query: (gene_exact:UBE2F) AND (taxonomy_id:9606) AND (reviewed:true)

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

value: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins (PubMed:19250909, PubMed:23201271). Together with the E3 ubiquitin ligase RNF7/RBX2, specifically neddylates cullin-5 (CUL5) (PubMed:19250909, PubMed:23201271, PubMed:23300442). Does not neddylate CUL1, CUL2, CUL3, CUL4A or CUL4B (PubMed:19250909, PubMed:23201271). Mediates neddylation of the CUL9-RBX1 complex (PubMed:38605244)

value: (Microbial infection) Following infection by HIV-1 virus, participates to HIV-1 Vif protein-mediated ubiquitination and degradation of APOBEC3G by mediating neddylation of cullin-5 (CUL5)

name: [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine = [E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine.

value: Protein modification; protein neddylation

value: Interacts with UBA3 and RBX2 (PubMed:19250909). Interacts (N-terminally acetylated form) with (via DCUN1 domain) DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5 (PubMed:23201271)

value: The acetylation of Met-1 increases affinity for DCUN1D3 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins

value: Belongs to the ubiquitin-conjugating enzyme family. UBE2F subfamily

description: NEDD8-conjugating enzyme UBE2F

description: UBC core

description: Interaction with UBA3

description: Glycyl thioester intermediate

description: N-acetylmethionine

description: in isoform 7

description: in isoform 3

description: in isoform 5

description: in isoform 4

description: in isoform 4

description: in isoform 6

description: in isoform 2

description: Abolished NEDD8 conjugating enzyme activity.

description: in Ref. 2; BAF82752

title: NEDD8-conjugating enzyme.

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

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

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5)

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.

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 [LARGE SCALE GENOMIC DNA]

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

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

authors:
Stanley D.J.
Bartholomeeusen K.
Crosby D.C.
Kim D.Y.
Kwon E.
Yen L.
Cartozo N.C.
Li M.
Jaeger S.
Mason-Herr J.
Hayashi F.
Yokoyama S.
Krogan N.J.
Harris R.S.
Peterlin B.M.
Gross J.D.

title: Inhibition of a NEDD8 Cascade Restores Restriction of HIV by APOBEC3G.

referencePositions:
FUNCTION (MICROBIAL INFECTION)
CATALYTIC ACTIVITY
PATHWAY
ACTIVE SITE
MUTAGENESIS OF CYS-116

authors:
Horn-Ghetko D.
Hopf L.V.M.
Tripathi-Giesgen I.
Du J.
Kostrhon S.
Vu D.T.
Beier V.
Steigenberger B.
Prabu J.R.
Stier L.
Bruss E.M.
Mann M.
Xiong Y.
Schulman B.A.

title: Noncanonical assembly, neddylation and chimeric cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex.

authors:
Huang D.T.
Ayrault O.
Hunt H.W.
Taherbhoy A.M.
Duda D.M.
Scott D.C.
Borg L.A.
Neale G.
Murray P.J.
Roussel M.F.
Schulman B.A.

title: E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-185 IN COMPLEX WITH UBA3

authoringGroup: RIKEN structural genomics initiative (RSGI)

title: Solution structure of the UQ_CON domain from human NEDD8-conjugating enzyme NCE2.

authors:
Monda J.K.
Scott D.C.
Miller D.J.
Lydeard J.
King D.
Harper J.W.
Bennett E.J.
Schulman B.A.

title: Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-25 IN COMPLEX WITH DCUN1D3

referencePositions: INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5

value: 4 GO annotations based on evolutionary models

value: Antigen processing: Ubiquitination & Proteasome degradation

value: Expressed in body of pancreas and 189 other cell types or tissues


query: (gene_exact:NARF) AND (taxonomy_id:9606) AND (reviewed:true)

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

value: Nemo-like kinase-associated RING finger protein

value: RING-type E3 ubiquitin transferase RNF138

value: E3 ubiquitin-protein ligase involved in DNA damage response by promoting DNA resection and homologous recombination (PubMed:26502055, PubMed:26502057). Recruited to sites of double-strand breaks following DNA damage and specifically promotes double-strand break repair via homologous recombination (PubMed:26502055, PubMed:26502057). Two different, non-exclusive, mechanisms have been proposed. According to a report, regulates the choice of double-strand break repair by favoring homologous recombination over non-homologous end joining (NHEJ): acts by mediating ubiquitination of XRCC5/Ku80, leading to remove the Ku complex from DNA breaks, thereby promoting homologous recombination (PubMed:26502055). According to another report, cooperates with UBE2Ds E2 ubiquitin ligases (UBE2D1, UBE2D2, UBE2D3 or UBE2D4) to promote homologous recombination by mediating ubiquitination of RBBP8/CtIP (PubMed:26502057). Together with NLK, involved in the ubiquitination and degradation of TCF/LEF (PubMed:16714285). Also exhibits auto-ubiquitination activity in combination with UBE2K (PubMed:16714285). May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway (PubMed:16714285)

name: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.

value: Protein modification; protein ubiquitination

value: Interacts with NLK (PubMed:16714285). Interacts with XRCC5/Ku80 (PubMed:26502055). Interacts with RBBP8/CtIP (PubMed:26502057)

value: Recruited at DNA damage sites (PubMed:26502055). Localizes to sites of double-strand break: localization to double-strand break sites is mediated by the zinc fingers (PubMed:26502055, PubMed:26502057)

value: The zinc finger domains (C2H2-type and C2HC-type zinc fingers) bind DNA and mediate recruitment to double-strand break sites. They show strong preference for DNA with 5'- or 3'-single-stranded overhangs, while they do not bind blunt-ended double-stranded DNA or poly(ADP-ribose) (PAR) polymers

description: Removed

description: E3 ubiquitin-protein ligase RNF138

description: UIM

description: RING-type

description: C2HC RNF-type

description: C2H2-type 1

description: C2H2-type 2

description: Disordered

description: N-acetylalanine

description: Phosphothreonine

description: in isoform 2

description: in dbSNP:rs7229690

description: Catalytic inactive mutant that abolishes ability to promote DNA resection and homologous recombination.

description: Catalytic inactive mutant that abolishes ability to promote DNA resection and homologous recombination; when associated with A-54.

description: Catalytic inactive mutant that abolishes ability to promote DNA resection and homologous recombination; when associated with A-18.

description: in Ref. 1; AAD46623

description: in Ref. 1; AAD46623

title: A new spermatogenesis-related gene.

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

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

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

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

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.

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

authors:
Ebert L.
Schick M.
Neubert P.
Schatten R.
Henze S.
Korn B.

title: Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).

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

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 [LARGE SCALE GENOMIC DNA]

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

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

authors:
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] OF 63-245 (ISOFORM 1)

authors:
Yamada M.
Ohnishi J.
Ohkawara B.
Iemura S.
Satoh K.
Hyodo-Miura J.
Kawachi K.
Natsume T.
Shibuya H.

title: NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF).

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.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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 ALA-2

referencePositions: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

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

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Ismail I.H.
Gagne J.P.
Genois M.M.
Strickfaden H.
McDonald D.
Xu Z.
Poirier G.G.
Masson J.Y.
Hendzel M.J.

title: The RNF138 E3 ligase displaces Ku to promote DNA end resection and regulate DNA repair pathway choice.

referencePositions:
FUNCTION
DNA-BINDING
SUBCELLULAR LOCATION
INTERACTION WITH XRCC5
DOMAIN
MUTAGENESIS OF CYS-18 AND CYS-54

authors:
Schmidt C.K.
Galanty Y.
Sczaniecka-Clift M.
Coates J.
Jhujh S.
Demir M.
Cornwell M.
Beli P.
Jackson S.P.

title: Systematic E2 screening reveals a UBE2D-RNF138-CtIP axis promoting DNA repair.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
INTERACTION WITH RBBP8
MUTAGENESIS OF 18-CYS--CYS-21

value: 5 GO annotations based on evolutionary models

value: Antigen processing: Ubiquitination & Proteasome degradation

value: Expressed in primordial germ cell in gonad and 207 other cell types or tissues

value: P:DNA double-strand break processing involved in repair via single-strand annealing

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

value: E3 ubiquitin-protein ligase RNF138 isoform X1

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

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

value: Interacts with LMNA and binds to the farnesylated C-terminal domain

value: Ubiquitous. Predominantly expressed in skeletal muscle, heart and brain

description: Nuclear prelamin A recognition factor

description: Disordered

description: Basic and acidic residues

description: Phosphoserine

description: in isoform 4

description: in isoform 3

description: in isoform 2

description: in Ref. 2; BAG51834

title: Prenylated prelamin A interacts with Narf, a novel nuclear protein.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
SUBCELLULAR LOCATION
TISSUE SPECIFICITY
INTERACTION WITH LMNA

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

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

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

authors:
Zody M.C.
Garber M.
Adams D.J.
Sharpe T.
Harrow J.
Lupski J.R.
Nicholson C.
Searle S.M.
Wilming L.
Young S.K.
Abouelleil A.
Allen N.R.
Bi W.
Bloom T.
Borowsky M.L.
Bugalter B.E.
Butler J.
Chang J.L.
Chen C.-K.
Cook A.
Corum B.
Cuomo C.A.
de Jong P.J.
DeCaprio D.
Dewar K.
FitzGerald M.
Gilbert J.
Gibson R.
Gnerre S.
Goldstein S.
Grafham D.V.
Grocock R.
Hafez N.
Hagopian D.S.
Hart E.
Norman C.H.
Humphray S.
Jaffe D.B.
Jones M.
Kamal M.
Khodiyar V.K.
LaButti K.
Laird G.
Lehoczky J.
Liu X.
Lokyitsang T.
Loveland J.
Lui A.
Macdonald P.
Major J.E.
Matthews L.
Mauceli E.
McCarroll S.A.
Mihalev A.H.
Mudge J.
Nguyen C.
Nicol R.
O'Leary S.B.
Osoegawa K.
Schwartz D.C.
Shaw-Smith C.
Stankiewicz P.
Steward C.
Swarbreck D.
Venkataraman V.
Whittaker C.A.
Yang X.
Zimmer A.R.
Bradley A.
Hubbard T.
Birren B.W.
Rogers J.
Lander E.S.
Nusbaum C.

title: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.

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 [LARGE SCALE GENOMIC DNA]

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 2 AND 3)

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-29

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

value: 2 GO annotations based on evolutionary models

value: Expressed in left testis and 198 other cell types or tissues

value: Cytosolic Fe-S cluster assembly factor NAR1

value: Fe-only Hydrogenase (Larger Subunit), Chain L, domain 3


query: (gene_exact:DTD1) AND (taxonomy_id:9606) AND (reviewed:true)

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

value: Possible ATPase (PubMed:15653697) involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes (PubMed:20065034)

value: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality

name: glycyl-tRNA(Ala) + H2O = tRNA(Ala) + glycine + H(+)

name: a D-aminoacyl-tRNA + H2O = a tRNA + a D-alpha-amino acid + H(+)

value: Homodimer (PubMed:15653697). Interacts with CDC45 and TOPBP1 (PubMed:20065034)

value: Associated with chromatin at some replication origins containing functional DNA-unwinding elements (PubMed:20065034)

value: Expressed in many adult and fetal tissues. Highest levels in testis, ovary, spleen and in adult and fetal brain

value: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids

value: Preferentially phosphorylated in cells arrested early in S phase (PubMed:15653697). Phosphorylation in the C-terminus weakens the interaction with CDC45 (PubMed:20065034)

description: D-aminoacyl-tRNA deacylase 1

description: Disordered

description: Gly-cisPro motif, important for rejection of L-amino acids

description: Basic and acidic residues

description: Basic and acidic residues

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: in Ref. 5; AAH45167

description: in Ref. 1; AAL57046

authors:
Meng X.X.
Chen J.J.
Yang Q.Q.
Wang S.
Chao Y.
Ying K.
Xie Y.
Mao Y.

title: Cloning and identification of a novel cDNA which may be associated with FKBP25.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA]
TISSUE SPECIFICITY

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

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

authors:
Deloukas P.
Matthews L.H.
Ashurst J.L.
Burton J.
Gilbert J.G.R.
Jones M.
Stavrides G.
Almeida J.P.
Babbage A.K.
Bagguley C.L.
Bailey J.
Barlow K.F.
Bates K.N.
Beard L.M.
Beare D.M.
Beasley O.P.
Bird C.P.
Blakey S.E.
Bridgeman A.M.
Brown A.J.
Buck D.
Burrill W.D.
Butler A.P.
Carder C.
Carter N.P.
Chapman J.C.
Clamp M.
Clark G.
Clark L.N.
Clark S.Y.
Clee C.M.
Clegg S.
Cobley V.E.
Collier R.E.
Connor R.E.
Corby N.R.
Coulson A.
Coville G.J.
Deadman R.
Dhami P.D.
Dunn M.
Ellington A.G.
Frankland J.A.
Fraser A.
French L.
Garner P.
Grafham D.V.
Griffiths C.
Griffiths M.N.D.
Gwilliam R.
Hall R.E.
Hammond S.
Harley J.L.
Heath P.D.
Ho S.
Holden J.L.
Howden P.J.
Huckle E.
Hunt A.R.
Hunt S.E.
Jekosch K.
Johnson C.M.
Johnson D.
Kay M.P.
Kimberley A.M.
King A.
Knights A.
Laird G.K.
Lawlor S.
Lehvaeslaiho M.H.
Leversha M.A.
Lloyd C.
Lloyd D.M.
Lovell J.D.
Marsh V.L.
Martin S.L.
McConnachie L.J.
McLay K.
McMurray A.A.
Milne S.A.
Mistry D.
Moore M.J.F.
Mullikin J.C.
Nickerson T.
Oliver K.
Parker A.
Patel R.
Pearce T.A.V.
Peck A.I.
Phillimore B.J.C.T.
Prathalingam S.R.
Plumb R.W.
Ramsay H.
Rice C.M.
Ross M.T.
Scott C.E.
Sehra H.K.
Shownkeen R.
Sims S.
Skuce C.D.
Smith M.L.
Soderlund C.
Steward C.A.
Sulston J.E.
Swann R.M.
Sycamore N.
Taylor R.
Tee L.
Thomas D.W.
Thorpe A.
Tracey A.
Tromans A.C.
Vaudin M.
Wall M.
Wallis J.M.
Whitehead S.L.
Whittaker P.
Willey D.L.
Williams L.
Williams S.A.
Wilming L.
Wray P.W.
Hubbard T.
Durbin R.M.
Bentley D.R.
Beck S.
Rogers J.

title: The DNA sequence and comparative analysis of human chromosome 20.

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 [LARGE SCALE GENOMIC DNA]

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

authors:
Casper J.M.
Kemp M.G.
Ghosh M.
Randall G.M.
Vaillant A.
Leffak M.

title: The c-myc DNA-unwinding element-binding protein modulates the assembly of DNA replication complexes in vitro.

referencePositions:
FUNCTION
PHOSPHORYLATION
SUBUNIT
SUBCELLULAR LOCATION

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.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

title: A quantitative atlas of mitotic phosphorylation.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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-197 AND SER-205

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Chowdhury A.
Liu G.
Kemp M.
Chen X.
Katrangi N.
Myers S.
Ghosh M.
Yao J.
Gao Y.
Bubulya P.
Leffak M.

title: The DNA unwinding element binding protein DUE-B interacts with Cdc45 in preinitiation complex formation.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
PHOSPHORYLATION
INTERACTION WITH CDC45 AND TOPBP1

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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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-197

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

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

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

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

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Kemp M.
Bae B.
Yu J.P.
Ghosh M.
Leffak M.
Nair S.K.

title: Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B.

referencePositions:
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
SUBUNIT
MAGNESIUM-BINDING SITES

value: 3 GO annotations based on evolutionary models

value: Expressed in gingival epithelium and 195 other cell types or tissues


query: (gene_exact:ACAD9) AND (taxonomy_id:9606) AND (reviewed:true)

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

value: Complex I assembly factor ACAD9, mitochondrial

value: Together with NDUFAF1 and ECSIT, forms part of the mitochondrial complex I (MCIA),which is required for the biogenesis of respiratory Complex I (CI) and is therefore crucial for the activation of the oxidative phosphorylation system (PubMed:20816094, PubMed:24158852, PubMed:32320651, PubMed:38086790). ECSIT binding triggers a large conformational change, switching ACAD9 from a fatty acid oxidation (FAO) enzyme to a CI assembly factor (PubMed:38086790). The function in CI assembly is independent of the fatty acid oxidation (FAO) activity of the protein (PubMed:24158852). As FAO enzyme, it catalyzes the first step in mitochondrial FAO, which consists in the proR-proR stereospecific alpha, beta-dehydrogenation of fatty acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, resulting in the formation of trans-2-enoyl-CoA ((2E)-enoyl-CoA) (PubMed:12359260, PubMed:16020546, PubMed:17564966, PubMed:21237683, PubMed:24158852). Its preferred substrates are both saturated and unsaturated long-chain acyl-CoA substrates, with optimum activity toward the latter (PubMed:12359260, PubMed:16020546, PubMed:17564966, PubMed:21237683, PubMed:24158852). In addition, based on its established catalytic mechanism, and combined genetic interaction or mutant phenotype evidence, it is predicted to act also on substrates that have not been tested experimentally but are metabolized by mitochondrial FAO, including long-chain unsaturated fatty acids such as linoleate (9Z,12Z-octadecadienoate), linolenate (9Z,12Z,15Z-octadecatrienoate), and others (PubMed:26474213). Among the different mitochondrial acyl-CoA dehydrogenases, its FAO activity overlaps with that of ACADV and ACADL, but plays a primary role in tissues where it is the main long-chain ACAD expressed, such as the central nervous system (PubMed:16020546, PubMed:17564966, PubMed:24158852, PubMed:25721401, PubMed:26474213). It differs significantly from ACADVL in the use of polyunsaturated substrates in vitro, especially docosahexaenoic acid (which is not primarily used for energy but mainly beta-oxidized in the peroxisomes) (PubMed:16020546, PubMed:17564966)

name: a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]

name: a medium-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]

name: eicosanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]

name: octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: oxidized [electron-transfer flavoprotein] + hexadecanoyl-CoA + H(+) = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: tetradecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-tetradecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: dodecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: decanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]

name: heptadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = trans-2-heptadecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: pentadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-pentadecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: undecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = trans-2-undecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: nonanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-nonenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (11Z)-octadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,11Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (9Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,9Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z)-tetradecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z)-tetradecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z)-dodecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z)-dodecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (9E)-octadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,9E)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (11Z)-eicosenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,11Z)-eicosadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: oxidized [electron-transfer flavoprotein] + (9Z)-octadecenoyl-CoA + H(+) = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z)-tetradecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z)-tetradecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (9Z)-eicosenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,9Z)-eicosadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z)-octadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z)-tetradecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z)-tetradecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z)-octadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (9Z,12Z)-octadecadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,9Z,12Z)-octadecatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z,10Z)-hexadecadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z,10Z)-hexadecatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z,8Z)-tetradecadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z,8Z)-tetradecatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z)-dodecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z)-dodecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z)-decenoyl-CoA(4-) + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z)-decadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (9Z,12Z,15Z)-octadecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,9Z,12Z,15Z)-octadecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z,10Z,13Z)-hexadecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z,10Z,13Z)-hexadecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z,8Z,11Z)-tetradecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z,8Z,11Z)-tetradecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z,9Z)-dodecadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z,9Z)-dodecatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z,7Z)-decadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z,7Z)-decatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z,9Z,12Z)-octadecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z,9Z,12Z)-octadecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z,7Z,10Z)-hexadecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z,7Z,10Z)-hexadecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z,9Z,12Z,15Z)-octadecapentaenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z,7Z,10Z,13Z)-hexadecatetraenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z,7Z,10Z,13Z)-hexadecapentaenoyl-CoA + reduced [electron-transfer flavoprotein]

value: Homodimer (PubMed:16020546). Interacts with NDUFAF1 and ECSIT (PubMed:20816094). Part of the mitochondrial complex I assembly/MCIA complex that comprises at least the core subunits TMEM126B, NDUFAF1, ECSIT and ACAD9 and complement subunits such as COA1 and TMEM186 (PubMed:32320651). Interacts with TMEM70 and TMEM242 (PubMed:33753518)

value: Ubiquitously expressed in most normal human tissues and cancer cell lines with higher levels in heart, skeletal muscles, and the central nervous system (where it is the highest expressed ACAD) (PubMed:12359260, PubMed:17564966). Highly expressed (at protein level) in the cerebellum (Purkinje neurons, dentate nucleus, and in the granular layer), where ACADV is not found (PubMed:17564966, PubMed:21237683)

diseaseId: Mitochondrial complex I deficiency, nuclear type 20

description: An autosomal recessive metabolic disorder associated with mitochondrial complex I deficiency, resulting in multisystemic and variable manifestations. Clinical features include infantile onset of acute metabolic acidosis, Reye-like episodes (brain edema and vomiting that may rapidly progress to seizures, coma and death), exercise intolerance, hypertrophic cardiomyopathy, liver failure, muscle weakness, and neurologic dysfunction.

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

value: Belongs to the acyl-CoA dehydrogenase family

value: Some reactions in this entry are inferred from combined genetic interaction or mutant phenotype evidence and direct experimental evidence in parent reaction

description: Mitochondrion

description: Complex I assembly factor ACAD9, mitochondrial

description: Proton acceptor

description: Phosphothreonine

description: N6-acetyllysine; alternate

description: N6-succinyllysine; alternate

description: in MC1DN20; dbSNP:rs387907041

description: in MC1DN20

description: in MC1DN20; uncertain significance; dbSNP:rs377547811

description: in MC1DN20

description: in MC1DN20; uncertain significance

description: in MC1DN20; dbSNP:rs387907042

description: in MC1DN20

description: in MC1DN20; uncertain significance; dbSNP:rs143383023

description: in MC1DN20; likely benign; dbSNP:rs115532916

description: in MC1DN20; dbSNP:rs1447947184

description: in MC1DN20; uncertain significance; dbSNP:rs149753643

description: in MC1DN20; dbSNP:rs777282696

description: in MC1DN20; dbSNP:rs368949613

description: in MC1DN20; dbSNP:rs139145143

description: in dbSNP:rs4494951

description: in MC1DN20; dbSNP:rs781149699

description: in MC1DN20; dbSNP:rs377022708

description: in MC1DN20

description: Loss of long-chain-acyl-CoA dehydrogenase activity. Does not affect mitochondrial complex I assembly.

description: in Ref. 1; AAL56011

authors:
Zhang J.
Zhang W.
Zou D.
Chen G.
Wan T.
Zhang M.
Cao X.

title: Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA]
FUNCTION
CATALYTIC ACTIVITY
TISSUE SPECIFICITY

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

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

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 [LARGE SCALE GENOMIC DNA]

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

authors:
Ensenauer R.
He M.
Willard J.M.
Goetzman E.S.
Corydon T.J.
Vandahl B.B.
Mohsen A.W.
Isaya G.
Vockley J.

title: Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids.

referencePositions: CLEAVAGE OF TRANSIT PEPTIDE AFTER ARG-37

authors:
He M.
Rutledge S.L.
Kelly D.R.
Palmer C.A.
Murdoch G.
Majumder N.
Nicholls R.D.
Pei Z.
Watkins P.A.
Vockley J.

title: A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency.

referencePositions:
INVOLVEMENT IN MC1DN20
FUNCTION
CATALYTIC ACTIVITY
TISSUE SPECIFICITY

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-41

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Nouws J.
Nijtmans L.
Houten S.M.
van den Brand M.
Huynen M.
Venselaar H.
Hoefs S.
Gloerich J.
Kronick J.
Hutchin T.
Willems P.
Rodenburg R.
Wanders R.
van den Heuvel L.
Smeitink J.
Vogel R.O.

title: Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex I.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
INTERACTION WITH NDUFAF1 AND ECSIT
INVOLVEMENT IN MC1DN20
VARIANTS MC1DN20 LYS-413 AND HIS-518

authors:
Haack T.B.
Danhauser K.
Haberberger B.
Hoser J.
Strecker V.
Boehm D.
Uziel G.
Lamantea E.
Invernizzi F.
Poulton J.
Rolinski B.
Iuso A.
Biskup S.
Schmidt T.
Mewes H.W.
Wittig I.
Meitinger T.
Zeviani M.
Prokisch H.

title: Exome sequencing identifies ACAD9 mutations as a cause of complex I deficiency.

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.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
He M.
Pei Z.
Mohsen A.W.
Watkins P.
Murdoch G.
Van Veldhoven P.P.
Ensenauer R.
Vockley J.

title: Identification and characterization of new long chain acyl-CoA dehydrogenases.

referencePositions:
FUNCTION
CATALYTIC ACTIVITY
TISSUE SPECIFICITY

authors:
Nouws J.
Te Brinke H.
Nijtmans L.G.
Houten S.M.

title: ACAD9, a complex I assembly factor with a moonlighting function in fatty acid oxidation deficiencies.

referencePositions:
FUNCTION
CATALYTIC ACTIVITY
ACTIVE SITE
MUTAGENESIS OF GLU-426

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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Schiff M.
Haberberger B.
Xia C.
Mohsen A.W.
Goetzman E.S.
Wang Y.
Uppala R.
Zhang Y.
Karunanidhi A.
Prabhu D.
Alharbi H.
Prochownik E.V.
Haack T.
Haeberle J.
Munnich A.
Roetig A.
Taylor R.W.
Nicholls R.D.
Kim J.J.
Prokisch H.
Vockley J.

title: Complex I assembly function and fatty acid oxidation enzyme activity of ACAD9 both contribute to disease severity in ACAD9 deficiency.

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.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Houten S.M.
Violante S.
Ventura F.V.
Wanders R.J.

title: The Biochemistry and Physiology of Mitochondrial Fatty Acid beta-Oxidation and Its Genetic Disorders.

referencePositions: REVIEW ON THE PHYSIOLOGICAL ROLE OF THE MITOCHONDRIAL FATTY ACID BETA-OXIDATION

authors:
Formosa L.E.
Muellner-Wong L.
Reljic B.
Sharpe A.J.
Jackson T.D.
Beilharz T.H.
Stojanovski D.
Lazarou M.
Stroud D.A.
Ryan M.T.

title: Dissecting the Roles of Mitochondrial Complex I Intermediate Assembly Complex Factors in the Biogenesis of Complex I.

referencePositions:
IDENTIFICATION IN THE MCIA COMPLEX
FUNCTION

authors:
Carroll J.
He J.
Ding S.
Fearnley I.M.
Walker J.E.

title: TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase and interact with assembly factors for complex I.

authors:
McGregor L.
Acajjaoui S.
Desfosses A.
Saidi M.
Bacia-Verloop M.
Schwarz J.J.
Juyoux P.
von Velsen J.
Bowler M.W.
McCarthy A.A.
Kandiah E.
Gutsche I.
Soler-Lopez M.

title: The assembly of the Mitochondrial Complex I Assembly complex uncovers a redox pathway coordination.

authors:
Fabbian S.
Masciovecchio B.
Schievano E.
Giachin G.

title: Hidden beta-gamma Dehydrogenation Products in Long-Chain Fatty Acid Oxidation Unveiled by NMR: Implications on Lipid Metabolism.

authors:
Gerards M.
van den Bosch B.J.
Danhauser K.
Serre V.
van Weeghel M.
Wanders R.J.
Nicolaes G.A.
Sluiter W.
Schoonderwoerd K.
Scholte H.R.
Prokisch H.
Rotig A.
de Coo I.F.
Smeets H.J.

title: Riboflavin-responsive oxidative phosphorylation complex I deficiency caused by defective ACAD9: new function for an old gene.

referencePositions: VARIANTS MC1DN20 LYS-127; TRP-469 AND TRP-532

authors:
Haack T.B.
Haberberger B.
Frisch E.M.
Wieland T.
Iuso A.
Gorza M.
Strecker V.
Graf E.
Mayr J.A.
Herberg U.
Hennermann J.B.
Klopstock T.
Kuhn K.A.
Ahting U.
Sperl W.
Wilichowski E.
Hoffmann G.F.
Tesarova M.
Hansikova H.
Zeman J.
Plecko B.
Zeviani M.
Wittig I.
Strom T.M.
Schuelke M.
Freisinger P.
Meitinger T.
Prokisch H.

title: Molecular diagnosis in mitochondrial complex I deficiency using exome sequencing.

authors:
Garone C.
Donati M.A.
Sacchini M.
Garcia-Diaz B.
Bruno C.
Calvo S.
Mootha V.K.
Dimauro S.

title: Mitochondrial encephalomyopathy due to a novel mutation in ACAD9.

authors:
Nouws J.
Wibrand F.
van den Brand M.
Venselaar H.
Duno M.
Lund A.M.
Trautner S.
Nijtmans L.
Ostergard E.

title: A patient with complex I deficiency caused by a novel ACAD9 mutation not responding to riboflavin treatment.

authors:
Kohda M.
Tokuzawa Y.
Kishita Y.
Nyuzuki H.
Moriyama Y.
Mizuno Y.
Hirata T.
Yatsuka Y.
Yamashita-Sugahara Y.
Nakachi Y.
Kato H.
Okuda A.
Tamaru S.
Borna N.N.
Banshoya K.
Aigaki T.
Sato-Miyata Y.
Ohnuma K.
Suzuki T.
Nagao A.
Maehata H.
Matsuda F.
Higasa K.
Nagasaki M.
Yasuda J.
Yamamoto M.
Fushimi T.
Shimura M.
Kaiho-Ichimoto K.
Harashima H.
Yamazaki T.
Mori M.
Murayama K.
Ohtake A.
Okazaki Y.

title: A comprehensive genomic analysis reveals the genetic landscape of mitochondrial respiratory chain complex deficiencies.

referencePositions: VARIANTS MC1DN20 GLY-271; MET-384 AND HIS-606

value: Mitochondrial complex I intermediate assembly (MCIA) complex

value: 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (3 sites)

value: 1 GO annotation based on evolutionary models

value: Expressed in upper arm skin and 178 other cell types or tissues

value: C:mitochondrial complex I intermediate assembly complex

value: F:long-chain fatty acyl-CoA dehydrogenase activity

value: F:medium-chain fatty acyl-CoA dehydrogenase activity

value: F:very-long-chain fatty acyl-CoA dehydrogenase activity

value: P:long-chain fatty acid metabolic process

value: P:medium-chain fatty acid metabolic process

value: P:mitochondrial respiratory chain complex I assembly

value: acyl-CoA dehydrogenase family member 9, mitochondrial

value: very long-chain specific acyl-CoA dehydrogenase, mitochondrial

value: Very long-chain-specific acyl-CoA dehydrogenase, mitochondrial

value: Acyl-CoA dehydrogenase/oxidase, N-terminal domain

value: Butyryl-CoA Dehydrogenase, subunit A, domain 2

value: Butyryl-CoA Dehydrogenase, subunit A, domain 3

value: COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL

value: Acyl-CoA dehydrogenase C-terminal domain-like


query: (gene_exact:RHOJ) AND (taxonomy_id:9606) AND (reviewed:true)

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

value: Plasma membrane-associated small GTPase specifically involved in angiogenesis (PubMed:21628409, PubMed:24434213, PubMed:30158707). Required for endothelial cell migration during vascular development via its interaction with GLUL (PubMed:30158707). Elicits the formation of F-actin-rich structures, thereby regulating endothelial cell migration (PubMed:30158707)

value: Interacts with the CRIB domains of proteins such as Pak1 and Was/Wasp (By similarity). Interacts with GLUL (PubMed:30158707)

value: Localization to the plasma membrane is regulated by GLUL

value: Specifically expressed in endothelial cells in different tissues, such as brain, heart, lung and liver

value: Expression is regulated by the transcription factor ERG

value: Palmitoylated; regulates localization to the plasma membrane and may be mediated by GLUL

value: Could be created by usage of an unusual splicing donor site

value: Belongs to the small GTPase superfamily. Rho family

description: Rho-related GTP-binding protein RhoJ

description: Removed in mature form

description: Effector region

description: Cysteine methyl ester

description: S-palmitoyl cysteine

description: S-palmitoyl cysteine

description: S-farnesyl cysteine

description: in isoform 2

description: Impaired localization to the plasma membrane.

description: Impaired localization to the plasma membrane.

description: Impaired localization to the plasma membrane.

description: Does not affect localization to the plasma membrane.

description: Impaired localization to the plasma membrane.

description: Causes constitutive activation.

description: Dominant negative mutant.

description: Causes constitutive activation.

description: in Ref. 3; BAB55013

authors:
Vignal E.
De Toledo M.
Comunale F.
Ladopoulou A.
Gauthier-Rouviere C.
Blangy A.
Fort P.

title: Characterization of TCL, a new GTPase of the Rho family related to TC10 and Cdc42.

authors:
Allen M.
Halford S.
Daniels H.
McIntosh B.
Kanuga N.
Greenwood J.
Carey A.H.
Adamson P.

title: A novel Rho GTPase (RhoI) induces loss of stress-fibers and results in apical actin reorganization.

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

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

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

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

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

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

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

authors:
Yuan L.
Sacharidou A.
Stratman A.N.
Le Bras A.
Zwiers P.J.
Spokes K.
Bhasin M.
Shih S.C.
Nagy J.A.
Molema G.
Aird W.C.
Davis G.E.
Oettgen P.

title: RhoJ is an endothelial cell-restricted Rho GTPase that mediates vascular morphogenesis and is regulated by the transcription factor ERG.

authors:
Kim C.
Yang H.
Fukushima Y.
Saw P.E.
Lee J.
Park J.S.
Park I.
Jung J.
Kataoka H.
Lee D.
Heo W.D.
Kim I.
Jon S.
Adams R.H.
Nishikawa S.
Uemura A.
Koh G.Y.

title: Vascular RhoJ is an effective and selective target for tumor angiogenesis and vascular disruption.

authors:
Ackermann K.L.
Florke R.R.
Reyes S.S.
Tader B.R.
Hamann M.J.

title: TCL/RhoJ plasma membrane localization and nucleotide exchange is coordinately regulated by amino acids within the n terminus and a distal loop region.

referencePositions: MUTAGENESIS OF 17-ASP--LYS-20; 17-ASP-ASP-18; 19-LYS-LYS-20; GLY-30; THR-35 AND GLN-79

authors:
Eelen G.
Dubois C.
Cantelmo A.R.
Goveia J.
Bruening U.
DeRan M.
Jarugumilli G.
van Rijssel J.
Saladino G.
Comitani F.
Zecchin A.
Rocha S.
Chen R.
Huang H.
Vandekeere S.
Kalucka J.
Lange C.
Morales-Rodriguez F.
Cruys B.
Treps L.
Ramer L.
Vinckier S.
Brepoels K.
Wyns S.
Souffreau J.
Schoonjans L.
Lamers W.H.
Wu Y.
Haustraete J.
Hofkens J.
Liekens S.
Cubbon R.
Ghesquiere B.
Dewerchin M.
Gervasio F.L.
Li X.
van Buul J.D.
Wu X.
Carmeliet P.

title: Role of glutamine synthetase in angiogenesis beyond glutamine synthesis.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
PALMITOYLATION AT CYS-3 AND CYS-11
MUTAGENESIS OF CYS-3 AND CYS-11

value: 8 GO annotations based on evolutionary models

value: Expressed in tendon of biceps brachii and 162 other cell types or tissues

value: P:positive regulation of cell migration involved in sprouting angiogenesis

value: P:regulation of endothelial cell migration

value: P:small GTPase-mediated signal transduction

value: P-loop containing nucleotide triphosphate hydrolases

value: P-loop containing nucleoside triphosphate hydrolases


query: (gene_exact:Spcs2) AND (taxonomy_id:10090) AND (reviewed:true)

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus

value: Microsomal signal peptidase 25 kDa subunit

value: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity)

value: Component of the signal peptidase complex paralog A (SPC-A) composed of a catalytic subunit SEC11A and three accessory subunits SPCS1, SPCS2 and SPCS3. Component of the signal peptidase complex paralog C (SPC-C) composed of a catalytic subunit SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3. Within the complex, interacts with SEC11A or SEC11C and SPCS1. The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids

description: Removed

description: Signal peptidase complex subunit 2

description: Cytoplasmic

description: Helical

description: Lumenal

description: Helical

description: Cytoplasmic

description: Disordered

description: Gly residues

description: N-acetylalanine

description: in Ref. 2; AAH50150

description: in Ref. 1; BAB29262

authors:
Carninci P.
Kasukawa T.
Katayama S.
Gough J.
Frith M.C.
Maeda N.
Oyama R.
Ravasi T.
Lenhard B.
Wells C.
Kodzius R.
Shimokawa K.
Bajic V.B.
Brenner S.E.
Batalov S.
Forrest A.R.
Zavolan M.
Davis M.J.
Wilming L.G.
Aidinis V.
Allen J.E.
Ambesi-Impiombato A.
Apweiler R.
Aturaliya R.N.
Bailey T.L.
Bansal M.
Baxter L.
Beisel K.W.
Bersano T.
Bono H.
Chalk A.M.
Chiu K.P.
Choudhary V.
Christoffels A.
Clutterbuck D.R.
Crowe M.L.
Dalla E.
Dalrymple B.P.
de Bono B.
Della Gatta G.
di Bernardo D.
Down T.
Engstrom P.
Fagiolini M.
Faulkner G.
Fletcher C.F.
Fukushima T.
Furuno M.
Futaki S.
Gariboldi M.
Georgii-Hemming P.
Gingeras T.R.
Gojobori T.
Green R.E.
Gustincich S.
Harbers M.
Hayashi Y.
Hensch T.K.
Hirokawa N.
Hill D.
Huminiecki L.
Iacono M.
Ikeo K.
Iwama A.
Ishikawa T.
Jakt M.
Kanapin A.
Katoh M.
Kawasawa Y.
Kelso J.
Kitamura H.
Kitano H.
Kollias G.
Krishnan S.P.
Kruger A.
Kummerfeld S.K.
Kurochkin I.V.
Lareau L.F.
Lazarevic D.
Lipovich L.
Liu J.
Liuni S.
McWilliam S.
Madan Babu M.
Madera M.
Marchionni L.
Matsuda H.
Matsuzawa S.
Miki H.
Mignone F.
Miyake S.
Morris K.
Mottagui-Tabar S.
Mulder N.
Nakano N.
Nakauchi H.
Ng P.
Nilsson R.
Nishiguchi S.
Nishikawa S.
Nori F.
Ohara O.
Okazaki Y.
Orlando V.
Pang K.C.
Pavan W.J.
Pavesi G.
Pesole G.
Petrovsky N.
Piazza S.
Reed J.
Reid J.F.
Ring B.Z.
Ringwald M.
Rost B.
Ruan Y.
Salzberg S.L.
Sandelin A.
Schneider C.
Schoenbach C.
Sekiguchi K.
Semple C.A.
Seno S.
Sessa L.
Sheng Y.
Shibata Y.
Shimada H.
Shimada K.
Silva D.
Sinclair B.
Sperling S.
Stupka E.
Sugiura K.
Sultana R.
Takenaka Y.
Taki K.
Tammoja K.
Tan S.L.
Tang S.
Taylor M.S.
Tegner J.
Teichmann S.A.
Ueda H.R.
van Nimwegen E.
Verardo R.
Wei C.L.
Yagi K.
Yamanishi H.
Zabarovsky E.
Zhu S.
Zimmer A.
Hide W.
Bult C.
Grimmond S.M.
Teasdale R.D.
Liu E.T.
Brusic V.
Quackenbush J.
Wahlestedt C.
Mattick J.S.
Hume D.A.
Kai C.
Sasaki D.
Tomaru Y.
Fukuda S.
Kanamori-Katayama M.
Suzuki M.
Aoki J.
Arakawa T.
Iida J.
Imamura K.
Itoh M.
Kato T.
Kawaji H.
Kawagashira N.
Kawashima T.
Kojima M.
Kondo S.
Konno H.
Nakano K.
Ninomiya N.
Nishio T.
Okada M.
Plessy C.
Shibata K.
Shiraki T.
Suzuki S.
Tagami M.
Waki K.
Watahiki A.
Okamura-Oho Y.
Suzuki H.
Kawai J.
Hayashizaki Y.

title: The transcriptional landscape of the mammalian genome.

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

authors:
Trinidad J.C.
Specht C.G.
Thalhammer A.
Schoepfer R.
Burlingame A.L.

title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.

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

referencePositions: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Huttlin E.L.
Jedrychowski M.P.
Elias J.E.
Goswami T.
Rad R.
Beausoleil S.A.
Villen J.
Haas W.
Sowa M.E.
Gygi S.P.

title: A tissue-specific atlas of mouse protein phosphorylation and expression.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

value: Synthesis, secretion, and deacylation of Ghrelin

value: Regulation of CDH1 posttranslational processing and trafficking to plasma membrane

value: Expressed in lacrimal gland and 260 other cell types or tissues

value: MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT


query: (gene_exact:Sdhaf2) AND (taxonomy_id:10090) AND (reviewed:true)

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus

value: Succinate dehydrogenase assembly factor 2, mitochondrial

value: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SDHA of the SDH catalytic dimer

value: Interacts with SDHA within the SDH catalytic dimer

description: Mitochondrion

description: Succinate dehydrogenase assembly factor 2, mitochondrial

description: in isoform 3

description: in isoform 2

description: in Ref. 1; BAB28863

authors:
Carninci P.
Kasukawa T.
Katayama S.
Gough J.
Frith M.C.
Maeda N.
Oyama R.
Ravasi T.
Lenhard B.
Wells C.
Kodzius R.
Shimokawa K.
Bajic V.B.
Brenner S.E.
Batalov S.
Forrest A.R.
Zavolan M.
Davis M.J.
Wilming L.G.
Aidinis V.
Allen J.E.
Ambesi-Impiombato A.
Apweiler R.
Aturaliya R.N.
Bailey T.L.
Bansal M.
Baxter L.
Beisel K.W.
Bersano T.
Bono H.
Chalk A.M.
Chiu K.P.
Choudhary V.
Christoffels A.
Clutterbuck D.R.
Crowe M.L.
Dalla E.
Dalrymple B.P.
de Bono B.
Della Gatta G.
di Bernardo D.
Down T.
Engstrom P.
Fagiolini M.
Faulkner G.
Fletcher C.F.
Fukushima T.
Furuno M.
Futaki S.
Gariboldi M.
Georgii-Hemming P.
Gingeras T.R.
Gojobori T.
Green R.E.
Gustincich S.
Harbers M.
Hayashi Y.
Hensch T.K.
Hirokawa N.
Hill D.
Huminiecki L.
Iacono M.
Ikeo K.
Iwama A.
Ishikawa T.
Jakt M.
Kanapin A.
Katoh M.
Kawasawa Y.
Kelso J.
Kitamura H.
Kitano H.
Kollias G.
Krishnan S.P.
Kruger A.
Kummerfeld S.K.
Kurochkin I.V.
Lareau L.F.
Lazarevic D.
Lipovich L.
Liu J.
Liuni S.
McWilliam S.
Madan Babu M.
Madera M.
Marchionni L.
Matsuda H.
Matsuzawa S.
Miki H.
Mignone F.
Miyake S.
Morris K.
Mottagui-Tabar S.
Mulder N.
Nakano N.
Nakauchi H.
Ng P.
Nilsson R.
Nishiguchi S.
Nishikawa S.
Nori F.
Ohara O.
Okazaki Y.
Orlando V.
Pang K.C.
Pavan W.J.
Pavesi G.
Pesole G.
Petrovsky N.
Piazza S.
Reed J.
Reid J.F.
Ring B.Z.
Ringwald M.
Rost B.
Ruan Y.
Salzberg S.L.
Sandelin A.
Schneider C.
Schoenbach C.
Sekiguchi K.
Semple C.A.
Seno S.
Sessa L.
Sheng Y.
Shibata Y.
Shimada H.
Shimada K.
Silva D.
Sinclair B.
Sperling S.
Stupka E.
Sugiura K.
Sultana R.
Takenaka Y.
Taki K.
Tammoja K.
Tan S.L.
Tang S.
Taylor M.S.
Tegner J.
Teichmann S.A.
Ueda H.R.
van Nimwegen E.
Verardo R.
Wei C.L.
Yagi K.
Yamanishi H.
Zabarovsky E.
Zhu S.
Zimmer A.
Hide W.
Bult C.
Grimmond S.M.
Teasdale R.D.
Liu E.T.
Brusic V.
Quackenbush J.
Wahlestedt C.
Mattick J.S.
Hume D.A.
Kai C.
Sasaki D.
Tomaru Y.
Fukuda S.
Kanamori-Katayama M.
Suzuki M.
Aoki J.
Arakawa T.
Iida J.
Imamura K.
Itoh M.
Kato T.
Kawaji H.
Kawagashira N.
Kawashima T.
Kojima M.
Kondo S.
Konno H.
Nakano K.
Ninomiya N.
Nishio T.
Okada M.
Plessy C.
Shibata K.
Shiraki T.
Suzuki S.
Tagami M.
Waki K.
Watahiki A.
Okamura-Oho Y.
Suzuki H.
Kawai J.
Hayashizaki Y.

title: The transcriptional landscape of the mammalian genome.

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

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; 2 AND 3)

authors:
Huttlin E.L.
Jedrychowski M.P.
Elias J.E.
Goswami T.
Rad R.
Beausoleil S.A.
Villen J.
Haas W.
Sowa M.E.
Gygi S.P.

title: A tissue-specific atlas of mouse protein phosphorylation and expression.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

value: Maturation of TCA enzymes and regulation of TCA cycle

value: Expressed in otic placode and 261 other cell types or tissues

value: P:mitochondrial electron transport, succinate to ubiquinone

value: P:mitochondrial respiratory chain complex II assembly

value: P:negative regulation of canonical Wnt signaling pathway

value: P:negative regulation of epithelial to mesenchymal transition

value: Succinate dehydrogenase assembly factor 2, mitochondrial

value: SUCCINATE DEHYDROGENASE ASSEMBLY FACTOR 2, MITOCHONDRIAL


query: (gene_exact:Vmn2r73) AND (taxonomy_id:10090) AND (reviewed:true)


query: (gene_exact:Pnkd) AND (taxonomy_id:10116) AND (reviewed:true)


query: (gene_exact:Mtmr12) AND (taxonomy_id:10116) AND (reviewed:true)

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Rattus

value: Inactive phosphatidylinositol 3-phosphatase 12

value: Acts as an adapter for the myotubularin-related phosphatases. Regulates phosphatase MTM1 protein stability and possibly its intracellular location. By stabilizing MTM1 protein levels, required for skeletal muscle maintenance but not for myogenesis

value: Heterodimer with lipid phosphatase MTM1 (By similarity). Heterodimer with lipid phosphatase MTMR2 (By similarity)

value: Localizes to punctate vesicles when associated with MTM1 (By similarity). Localizes to triads, a structure formed by a T tubule and two sarcoplasmic reticulum terminal cisterna. In skeletal muscles, co-localizes with MTM1 in the sarcomere. Partially localizes to the sarcoplasmic reticulum in skeletal muscles (By similarity)

value: Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily

value: Although it belongs to the non-receptor class myotubularin subfamily, lacks the conserved active site cysteine residue at position 392 in the dsPTPase catalytic loop and does not have phosphatase activity

description: Myotubularin-related protein 12

description: Myotubularin phosphatase

description: Interaction with MTM1

description: Disordered

description: Basic residues

description: Polar residues

description: Phosphoserine

description: Phosphoserine

description: in isoform 2

description: in isoform 2

authors:
Gibbs R.A.
Weinstock G.M.
Metzker M.L.
Muzny D.M.
Sodergren E.J.
Scherer S.
Scott G.
Steffen D.
Worley K.C.
Burch P.E.
Okwuonu G.
Hines S.
Lewis L.
Deramo C.
Delgado O.
Dugan-Rocha S.
Miner G.
Morgan M.
Hawes A.
Gill R.
Holt R.A.
Adams M.D.
Amanatides P.G.
Baden-Tillson H.
Barnstead M.
Chin S.
Evans C.A.
Ferriera S.
Fosler C.
Glodek A.
Gu Z.
Jennings D.
Kraft C.L.
Nguyen T.
Pfannkoch C.M.
Sitter C.
Sutton G.G.
Venter J.C.
Woodage T.
Smith D.
Lee H.-M.
Gustafson E.
Cahill P.
Kana A.
Doucette-Stamm L.
Weinstock K.
Fechtel K.
Weiss R.B.
Dunn D.M.
Green E.D.
Blakesley R.W.
Bouffard G.G.
De Jong P.J.
Osoegawa K.
Zhu B.
Marra M.
Schein J.
Bosdet I.
Fjell C.
Jones S.
Krzywinski M.
Mathewson C.
Siddiqui A.
Wye N.
McPherson J.
Zhao S.
Fraser C.M.
Shetty J.
Shatsman S.
Geer K.
Chen Y.
Abramzon S.
Nierman W.C.
Havlak P.H.
Chen R.
Durbin K.J.
Egan A.
Ren Y.
Song X.-Z.
Li B.
Liu Y.
Qin X.
Cawley S.
Cooney A.J.
D'Souza L.M.
Martin K.
Wu J.Q.
Gonzalez-Garay M.L.
Jackson A.R.
Kalafus K.J.
McLeod M.P.
Milosavljevic A.
Virk D.
Volkov A.
Wheeler D.A.
Zhang Z.
Bailey J.A.
Eichler E.E.
Tuzun E.
Birney E.
Mongin E.
Ureta-Vidal A.
Woodwark C.
Zdobnov E.
Bork P.
Suyama M.
Torrents D.
Alexandersson M.
Trask B.J.
Young J.M.
Huang H.
Wang H.
Xing H.
Daniels S.
Gietzen D.
Schmidt J.
Stevens K.
Vitt U.
Wingrove J.
Camara F.
Mar Alba M.
Abril J.F.
Guigo R.
Smit A.
Dubchak I.
Rubin E.M.
Couronne O.
Poliakov A.
Huebner N.
Ganten D.
Goesele C.
Hummel O.
Kreitler T.
Lee Y.-A.
Monti J.
Schulz H.
Zimdahl H.
Himmelbauer H.
Lehrach H.
Jacob H.J.
Bromberg S.
Gullings-Handley J.
Jensen-Seaman M.I.
Kwitek A.E.
Lazar J.
Pasko D.
Tonellato P.J.
Twigger S.
Ponting C.P.
Duarte J.M.
Rice S.
Goodstadt L.
Beatson S.A.
Emes R.D.
Winter E.E.
Webber C.
Brandt P.
Nyakatura G.
Adetobi M.
Chiaromonte F.
Elnitski L.
Eswara P.
Hardison R.C.
Hou M.
Kolbe D.
Makova K.
Miller W.
Nekrutenko A.
Riemer C.
Schwartz S.
Taylor J.
Yang S.
Zhang Y.
Lindpaintner K.
Andrews T.D.
Caccamo M.
Clamp M.
Clarke L.
Curwen V.
Durbin R.M.
Eyras E.
Searle S.M.
Cooper G.M.
Batzoglou S.
Brudno M.
Sidow A.
Stone E.A.
Payseur B.A.
Bourque G.
Lopez-Otin C.
Puente X.S.
Chakrabarti K.
Chatterji S.
Dewey C.
Pachter L.
Bray N.
Yap V.B.
Caspi A.
Tesler G.
Pevzner P.A.
Haussler D.
Roskin K.M.
Baertsch R.
Clawson H.
Furey T.S.
Hinrichs A.S.
Karolchik D.
Kent W.J.
Rosenbloom K.R.
Trumbower H.
Weirauch M.
Cooper D.N.
Stenson P.D.
Ma B.
Brent M.
Arumugam M.
Shteynberg D.
Copley R.R.
Taylor M.S.
Riethman H.
Mudunuri U.
Peterson J.
Guyer M.
Felsenfeld A.
Old S.
Mockrin S.
Collins F.S.

title: Genome sequence of the Brown Norway rat yields insights into mammalian evolution.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

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

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

authors:
Lundby A.
Secher A.
Lage K.
Nordsborg N.B.
Dmytriyev A.
Lundby C.
Olsen J.V.

title: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

value: Synthesis of PIPs at the early endosome membrane

value: Expressed in lung and 18 other cell types or tissues

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

value: (Phosphotyrosine protein) phosphatases II


query: (gene_exact:Ptk7) AND (taxonomy_id:10116) AND (reviewed:true)


query: (gene_exact:dpm-1) AND (taxonomy_id:6239) AND (reviewed:true)


query: (gene_exact:wdr-23) AND (taxonomy_id:6239) AND (reviewed:true)

lineage: Eukaryota Metazoa Ecdysozoa Nematoda Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis

value: DDB1- and CUL4-associated factor 11 homolog

value: Involved in regulation of lifespan (PubMed:17411345). Required for dopaminergic CEP neuron degeneration in response to Mn(2+) (PubMed:23721876). Inhibits the skn-1-mediated up-regulation of tatn-1 (PubMed:31043480)

value: Increased lifespan (PubMed:17411345). RNAi-mediated knockdown significantly prevents Mn(2+)-induced dopaminergic CEP neuron degeneration (PubMed:23721876). RNAi-mediated knockdown increases tatn-1 expression and enzymatic activity (PubMed:31043480)

description: DDB1- and CUL4-associated factor 11 homolog

description: WD 1

description: WD 2

description: WD 3

description: WD 4

description: WD 5

description: WD 6

description: Disordered

description: Acidic residues

description: in isoform b

description: in isoform b

title: Genome sequence of the nematode C. elegans: a platform for investigating biology.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

title: Lifespan regulation by evolutionarily conserved genes essential for viability.

authors:
Settivari R.
VanDuyn N.
LeVora J.
Nass R.

title: The Nrf2/SKN-1-dependent glutathione S-transferase pi homologue GST-1 inhibits dopamine neuron degeneration in a Caenorhabditis elegans model of manganism.

authors:
Ipson B.R.
Green R.A.
Wilson J.T.
Watson J.N.
Faull K.F.
Fisher A.L.

title: Tyrosine aminotransferase is involved in the oxidative stress response by metabolizing meta-tyrosine in Caenorhabditis elegans.

value: Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues

value: F:RNA polymerase II-specific DNA-binding transcription factor binding

value: P:negative regulation of cellular response to manganese ion

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

value: P:positive regulation of multicellular organism growth

value: P:proteasome-mediated ubiquitin-dependent protein catabolic process

value: P:regulation of cellular response to stress

value: DDB1-and CUL4-associated factor 11 homolog

value: DDB1-and CUL4-associated factor 11 homolog

value: YVTN repeat-like/Quinoprotein amine dehydrogenase


query: (gene_exact:FTSH12) AND (taxonomy_id:3702) AND (reviewed:true)

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

value: ATP-dependent zinc metalloprotease FTSH 12, chloroplastic

value: Probable ATP-dependent zinc metallopeptidase

value: In the N-terminal section; belongs to the AAA ATPase family

value: In the C-terminal section; belongs to the peptidase M41 family

description: Chloroplast

description: Thylakoid

description: ATP-dependent zinc metalloprotease FTSH 12, chloroplastic

description: Helical

description: Helical

authors:
Theologis A.
Ecker J.R.
Palm C.J.
Federspiel N.A.
Kaul S.
White O.
Alonso J.
Altafi H.
Araujo R.
Bowman C.L.
Brooks S.Y.
Buehler E.
Chan A.
Chao Q.
Chen H.
Cheuk R.F.
Chin C.W.
Chung M.K.
Conn L.
Conway A.B.
Conway A.R.
Creasy T.H.
Dewar K.
Dunn P.
Etgu P.
Feldblyum T.V.
Feng J.-D.
Fong B.
Fujii C.Y.
Gill J.E.
Goldsmith A.D.
Haas B.
Hansen N.F.
Hughes B.
Huizar L.
Hunter J.L.
Jenkins J.
Johnson-Hopson C.
Khan S.
Khaykin E.
Kim C.J.
Koo H.L.
Kremenetskaia I.
Kurtz D.B.
Kwan A.
Lam B.
Langin-Hooper S.
Lee A.
Lee J.M.
Lenz C.A.
Li J.H.
Li Y.-P.
Lin X.
Liu S.X.
Liu Z.A.
Luros J.S.
Maiti R.
Marziali A.
Militscher J.
Miranda M.
Nguyen M.
Nierman W.C.
Osborne B.I.
Pai G.
Peterson J.
Pham P.K.
Rizzo M.
Rooney T.
Rowley D.
Sakano H.
Salzberg S.L.
Schwartz J.R.
Shinn P.
Southwick A.M.
Sun H.
Tallon L.J.
Tambunga G.
Toriumi M.J.
Town C.D.
Utterback T.
Van Aken S.
Vaysberg M.
Vysotskaia V.S.
Walker M.
Wu D.
Yu G.
Fraser C.M.
Venter J.C.
Davis R.W.

title: Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

authors:
Cheng C.Y.
Krishnakumar V.
Chan A.P.
Thibaud-Nissen F.
Schobel S.
Town C.D.

title: Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.

authoringGroup: The Arabidopsis Information Resource (TAIR)

title: Community-consensus reference genome of Arabidopsis thaliana Col-0.

authors:
Yamada K.
Lim J.
Dale J.M.
Chen H.
Shinn P.
Palm C.J.
Southwick A.M.
Wu H.C.
Kim C.J.
Nguyen M.
Pham P.K.
Cheuk R.F.
Karlin-Newmann G.
Liu S.X.
Lam B.
Sakano H.
Wu T.
Yu G.
Miranda M.
Quach H.L.
Tripp M.
Chang C.H.
Lee J.M.
Toriumi M.J.
Chan M.M.
Tang C.C.
Onodera C.S.
Deng J.M.
Akiyama K.
Ansari Y.
Arakawa T.
Banh J.
Banno F.
Bowser L.
Brooks S.Y.
Carninci P.
Chao Q.
Choy N.
Enju A.
Goldsmith A.D.
Gurjal M.
Hansen N.F.
Hayashizaki Y.
Johnson-Hopson C.
Hsuan V.W.
Iida K.
Karnes M.
Khan S.
Koesema E.
Ishida J.
Jiang P.X.
Jones T.
Kawai J.
Kamiya A.
Meyers C.
Nakajima M.
Narusaka M.
Seki M.
Sakurai T.
Satou M.
Tamse R.
Vaysberg M.
Wallender E.K.
Wong C.
Yamamura Y.
Yuan S.
Shinozaki K.
Davis R.W.
Theologis A.
Ecker J.R.

title: Empirical analysis of transcriptional activity in the Arabidopsis genome.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 363-1008

authors:
Sakamoto W.
Zaltsman A.
Adam Z.
Takahashi Y.

title: Coordinated regulation and complex formation of yellow variegated1 and yellow variegated2, chloroplastic FtsH metalloproteases involved in the repair cycle of photosystem II in Arabidopsis thylakoid membranes.

authors:
Sinvany-Villalobo G.
Davydov O.
Ben-Ari G.
Zaltsman A.
Raskind A.
Adam Z.

title: Expression in multigene families. Analysis of chloroplast and mitochondrial proteases.

title: The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes.

value: F:chloroplast protein-transporting ATPase activity

value: P:protein import into chloroplast stroma

value: ATP-dependent zinc metalloprotease FTSH 12, chloroplastic

value: ATP-dependent zinc metalloprotease FTSH 12, chloroplastic

value: ATP-dependent zinc metalloprotease FTSH 12, chloroplastic

value: P-loop containing nucleotide triphosphate hydrolases

value: ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 12, CHLOROPLASTIC

value: P-loop containing nucleoside triphosphate hydrolases


query: (gene_exact:DRS1) AND (taxonomy_id:3702) AND (reviewed:true)


query: (gene_exact:dcxr) AND (taxonomy_id:7955) AND (reviewed:true)


query: (gene_exact:hes6) AND (taxonomy_id:7955) AND (reviewed:true)


query: (gene_exact:uap1.S) AND (taxonomy_id:8355) AND (reviewed:true)