U.
Braeuninger A.
Wolf G.
Strebhardt K.
Ruebsamen-Waigmann H.

title: Human and Xenopus MO15 mRNA are highly conserved but show different patterns of expression in adult tissues.

referencePositions:
NUCLEOTIDE SEQUENCE [GENOMIC DNA]
VARIANTS ALA-163 AND MET-285

title: A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase.

authors:
Ko L.J.
Shieh S.-Y.
Chen X.
Jayaraman L.
Tamai K.
Taya Y.
Prives C.
Pan Z.-Q.

title: p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner.

title: The molecular mechanism of mitotic inhibition of TFIIH is mediated by phosphorylation of CDK7.

referencePositions:
PHOSPHORYLATION AT SER-164 AND THR-170
MUTAGENESIS OF SER-164 AND THR-170

title: Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes.

referencePositions: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR

title: Regulation of CAK kinase activity by p53.

referencePositions:
FUNCTION AS CDK2 KINASE
IDENTIFICATION IN COMPLEX WITH TP53
ACTIVITY REGULATION

title: Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7.

title: Interactions of Cdk7 and Kin28 with Hint/PKCI-1 and Hnt1 histidine triad proteins.

referencePositions:
INTERACTION WITH HINTI
MUTAGENESIS OF LYS-41 AND THR-170
SUBCELLULAR LOCATION

authors:
Liu J.
He L.
Collins I.
Ge H.
Libutti D.
Li J.
Egly J.-M.
Levens D.

title: The FBP interacting repressor targets TFIIH to inhibit activated transcription.

authors:
Garrett S.
Barton W.A.
Knights R.
Jin P.
Morgan D.O.
Fisher R.P.

title: Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop.

referencePositions: PHOSPHORYLATION AT SER-164 AND THR-170 BY CDK2

title: Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-iota in human glioma cells.

referencePositions:
INTERACTION WITH PRKCI
SUBCELLULAR LOCATION

authors:
Larochelle S.
Batliner J.
Gamble M.J.
Barboza N.M.
Kraybill B.C.
Blethrow J.D.
Shokat K.M.
Fisher R.P.

title: Dichotomous but stringent substrate selection by the dual-function Cdk7 complex revealed by chemical genetics.

referencePositions:
FUNCTION AS SPT5/SUPT5H AND CDK KINASE
MUTAGENESIS OF PHE-91
IDENTIFICATION IN CAK COMPLEX

authors:
Larochelle S.
Merrick K.A.
Terret M.-E.
Wohlbold L.
Barboza N.M.
Zhang C.
Shokat K.M.
Jallepalli P.V.
Fisher R.P.

title: Requirements for Cdk7 in the assembly of Cdk1/cyclin B and activation of Cdk2 revealed by chemical genetics in human cells.

title: Recognition of Cdk2 by Cdk7.

referencePositions:
FUNCTION AS CDK2 KINASE
INTERACTION WITH CDK2

authors:
Cantin G.T.
Yi W.
Lu B.
Park S.K.
Xu T.
Lee J.-D.
Yates J.R. III

title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Daub H.
Olsen J.V.
Bairlein M.
Gnad F.
Oppermann F.S.
Korner R.
Greff Z.
Keri G.
Stemmann O.
Mann M.

title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-164 AND SER-321

authors:
Lewis A.E.
Rusten M.
Hoivik E.A.
Vikse E.L.
Hansson M.L.
Wallberg A.E.
Bakke M.

title: Phosphorylation of steroidogenic factor 1 is mediated by cyclin-dependent kinase 7.

referencePositions:
FUNCTION AS SF1/NR5A1 KINASE
INTERACTION WITH SF1/NR5A1

authors:
Dephoure N.
Zhou C.
Villen J.
Beausoleil S.A.
Bakalarski C.E.
Elledge S.J.
Gygi S.P.

title: A quantitative atlas of mitotic phosphorylation.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND THR-170

authors:
Akhtar M.S.
Heidemann M.
Tietjen J.R.
Zhang D.W.
Chapman R.D.
Eick D.
Ansari A.Z.

title: TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II.

authors:
Yang W.-H.
Heaton J.H.
Brevig H.
Mukherjee S.
Iniguez-Lluhi J.A.
Hammer G.D.

title: SUMOylation inhibits SF-1 activity by reducing CDK7-mediated serine 203 phosphorylation.

authors:
Glover-Cutter K.
Larochelle S.
Erickson B.
Zhang C.
Shokat K.
Fisher R.P.
Bentley D.L.

title: TFIIH-associated Cdk7 kinase functions in phosphorylation of C-terminal domain Ser7 residues, promoter-proximal pausing, and termination by RNA polymerase II.

authors:
Oppermann F.S.
Gnad F.
Olsen J.V.
Hornberger R.
Greff Z.
Keri G.
Mann M.
Daub H.

title: Large-scale proteomics analysis of the human kinome.

title: Binding to DNA of the RNA-polymerase II C-terminal domain allows discrimination between Cdk7 and Cdk9 phosphorylation.

title: DNA-Bound peptides control the mRNA transcription through CDK7.

referencePositions: FUNCTION IN DNA-BOUND PEPTIDES TRANSCRIPTION INHIBITION

authors:
Mayya V.
Lundgren D.H.
Hwang S.-I.
Rezaul K.
Wu L.
Eng J.K.
Rodionov V.
Han D.K.

title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170

authors:
Timofeev O.
Cizmecioglu O.
Settele F.
Kempf T.
Hoffmann I.

title: Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B at the G2/M transition.

authors:
Rogalinska M.
Blonski J.Z.
Komina O.
Goralski P.
Zolnierczyk J.D.
Piekarski H.
Robak T.
Kilianska Z.M.
Wesierska-Gadek J.

title: R-roscovitine (Seliciclib) affects CLL cells more strongly than combinations of fludarabine or cladribine with cyclophosphamide: Inhibition of CDK7 sensitizes leukemic cells to caspase-dependent apoptosis.

title: CAK-Cyclin-dependent Activating Kinase: a key kinase in cell cycle control and a target for drugs?

title: Cell cycle, CDKs and cancer: a changing paradigm.

authors:
Olsen J.V.
Vermeulen M.
Santamaria A.
Kumar C.
Miller M.L.
Jensen L.J.
Gnad F.
Cox J.
Jensen T.S.
Nigg E.A.
Brunak S.
Mann M.

title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170 AND SER-321

authors:
Burkard T.R.
Planyavsky M.
Kaupe I.
Breitwieser F.P.
Buerckstuemmer T.
Bennett K.L.
Superti-Furga G.
Colinge J.

title: Initial characterization of the human central proteome.

title: A history of TFIIH: Two decades of molecular biology on a pivotal transcription/repair factor.

authors:
Rigbolt K.T.
Prokhorova T.A.
Akimov V.
Henningsen J.
Johansen P.T.
Kratchmarova I.
Kassem M.
Mann M.
Olsen J.V.
Blagoev B.

title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

authors:
Van Damme P.
Lasa M.
Polevoda B.
Gazquez C.
Elosegui-Artola A.
Kim D.S.
De Juan-Pardo E.
Demeyer K.
Hole K.
Larrea E.
Timmerman E.
Prieto J.
Arnesen T.
Sherman F.
Gevaert K.
Aldabe R.

title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

referencePositions: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2

referencePositions: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]

authors:
Zhou H.
Di Palma S.
Preisinger C.
Peng M.
Polat A.N.
Heck A.J.
Mohammed S.

title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

authors:
Bian Y.
Song C.
Cheng K.
Dong M.
Wang F.
Huang J.
Sun D.
Wang L.
Ye M.
Zou H.

title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

authors:
Nilson K.A.
Guo J.
Turek M.E.
Brogie J.E.
Delaney E.
Luse D.S.
Price D.H.

title: THZ1 Reveals Roles for Cdk7 in Co-transcriptional Capping and Pausing.

referencePositions:
FUNCTION
CATALYTIC ACTIVITY
ACTIVITY REGULATION

authors:
Ebmeier C.C.
Erickson B.
Allen B.L.
Allen M.A.
Kim H.
Fong N.
Jacobsen J.R.
Liang K.
Shilatifard A.
Dowell R.D.
Old W.M.
Bentley D.L.
Taatjes D.J.

title: Human TFIIH Kinase CDK7 Regulates Transcription-Associated Chromatin Modifications.

authors:
Lolli G.
Lowe E.D.
Brown N.R.
Johnson L.N.

title: The crystal structure of human CDK7 and its protein recognition properties.

referencePositions: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) IN COMPLEX WITH ATP

authors:
Cushing V.I.
McGeoch A.J.S.
Williams S.L.
Roumeliotis T.I.
Feng J.
Dan L.M.
Choudhary J.S.
Davey N.E.
Greber B.J.

title: Structural basis of T-loop-independent recognition and activation of CDKs by the CDK-activating kinase.

referencePositions: STRUCTURE BY ELECTRON MICROSCOPY (2.40 ANGSTROMS) IN COMPLEX WITH ADP AND MG(2+)

referencePositions: MUTAGENESIS OF ARG-176; SER-217; LEU-219 AND THR-223

authors:
Greenman C.
Stephens P.
Smith R.
Dalgliesh G.L.
Hunter C.
Bignell G.
Davies H.
Teague J.
Butler A.
Stevens C.
Edkins S.
O'Meara S.
Vastrik I.
Schmidt E.E.
Avis T.
Barthorpe S.
Bhamra G.
Buck G.
Choudhury B.
Clements J.
Cole J.
Dicks E.
Forbes S.
Gray K.
Halliday K.
Harrison R.
Hills K.
Hinton J.
Jenkinson A.
Jones D.
Menzies A.
Mironenko T.
Perry J.
Raine K.
Richardson D.
Shepherd R.
Small A.
Tofts C.
Varian J.
Webb T.
West S.
Widaa S.
Yates A.
Cahill D.P.
Louis D.N.
Goldstraw P.
Nicholson A.G.
Brasseur F.
Looijenga L.
Weber B.L.
Chiew Y.-E.
DeFazio A.
Greaves M.F.
Green A.R.
Campbell P.
Birney E.
Easton D.F.
Chenevix-Trench G.
Tan M.-H.
Khoo S.K.
Teh B.T.
Yuen S.T.
Leung S.Y.
Wooster R.
Futreal P.A.
Stratton M.R.

title: Patterns of somatic mutation in human cancer genomes.

value: General transcription factor TFIIH complex

value: Cyclin-dependent protein kinase-activating kinase complex

value: Formation of RNA Pol II elongation complex

value: Formation of the Early Elongation Complex

value: Formation of HIV elongation complex in the absence of HIV Tat

value: Formation of the HIV-1 Early Elongation Complex

value: RNA Pol II CTD phosphorylation and interaction with CE during HIV infection

value: Formation of HIV-1 elongation complex containing HIV-1 Tat

value: Tat-mediated elongation of the HIV-1 transcript

value: NoRC negatively regulates rRNA expression

value: RNA Polymerase II Pre-transcription Events

value: Formation of TC-NER Pre-Incision Complex

value: Transcription-Coupled Nucleotide Excision Repair (TC-NER)

value: Gap-filling DNA repair synthesis and ligation in TC-NER

value: TP53 Regulates Transcription of DNA Repair Genes

value: RNA polymerase II transcribes snRNA genes

value: Cyclin E associated events during G1/S transition

value: Cyclin A/B1/B2 associated events during G2/M transition

value: Cyclin A:Cdk2-associated events at S phase entry

value: RNA Polymerase I Transcription Initiation

value: RNA Polymerase II Transcription Pre-Initiation And Promoter Opening

value: RNA Polymerase I Transcription Termination

value: RNA Polymerase II Transcription Initiation

value: RNA Polymerase II Transcription Elongation

value: RNA Polymerase II Transcription Initiation And Promoter Clearance

value: RNA Pol II CTD phosphorylation and interaction with CE

value: RUNX1 regulates transcription of genes involved in differentiation of HSCs

value: Expressed in placenta and 102 other cell types or tissues

value: C:cyclin-dependent protein kinase holoenzyme complex

value: C:transcription factor TFIIH core complex

value: C:transcription factor TFIIH holo complex

value: F:cyclin-dependent protein serine/threonine kinase activity

value: F:protein serine/threonine kinase activity

value: F:RNA polymerase II CTD heptapeptide repeat kinase activity

value: F:RNA polymerase II CTD heptapeptide repeat S5 kinase activity

value: P:regulation of G1/S transition of mitotic cell cycle

value: P:snRNA transcription by RNA polymerase II

value: P:transcription initiation at RNA polymerase II promoter


scientificName: Drosophila melanogaster

commonName: Fruit fly

lineage: Eukaryota Metazoa Ecdysozoa Arthropoda Altocrustacea Allotriocarida Hexapoda Insecta Pterygota Neoptera Eumetabola Endopterygota Aparaglossata Panorpida Diptera Brachycera Muscomorpha Ephydroidea Drosophilidae Drosophila Sophophora

proteinExistence: 2: Evidence at transcript level

source: FlyBase

source: UniProtKB

value: alpha-Man-Ia

value: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2)

name: N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) + 4 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 4 beta-D-mannose

name: N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) + 3 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 3 beta-D-mannose

commentType: COFACTOR

value: Protein modification; protein glycosylation

commentType: PATHWAY

value: Golgi apparatus membrane

value: Single-pass type II membrane protein

value: H

value: A

value: J

value: L

value: M

value: N

value: O

value: K

value: B

value: P

value: Complex spatial distribution during embryogenesis, including expression in lobula plate giant neurons. Also expressed in adult wing and eyes

value: Expressed both maternally and zygotically during embryonic stages

commentType: DEVELOPMENTAL STAGE

source: RuleBase

value: Belongs to the glycosyl hydrolase 47 family

description: Mannosyl-oligosaccharide alpha-1,2-mannosidase IA

description: Cytoplasmic

description: Helical; Signal-anchor for type II membrane protein

description: Lumenal

type: Region

description: Disordered

source: SAM

type: Compositional bias

description: Low complexity

type: Active site

description: Proton donor

type: Binding site

description: N-linked (GlcNAc...) asparagine

description: in isoform K

description: in Ref. 1; CAA57962

description: in Ref. 1; CAA57962

authors:
Kerscher S.
Albert S.
Wucherpfennig D.
Heisenberg M.
Schneuwly S.

title: Molecular and genetic analysis of the Drosophila mas-1 (mannosidase-1) gene which encodes a glycoprotein processing alpha 1,2-mannosidase.

referencePositions: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H AND K)

authors:
Adams M.D.
Celniker S.E.
Holt R.A.
Evans C.A.
Gocayne J.D.
Amanatides P.G.
Scherer S.E.
Li P.W.
Hoskins R.A.
Galle R.F.
George R.A.
Lewis S.E.
Richards S.
Ashburner M.
Henderson S.N.
Sutton G.G.
Wortman J.R.
Yandell M.D.
Zhang Q.
Chen L.X.
Brandon R.C.
Rogers Y.-H.C.
Blazej R.G.
Champe M.
Pfeiffer B.D.
Wan K.H.
Doyle C.
Baxter E.G.
Helt G.
Nelson C.R.
Miklos G.L.G.
Abril J.F.
Agbayani A.
An H.-J.
Andrews-Pfannkoch C.
Baldwin D.
Ballew R.M.
Basu A.
Baxendale J.
Bayraktaroglu L.
Beasley E.M.
Beeson K.Y.
Benos P.V.
Berman B.P.
Bhandari D.
Bolshakov S.
Borkova D.
Botchan M.R.
Bouck J.
Brokstein P.
Brottier P.
Burtis K.C.
Busam D.A.
Butler H.
Cadieu E.
Center A.
Chandra I.
Cherry J.M.
Cawley S.
Dahlke C.
Davenport L.B.
Davies P.
de Pablos B.
Delcher A.
Deng Z.
Mays A.D.
Dew I.
Dietz S.M.
Dodson K.
Doup L.E.
Downes M.
Dugan-Rocha S.
Dunkov B.C.
Dunn P.
Durbin K.J.
Evangelista C.C.
Ferraz C.
Ferriera S.
Fleischmann W.
Fosler C.
Gabrielian A.E.
Garg N.S.
Gelbart W.M.
Glasser K.
Glodek A.
Gong F.
Gorrell J.H.
Gu Z.
Guan P.
Harris M.
Harris N.L.
Harvey D.A.
Heiman T.J.
Hernandez J.R.
Houck J.
Hostin D.
Houston K.A.
Howland T.J.
Wei M.-H.
Ibegwam C.
Jalali M.
Kalush F.
Karpen G.H.
Ke Z.
Kennison J.A.
Ketchum K.A.
Kimmel B.E.
Kodira C.D.
Kraft C.L.
Kravitz S.
Kulp D.
Lai Z.
Lasko P.
Lei Y.
Levitsky A.A.
Li J.H.
Li Z.
Liang Y.
Lin X.
Liu X.
Mattei B.
McIntosh T.C.
McLeod M.P.
McPherson D.
Merkulov G.
Milshina N.V.
Mobarry C.
Morris J.
Moshrefi A.
Mount S.M.
Moy M.
Murphy B.
Murphy L.
Muzny D.M.
Nelson D.L.
Nelson D.R.
Nelson K.A.
Nixon K.
Nusskern D.R.
Pacleb J.M.
Palazzolo M.
Pittman G.S.
Pan S.
Pollard J.
Puri V.
Reese M.G.
Reinert K.
Remington K.
Saunders R.D.C.
Scheeler F.
Shen H.
Shue B.C.
Siden-Kiamos I.
Simpson M.
Skupski M.P.
Smith T.J.
Spier E.
Spradling A.C.
Stapleton M.
Strong R.
Sun E.
Svirskas R.
Tector C.
Turner R.
Venter E.
Wang A.H.
Wang X.
Wang Z.-Y.
Wassarman D.A.
Weinstock G.M.
Weissenbach J.
Williams S.M.
Woodage T.
Worley K.C.
Wu D.
Yang S.
Yao Q.A.
Ye J.
Yeh R.-F.
Zaveri J.S.
Zhan M.
Zhang G.
Zhao Q.
Zheng L.
Zheng X.H.
Zhong F.N.
Zhong W.
Zhou X.
Zhu S.C.
Zhu X.
Smith H.O.
Gibbs R.A.
Myers E.W.
Rubin G.M.
Venter J.C.

title: The genome sequence of Drosophila melanogaster.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

authors:
Misra S.
Crosby M.A.
Mungall C.J.
Matthews B.B.
Campbell K.S.
Hradecky P.
Huang Y.
Kaminker J.S.
Millburn G.H.
Prochnik S.E.
Smith C.D.
Tupy J.L.
Whitfield E.J.
Bayraktaroglu L.
Berman B.P.
Bettencourt B.R.
Celniker S.E.
de Grey A.D.N.J.
Drysdale R.A.
Harris N.L.
Richter J.
Russo S.
Schroeder A.J.
Shu S.Q.
Stapleton M.
Yamada C.
Ashburner M.
Gelbart W.M.
Rubin G.M.
Lewis S.E.

title: Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.

authors:
Stapleton M.
Brokstein P.
Hong L.
Agbayani A.
Carlson J.W.
Champe M.
Chavez C.
Dorsett V.
Dresnek D.
Farfan D.
Frise E.
George R.A.
Gonzalez M.
Guarin H.
Kronmiller B.
Li P.W.
Liao G.
Miranda A.
Mungall C.J.
Nunoo J.
Pacleb J.M.
Paragas V.
Park S.
Patel S.
Phouanenavong S.
Wan K.H.
Yu C.
Lewis S.E.
Rubin G.M.
Celniker S.E.

value: Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2

value: Expressed in distal medullary amacrine neuron Dm1-5 (Drosophila) in insect head and 274 other cell types or tissues

value: P:Golgi apparatus N-glycan mannose trimming


value: Voltage-dependent L-type calcium channel subunit beta-3

value: Calcium channel voltage-dependent subunit beta 3

value: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:8119293). Increases CACNA1B peak calcium current and shifts the voltage dependencies of channel activation and inactivation (By similarity). Increases CACNA1C peak calcium current and shifts the voltage dependencies of channel activation and inactivation (By similarity)

value: Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1C) and the ancillary subunits CACNB3 and CACNA2D1 (PubMed:29742403). The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio (Probable). Interacts with CACNA2D4 (PubMed:12181424). Interacts with FASLG (PubMed:19807924). Interacts with CBARP; prevents the interaction of CACNB3 with the alpha subunit CACNA1C thereby negatively regulating the activity of the corresponding calcium channel (By similarity)

commentType: SUBUNIT

geneName: GEM

value: Cytoplasm

value: Expressed mostly in brain, colon and ovary

value: Belongs to the calcium channel beta subunit family

type: Domain

description: Disordered

description: Disordered

description: Mediates interaction with the alpha subunit

description: Disordered

description: Basic and acidic residues

description: Polar residues

description: Basic and acidic residues

type: Modified residue

description: Phosphoserine

description: Phosphoserine

type: Alternative sequence

description: in isoform 3

originalSequence: MYDDSYVPGFEDSEA

description: in isoform 4

description: in isoform 5

description: in isoform 2

source: Reference

type: Natural variant

description: in dbSNP:rs2229954

database: dbSNP

originalSequence: R

type: Sequence conflict

description: in Ref. 4; AAA19799

originalSequence: V

description: in Ref. 4; AAA19799

description: in Ref. 4; AAA19799

description: in Ref. 5; BAH14694

description: in Ref. 5; BAH14209

description: in Ref. 5; BAH12637

description: in Ref. 5; BAH12637

description: in Ref. 4; AAA19799

description: in Ref. 4; AAA19799

description: in Ref. 4; AAA19799

referencePositions: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2)

authors:
Yamada Y.
Masuda K.
Li Q.
Ihara Y.
Kubota A.
Miura T.
Nakamura K.
Fujii Y.
Seino S.
Seino Y.

title: The structures of the human calcium channel alpha 1 subunit (CACNL1A2) and beta subunit (CACNLB3) genes.

authors:
Collin T.
Lory P.
Taviaux S.
Courtieu C.
Guilbault P.
Berta P.
Nargeot J.

title: Cloning, chromosomal location and functional expression of the human voltage-dependent calcium-channel beta 3 subunit.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
FUNCTION
TISSUE SPECIFICITY

authors:
Ota T.
Suzuki Y.
Nishikawa T.
Otsuki T.
Sugiyama T.
Irie R.
Wakamatsu A.
Hayashi K.
Sato H.
Nagai K.
Kimura K.
Makita H.
Sekine M.
Obayashi M.
Nishi T.
Shibahara T.
Tanaka T.
Ishii S.
Yamamoto J.
Saito K.
Kawai Y.
Isono Y.
Nakamura Y.
Nagahari K.
Murakami K.
Yasuda T.
Iwayanagi T.
Wagatsuma M.
Shiratori A.
Sudo H.
Hosoiri T.
Kaku Y.
Kodaira H.
Kondo H.
Sugawara M.
Takahashi M.
Kanda K.
Yokoi T.
Furuya T.
Kikkawa E.
Omura Y.
Abe K.
Kamihara K.
Katsuta N.
Sato K.
Tanikawa M.
Yamazaki M.
Ninomiya K.
Ishibashi T.
Yamashita H.
Murakawa K.
Fujimori K.
Tanai H.
Kimata M.
Watanabe M.
Hiraoka S.
Chiba Y.
Ishida S.
Ono Y.
Takiguchi S.
Watanabe S.
Yosida M.
Hotuta T.
Kusano J.
Kanehori K.
Takahashi-Fujii A.
Hara H.
Tanase T.-O.
Nomura Y.
Togiya S.
Komai F.
Hara R.
Takeuchi K.
Arita M.
Imose N.
Musashino K.
Yuuki H.
Oshima A.
Sasaki N.
Aotsuka S.
Yoshikawa Y.
Matsunawa H.
Ichihara T.
Shiohata N.
Sano S.
Moriya S.
Momiyama H.
Satoh N.
Takami S.
Terashima Y.
Suzuki O.
Nakagawa S.
Senoh A.
Mizoguchi H.
Goto Y.
Shimizu F.
Wakebe H.
Hishigaki H.
Watanabe T.
Sugiyama A.
Takemoto M.
Kawakami B.
Yamazaki M.
Watanabe K.
Kumagai A.
Itakura S.
Fukuzumi Y.
Fujimori Y.
Komiyama M.
Tashiro H.
Tanigami A.
Fujiwara T.
Ono T.
Yamada K.
Fujii Y.
Ozaki K.
Hirao M.
Ohmori Y.
Kawabata A.
Hikiji T.
Kobatake N.
Inagaki H.
Ikema Y.
Okamoto S.
Okitani R.
Kawakami T.
Noguchi S.
Itoh T.
Shigeta K.
Senba T.
Matsumura K.
Nakajima Y.
Mizuno T.
Morinaga M.
Sasaki M.
Togashi T.
Oyama M.
Hata H.
Watanabe M.
Komatsu T.
Mizushima-Sugano J.
Satoh T.
Shirai Y.
Takahashi Y.
Nakagawa K.
Okumura K.
Nagase T.
Nomura N.
Kikuchi H.
Masuho Y.
Yamashita R.
Nakai K.
Yada T.
Nakamura Y.
Ohara O.
Isogai T.
Sugano S.

title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4)

authors:
Scherer S.E.
Muzny D.M.
Buhay C.J.
Chen R.
Cree A.
Ding Y.
Dugan-Rocha S.
Gill R.
Gunaratne P.
Harris R.A.
Hawes A.C.
Hernandez J.
Hodgson A.V.
Hume J.
Jackson A.
Khan Z.M.
Kovar-Smith C.
Lewis L.R.
Lozado R.J.
Metzker M.L.
Milosavljevic A.
Miner G.R.
Montgomery K.T.
Morgan M.B.
Nazareth L.V.
Scott G.
Sodergren E.
Song X.-Z.
Steffen D.
Lovering R.C.
Wheeler D.A.
Worley K.C.
Yuan Y.
Zhang Z.
Adams C.Q.
Ansari-Lari M.A.
Ayele M.
Brown M.J.
Chen G.
Chen Z.
Clerc-Blankenburg K.P.
Davis C.
Delgado O.
Dinh H.H.
Draper H.
Gonzalez-Garay M.L.
Havlak P.
Jackson L.R.
Jacob L.S.
Kelly S.H.
Li L.
Li Z.
Liu J.
Liu W.
Lu J.
Maheshwari M.
Nguyen B.-V.
Okwuonu G.O.
Pasternak S.
Perez L.M.
Plopper F.J.H.
Santibanez J.
Shen H.
Tabor P.E.
Verduzco D.
Waldron L.
Wang Q.
Williams G.A.
Zhang J.
Zhou J.
Allen C.C.
Amin A.G.
Anyalebechi V.
Bailey M.
Barbaria J.A.
Bimage K.E.
Bryant N.P.
Burch P.E.
Burkett C.E.
Burrell K.L.
Calderon E.
Cardenas V.
Carter K.
Casias K.
Cavazos I.
Cavazos S.R.
Ceasar H.
Chacko J.
Chan S.N.
Chavez D.
Christopoulos C.
Chu J.
Cockrell R.
Cox C.D.
Dang M.
Dathorne S.R.
David R.
Davis C.M.
Davy-Carroll L.
Deshazo D.R.
Donlin J.E.
D'Souza L.
Eaves K.A.
Egan A.
Emery-Cohen A.J.
Escotto M.
Flagg N.
Forbes L.D.
Gabisi A.M.
Garza M.
Hamilton C.
Henderson N.
Hernandez O.
Hines S.
Hogues M.E.
Huang M.
Idlebird D.G.
Johnson R.
Jolivet A.
Jones S.
Kagan R.
King L.M.
Leal B.
Lebow H.
Lee S.
LeVan J.M.
Lewis L.C.
London P.
Lorensuhewa L.M.
Loulseged H.
Lovett D.A.
Lucier A.
Lucier R.L.
Ma J.
Madu R.C.
Mapua P.
Martindale A.D.
Martinez E.
Massey E.
Mawhiney S.
Meador M.G.
Mendez S.
Mercado C.
Mercado I.C.
Merritt C.E.
Miner Z.L.
Minja E.
Mitchell T.
Mohabbat F.
Mohabbat K.
Montgomery B.
Moore N.
Morris S.
Munidasa M.
Ngo R.N.
Nguyen N.B.
Nickerson E.
Nwaokelemeh O.O.
Nwokenkwo S.
Obregon M.
Oguh M.
Oragunye N.
Oviedo R.J.
Parish B.J.
Parker D.N.
Parrish J.
Parks K.L.
Paul H.A.
Payton B.A.
Perez A.
Perrin W.
Pickens A.
Primus E.L.
Pu L.-L.
Puazo M.
Quiles M.M.
Quiroz J.B.
Rabata D.
Reeves K.
Ruiz S.J.
Shao H.
Sisson I.
Sonaike T.
Sorelle R.P.
Sutton A.E.
Svatek A.F.
Svetz L.A.
Tamerisa K.S.
Taylor T.R.
Teague B.
Thomas N.
Thorn R.D.
Trejos Z.Y.
Trevino B.K.
Ukegbu O.N.
Urban J.B.
Vasquez L.I.
Vera V.A.
Villasana D.M.
Wang L.
Ward-Moore S.
Warren J.T.
Wei X.
White F.
Williamson A.L.
Wleczyk R.
Wooden H.S.
Wooden S.H.
Yen J.
Yoon L.
Yoon V.
Zorrilla S.E.
Nelson D.
Kucherlapati R.
Weinstock G.
Gibbs R.A.

title: The finished DNA sequence of human chromosome 12.

authors:
Mural R.J.
Istrail S.
Sutton G.G.
Florea L.
Halpern A.L.
Mobarry C.M.
Lippert R.
Walenz B.
Shatkay H.
Dew I.
Miller J.R.
Flanigan M.J.
Edwards N.J.
Bolanos R.
Fasulo D.
Halldorsson B.V.
Hannenhalli S.
Turner R.
Yooseph S.
Lu F.
Nusskern D.R.
Shue B.C.
Zheng X.H.
Zhong F.
Delcher A.L.
Huson D.H.
Kravitz S.A.
Mouchard L.
Reinert K.
Remington K.A.
Clark A.G.
Waterman M.S.
Eichler E.E.
Adams M.D.
Hunkapiller M.W.
Myers E.W.
Venter J.C.

title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)

authors:
Qin N.
Yagel S.
Momplaisir M.-L.
Codd E.E.
D'Andrea M.R.

title: Molecular cloning and characterization of the human voltage-gated calcium channel alpha(2)delta-4 subunit.

referencePositions: IDENTIFICATION IN A COMPLEX WITH CACNA1C

title: Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening.

authors:
Bartels P.
Yu D.
Huang H.
Hu Z.
Herzig S.
Soong T.W.

title: Alternative Splicing at N Terminus and Domain I Modulates CaV1.2 Inactivation and Surface Expression.

title: Structure of human Cav2.2 channel blocked by the painkiller ziconotide.

referencePositions: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 38-361 IN COMPLEX WITH HUMAN CAV2.2/CACNA1B AND ALPHA2DELTA-1 SUBUNIT IN PRESENCE AND ABSENCE OF THE OMEGA-CONOTOXIN MVIIA

authors:
Gao S.
Yao X.
Chen J.
Huang G.
Fan X.
Xue L.
Li Z.
Wu T.
Zheng Y.
Huang J.
Jin X.
Wang Y.
Wang Z.
Yu Y.
Liu L.
Pan X.
Song C.
Yan N.

title: Structural basis for human Cav1.2 inhibition by multiple drugs and the neurotoxin calciseptine.

referencePositions: STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) IN COMPLEX WITH CAV1.2/CACNA1C AND ALPHA-2/DELTA-1 SUBUNIT

value: Cav1.1 voltage-gated calcium channel complex, CACNA2D1-CACNB3-CACNG1 variant

value: Cav1.1 voltage-gated calcium channel complex, CACNA2D2-CACNB3-CACNG1 variant

value: Cav1.1 voltage-gated calcium channel complex, CACNA2D3-CACNB3-CACNG1 variant

value: Cav1.1 voltage-gated calcium channel complex, CACNA2D4-CACNB3-CACNG1 variant

value: Cav1.2 voltage-gated calcium channel complex, CACNA2D1-CACNB3 variant

value: Cav1.2 voltage-gated calcium channel complex, CACNA2D2-CACNB3 variant

value: Cav1.2 voltage-gated calcium channel complex, CACNA2D3-CACNB3 variant

value: Cav1.2 voltage-gated calcium channel complex, CACNA2D4-CACNB3 variant

value: the ca(2+) channel auxiliary subunit Beta types 1-4 (cca-Beta) family

value: 4 GO annotations based on evolutionary models

value: Presynaptic depolarization and calcium channel opening

value: Adrenaline,noradrenaline inhibits insulin secretion

value: Mechanical load activates signaling by PIEZO1 and integrins in osteocytes

value: Presynaptic clusters and postsynaptic densities

value: Expressed in cortical plate and 174 other cell types or tissues

value: C:L-type voltage-gated calcium channel complex

value: F:high voltage-gated calcium channel activity

value: F:voltage-gated calcium channel activity

value: P:calcium ion transmembrane transport via high voltage-gated calcium channel

value: P:positive regulation of high voltage-gated calcium channel activity

value: P:positive regulation of muscle contraction

value: P:protein localization to plasma membrane

value: P:regulation of membrane repolarization during action potential

value: Voltage-dependent L-type calcium channel subunit beta-2

value: P-loop containing nucleotide triphosphate hydrolases

value: VOLTAGE-DEPENDENT CALCIUM CHANNEL BETA SUBUNIT

value: P-loop containing nucleoside triphosphate hydrolases


scientificName: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

commonName: Fission yeast

lineage: Eukaryota Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces

value: Double-strand break repair protein rad32

source: PomBase

value: Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:15654094, PubMed:22705791, PubMed:23080121, PubMed:7885834). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (By similarity). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). Within the MRN complex, rad32 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (Probable) (PubMed:22705791). Rad32 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR (By similarity). It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which is required for single-strand invasion and recombination (By similarity)

value: Forms a multisubunit endonuclease complex, MRN, together with nbn and rad50

value: Localizes to discrete nuclear foci after treatment with genotoxic agents

value: Nucleus

value: Chromosome, telomere

value: Chromosome

value: Belongs to the MRE11/RAD32 family

description: Disordered

description: Polar residues

description: Polar residues

description: Acidic residues

description: Proton donor

source: PIRSR

source: PDB

description: Decreased repair of double strand breaks (DSBs).

authors:
Tavassoli M.
Shayeghi M.
Nasim A.
Watts F.Z.

title: Cloning and characterisation of the Schizosaccharomyces pombe rad32 gene: a gene required for repair of double strand breaks and recombination.

referencePositions:
NUCLEOTIDE SEQUENCE [GENOMIC DNA]
FUNCTION

authors:
Wood V.
Gwilliam R.
Rajandream M.A.
Lyne M.H.
Lyne R.
Stewart A.
Sgouros J.G.
Peat N.
Hayles J.
Baker S.G.
Basham D.
Bowman S.
Brooks K.
Brown D.
Brown S.
Chillingworth T.
Churcher C.M.
Collins M.
Connor R.
Cronin A.
Davis P.
Feltwell T.
Fraser A.
Gentles S.
Goble A.
Hamlin N.
Harris D.E.
Hidalgo J.
Hodgson G.
Holroyd S.
Hornsby T.
Howarth S.
Huckle E.J.
Hunt S.
Jagels K.
James K.D.
Jones L.
Jones M.
Leather S.
McDonald S.
McLean J.
Mooney P.
Moule S.
Mungall K.L.
Murphy L.D.
Niblett D.
Odell C.
Oliver K.
O'Neil S.
Pearson D.
Quail M.A.
Rabbinowitsch E.
Rutherford K.M.
Rutter S.
Saunders D.
Seeger K.
Sharp S.
Skelton J.
Simmonds M.N.
Squares R.
Squares S.
Stevens K.
Taylor K.
Taylor R.G.
Tivey A.
Walsh S.V.
Warren T.
Whitehead S.
Woodward J.R.
Volckaert G.
Aert R.
Robben J.
Grymonprez B.
Weltjens I.
Vanstreels E.
Rieger M.
Schaefer M.
Mueller-Auer S.
Gabel C.
Fuchs M.
Duesterhoeft A.
Fritzc C.
Holzer E.
Moestl D.
Hilbert H.
Borzym K.
Langer I.
Beck A.
Lehrach H.
Reinhardt R.
Pohl T.M.
Eger P.
Zimmermann W.
Wedler H.
Wambutt R.
Purnelle B.
Goffeau A.
Cadieu E.
Dreano S.
Gloux S.
Lelaure V.
Mottier S.
Galibert F.
Aves S.J.
Xiang Z.
Hunt C.
Moore K.
Hurst S.M.
Lucas M.
Rochet M.
Gaillardin C.
Tallada V.A.
Garzon A.
Thode G.
Daga R.R.
Cruzado L.
Jimenez J.
Sanchez M.
del Rey F.
Benito J.
Dominguez A.
Revuelta J.L.
Moreno S.
Armstrong J.
Forsburg S.L.
Cerutti L.
Lowe T.
McCombie W.R.
Paulsen I.
Potashkin J.
Shpakovski G.V.
Ussery D.
Barrell B.G.
Nurse P.

title: The genome sequence of Schizosaccharomyces pombe.

authors:
Chahwan C.
Nakamura T.M.
Sivakumar S.
Russell P.
Rhind N.

title: The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint.

authors:
Farah J.A.
Cromie G.
Steiner W.W.
Smith G.R.

title: A novel recombination pathway initiated by the Mre11/Rad50/Nbs1 complex eliminates palindromes during meiosis in Schizosaccharomyces pombe.

authors:
Limbo O.
Moiani D.
Kertokalio A.
Wyman C.
Tainer J.A.
Russell P.

title: Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
MUTAGENESIS OF TRP-248

authors:
Schiller C.B.
Lammens K.
Guerini I.
Coordes B.
Feldmann H.
Schlauderer F.
Moeckel C.
Schele A.
Straesser K.
Jackson S.P.
Hopfner K.P.

title: Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 7-413 IN COMPLEX WITH MANGANESE AND NBS1

value: Cytosolic sensors of pathogen-associated DNA

value: DNA Damage/Telomere Stress Induced Senescence

value: Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks

value: F:double-stranded DNA 3'-5' DNA exonuclease activity

value: F:single-stranded DNA endonuclease activity

value: P:double-strand break repair involved in meiotic recombination

value: P:double-strand break repair via homologous recombination

value: P:double-strand break repair via nonhomologous end joining

value: P:meiotic DNA double-strand break formation

value: P:mitochondrial double-strand break repair via homologous recombination

value: P:mitotic G2 DNA damage checkpoint signaling

value: P:mitotic intra-S DNA damage checkpoint signaling

value: DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11


entryType: UniProtKB unreviewed (TrEMBL)

source: EMBL

source: Proteomes

source: Google

value: Protein HID1

source: ARBA

value: Belongs to the hid-1 family

description: Disordered

description: Acidic residues

description: Polar residues

description: Basic and acidic residues

Proteomics identification

source: PeptideAtlas

category: Technical term

citationType: journal article

authors:
Adams M.D.
Celniker S.E.
Holt R.A.
Evans C.A.
Gocayne J.D.
Amanatides P.G.
Scherer S.E.
Li P.W.
Hoskins R.A.
Galle R.F.
George R.A.
Lewis S.E.
Richards S.
Ashburner M.
Henderson S.N.
Sutton G.G.
Wortman J.R.
Yandell M.D.
Zhang Q.
Chen L.X.
Brandon R.C.
Rogers Y.H.
Blazej R.G.
Champe M.
Pfeiffer B.D.
Wan K.H.
Doyle C.
Baxter E.G.
Helt G.
Nelson C.R.
Gabor G.L.
Abril J.F.
Agbayani A.
An H.J.
Andrews-Pfannkoch C.
Baldwin D.
Ballew R.M.
Basu A.
Baxendale J.
Bayraktaroglu L.
Beasley E.M.
Beeson K.Y.
Benos P.V.
Berman B.P.
Bhandari D.
Bolshakov S.
Borkova D.
Botchan M.R.
Bouck J.
Brokstein P.
Brottier P.
Burtis K.C.
Busam D.A.
Butler H.
Cadieu E.
Center A.
Chandra I.
Cherry J.M.
Cawley S.
Dahlke C.
Davenport L.B.
Davies P.
de Pablos B.
Delcher A.
Deng Z.
Mays A.D.
Dew I.
Dietz S.M.
Dodson K.
Doup L.E.
Downes M.
Dugan-Rocha S.
Dunkov B.C.
Dunn P.
Durbin K.J.
Evangelista C.C.
Ferraz C.
Ferriera S.
Fleischmann W.
Fosler C.
Gabrielian A.E.
Garg N.S.
Gelbart W.M.
Glasser K.
Glodek A.
Gong F.
Gorrell J.H.
Gu Z.
Guan P.
Harris M.
Harris N.L.
Harvey D.
Heiman T.J.
Hernandez J.R.
Houck J.
Hostin D.
Houston K.A.
Howland T.J.
Wei M.H.
Ibegwam C.
Jalali M.
Kalush F.
Karpen G.H.
Ke Z.
Kennison J.A.
Ketchum K.A.
Kimmel B.E.
Kodira C.D.
Kraft C.
Kravitz S.
Kulp D.
Lai Z.
Lasko P.
Lei Y.
Levitsky A.A.
Li J.
Li Z.
Liang Y.
Lin X.
Liu X.
Mattei B.
McIntosh T.C.
McLeod M.P.
McPherson D.
Merkulov G.
Milshina N.V.
Mobarry C.
Morris J.
Moshrefi A.
Mount S.M.
Moy M.
Murphy B.
Murphy L.
Muzny D.M.
Nelson D.L.
Nelson D.R.
Nelson K.A.
Nixon K.
Nusskern D.R.
Pacleb J.M.
Palazzolo M.
Pittman G.S.
Pan S.
Pollard J.
Puri V.
Reese M.G.
Reinert K.
Remington K.
Saunders R.D.
Scheeler F.
Shen H.
Shue B.C.
Siden-Kiamos I.
Simpson M.
Skupski M.P.
Smith T.
Spier E.
Spradling A.C.
Stapleton M.
Strong R.
Sun E.
Svirskas R.
Tector C.
Turner R.
Venter E.
Wang A.H.
Wang X.
Wang Z.Y.
Wassarman D.A.
Weinstock G.M.
Weissenbach J.
Williams S.M.
WoodageT
Worley K.C.
Wu D.
Yang S.
Yao Q.A.
Ye J.
Yeh R.F.
Zaveri J.S.
Zhan M.
Zhang G.
Zhao Q.
Zheng L.
Zheng X.H.
Zhong F.N.
Zhong W.
Zhou X.
Zhu S.
Zhu X.
Smith H.O.
Gibbs R.A.
Myers E.W.
Rubin G.M.
Venter J.C.

database: PubMed

database: DOI

title: The genome sequence of Drosophila melanogaster.

journal: Science

value: Berkeley

type: STRAIN

authors:
Celniker S.E.
Wheeler D.A.
Kronmiller B.
Carlson J.W.
Halpern A.
Patel S.
Adams M.
Champe M.
Dugan S.P.
Frise E.
Hodgson A.
George R.A.
Hoskins R.A.
Laverty T.
Muzny D.M.
Nelson C.R.
Pacleb J.M.
Park S.
Pfeiffer B.D.
Richards S.
Sodergren E.J.
Svirskas R.
Tabor P.E.
Wan K.
Stapleton M.
Sutton G.G.
Venter C.
Weinstock G.
Scherer S.E.
Myers E.W.
Gibbs R.A.
Rubin G.M.

title: Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence.

journal: Genome Biol.

authors:
Misra S.
Crosby M.A.
Mungall C.J.
Matthews B.B.
Campbell K.S.
Hradecky P.
Huang Y.
Kaminker J.S.
Millburn G.H.
Prochnik S.E.
Smith C.D.
Tupy J.L.
Whitfied E.J.
Bayraktaroglu L.
Berman B.P.
Bettencourt B.R.
Celniker S.E.
de Grey A.D.
Drysdale R.A.
Harris N.L.
Richter J.
Russo S.
Schroeder A.J.
Shu S.Q.
Stapleton M.
Yamada C.
Ashburner M.
Gelbart W.M.
Rubin G.M.
Lewis S.E.

title: Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.

authors:
Kaminker J.S.
Bergman C.M.
Kronmiller B.
Carlson J.
Svirskas R.
Patel S.
Frise E.
Wheeler D.A.
Lewis S.E.
Rubin G.M.
Ashburner M.
Celniker S.E.

title: The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective.

authors:
Hoskins R.A.
Smith C.D.
Carlson J.W.
Carvalho A.B.
Halpern A.
Kaminker J.S.
Kennedy C.
Mungall C.J.
Sullivan B.A.
Sutton G.G.
Yasuhara J.C.
Wakimoto B.T.
Myers E.W.
Celniker S.E.
Rubin G.M.
Karpen G.H.

title: Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.

authors:
Quesneville H.
Bergman C.M.
Andrieu O.
Autard D.
Nouaud D.
Ashburner M.
Anxolabehere D.

title: Combined evidence annotation of transposable elements in genome sequences.

journal: PLoS Comput. Biol.

citationType: submission

authors:
Celniker S.
Carlson J.
Wan K.
Frise E.
Hoskins R.
Park S.
Svirskas R.
Rubin G.

submissionDatabase: EMBL/GenBank/DDBJ databases

authors:
Smith C.D.
Shu S.
Mungall C.J.
Karpen G.H.

title: The Release 5.1 annotation of Drosophila melanogaster heterochromatin.

authors:
Hoskins R.A.
Carlson J.W.
Kennedy C.
Acevedo D.
Evans-Holm M.
Frise E.
Wan K.H.
Park S.
Mendez-Lago M.
Rossi F.
Villasante A.
Dimitri P.
Karpen G.H.
Celniker S.E.

title: Sequence finishing and mapping of Drosophila melanogaster heterochromatin.

authors:
Matthews B.B.
Dos Santos G.
Crosby M.A.
Emmert D.B.
St Pierre S.E.
Gramates L.S.
Zhou P.
Schroeder A.J.
Falls K.
Strelets V.
Russo S.M.
Gelbart W.M.

title: Gene Model Annotations for Drosophila melanogaster: Impact of High-Throughput Data.

authors:
Crosby M.A.
Gramates L.S.
Dos Santos G.
Matthews B.B.
St Pierre S.E.
Zhou P.
Schroeder A.J.
Falls K.
Emmert D.B.
Russo S.M.
Gelbart W.M.

title: Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.

authors:
Hoskins R.A.
Carlson J.W.
Wan K.H.
Park S.
Mendez I.
Galle S.E.
Booth B.W.
Pfeiffer B.D.
George R.A.
Svirskas R.
Krzywinski M.
Schein J.
Accardo M.C.
Damia E.
Messina G.
Mendez-Lago M.
de Pablos B.
Demakova O.V.
Andreyeva E.N.
Boldyreva L.V.
Marra M.
Carvalho A.B.
Dimitri P.
Villasante A.
Zhimulev I.F.
Rubin G.M.
Karpen G.H.
Celniker S.E.

title: The Release 6 reference sequence of the Drosophila melanogaster genome.

authors:
Celniker S.
Carlson J.
Wan K.
Pfeiffer B.
Frise E.
George R.
Hoskins R.
Stapleton M.
Pacleb J.
Park S.
Svirskas R.
Smith E.
Yu C.
Rubin G.

title: Drosophila melanogaster release 4 sequence.

value: Expressed in cleaving embryo and 51 other cell types or tissues


value: Sticks and stones, isoform B

value: sns

value: rost

value: SNS

value: SnS

value: Sns

geneName: kirre

geneName: rst

value: Membrane

value: Single-pass type I membrane protein

value: Lacks conserved residue(s) required for the propagation of feature annotation

description: Helical

description: Helical

description: Ig-like

source: PROSITE

description: Ig-like

description: Ig-like

description: Ig-like

description: Ig-like

description: Ig-like

description: Ig-like

description: Ig-like

description: Ig-like

description: Fibronectin type-III

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Low complexity

description: Low complexity

description: Low complexity

description: Low complexity

value: Expressed in adult abdominal pericardial cell (Drosophila) in dorsal vessel heart and 94 other cell types or tissues

value: C:protein complex involved in cell adhesion

value: P:compound eye photoreceptor cell differentiation

value: P:regulation of striated muscle tissue development

value: Kirre like nephrin family adhesion molecule 3


proteinExistence: 3: Inferred from homology

value: Protein FMC1 homolog

value: Belongs to the FMC1 family

journal: G3 (Bethesda)

value: Expressed in adult posterior midgut class II enteroendocrine cell in adult midgut (Drosophila) and 150 other cell types or tissues

value: P:mitochondrial proton-transporting ATP synthase complex assembly


scientificName: Arabidopsis thaliana

commonName: Mouse-ear cress

lineage: Eukaryota Viridiplantae Streptophyta Embryophyta Tracheophyta Spermatophyta Magnoliopsida eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis

value: Uncharacterized protein At4g38370

authors:
Totoki Y.
Seki M.
Ishida J.
Nakajima M.
Enju A.
Morosawa T.
Kamiya A.
Narusaka M.
Shin-i T.
Nakagawa M.
Sakamoto N.
Oishi K.
Kohara Y.
Kobayashi M.
Toyoda A.
Sakaki Y.
Sakurai T.
Iida K.
Akiyama K.
Satou M.
Toyoda T.
Konagaya A.
Carninci P.
Kawai J.
Hayashizaki Y.
Shinozaki K.

title: Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.

authors:
Bienvenut W.V.
Sumpton D.
Martinez A.
Lilla S.
Espagne C.
Meinnel T.
Giglione C.

title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

journal: Mol. Cell. Proteomics

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

source: PubMed

database: EMBL

key: ProteinId

key: Status

key: MoleculeType

value: mRNA

database: RefSeq

key: NucleotideSequenceId

database: AlphaFoldDB

key: Description

database: SMR

database: STRING

database: PaxDb

database: ProteomicsDB

database: GeneID

database: KEGG

database: TAIR

key: GeneName

database: eggNOG

key: ToxonomicScope

value: Eukaryota

database: HOGENOM

database: OMA

key: Fingerprint

database: CDD

key: EntryName

key: MatchStatus

database: FunFam

value: Phosphoglycerate mutase family protein

value: Phosphoglycerate mutase-like

database: InterPro

database: PANTHER

value: PHOSPHOGLYCERATE MUTASE FAMILY PROTEIN

database: Pfam

database: SMART

value: PGAM

database: SUPFAM


value: mRNA cleavage and polyadenylation specificity factor complex subunit pta1

value: Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB

value: Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of cft1, cft2, ysh1, pta1, swd2, pfs2, dis2, yth1, ssu72, and fip1

value: Nucleus

value: To yeast PTA1

mRNA processing

category: Biological process

Nucleus

category: Cellular component

authors:
Wood V.
Gwilliam R.
Rajandream M.A.
Lyne M.H.
Lyne R.
Stewart A.
Sgouros J.G.
Peat N.
Hayles J.
Baker S.G.
Basham D.
Bowman S.
Brooks K.
Brown D.
Brown S.
Chillingworth T.
Churcher C.M.
Collins M.
Connor R.
Cronin A.
Davis P.
Feltwell T.
Fraser A.
Gentles S.
Goble A.
Hamlin N.
Harris D.E.
Hidalgo J.
Hodgson G.
Holroyd S.
Hornsby T.
Howarth S.
Huckle E.J.
Hunt S.
Jagels K.
James K.D.
Jones L.
Jones M.
Leather S.
McDonald S.
McLean J.
Mooney P.
Moule S.
Mungall K.L.
Murphy L.D.
Niblett D.
Odell C.
Oliver K.
O'Neil S.
Pearson D.
Quail M.A.
Rabbinowitsch E.
Rutherford K.M.
Rutter S.
Saunders D.
Seeger K.
Sharp S.
Skelton J.
Simmonds M.N.
Squares R.
Squares S.
Stevens K.
Taylor K.
Taylor R.G.
Tivey A.
Walsh S.V.
Warren T.
Whitehead S.
Woodward J.R.
Volckaert G.
Aert R.
Robben J.
Grymonprez B.
Weltjens I.
Vanstreels E.
Rieger M.
Schaefer M.
Mueller-Auer S.
Gabel C.
Fuchs M.
Duesterhoeft A.
Fritzc C.
Holzer E.
Moestl D.
Hilbert H.
Borzym K.
Langer I.
Beck A.
Lehrach H.
Reinhardt R.
Pohl T.M.
Eger P.
Zimmermann W.
Wedler H.
Wambutt R.
Purnelle B.
Goffeau A.
Cadieu E.
Dreano S.
Gloux S.
Lelaure V.
Mottier S.
Galibert F.
Aves S.J.
Xiang Z.
Hunt C.
Moore K.
Hurst S.M.
Lucas M.
Rochet M.
Gaillardin C.
Tallada V.A.
Garzon A.
Thode G.
Daga R.R.
Cruzado L.
Jimenez J.
Sanchez M.
del Rey F.
Benito J.
Dominguez A.
Revuelta J.L.
Moreno S.
Armstrong J.
Forsburg S.L.
Cerutti L.
Lowe T.
McCombie W.R.
Paulsen I.
Potashkin J.
Shpakovski G.V.
Ussery D.
Barrell B.G.
Nurse P.

database: PubMed

database: DOI

title: The genome sequence of Schizosaccharomyces pombe.

journal: Nature

authors:
Roguev A.
Shevchenko A.
Schaft D.
Thomas H.
Stewart A.F.
Shevchenko A.

title: A comparative analysis of an orthologous proteomic environment in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.

authors:
Matsuyama A.
Arai R.
Yashiroda Y.
Shirai A.
Kamata A.
Sekido S.
Kobayashi Y.
Hashimoto A.
Hamamoto M.
Hiraoka Y.
Horinouchi S.
Yoshida M.

title: ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.

journal: Nat. Biotechnol.

referencePositions: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]

authors:
Hu W.
Suo F.
Du L.L.

title: Bulk segregant analysis reveals the genetic basis of a natural trait variation in fission yeast.

journal: Genome Biol. Evol.

database: EMBL

database: PIR

database: RefSeq

database: AlphaFoldDB

database: SMR

database: BioGRID

key: Interactions

database: ComplexPortal

value: Cleavage and polyadenylation specificity factor complex

database: FunCoup

key: Number of interactors

database: iPTMnet

database: PomBase

database: VEuPathDB

database: InParanoid

database: PhylomeDB

database: Reactome

key: PathwayName

value: Transport of Mature mRNA Derived from an Intronless Transcript

value: Processing of Intronless Pre-mRNAs

value: mRNA Polyadenylation

database: PRO

database: Proteomes

key: Component

value: Chromosome I

database: GO

key: GoTerm

value: C:mRNA cleavage and polyadenylation specificity factor complex

key: GoEvidenceType

value: P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway

value: P:termination of RNA polymerase II transcription, poly(A)-coupled