value: Replication factor C subunit 3

value: Replication factor C3

value: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 3 binds ATP. Also involved in replication and DNA damage checkpoint controls, probably functioning as a checkpoint sensor

value: Heteropentamer of subunits rfc1, rfc2, rfc3, rfc4 and rfc5 that forms a complex (RFC) with PCNA in the presence of ATP. Two other complexes exist where rfc1 can be replaced by either ctf18 or elg1 to form the ctf18-RFC or the elg1-RFC complexes respectively

value: Nucleus

value: Belongs to the activator 1 small subunits family

description: Replication factor C subunit 3

description: Defective DNA replication.

originalSequence: R

authors:
Shimada M.
Okuzaki D.
Tanaka S.
Tougan T.
Tamai K.K.
Shimoda C.
Nojima H.

database: PubMed

database: DOI

title: Replication factor C3 of Schizosaccharomyces pombe, a small subunit of replication factor C complex, plays a role in both replication and damage checkpoints.

referencePositions: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]

authors:
Gray F.C.
MacNeill S.A.

title: The Schizosaccharomyces pombe rfc3+ gene encodes a homologue of the human hRFC36 and Saccharomyces cerevisiae Rfc3 subunits of replication factor C.

journal: Curr. Genet.

authors:
Kim J.
Robertson K.
Mylonas K.J.L.
Gray F.C.
Charapitsa I.
MacNeill S.A.

title: Contrasting effects of Elg1-RFC and Ctf18-RFC inactivation in the absence of fully functional RFC in fission yeast.

database: EMBL

value: mRNA

database: PIR

database: AlphaFoldDB

database: SMR

database: ComplexPortal

value: DNA replication factor C complex, rad17 variant

value: DNA replication factor C complex, ctf18 variant

value: DNA replication factor C complex, elg1 variant

value: DNA replication factor C complex, RFC1 variant

key: GeneName

value: Recognition of DNA damage by PCNA-containing replication complex

value: Activation of ATR in response to replication stress

value: PCNA-Dependent Long Patch Base Excision Repair

value: Termination of translesion DNA synthesis

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

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

value: P:DNA strand elongation involved in mitotic DNA replication

value: P:mitotic DNA replication leading strand elongation

value: P-loop containing nucleotide triphosphate hydrolases

value: REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT

value: P-loop containing nucleoside triphosphate hydrolases


entryType: UniProtKB reviewed (Swiss-Prot)

scientificName: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

commonName: Fission yeast

lineage: Eukaryota Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces

proteinExistence: 2: Evidence at transcript level

value: DNA-directed RNA polymerase I subunit rpa49

value: RNA polymerase I subunit A49

value: DNA-directed RNA polymerase I 49 kDa polypeptide

value: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors

commentType: FUNCTION

value: Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits

commentType: SUBUNIT

commentType: SUBCELLULAR LOCATION

value: Nucleus, nucleolus

value: Belongs to the eukaryotic RPA49/POLR1E RNA polymerase subunit family

commentType: SIMILARITY

type: Chain

modifier: EXACT

type: Region

description: Disordered

source: SAM

type: Compositional bias

description: Basic and acidic residues

DNA-directed RNA polymerase

category: Cellular component

Reference proteome

category: Technical term

Transcription

category: Biological process

citationType: submission

authors:
Shematorova E.K.
Shpakovski G.V.

title: Molecular cloning and complementation studies of the fission yeast genes encoding subunits Rpa12 and Rpa49 specific for nuclear RNA polymerase I.

submissionDatabase: EMBL/GenBank/DDBJ databases

type: STRAIN

citationType: journal article

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.

journal: Nature

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

key: ProteinId

key: Status

key: MoleculeType

key: EntryName

database: RefSeq

key: NucleotideSequenceId

key: Description

database: BioGRID

key: Interactions

database: FunCoup

key: Number of interactors

database: STRING

database: iPTMnet

database: PaxDb

database: GeneID

database: KEGG

database: PomBase

database: VEuPathDB

database: eggNOG

key: ToxonomicScope

value: Eukaryota

database: HOGENOM

database: InParanoid

database: OMA

key: Fingerprint

database: PhylomeDB

database: Reactome

key: PathwayName

value: RNA Polymerase I Transcription Initiation

value: RNA Polymerase I Promoter Escape

database: PRO

database: Proteomes

key: Component

value: Chromosome I

database: GO

key: GoTerm

key: GoEvidenceType

source: PubMed

value: C:RNA polymerase I complex

value: P:RNA polymerase I preinitiation complex assembly

value: P:transcription elongation by RNA polymerase I

value: DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA49


proteinExistence: 1: Evidence at protein level

value: CENP-B homolog protein 1

value: cbh

value: Binds to centromeric K-type repeat DNA and ARS3002 DNA. The CBH-binding consensus sequence is Py-Pu-A-T-A-T-Py-Pu-T-A

value: Nucleus

value: Chromosome, centromere

description: CENP-B homolog protein 1

type: Domain

description: HTH CENPB-type

source: PROSITE-ProRule

type: Sequence conflict

description: in Ref. 1; AAB80698

originalSequence: I

DNA-binding

category: Molecular function

authors:
Lee J.-K.
Huberman J.A.
Hurwitz J.

database: PubMed

database: DOI

title: Purification and characterization of a CENP-B homologue protein that binds to the centromeric K-type repeat DNA of Schizosaccharomyces pombe.

journal: Proc. Natl. Acad. Sci. U.S.A.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA]
PARTIAL PROTEIN SEQUENCE
FUNCTION

database: EMBL

value: mRNA

database: PIR

database: RefSeq

database: AlphaFoldDB

database: SMR

database: BioGRID

database: FunCoup

database: IntAct

value: C:condensed chromosome, centromeric region


scientificName: Homo sapiens

commonName: Human

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

value: Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2

value: Nuclear LIM interactor-interacting factor 2

value: NLI-interacting factor 2

value: Protein OS-4

value: Small C-terminal domain phosphatase 2

value: Small CTD phosphatase 2

value: Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. May contribute to the development of sarcomas

commentType: CATALYTIC ACTIVITY

name: O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate

database: Rhea

database: ChEBI

name: O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate

commentType: COFACTOR

value: Binds 1 Mg(2+) ion per monomer.

value: Monomer (By similarity). Interacts with REST

commentType: INTERACTION

geneName: AR

geneName: tax

value: Expression is restricted to non-neuronal tissues. Highest expression in pancreas and lowest in liver

commentType: TISSUE SPECIFICITY

value: In primary sarcomas

commentType: INDUCTION

commentType: SEQUENCE CAUTION

sequenceCautionType: Frameshift

description: FCP1 homology

type: Active site

description: 4-aspartylphosphate intermediate

description: Proton donor

type: Binding site

type: Site

description: Transition state stabilizer

description: Transition state stabilizer

type: Modified residue

description: Phosphoserine

description: in Ref. 3; AAD09331

originalSequence: Q

type: Helix

source: PDB

type: Turn

type: Beta strand

authors:
Su Y.A.
Lee M.M.
Hutter C.M.
Meltzer P.S.

title: Characterization of a highly conserved gene (OS4) amplified with CDK4 in human sarcomas.

title: A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5.

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.

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).

authors:
Yeo M.
Lee S.-K.
Lee B.
Ruiz E.C.
Pfaff S.L.
Gill G.N.

title: Small CTD phosphatases function in silencing neuronal gene expression.

referencePositions:
FUNCTION
TISSUE SPECIFICITY
INTERACTION WITH REST

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-5

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Almo S.C.
Bonanno J.B.
Sauder J.M.
Emtage S.
Dilorenzo T.P.
Malashkevich V.
Wasserman S.R.
Swaminathan S.
Eswaramoorthy S.
Agarwal R.
Kumaran D.
Madegowda M.
Ragumani S.
Patskovsky Y.
Alvarado J.
Ramagopal U.A.
Faber-Barata J.
Chance M.R.
Sali A.
Fiser A.
Zhang Z.Y.
Lawrence D.S.
Burley S.K.

title: Structural genomics of protein phosphatases.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 87-271 IN COMPLEX WITH MAGNESIUM

value: 1 GO annotation based on evolutionary models

value: Expressed in mucosa of stomach and 211 other cell types or tissues

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


value: BCAT(m)

value: Placental protein 18

flag: Precursor

source: HGNC

value: BCATM

source: UniProtKB

value: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine (PubMed:17050531, PubMed:25653144, PubMed:8702755). Branched chain amino acid catabolism plays a role in adipocyte differentiation by providing lipogenic acetyl-CoA pools in differentiated adipocytes (By similarity). Mechanistically, acetyl-CoA derived from branched chain amino acid catabolism is used by EP300/p300 to acetylate and inhibit PRDM16, thereby preventing adipose tissue browning (By similarity). May also function as a transporter of branched chain alpha-keto acids (By similarity)

name: L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate

name: L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate

name: L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate

value: Homodimer

geneName: YBEY

value: Mitochondrion

commentType: ALTERNATIVE PRODUCTS

value: A

isoformSequenceStatus: Displayed

value: B

isoformSequenceStatus: Described

value: Ubiquitous

commentType: DISEASE

acronym: HVLI

description: An autosomal recessive metabolic disorder characterized by highly elevated plasma concentrations of valine and leucine/isoleucine. Affected individuals suffer from headache and mild memory impairment.

database: MIM

value: The disease is caused by variants affecting the gene represented in this entry. A patient with hypervalinemia and hyperleucine-isoleucinemia was identified as compound heterozygote for Gln-170 (inherited from his father) and Lys-264 (inherited from his mother), both variants reduced the catalytic activity of the enzyme. After treatment with vitamin B6, a precursor of pyridoxal 5'-phosphate, a BCAT2 cofactor, the blood levels of branched chain amino acids, especially valine, were decreased and brain lesions were improved

value: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family

sequenceCautionType: Erroneous initiation

type: Transit peptide

description: Mitochondrion

description: Branched-chain-amino-acid aminotransferase, mitochondrial

description: N6-(pyridoxal phosphate)lysine

description: in isoform B

description: in HVLI; reduced catalytic activity; dbSNP:rs749866079

description: in HVLI

description: in dbSNP:rs11548193

description: in HVLI

description: in HVLI; reduced catalytic activity; dbSNP:rs767653663

description: in HVLI; dbSNP:rs779570956

description: Reduces activity about 6-fold.

description: Slight reduction of activity.

description: in Ref. 6; AAB53087

description: in Ref. 6; AAB53087

description: in Ref. 6; AAB53087

description: in Ref. 6; AAB53087

description: in Ref. 6; AAB53087

description: in Ref. 6; AAB53087

description: in Ref. 6; AAB53087

description: in Ref. 6; AAB53087

description: in Ref. 6; AAB53087

title: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm).

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A)
VARIANT ARG-186

authors:
Than N.G.
Sumegi B.
Than G.N.
Bellyei S.
Bohn H.

title: Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant.

referencePositions: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B)

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

title: Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases.

referencePositions: NUCLEOTIDE SEQUENCE [MRNA] OF 27-392 (ISOFORM A)

authors:
Choudhary C.
Kumar C.
Gnad F.
Nielsen M.L.
Rehman M.
Walther T.C.
Olsen J.V.
Mann M.

title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

referencePositions: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-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.

authors:
Wang X.L.
Li C.J.
Xing Y.
Yang Y.H.
Jia J.P.

title: Hypervalinemia and hyperleucine-isoleucinemia caused by mutations in the branched-chain-amino-acid aminotransferase gene.

referencePositions:
INVOLVEMENT IN HVLI
VARIANTS HVLI GLN-170 AND LYS-264
FUNCTION

authors:
Vaca Jacome A.S.
Rabilloud T.
Schaeffer-Reiss C.
Rompais M.
Ayoub D.
Lane L.
Bairoch A.
Van Dorsselaer A.
Carapito C.

title: N-terminome analysis of the human mitochondrial proteome.

authors:
Knerr I.
Colombo R.
Urquhart J.
Morais A.
Merinero B.
Oyarzabal A.
Perez B.
Jones S.A.
Perveen R.
Preece M.A.
Rogers Y.
Treacy E.P.
Mayne P.
Zampino G.
MacKinnon S.
Wassmer E.
Yue W.W.
Robinson I.
Rodriguez-Pombo P.
Olpin S.E.
Banka S.

title: Expanding the genetic and phenotypic spectrum of branched-chain amino acid transferase 2 deficiency.

referencePositions: VARIANTS HVLI GLY-182; 200-TYR--VAL-392 DEL AND THR-341

authors:
Yennawar N.H.
Dunbar J.
Conway M.E.
Hutson S.M.
Farber G.K.

title: The structure of human mitochondrial branched-chain aminotransferase.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-392 IN COMPLEX WITH COFACTOR

authors:
Yennawar N.H.
Conway M.E.
Yennawar H.P.
Farber G.K.
Hutson S.M.

title: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 28-392 IN COMPLEXES WITH COFACTOR AND SUBSTRATES

authors:
Goto M.
Miyahara I.
Hirotsu K.
Conway M.
Yennawar N.
Islam M.M.
Hutson S.M.

title: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-392 IN COMPLEXES WITH COFACTOR AND SUBSTRATE ANALOGS

authors:
Yennawar N.H.
Islam M.M.
Conway M.
Wallin R.
Hutson S.M.

title: Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis.

value: 4 GO annotations based on evolutionary models

value: Expressed in right adrenal gland cortex and 188 other cell types or tissues

value: P:branched-chain amino acid biosynthetic process

value: P:branched-chain amino acid catabolic process

value: P:negative regulation of brown fat cell differentiation

value: D-amino Acid Aminotransferase, subunit A, domain 2

value: D-aminoacid aminotransferase-like PLP-dependent enzymes


proteinExistence: 4: Predicted

value: Uncharacterized WD repeat-containing protein C27B12.05

value: Cytoplasm

value: Nucleus

sequenceCautionType: Erroneous gene model prediction

type: Repeat

description: WD 1

description: WD 2

Repeat

category: Domain

authors:
Machida M.
Yamazaki S.
Kunihiro S.
Tanaka T.
Kushida N.
Jinno K.
Haikawa Y.
Yamazaki J.
Yamamoto S.
Sekine M.
Oguchi A.
Nagai Y.
Sakai M.
Aoki K.
Ogura K.
Kudoh Y.
Kikuchi H.
Zhang M.Q.
Yanagida M.

title: A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment.

journal: Yeast

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:
Rhind N.
Chen Z.
Yassour M.
Thompson D.A.
Haas B.J.
Habib N.
Wapinski I.
Roy S.
Lin M.F.
Heiman D.I.
Young S.K.
Furuya K.
Guo Y.
Pidoux A.
Chen H.M.
Robbertse B.
Goldberg J.M.
Aoki K.
Bayne E.H.
Berlin A.M.
Desjardins C.A.
Dobbs E.
Dukaj L.
Fan L.
FitzGerald M.G.
French C.
Gujja S.
Hansen K.
Keifenheim D.
Levin J.Z.
Mosher R.A.
Mueller C.A.
Pfiffner J.
Priest M.
Russ C.
Smialowska A.
Swoboda P.
Sykes S.M.
Vaughn M.
Vengrova S.
Yoder R.
Zeng Q.
Allshire R.
Baulcombe D.
Birren B.W.
Brown W.
Ekwall K.
Kellis M.
Leatherwood J.
Levin H.
Margalit H.
Martienssen R.
Nieduszynski C.A.
Spatafora J.W.
Friedman N.
Dalgaard J.Z.
Baumann P.
Niki H.
Regev A.
Nusbaum C.

title: Comparative functional genomics of the fission yeasts.

journal: Science

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]

database: STRING

database: PaxDb

database: KEGG

database: PomBase

database: VEuPathDB

database: eggNOG

value: Eukaryota

database: HOGENOM

database: InParanoid

database: OMA

value: Chromosome II

value: P:nonfunctional rRNA decay

database: FunFam

value: YVTN repeat-like/Quinoprotein amine dehydrogenase


proteinExistence: 3: Inferred from homology

value: Small ribosomal subunit protein uS13m

value: 37S ribosomal protein subunit sws2, mitochondrial

value: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane

value: Component of the mitochondrial small ribosomal subunit (mt-SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and at least 32 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and at least 45 different proteins

value: Mitochondrion

value: Belongs to the universal ribosomal protein uS13 family

description: Small ribosomal subunit protein uS13m

database: PubMed

database: DOI

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

database: EMBL

database: PIR

database: RefSeq

database: AlphaFoldDB

database: SMR

database: ComplexPortal

value: 37S mitochondrial small ribosomal subunit

database: GeneID

database: PhylomeDB

database: PRO

database: Proteomes

value: Chromosome III

database: GO

value: C:mitochondrial small ribosomal subunit

value: C:small ribosomal subunit

value: F:RNA binding

value: F:structural constituent of ribosome

value: P:mitochondrial translation

value: 30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18


value: Large ribosomal subunit protein uL4m

value: 54S ribosomal protein yml6, mitochondrial

value: Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and at least 32 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and at least 45 different proteins

value: Belongs to the universal ribosomal protein uL4 family

description: Mitochondrion

description: Large ribosomal subunit protein uL4m

description: Disordered

source: EMBL

database: BioGRID

value: 54S mitochondrial large ribosomal subunit

database: FunCoup

database: STRING

database: PaxDb

database: KEGG

database: PomBase

database: VEuPathDB

database: eggNOG

value: Eukaryota

database: HOGENOM

value: Chromosome II

value: C:mitochondrial large ribosomal subunit


entryType: UniProtKB unreviewed (TrEMBL)

scientificName: Drosophila melanogaster

commonName: Fruit fly

source: Proteomes

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

source: ARBA

value: nucleoside diphosphate phosphatase

source: FlyBase

value: NTPase

value: dmNTPase

value: Belongs to the GDA1/CD39 NTPase family

type: Transmembrane

description: Helical

description: Disordered

description: Low complexity

description: Proton acceptor

source: PIRSR

ATP-binding

category: Ligand

Proteomics identification

source: PeptideAtlas

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.

value: Berkeley

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.

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.

value: Expressed in crop (Drosophila) and 218 other cell types or tissues

value: Ectonucleoside triphosphate diphosphohydrolase 5


value: FACT complex subunit spt16

value: Facilitates chromatin transcription complex subunit spt16

value: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure (By similarity). It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (PubMed:28218250)

value: Forms a stable heterodimer with pob3 (By similarity). The spt16-pob3 dimer weakly associates with multiple molecules of nhp6 to form the FACT complex (By similarity). Interacts with abo1 (PubMed:26582768). Interacts with chromatin remodeling protein fft3; to mediate nucleosome disassembly at transcribing regions and promote the efficient passage of RNAPII through chromatin (PubMed:28218250)

value: Nucleus

value: Chromosome

value: Belongs to the peptidase M24 family. SPT16 subfamily

value: Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity

commentType: CAUTION

description: FACT complex subunit spt16

description: Disordered

description: Disordered

type: Coiled coil

description: Basic and acidic residues

description: Acidic residues

description: Basic and acidic residues

description: Phosphoserine

description: Phosphoserine

title: Phosphoproteome analysis of fission yeast.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444 AND SER-445

authors:
Gal C.
Murton H.E.
Subramanian L.
Whale A.J.
Moore K.M.
Paszkiewicz K.
Codlin S.
Baehler J.
Creamer K.M.
Partridge J.F.
Allshire R.C.
Kent N.A.
Whitehall S.K.

title: Abo1, a conserved bromodomain AAA-ATPase, maintains global nucleosome occupancy and organisation.

authors:
Lee J.
Choi E.S.
Seo H.D.
Kang K.
Gilmore J.M.
Florens L.
Washburn M.P.
Choe J.
Workman J.L.
Lee D.

title: Chromatin remodeller Fun30Fft3 induces nucleosome disassembly to facilitate RNA polymerase II elongation.

value: RNA Polymerase II Pre-transcription Events

value: TP53 Regulates Transcription of DNA Repair Genes

value: Regulation of TP53 Activity through Phosphorylation

value: F:H2A-H2B histone complex chaperone activity

value: P:DNA replication-dependent chromatin assembly

value: P:regulation of DNA-templated transcription elongation

value: P:transcription elongation-coupled chromatin remodeling

value: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)


value: Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial

value: Beta-ketoacyl-ACP synthase

value: mtKAS

value: May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function

name: a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP] + holo-[ACP] + CO2

database: Rhea

database: ChEBI

directionType: left-to-right

name: butanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxohexanoyl-[ACP] + holo-[ACP] + CO2

name: hexanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxooctanoyl-[ACP] + holo-[ACP] + CO2

name: octanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxodecanoyl-[ACP] + holo-[ACP] + CO2

name: decanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxododecanoyl-[ACP] + holo-[ACP] + CO2

name: dodecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxotetradecanoyl-[ACP] + holo-[ACP] + CO2

name: tetradecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxohexadecanoyl-[ACP] + holo-[ACP] + CO2

value: Lipid metabolism; fatty acid biosynthesis

value: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family

description: Mitochondrion

description: Ketosynthase family 3 (KS3)

description: For beta-ketoacyl synthase activity

description: For beta-ketoacyl synthase activity

description: For beta-ketoacyl synthase activity

title: The genome sequence of Schizosaccharomyces pombe.


value: GPI transamidase component PIG-T homolog

value: Component of the GPI transamidase complex. Involved in transfer of GPI to proteins (By similarity)

value: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis

commentType: PATHWAY

value: Forms a complex with PIG-S homolog, PIG-U homolog and GPI8

value: Endoplasmic reticulum membrane

value: Single-pass type I membrane protein

value: The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity

commentType: PTM

value: Belongs to the PIGT family

type: Signal

type: Chain

type: Topological domain

description: Lumenal

description: Helical

description: Cytoplasmic

type: Glycosylation

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

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

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

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

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

type: Disulfide bond

description: Interchain (with C-73 in PIGK/GPI8)

Disulfide bond

category: PTM

database: EMBL

database: PIR

database: RefSeq

database: AlphaFoldDB

database: SMR

database: ComplexPortal

value: GPI-anchor transamidase complex

database: GlyCosmos

key: glycosylation

value: 5 sites, No reported glycans

database: GeneID

value: C:lumenal side of endoplasmic reticulum membrane

value: GPI TRANSAMIDASE COMPONENT PIG-T-RELATED


value: PHD and RING finger domain-containing protein C126.07c

value: Cytoplasm

value: Nucleus

type: Zinc finger

description: RING-type 1; atypical

description: PHD-type

description: RING-type 2; degenerate

type: Region

description: Disordered

type: Compositional bias

description: Polar residues

description: Basic residues

description: Polar residues

type: STRAIN

database: BioGRID

database: STRING

database: iPTMnet

database: PaxDb

database: KEGG

value: Eukaryota

database: InParanoid

database: OMA

database: PhylomeDB

database: PRO

database: Proteomes

value: Chromosome III

database: GO

value: Zinc/RING finger domain, C3HC4 (zinc finger)

value: PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1


value: WD repeat-containing and planar cell polarity effector protein fritz homolog

value: hFRTZ

value: Bardet-Biedl syndrome 15 protein

value: WDPCP

value: FRITZ

value: Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Together with FUZ and WDPCP proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (By similarity). Binds phosphatidylinositol 3-phosphate with highest affinity, followed by phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate (PubMed:35427153)

value: Component of the CPLANE (ciliogenesis and planar polarity effectors) complex, composed of INTU, FUZ and WDPCP (PubMed:35427153). Interacts with CPLANE1 (By similarity)

value: Cell membrane

value: Cytoplasm, cytoskeleton, cilium axoneme

value: Cytoplasm, cytoskeleton, cilium basal body

diseaseId: Bardet-Biedl syndrome 15

description: A syndrome characterized by usually severe pigmentary retinopathy, early-onset obesity, polydactyly, hypogenitalism, renal malformation and intellectual disability. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease.

database: MIM

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

diseaseId: Congenital heart defects, hamartomas of tongue, and polysyndactyly

acronym: CHDTHP

description: A disease characterized by a constellation of anomalies including tongue hamartomas, polysyndactyly, and congenital heart defects such as atrioventricular canal and coarctation of the aorta.

value: Mutations in WDPCP may act as modifiers of the phenotypic expression of Bardet-Biedl syndrome and Meckel syndrome by interacting in trans with primary BBS and MKS loci

value: Belongs to the WD repeat fritz family

value: It is uncertain whether Met-1 or Met-34 is the initiator

description: WD 1

description: WD 2

type: Alternative sequence

description: in isoform 3

source: Reference

description: in isoform 2

originalSequence: DIHYLALDKGELAL

description: in isoform 2

type: Natural variant

description: in CHDTHP; impairs protein stability; no effect on the assembly of the CPLANE complex; dbSNP:rs200322968

database: dbSNP

originalSequence: D

description: in a patient with Meckel syndrome compound heterozygous for mutations in CC2D2A; no effect on the assembly of the CPLANE complex; dbSNP:rs267606693

description: in a patient with Bardet-Biedl syndrome compound heterozygous for mutations in BBS12; no effect on the assembly of the CPLANE complex

originalSequence: L

description: in dbSNP:rs17617459

originalSequence: G

description: no effect on the assembly of the CPLANE complex; increased binding to phosphoinositides

originalSequence: S

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3)

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.

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

authors:
Hillier L.W.
Graves T.A.
Fulton R.S.
Fulton L.A.
Pepin K.H.
Minx P.
Wagner-McPherson C.
Layman D.
Wylie K.
Sekhon M.
Becker M.C.
Fewell G.A.
Delehaunty K.D.
Miner T.L.
Nash W.E.
Kremitzki C.
Oddy L.
Du H.
Sun H.
Bradshaw-Cordum H.
Ali J.
Carter J.
Cordes M.
Harris A.
Isak A.
van Brunt A.
Nguyen C.
Du F.
Courtney L.
Kalicki J.
Ozersky P.
Abbott S.
Armstrong J.
Belter E.A.
Caruso L.
Cedroni M.
Cotton M.
Davidson T.
Desai A.
Elliott G.
Erb T.
Fronick C.
Gaige T.
Haakenson W.
Haglund K.
Holmes A.
Harkins R.
Kim K.
Kruchowski S.S.
Strong C.M.
Grewal N.
Goyea E.
Hou S.
Levy A.
Martinka S.
Mead K.
McLellan M.D.
Meyer R.
Randall-Maher J.
Tomlinson C.
Dauphin-Kohlberg S.
Kozlowicz-Reilly A.
Shah N.
Swearengen-Shahid S.
Snider J.
Strong J.T.
Thompson J.
Yoakum M.
Leonard S.
Pearman C.
Trani L.
Radionenko M.
Waligorski J.E.
Wang C.
Rock S.M.
Tin-Wollam A.-M.
Maupin R.
Latreille P.
Wendl M.C.
Yang S.-P.
Pohl C.
Wallis J.W.
Spieth J.
Bieri T.A.
Berkowicz N.
Nelson J.O.
Osborne J.
Ding L.
Meyer R.
Sabo A.
Shotland Y.
Sinha P.
Wohldmann P.E.
Cook L.L.
Hickenbotham M.T.
Eldred J.
Williams D.
Jones T.A.
She X.
Ciccarelli F.D.
Izaurralde E.
Taylor J.
Schmutz J.
Myers R.M.
Cox D.R.
Huang X.
McPherson J.D.
Mardis E.R.
Clifton S.W.
Warren W.C.
Chinwalla A.T.
Eddy S.R.
Marra M.A.
Ovcharenko I.
Furey T.S.
Miller W.
Eichler E.E.
Bork P.
Suyama M.
Torrents D.
Waterston R.H.
Wilson R.K.

title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.

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

authors:
Langousis G.
Cavadini S.
Boegholm N.
Lorentzen E.
Kempf G.
Matthias P.

title: Structure of the ciliogenesis-associated CPLANE complex.

referencePositions: STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS) OF 2-746

referencePositions: CHARACTERIZATION OF VARIANT CHDTHP ASN-54

referencePositions: CHARACTERIZATION OF VARIANTS LYS-55; PHE-205 AND PHE-708

authors:
Kim S.K.
Shindo A.
Park T.J.
Oh E.C.
Ghosh S.
Gray R.S.
Lewis R.A.
Johnson C.A.
Attie-Bittach T.
Katsanis N.
Wallingford J.B.

title: Planar cell polarity acts through septins to control collective cell movement and ciliogenesis.

referencePositions:
INVOLVEMENT IN BBS15
INVOLVEMENT IN MECKEL SYNDROME
VARIANTS LYS-55; PHE-205 AND PHE-708

authors:
Saari J.
Lovell M.A.
Yu H.C.
Bellus G.A.

title: Compound heterozygosity for a frame shift mutation and a likely pathogenic sequence variant in the planar cell polarity-ciliogenesis gene WDPCP in a girl with polysyndactyly, coarctation of the aorta, and tongue hamartomas.

referencePositions:
INVOLVEMENT IN CHDTHP
VARIANT CHDTHP ASN-54

authors:
Toriyama M.
Lee C.
Taylor S.P.
Duran I.
Cohn D.H.
Bruel A.L.
Tabler J.M.
Drew K.
Kelly M.R.
Kim S.
Park T.J.
Braun D.A.
Pierquin G.
Biver A.
Wagner K.
Malfroot A.
Panigrahi I.
Franco B.
Al-Lami H.A.
Yeung Y.
Choi Y.J.
Duffourd Y.
Faivre L.
Riviere J.B.
Chen J.
Liu K.J.
Marcotte E.M.
Hildebrandt F.
Thauvin-Robinet C.
Krakow D.
Jackson P.K.
Wallingford J.B.

title: The ciliopathy-associated CPLANE proteins direct basal body recruitment of intraflagellar transport machinery.

value: Heart defect-tongue hamartoma-polysyndactyly syndrome

value: 4 GO annotations based on evolutionary models

value: Expressed in kidney epithelium and 198 other cell types or tissues

value: YVTN repeat-like/Quinoprotein amine dehydrogenase

value: WD REPEAT-CONTAINING AND PLANAR CELL POLARITY EFFECTOR PROTEIN FRITZ HOMOLOG


value: Cholesterol 25-hydroxylase

value: Cholesterol 25-monooxygenase

value: Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes (PubMed:9852097). Plays a key role in cell positioning and movement in lymphoid tissues: 25-hydroxycholesterol is an intermediate in biosynthesis of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC), an oxysterol that acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (By similarity). May play an important role in regulating lipid metabolism by synthesizing a corepressor that blocks sterol regulatory element binding protein (SREBP) processing (PubMed:9852097). As an interferon-stimulated gene, has broad antiviral activities against a wide range of enveloped viruses, such as vesicular stomatitis virus (VSV) and SARS coronavirus-2 (SARS-CoV-2). Its product, 25-hydroxycholesterol, activates the ER-localized enzyme ACAT to induce internalization of accessible cholesterol on the plasma membrane and restricts SARS-CoV-2 S protein-mediated fusion which inhibits virus replication (PubMed:32944968, PubMed:33239446). In testis, production of 25-hydroxycholesterol by macrophages plays a role in Leydig cell differentiation (By similarity). Required to restrain inflammation in macrophages: production of 25-hydroxycholesterol protects macrophages from cholesterol overload, thereby preventing mitochondrial DNA release and subsequent activation of the AIM2 inflammasome (By similarity)

name: cholesterol + AH2 + O2 = 25-hydroxycholesterol + A + H2O

database: Rhea

database: ChEBI

name: cholesterol + NADPH + O2 + H(+) = 25-hydroxycholesterol + NADP(+) + H2O

value: Endoplasmic reticulum membrane

value: Multi-pass membrane protein

value: Induced by interferon (IFN) upon infection by virus like SARS-CoV-2

value: N-glycosylated

value: Belongs to the sterol desaturase family

description: Cholesterol 25-hydroxylase

description: Helical

description: Helical

description: Helical

type: Domain

description: Fatty acid hydroxylase

type: Motif

description: Histidine box-1

description: Histidine box-2

description: Histidine box-3

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

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

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

description: in dbSNP:rs17117295

type: Mutagenesis

description: Loss of cholesterol 25-hydroxylase activity. Loss of inhibition of infection by SARS-COV-2.

authors:
Lund E.G.
Kerr T.A.
Sakai J.
Li W.-P.
Russell D.W.

title: cDNA cloning of mouse and human cholesterol 25-hydroxylases, polytopic membrane proteins that synthesize a potent oxysterol regulator of lipid metabolism.

referencePositions: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]

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.

authors:
Deloukas P.
Earthrowl M.E.
Grafham D.V.
Rubenfield M.
French L.
Steward C.A.
Sims S.K.
Jones M.C.
Searle S.
Scott C.
Howe K.
Hunt S.E.
Andrews T.D.
Gilbert J.G.R.
Swarbreck D.
Ashurst J.L.
Taylor A.
Battles J.
Bird C.P.
Ainscough R.
Almeida J.P.
Ashwell R.I.S.
Ambrose K.D.
Babbage A.K.
Bagguley C.L.
Bailey J.
Banerjee R.
Bates K.
Beasley H.
Bray-Allen S.
Brown A.J.
Brown J.Y.
Burford D.C.
Burrill W.
Burton J.
Cahill P.
Camire D.
Carter N.P.
Chapman J.C.
Clark S.Y.
Clarke G.
Clee C.M.
Clegg S.
Corby N.
Coulson A.
Dhami P.
Dutta I.
Dunn M.
Faulkner L.
Frankish A.
Frankland J.A.
Garner P.
Garnett J.
Gribble S.
Griffiths C.
Grocock R.
Gustafson E.
Hammond S.
Harley J.L.
Hart E.
Heath P.D.
Ho T.P.
Hopkins B.
Horne J.
Howden P.J.
Huckle E.
Hynds C.
Johnson C.
Johnson D.
Kana A.
Kay M.
Kimberley A.M.
Kershaw J.K.
Kokkinaki M.
Laird G.K.
Lawlor S.
Lee H.M.
Leongamornlert D.A.
Laird G.
Lloyd C.
Lloyd D.M.
Loveland J.
Lovell J.
McLaren S.
McLay K.E.
McMurray A.
Mashreghi-Mohammadi M.
Matthews L.
Milne S.
Nickerson T.
Nguyen M.
Overton-Larty E.
Palmer S.A.
Pearce A.V.
Peck A.I.
Pelan S.
Phillimore B.
Porter K.
Rice C.M.
Rogosin A.
Ross M.T.
Sarafidou T.
Sehra H.K.
Shownkeen R.
Skuce C.D.
Smith M.
Standring L.
Sycamore N.
Tester J.
Thorpe A.
Torcasso W.
Tracey A.
Tromans A.
Tsolas J.
Wall M.
Walsh J.
Wang H.
Weinstock K.
West A.P.
Willey D.L.
Whitehead S.L.
Wilming L.
Wray P.W.
Young L.
Chen Y.
Lovering R.C.
Moschonas N.K.
Siebert R.
Fechtel K.
Bentley D.
Durbin R.M.
Hubbard T.
Doucette-Stamm L.
Beck S.
Smith D.R.
Rogers J.

title: The DNA sequence and comparative analysis of human chromosome 10.

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.

authors:
Riemenschneider M.
Mahmoodzadeh S.
Eisele T.
Klopp N.
Schwarz S.
Wagenpfeil S.
Diehl J.
Mueller U.
Foerstl H.
Illig T.
Kurz A.

title: Association analysis of genes involved in cholesterol metabolism located within the linkage region on chromosome 10 and Alzheimer's disease.

referencePositions: LACK OF INVOLVEMENT IN ALZHEIMER DISEASE

authors:
Shibata N.
Kawarai T.
Lee J.H.
Lee H.-S.
Shibata E.
Sato C.
Liang Y.
Duara R.
Mayeux R.P.
St George-Hyslop P.H.
Rogaeva E.

title: Association studies of cholesterol metabolism genes (CH25H, ABCA1 and CH24H) in Alzheimer's disease.

authors:
Wang S.
Li W.
Hui H.
Tiwari S.K.
Zhang Q.
Croker B.A.
Rawlings S.
Smith D.
Carlin A.F.
Rana T.M.

title: Cholesterol 25-Hydroxylase inhibits SARS-CoV-2 and other coronaviruses by depleting membrane cholesterol.

authors:
Zang R.
Case J.B.
Yutuc E.
Ma X.
Shen S.
Gomez Castro M.F.
Liu Z.
Zeng Q.
Zhao H.
Son J.
Rothlauf P.W.
Kreutzberger A.J.B.
Hou G.
Zhang H.
Bose S.
Wang X.
Vahey M.D.
Mani K.
Griffiths W.J.
Kirchhausen T.
Fremont D.H.
Guo H.
Diwan A.
Wang Y.
Diamond M.S.
Whelan S.P.J.
Ding S.

title: Cholesterol 25-hydroxylase suppresses SARS-CoV-2 replication by blocking membrane fusion.

referencePositions:
FUNCTION
MUTAGENESIS OF 242-HIS-HIS-243
CATALYTIC ACTIVITY

value: 5 GO annotations based on evolutionary models

value: Expressed in mucosa of paranasal sinus and 157 other cell types or tissues

value: P:cholesterol biosynthetic process via desmosterol

value: P:negative regulation of cholesterol metabolic process

value: P:negative regulation of fusion of virus membrane with host plasma membrane


value: 60 kDa heat shock protein, mitochondrial

value: 60 kDa chaperonin

value: Chaperonin 60

value: Heat shock protein 60

value: Heat shock protein family D member 1

value: Mitochondrial matrix protein P1

value: P60 lymphocyte protein

value: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable)

name: ATP + H2O + an unfolded polypeptide = ADP + phosphate + a folded polypeptide.

value: Homoheptamer arranged in a ring structure (PubMed:11422376, PubMed:1346131, PubMed:25918392). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. Interacts with 2 heptameric Hsp10 rings to form the symmetrical football complex (PubMed:25918392). Interacts with HRAS (By similarity). Interacts with ATAD3A (PubMed:22664726). Interacts with ETFBKMT and EEF1AKMT3 (PubMed:23349634). Interacts with MFHAS1 (PubMed:24286120)

value: (Microbial infection) Interacts with hepatitis B virus/HBV protein X

value: (Microbial infection) Interacts with HTLV-1 protein p40tax

geneName: APP

geneName: BOK

geneName: CFTR

geneName: CHAT

geneName: DXO

geneName: HRAS

geneName: JUN

geneName: NEFH

value: Mitochondrion matrix

diseaseId: Spastic paraplegia 13, autosomal dominant

description: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.

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

diseaseId: Leukodystrophy, hypomyelinating, 4

description: A severe autosomal recessive hypomyelinating leukodystrophy. Clinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound intellectual disability. Death usually occurs within the first two decades of life.

value: Belongs to the chaperonin (HSP60) family

commentType: WEB RESOURCE

resourceName: Atlas of Genetics and Cytogenetics in Oncology and Haematology

type: Transit peptide

description: Mitochondrion

description: 60 kDa heat shock protein, mitochondrial

type: Binding site

type: Modified residue

description: Phosphoserine

description: Phosphoserine

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: Phosphotyrosine

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: N6-acetyllysine; alternate

description: N6-malonyllysine; alternate

description: N6-succinyllysine; alternate

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: Phosphoserine

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: Phosphoserine

description: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

description: in isoform 2

description: in isoform 2

description: in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature; dbSNP:rs72466451

description: in SPG13; dbSNP:rs66468541

description: in Ref. 2; AAA36022

description: in Ref. 5; BAG35173

description: in Ref. 5; BAG35173

description: in Ref. 4; ABB01006

description: in Ref. 5; BAG35173

authors:
Jindal S.
Dudani A.K.
Singh B.
Harley C.B.
Gupta R.S.

title: Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen.

title: Nucleotide sequences and novel structural features of human and Chinese hamster hsp60 (chaperonin) gene families.

authors:
Hansen J.J.
Bross P.
Westergaard M.
Nielsen M.N.
Eiberg H.
Boerglum A.D.
Mogensen J.
Kristiansen K.
Bolund L.
Gregersen N.

title: Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter.

title: Genetic variation in immune response genes.

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

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

authors:
Waldinger D.
Eckerskorn C.
Lottspeich F.
Cleve H.

title: Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (Rubisco-binding protein).

authors:
Ward L.D.
Hong J.
Whitehead R.H.
Simpson R.J.

title: Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis.

authors:
Nagata K.
Ide Y.
Takagi T.
Ohtani K.
Aoshima M.
Tozawa H.
Nakamura M.
Sugamura K.

title: Complex formation of human T-cell leukemia virus type I p40tax transactivator with cellular polypeptides.

referencePositions: INTERACTION WITH HTLV-1 P40TAX (MICROBIAL INFECTION)

authors:
Rasmussen R.K.
Ji H.
Eddes J.S.
Moritz R.L.
Reid G.E.
Simpson R.J.
Dorow D.S.

title: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2.

authors:
Corbett J.M.
Wheeler C.H.
Baker C.S.
Yacoub M.H.
Dunn M.J.

title: The human myocardial two-dimensional gel protein database: update 1994.

authors:
Gevaert K.
Goethals M.
Martens L.
Van Damme J.
Staes A.
Thomas G.R.
Vandekerckhove J.

title: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.

authors:
Hochstrasser D.F.
Frutiger S.
Paquet N.
Bairoch A.
Ravier F.
Pasquali C.
Sanchez J.-C.
Tissot J.-D.
Bjellqvist B.
Vargas R.
Appel R.D.
Hughes G.J.

title: Human liver protein map: a reference database established by microsequencing and gel comparison.

referencePositions:
PROTEIN SEQUENCE OF 61-72
IDENTIFICATION BY MASS SPECTROMETRY

authors:
Lubec G.
Vishwanath V.
Chen W.-Q.
Sun Y.

authors:
Aboulaich N.
Vainonen J.P.
Stralfors P.
Vener A.V.

title: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.

authors:
Ji H.
Reid G.E.
Moritz R.L.
Eddes J.S.
Burgess A.W.
Simpson R.J.

title: A two-dimensional gel database of human colon carcinoma proteins.

authors:
Singh B.
Patel H.V.
Ridley R.G.
Freeman K.B.
Gupta R.S.

title: Mitochondrial import of the human chaperonin (HSP60) protein.

authors:
Viitanen P.V.
Lorimer G.H.
Seetharam R.
Gupta R.S.
Oppenheim J.
Thomas J.O.
Cowan N.J.

title: Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring.

authors:
Levy-Rimler G.
Viitanen P.
Weiss C.
Sharkia R.
Greenberg A.
Niv A.
Lustig A.
Delarea Y.
Azem A.

title: The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60.

authors:
Andersen J.S.
Wilkinson C.J.
Mayor T.
Mortensen P.
Nigg E.A.
Mann M.

title: Proteomic characterization of the human centrosome by protein correlation profiling.

authors:
Tanaka Y.
Kanai F.
Kawakami T.
Tateishi K.
Ijichi H.
Kawabe T.
Arakawa Y.
Kawakami T.
Nishimura T.
Shirakata Y.
Koike K.
Omata M.

title: Interaction of the hepatitis B virus X protein (HBx) with heat shock protein 60 enhances HBx-mediated apoptosis.

referencePositions: INTERACTION WITH HBV PROTEIN X (MICROBIAL INFECTION)

authors:
Rush J.
Moritz A.
Lee K.A.
Guo A.
Goss V.L.
Spek E.J.
Zhang H.
Zha X.-M.
Polakiewicz R.D.
Comb M.J.

title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70

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.

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.

authors:
Choudhary C.
Kumar C.
Gnad F.
Nielsen M.L.
Rehman M.
Walther T.C.
Olsen J.V.
Mann M.

title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

referencePositions: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82; LYS-125; LYS-130; LYS-202; LYS-218; LYS-269; LYS-352; LYS-359; LYS-396 AND LYS-469

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.

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:
Peng C.
Lu Z.
Xie Z.
Cheng Z.
Chen Y.
Tan M.
Luo H.
Zhang Y.
He W.
Yang K.
Zwaans B.M.
Tishkoff D.
Ho L.
Lombard D.
He T.C.
Dai J.
Verdin E.
Ye Y.
Zhao Y.

title: The first identification of lysine malonylation substrates and its regulatory enzyme.

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:
Rosenow A.
Noben J.P.
Jocken J.
Kallendrusch S.
Fischer-Posovszky P.
Mariman E.C.
Renes J.

title: Resveratrol-induced changes of the human adipocyte secretion profile.

authors:
Merle N.
Feraud O.
Gilquin B.
Hubstenberger A.
Kieffer-Jacquinot S.
Assard N.
Bennaceur-Griscelli A.
Honnorat J.
Baudier J.

title: ATAD3B is a human embryonic stem cell specific mitochondrial protein, re-expressed in cancer cells, that functions as dominant negative for the ubiquitous ATAD3A.

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-70 AND SER-488

authors:
Cloutier P.
Lavallee-Adam M.
Faubert D.
Blanchette M.
Coulombe B.

title: A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.

authors:
Dihanich S.
Civiero L.
Manzoni C.
Mamais A.
Bandopadhyay R.
Greggio E.
Lewis P.A.

title: GTP binding controls complex formation by the human ROCO protein MASL1.

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.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND TYR-90

authors:
Vaca Jacome A.S.
Rabilloud T.
Schaeffer-Reiss C.
Rompais M.
Ayoub D.
Lane L.
Bairoch A.
Van Dorsselaer A.
Carapito C.

title: N-terminome analysis of the human mitochondrial proteome.

authors:
Hendriks I.A.
Lyon D.
Young C.
Jensen L.J.
Vertegaal A.C.
Nielsen M.L.

title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

referencePositions: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-551

authors:
Nisemblat S.
Yaniv O.
Parnas A.
Frolow F.
Azem A.

title: Crystal structure of the human mitochondrial chaperonin symmetrical football complex.

referencePositions: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 27-556 IN COMPLEX WITH ADP

authors:
Hansen J.J.
Durr A.
Cournu-Rebeix I.
Georgopoulos C.
Ang D.
Nielsen M.N.
Davoine C.-S.
Brice A.
Fontaine B.
Gregersen N.
Bross P.

title: Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60.

authors:
Magen D.
Georgopoulos C.
Bross P.
Ang D.
Segev Y.
Goldsher D.
Nemirovski A.
Shahar E.
Ravid S.
Luder A.
Heno B.
Gershoni-Baruch R.
Skorecki K.
Mandel H.

title: Mitochondrial Hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy.

referencePositions:
VARIANT HLD4 GLY-29
CHARACTERIZATION OF VARIANT HLD4 GLY-29

value: 7 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (6 sites)

value: Autosomal dominant spastic paraplegia type 13

value: Pelizaeus-Merzbacher-like disease due to HSPD1 mutation

value: 12 GO annotations based on evolutionary models

value: TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation

value: Mitochondrial unfolded protein response (UPRmt)

value: Presynaptic clusters and postsynaptic densities

value: Expressed in adrenal tissue and 152 other cell types or tissues

value: F:ATP-dependent protein folding chaperone

value: F:cysteine-type endopeptidase activator activity

value: F:high-density lipoprotein particle binding

value: P:biological process involved in interaction with symbiont

value: P:chaperone-mediated protein complex assembly

value: P:mitochondrial unfolded protein response

value: P:MyD88-dependent toll-like receptor signaling pathway

value: P:negative regulation of apoptotic process

value: P:negative regulation of execution phase of apoptosis

value: P:positive regulation of execution phase of apoptosis

value: P:positive regulation of interferon-alpha production

value: P:positive regulation of interleukin-10 production

value: P:positive regulation of interleukin-12 production

value: P:positive regulation of interleukin-6 production

value: P:positive regulation of macrophage activation

value: P:positive regulation of T cell activation

value: P:positive regulation of T cell mediated immune response to tumor cell

value: P:positive regulation of type II interferon production

value: P:protein import into mitochondrial intermembrane space

value: Chaperonin 60 subunit alpha 2 chloroplastic

value: TCP-1-like chaperonin intermediate domain

value: 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL


value: Wee1-like protein kinase

value: Wee1A kinase

value: Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15' (PubMed:15070733, PubMed:7743995, PubMed:8348613, PubMed:8428596). Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase (PubMed:7743995, PubMed:8348613, PubMed:8428596). Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur (PubMed:7743995, PubMed:8348613, PubMed:8428596). Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated (PubMed:7743995). A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation (PubMed:7743995)

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

value: Binds 2 magnesium ions per subunit.

value: Synthesis is increased during S and G2 phases, presumably by an increase in transcription; activity is decreased by phosphorylation during M phase (PubMed:7743995). Protein levels fall in M phase as a result of decreased synthesis combined with degradation (PubMed:7743995). Activity seems to be negatively regulated by phosphorylation upon entry into mitosis, although N-terminal phosphorylation might also regulate the protein stability via protection from proteolysis or might regulate the subcellular location (PubMed:7743995)

commentType: ACTIVITY REGULATION

geneName: BTRC

geneName: SFN

geneName: YWHAE

geneName: YWHAZ

value: Nucleus

value: Phosphorylated during M and G1 phases. Also autophosphorylated. Phosphorylation at Ser-642 by BRSK1 and BRSK2 in post-mitotic neurons, leads to down-regulate WEE1 activity in polarized neurons. Phosphorylated at Ser-53 and Ser-123 by PLK1 and CDK1, respectively, generating an signal for degradation that can be recognized by the SCF(BTRC) complex, leading to its ubiquitination and degradation at the onset of G2/M phase

value: Dephosphorylated at Thr-239 by CTDP1 (PubMed:22692537). Dephosphorylated at Ser-53 and Ser-123 by the serine/threonine-protein phosphatase 2A preventing its ubiquitin-mediated degradation (PubMed:33108758)

value: Ubiquitinated and degraded at the onset of G2/M phase

value: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily

description: Wee1-like protein kinase

description: Protein kinase

description: Disordered

description: Acidic residues

description: Low complexity

description: Basic and acidic residues

type: Active site

description: Proton acceptor

description: Phosphoserine; by PLK1

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine; by CDK1

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: Phosphothreonine

description: Phosphothreonine

description: Phosphothreonine

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine; by BRSK1 and BRSK2

description: in isoform 2

description: in dbSNP:rs34412975

description: in dbSNP:rs56411856

description: Abolishes phosphorylation by PLK1 and CDK1 and binding of the SCF(BTRC) complex, leading to stabilization of the protein; when associated with A-123.

description: Impairs binding of the SCF(BTRC) complex.

description: Abolishes phosphorylation by PLK1 and CDK1 and binding of the SCF(BTRC) complex, leading to stabilization of the protein; when associated with A-53.

description: Abolishes activity.

description: Abolishes phosphorylation by BRSK1 and BRSK2.

description: in Ref. 6; CAA43979

title: Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
FUNCTION
CATALYTIC ACTIVITY
ACTIVITY REGULATION

authors:
Cichutek A.
Brueckmann T.
Seipel B.
Hauser H.
Schlaubitz S.
Prawitt D.
Hankeln T.
Schmidt E.R.
Winterpacht A.
Zabel B.U.

title: Comparative architectural aspects of regions of conserved synteny on human chromosome 11p15.3 and mouse chromosome 7 (including genes WEE1 and LMO1).

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:
Taylor T.D.
Noguchi H.
Totoki Y.
Toyoda A.
Kuroki Y.
Dewar K.
Lloyd C.
Itoh T.
Takeda T.
Kim D.-W.
She X.
Barlow K.F.
Bloom T.
Bruford E.
Chang J.L.
Cuomo C.A.
Eichler E.
FitzGerald M.G.
Jaffe D.B.
LaButti K.
Nicol R.
Park H.-S.
Seaman C.
Sougnez C.
Yang X.
Zimmer A.R.
Zody M.C.
Birren B.W.
Nusbaum C.
Fujiyama A.
Hattori M.
Rogers J.
Lander E.S.
Sakaki Y.

title: Human chromosome 11 DNA sequence and analysis including novel gene identification.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

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.

referencePositions: NUCLEOTIDE SEQUENCE [MRNA] OF 1-214 (ISOFORM 1)

authors:
Igarashi M.
Nagata A.
Jinno S.
Suto K.
Okayama H.

title: Wee1(+)-like gene in human cells.

referencePositions: NUCLEOTIDE SEQUENCE [MRNA] OF 215-646 (ISOFORM 1)

title: Human wee1 maintains mitotic timing by protecting the nucleus from cytoplasmically activated Cdc2 kinase.

title: Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15.

referencePositions:
FUNCTION
CATALYTIC ACTIVITY
MUTAGENESIS OF LYS-328

title: Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function.

authors:
Watanabe N.
Arai H.
Nishihara Y.
Taniguchi M.
Watanabe N.
Hunter T.
Osada H.

title: M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP.

referencePositions: MUTAGENESIS OF SER-53; 116-GLU-GLU-117 AND SER-123

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.

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-85; SER-150; THR-190 AND SER-312

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 SER-139

title: Persistence of the cell-cycle checkpoint kinase Wee1 in SadA- and SadB-deficient neurons disrupts neuronal polarity.

referencePositions:
PHOSPHORYLATION AT SER-642
MUTAGENESIS OF SER-642

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-139

authors:
Visconti R.
Palazzo L.
Della Monica R.
Grieco D.

title: Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit.

referencePositions:
PHOSPHORYLATION AT THR-239
DEPHOSPHORYLATION

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-139; THR-187; THR-190; SER-270; SER-307 AND SER-312

authors:
Li F.
Kozono D.
Deraska P.
Branigan T.
Dunn C.
Zheng X.F.
Parmar K.
Nguyen H.
DeCaprio J.
Shapiro G.I.
Chowdhury D.
D'Andrea A.D.

title: CHK1 Inhibitor Blocks Phosphorylation of FAM122A and Promotes Replication Stress.

referencePositions: DEPHOSPHORYLATION AT SER-53 AND SER-123 BY SERINE/THREONINE-PROTEIN PHOSPHATASE 2A

authors:
Squire C.J.
Dickson J.M.
Ivanovic I.
Baker E.N.

title: Structure and inhibition of the human cell cycle checkpoint kinase, Wee1A kinase: an atypical tyrosine kinase with a key role in CDK1 regulation.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 291-575 IN COMPLEX WITH MAGNESIUM AND AN INHIBITOR

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.

referencePositions: VARIANTS [LARGE SCALE ANALYSIS] CYS-210 AND ILE-472

value: 6 evidence items across 3 molecular profiles

value: 4 GO annotations based on evolutionary models

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: Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex

value: Factors involved in megakaryocyte development and platelet production

value: Expressed in ventricular zone and 184 other cell types or tissues

value: F:non-membrane spanning protein tyrosine kinase activity

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

value: P:negative regulation of G2/M transition of mitotic cell cycle

value: P:positive regulation of DNA replication

value: EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED


value: Heat shock 70 kDa protein 4

value: Heat shock 70-related protein APG-2

value: Heat shock protein family H member 2

value: Interacts with TJP1/ZO-1

geneName: AGTRAP

geneName: EGFR

value: Cytoplasm

value: Belongs to the heat shock protein 70 family

type: Chain

description: Heat shock 70 kDa protein 4

description: Disordered

description: Disordered

description: Basic and acidic residues

description: Basic and acidic residues

description: Basic and acidic residues

description: Phosphoserine

description: Phosphotyrosine

description: Phosphotyrosine

description: Phosphoserine

description: Phosphoserine

description: Phosphothreonine

description: Phosphoserine

description: Phosphoserine

description: Phosphotyrosine

description: Phosphoserine

description: in isoform 2

description: in Ref. 5; AAA02807

description: in Ref. 5; AAA02807

description: in Ref. 5; AAA02807

description: in Ref. 1; BAA75062

description: in Ref. 1; BAA75062

description: in Ref. 5; AAA02807

title: Cloning and characterization of human apg-1 and apg-2, members of the hsp110 family, cDNAs and chromosomal assignment of the genes.

authors:
Kalnine N.
Chen X.
Rolfs A.
Halleck A.
Hines L.
Eisenstein S.
Koundinya M.
Raphael J.
Moreira D.
Kelley T.
LaBaer J.
Lin Y.
Phelan M.
Farmer A.

title: Cloning of human full-length CDSs in BD Creator(TM) system donor vector.

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).

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

authors:
Fathallah D.M.
Cherif D.
Dellagi K.
Arnaout M.A.

title: Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5.

referencePositions: NUCLEOTIDE SEQUENCE [MRNA] OF 1-749 (ISOFORM 1)

authors:
Lubec G.
Afjehi-Sadat L.
Chen W.-Q.
Sun Y.

authors:
Rush J.
Moritz A.
Lee K.A.
Guo A.
Goss V.L.
Spek E.J.
Zhang H.
Zha X.-M.
Polakiewicz R.D.
Comb M.J.

title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89 AND TYR-336

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Matsuoka S.
Ballif B.A.
Smogorzewska A.
McDonald E.R. III
Hurov K.E.
Luo J.
Bakalarski C.E.
Zhao Z.
Solimini N.
Lerenthal Y.
Shiloh Y.
Gygi S.P.
Elledge S.J.

title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

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 THR-538

authors:
Kampinga H.H.
Hageman J.
Vos M.J.
Kubota H.
Tanguay R.M.
Bruford E.A.
Cheetham M.E.
Chen B.
Hightower L.E.

title: Guidelines for the nomenclature of the human heat shock proteins.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND TYR-336

authors:
Choudhary C.
Kumar C.
Gnad F.
Nielsen M.L.
Rehman M.
Walther T.C.
Olsen J.V.
Mann M.

title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

referencePositions: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430 AND LYS-679

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 SER-76 AND SER-546

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-76; SER-393; THR-538; SER-647 AND SER-756

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:
Guo A.
Gu H.
Zhou J.
Mulhern D.
Wang Y.
Lee K.A.
Yang V.
Aguiar M.
Kornhauser J.
Jia X.
Ren J.
Beausoleil S.A.
Silva J.C.
Vemulapalli V.
Bedford M.T.
Comb M.J.

title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

referencePositions: METHYLATION [LARGE SCALE ANALYSIS] AT LYS-773

value: Regulation of HSF1-mediated heat shock response

value: Presynaptic clusters and postsynaptic densities

value: Expressed in primordial germ cell in gonad and 210 other cell types or tissues

value: F:adenyl-nucleotide exchange factor activity

value: P:chaperone-mediated protein complex assembly

value: P:protein import into mitochondrial matrix

value: Heat shock protein 70 (HSP70)-4, putative

value: Substrate Binding Domain Of DNAk, Chain A, domain 1

value: Heat shock protein 70kD (HSP70), C-terminal subdomain

value: Heat shock protein 70kD (HSP70), peptide-binding domain


value: Dual specificity mitogen-activated protein kinase kinase 2

value: MAP kinase kinase 2

value: MAPKK 2

value: ERK activator kinase 2

value: MAPK/ERK kinase 2

value: MEK 2

value: Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation (PubMed:29433126)

commentType: FUNCTION

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

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

value: Interacts with MORG1 (By similarity). Interacts with SGK1 (PubMed:19447520). Interacts with KSR1 (PubMed:10409742). Interacts with KSR1 and BRAF; the interaction with KSR1 mediates KSR1-BRAF dimerization (PubMed:29433126). Interacts with GLS (PubMed:22538822)

geneName: ARAF

geneName: BRAF

geneName: HNRNPK

geneName: MOS

geneName: MPDZ

geneName: PATJ

geneName: SCRIB

geneName: SDCBP

geneName: WHRN

value: Membrane localization is probably regulated by its interaction with KSR1

value: Membrane

value: Peripheral membrane protein

value: MAPKK is itself dependent on Ser/Thr phosphorylation for activity catalyzed by MAP kinase kinase kinases (RAF or MEKK1). Phosphorylated by MAP2K1/MEK1 (By similarity)

value: (Microbial infection) Acetylation of Ser-222 and Ser-226 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway

diseaseId: Cardiofaciocutaneous syndrome 4

description: A form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and intellectual disability. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices.

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

value: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily

description: Protein kinase

description: Disordered

description: Proton acceptor

description: Cleavage; by anthrax lethal factor

description: N-acetylmethionine

description: Phosphoserine

description: (Microbial infection) O-acetylserine; by Yersinia YopJ; alternate

description: Phosphoserine; by RAF; alternate

description: Phosphoserine; alternate

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: Phosphothreonine

description: Phosphothreonine

description: in CFC4; dbSNP:rs121434497

description: in CFC4; dbSNP:rs121434498

description: in CFC4; results in increased kinase activity; dbSNP:rs267607230

description: in CFC4; dbSNP:rs121434499

description: in Ref. 6; AA sequence

title: Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2.

title: Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling.

referencePositions: INACTIVATION BY YERSINIA YOPJ (MICROBIAL INFECTION)

authors:
Duesbery N.S.
Webb C.P.
Leppla S.H.
Gordon V.M.
Klimpel K.R.
Copeland T.D.
Ahn N.G.
Oskarsson M.K.
Fukasawa K.
Paull K.D.
Vande Woude G.F.

title: Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor.

authors:
Stewart S.
Sundaram M.
Zhang Y.
Lee J.
Han M.
Guan K.L.

title: Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization.

referencePositions: PROTEIN SEQUENCE OF 39-49; 52-61 AND 352-361

authors:
Vitale G.
Bernardi L.
Napolitani G.
Mock M.
Montecucco C.

title: Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor.

authors:
Olsen J.V.
Blagoev B.
Gnad F.
Macek B.
Kumar C.
Mortensen P.
Mann M.

title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

authors:
Zahedi R.P.
Lewandrowski U.
Wiesner J.
Wortelkamp S.
Moebius J.
Schuetz C.
Walter U.
Gambaryan S.
Sickmann A.

title: Phosphoproteome of resting human platelets.

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-293 AND SER-295

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND THR-396

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 MET-1

authors:
Won M.
Park K.A.
Byun H.S.
Kim Y.R.
Choi B.L.
Hong J.H.
Park J.
Seok J.H.
Lee Y.H.
Cho C.H.
Song I.S.
Kim Y.K.
Shen H.M.
Hur G.M.

title: Protein kinase SGK1 enhances MEK/ERK complex formation through the phosphorylation of ERK2: implication for the positive regulatory role of SGK1 on the ERK function during liver regeneration.

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.

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.

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 SER-295 AND THR-394

authors:
Thangavelu K.
Pan C.Q.
Karlberg T.
Balaji G.
Uttamchandani M.
Suresh V.
Schuler H.
Low B.C.
Sivaraman J.

title: Structural basis for the allosteric inhibitory mechanism of human kidney-type glutaminase (KGA) and its regulation by Raf-Mek-Erk signaling in cancer cell metabolism.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND THR-396

authors:
Lavoie H.
Sahmi M.
Maisonneuve P.
Marullo S.A.
Thevakumaran N.
Jin T.
Kurinov I.
Sicheri F.
Therrien M.

title: MEK drives BRAF activation through allosteric control of KSR proteins.

authors:
Rodriguez-Viciana P.
Tetsu O.
Tidyman W.E.
Estep A.L.
Conger B.A.
Cruz M.S.
McCormick F.
Rauen K.A.

title: Germline mutations in genes within the MAPK pathway cause cardio-facio-cutaneous syndrome.

authors:
Schulz A.L.
Albrecht B.
Arici C.
van der Burgt I.
Buske A.
Gillessen-Kaesbach G.
Heller R.
Horn D.
Hubner C.A.
Korenke G.C.
Konig R.
Kress W.
Kruger G.
Meinecke P.
Mucke J.
Plecko B.
Rossier E.
Schinzel A.
Schulze A.
Seemanova E.
Seidel H.
Spranger S.
Tuysuz B.
Uhrig S.
Wieczorek D.
Kutsche K.
Zenker M.

title: Mutation and phenotypic spectrum in patients with cardio-facio-cutaneous and Costello syndrome.

authors:
Rauen K.A.
Tidyman W.E.
Estep A.L.
Sampath S.
Peltier H.M.
Bale S.J.
Lacassie Y.

title: Molecular and functional analysis of a novel MEK2 mutation in cardio-facio-cutaneous syndrome: transmission through four generations.

referencePositions: CHARACTERIZATION OF VARIANT CFC4 GLN-128

value: 11 evidence items across 10 molecular profiles

value: 2 GO annotations based on evolutionary models

value: Negative feedback regulation of MAPK pathway

value: Signaling by moderate kinase activity BRAF mutants

value: Signaling by high-kinase activity BRAF mutants

value: Paradoxical activation of RAF signaling by kinase inactive BRAF

value: Expressed in mucosa of transverse colon and 202 other cell types or tissues

value: F:protein serine/threonine kinase activator activity

value: F:protein serine/threonine kinase activity

value: F:protein serine/threonine/tyrosine kinase activity

value: P:positive regulation of DNA-templated transcription

value: P:positive regulation of gene expression

value: P:positive regulation of protein serine/threonine kinase activity

value: P:regulation of early endosome to late endosome transport

value: P:regulation of stress-activated MAPK cascade

value: Dual specificity mitogen-activated protein kinase kinase 1

value: DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE DSOR1-LIKE PROTEIN

value: MITOGEN-ACTIVATED PROTEIN KINASE KINASE 2