Full text data of UBE2V1
UBE2V1
(CROC1, UBE2V, UEV1)
[Confidence: high (present in two of the MS resources)]
Ubiquitin-conjugating enzyme E2 variant 1; UEV-1 (CROC-1; TRAF6-regulated IKK activator 1 beta Uev1A)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-conjugating enzyme E2 variant 1; UEV-1 (CROC-1; TRAF6-regulated IKK activator 1 beta Uev1A)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00019599
IPI00019599 Splice Isoform 1 Of Ubiquitin-conjugating enzyme E2 variant 1 Has no ubiquitin ligase activity on its own. The UBE2V1/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic variant 1 or variant 2 found at its expected molecular weight found at molecular weight
IPI00019599 Splice Isoform 1 Of Ubiquitin-conjugating enzyme E2 variant 1 Has no ubiquitin ligase activity on its own. The UBE2V1/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic variant 1 or variant 2 found at its expected molecular weight found at molecular weight
UniProt
Q13404
ID UB2V1_HUMAN Reviewed; 147 AA.
AC Q13404; E1P629; Q13403; Q13532; Q5TGE0; Q5TGE3; Q96H34; Q9GZT0;
read moreAC Q9GZW1; Q9H4J3; Q9H4J4; Q9UKL1; Q9UM48; Q9UM49; Q9UM50;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 139.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 1;
DE Short=UEV-1;
DE AltName: Full=CROC-1;
DE AltName: Full=TRAF6-regulated IKK activator 1 beta Uev1A;
GN Name=UBE2V1; Synonyms=CROC1, UBE2V, UEV1; ORFNames=P/OKcl.19;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9305758; DOI=10.1016/S0378-1119(97)00097-8;
RA Rothofsky M.L., Lin S.L.;
RT "CROC-1 encodes a protein which mediates transcriptional activation of
RT the human FOS promoter.";
RL Gene 195:141-149(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION, INDUCTION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Colon adenocarcinoma;
RX PubMed=9418904;
RA Sancho E., Vila M.R., Sanchez-Pulido L., Lozano J.J., Paciucci R.,
RA Nadal M., Fox M., Harvey C., Bercovich B., Loukili N., Ciechanover A.,
RA Lin S.L., Sanz F., Estivill X., Valencia A., Thomson T.M.;
RT "Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating
RT enzymes, in in vitro differentiation and cell cycle behavior of HT-29-
RT M6 intestinal mucosecretory cells.";
RL Mol. Cell. Biol. 18:576-589(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH
RP TRAF6 AND UBE2N, AND MASS SPECTROMETRY.
RX PubMed=11057907; DOI=10.1016/S0092-8674(00)00126-4;
RA Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C.,
RA Pickart C., Chen Z.J.;
RT "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric
RT ubiquitin-conjugating enzyme complex and a unique polyubiquitin
RT chain.";
RL Cell 103:351-361(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 2-13 (ISOFORM 3), CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung fibroblast;
RA Bienvenut W.V., Pchelintsev N., Adams P.D.;
RL Submitted (JUL-2009) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-147 (ISOFORMS 1 AND 3).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP FUNCTION.
RX PubMed=9580084; DOI=10.1016/S0014-5793(98)00060-X;
RA Thomson T.M., Khalid H., Lozano J.J., Sancho E., Arino J.;
RT "Role of UEV-1A, a homologue of the tumor suppressor protein TSG101,
RT in protection from DNA damage.";
RL FEBS Lett. 423:49-52(1998).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9705497; DOI=10.1093/nar/26.17.3908;
RA Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.-F.;
RT "The products of the yeast MMS2 and two human homologs (hMMS2 and
RT CROC-1) define a structurally and functionally conserved Ubc-like
RT protein family.";
RL Nucleic Acids Res. 26:3908-3914(1998).
RN [12]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION OF TMEM189-UBE2V1 FUSION
RP PROTEIN.
RC TISSUE=Colon cancer;
RX PubMed=11076860; DOI=10.1101/gr.GR-1405R;
RA Thomson T.M., Lozano J.J., Loukili N., Carrio R., Serras F.,
RA Cormand B., Valeri M., Diaz V.M., Abril J., Burset M., Merino J.,
RA Macaya A., Corominas M., Guigo R.;
RT "Fusion of the human gene for the polyubiquitination coeffector UEV1
RT with Kua, a newly identified gene.";
RL Genome Res. 10:1743-1756(2000).
RN [13]
RP FUNCTION.
RX PubMed=20061386; DOI=10.1074/jbc.M109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [14]
RP FUNCTION.
RX PubMed=21512573; DOI=10.1038/nature09976;
RA Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J.,
RA Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A.,
RA Albert M.L., Strambio-De-Castillia C., Mothes W., Pizzato M.,
RA Gruetter M.G., Luban J.;
RT "TRIM5 is an innate immune sensor for the retrovirus capsid lattice.";
RL Nature 472:361-365(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 8-147 IN COMPLEX WITH STUB1
RP AND UBE2N.
RX PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
RA Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
RA Pearl L.H.;
RT "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
RT ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
RL Mol. Cell 20:525-538(2005).
CC -!- FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V1-
CC UBE2N heterodimer catalyzes the synthesis of non-canonical poly-
CC ubiquitin chains that are linked through Lys-63. This type of
CC poly-ubiquitination activates IKK and does not seem to involve
CC protein degradation by the proteasome. Plays a role in the
CC activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2.
CC Mediates transcriptional activation of target genes. Plays a role
CC in the control of progress through the cell cycle and
CC differentiation. Plays a role in the error-free DNA repair pathway
CC and contributes to the survival of cells after DNA damage.
CC Promotes TRIM5 capsid-specific restriction activity and the
CC UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate
CC 'Lys-63'-linked polyubiquitin chains which activate the
CC MAP3K7/TAK1 complex which in turn results in the induction and
CC expression of NF-kappa-B and MAPK-responsive inflammatory genes.
CC -!- SUBUNIT: Heterodimer with UBE2N. Interacts (UBE2V2-UBE2N
CC heterodimer) with the E3 ligase STUB1 (via the U-box domain); the
CC complex has a specific 'Lys-63'-linked polyubiquitination
CC activity. Interacts with TRAF6.
CC -!- INTERACTION:
CC P61088:UBE2N; NbExp=9; IntAct=EBI-1050671, EBI-1052908;
CC P98170:XIAP; NbExp=2; IntAct=EBI-1050671, EBI-517127;
CC Q8ND25:ZNRF1; NbExp=2; IntAct=EBI-1050671, EBI-2129250;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Excluded from the nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist;
CC Name=3; Synonyms=Isoform 2;
CC IsoId=Q13404-4; Sequence=Displayed;
CC Name=1; Synonyms=CROC-1B, UEV-1B, Isoform 4;
CC IsoId=Q13404-1; Sequence=VSP_038034;
CC Note=Ref.2 (AAC02755) sequence is in conflict in positions:
CC 71:SPHETYFCITT->WPTSSAQCYSP;
CC Name=2; Synonyms=CROC-1A, UEV-1A;
CC IsoId=Q13404-2; Sequence=VSP_038033;
CC Name=4; Synonyms=UEV-1As;
CC IsoId=Q13404-6; Sequence=VSP_038032, VSP_038036;
CC Name=5; Synonyms=Isoform 3;
CC IsoId=Q13404-7; Sequence=VSP_038035;
CC Name=6;
CC IsoId=Q13404-8; Sequence=VSP_044818;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in thyroid, pancreas, spinal
CC cord, lymph node, trachea, adrenal gland, bone marrow and
CC pancreas. Detected at low levels in heart, breast, placenta,
CC brain, liver, kidney, stomach and lung.
CC -!- INDUCTION: Down-regulated during differentiation of cultured colon
CC adenocarcinoma cells.
CC -!- MISCELLANEOUS: In human, TMEM189/KUA and UBE2V1/UEV1 are adjacent
CC genes which can produce independent proteins and can also be fused
CC to form a TMEM189-UBE2V1 hybrid protein.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08944.2; Type=Erroneous initiation;
CC Sequence=CAC16955.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; U39360; AAB72015.1; -; mRNA.
DR EMBL; U39361; AAB72016.1; -; mRNA.
DR EMBL; U49278; AAC02757.1; -; mRNA.
DR EMBL; U97279; AAC02780.1; -; mRNA.
DR EMBL; U97280; AAC02755.1; -; mRNA.
DR EMBL; U97281; AAC02756.1; -; mRNA.
DR EMBL; AY008273; AAG24229.1; -; mRNA.
DR EMBL; BT007382; AAP36046.1; -; mRNA.
DR EMBL; DA580976; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL034423; CAB76864.1; -; Genomic_DNA.
DR EMBL; AL034423; CAB76865.1; -; Genomic_DNA.
DR EMBL; AL034423; CAC16954.1; -; Genomic_DNA.
DR EMBL; AL034423; CAC16955.2; ALT_INIT; Genomic_DNA.
DR EMBL; AL034423; CAI19382.1; -; Genomic_DNA.
DR EMBL; AL034423; CAI19383.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75635.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75634.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75636.1; -; Genomic_DNA.
DR EMBL; BC000468; AAH00468.1; -; mRNA.
DR EMBL; BC008944; AAH08944.2; ALT_INIT; mRNA.
DR RefSeq; NP_001027459.1; NM_001032288.2.
DR RefSeq; NP_001244322.1; NM_001257393.1.
DR RefSeq; NP_001244323.1; NM_001257394.1.
DR RefSeq; NP_001244325.1; NM_001257396.1.
DR RefSeq; NP_068823.2; NM_021988.5.
DR RefSeq; NP_071887.1; NM_022442.5.
DR RefSeq; NP_954595.1; NM_199144.2.
DR RefSeq; NP_954673.1; NM_199203.2.
DR UniGene; Hs.420529; -.
DR UniGene; Hs.744839; -.
DR PDB; 2A4D; X-ray; 1.69 A; A=8-147.
DR PDB; 2C2V; X-ray; 2.90 A; C/F/I/L=8-147.
DR PDB; 2HLW; NMR; -; A=8-147.
DR PDBsum; 2A4D; -.
DR PDBsum; 2C2V; -.
DR PDBsum; 2HLW; -.
DR ProteinModelPortal; Q13404; -.
DR SMR; Q13404; 8-146.
DR DIP; DIP-41911N; -.
DR IntAct; Q13404; 27.
DR MINT; MINT-5002796; -.
DR DMDM; 259016163; -.
DR PaxDb; Q13404; -.
DR PRIDE; Q13404; -.
DR DNASU; 387522; -.
DR DNASU; 7335; -.
DR Ensembl; ENST00000340309; ENSP00000340305; ENSG00000244687.
DR Ensembl; ENST00000371657; ENSP00000360720; ENSG00000244687.
DR Ensembl; ENST00000371674; ENSP00000360739; ENSG00000244687.
DR Ensembl; ENST00000371677; ENSP00000360742; ENSG00000244687.
DR Ensembl; ENST00000415862; ENSP00000407770; ENSG00000244687.
DR Ensembl; ENST00000420027; ENSP00000395264; ENSG00000244687.
DR GeneID; 387522; -.
DR GeneID; 7335; -.
DR KEGG; hsa:387522; -.
DR KEGG; hsa:7335; -.
DR UCSC; uc002xva.4; human.
DR CTD; 387522; -.
DR CTD; 7335; -.
DR GeneCards; GC20M048698; -.
DR HGNC; HGNC:12494; UBE2V1.
DR MIM; 602995; gene.
DR neXtProt; NX_Q13404; -.
DR PharmGKB; PA37142; -.
DR eggNOG; NOG119330; -.
DR HOVERGEN; HBG054552; -.
DR InParanoid; Q13404; -.
DR KO; K10704; -.
DR OMA; TVHENRI; -.
DR OrthoDB; EOG77M8R5; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q13404; -.
DR ChiTaRS; UBE2V1; human.
DR EvolutionaryTrace; Q13404; -.
DR GeneWiki; UBE2V1; -.
DR NextBio; 101372; -.
DR PRO; PR:Q13404; -.
DR ArrayExpress; Q13404; -.
DR Bgee; Q13404; -.
DR Genevestigator; Q13404; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0035370; C:UBC13-UEV1A complex; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:HGNC.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:HGNC.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; TAS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; TAS:ProtInc.
DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 147 Ubiquitin-conjugating enzyme E2 variant
FT 1.
FT /FTId=PRO_0000082600.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 44 Missing (in isoform 4).
FT /FTId=VSP_038032.
FT VAR_SEQ 1 14 MAATTGSGVKVPRN -> MPGEVQASYLKSQSKLSDEGRLE
FT PRKFHCKGSKSPSQ (in isoform 2).
FT /FTId=VSP_038033.
FT VAR_SEQ 1 7 MAATTGS -> MAYKFRTHSPEALEQLYPWECFVFCLIIFG
FT TFTNQIHKWSHTYFGLPRWVTLLQDWHVILPRKHHRIHHVS
FT PHETYFCITT (in isoform 1).
FT /FTId=VSP_038034.
FT VAR_SEQ 1 7 MAATTGS -> MPGEVQASYLKSQSKLSDEGRLEPRKFHCK
FT (in isoform 5).
FT /FTId=VSP_038035.
FT VAR_SEQ 45 57 LTRWTGMIIGPPR -> MKEDLNLENFTAK (in
FT isoform 4).
FT /FTId=VSP_038036.
FT VAR_SEQ 58 99 Missing (in isoform 6).
FT /FTId=VSP_044818.
FT HELIX 11 25
FT STRAND 31 39
FT STRAND 47 53
FT STRAND 56 58
FT TURN 59 62
FT STRAND 64 70
FT TURN 73 77
FT STRAND 81 86
FT STRAND 91 93
FT TURN 95 97
FT HELIX 102 104
FT HELIX 106 109
FT HELIX 117 128
FT TURN 131 135
SQ SEQUENCE 147 AA; 16495 MW; BA53837F21977B3F CRC64;
MAATTGSGVK VPRNFRLLEE LEEGQKGVGD GTVSWGLEDD EDMTLTRWTG MIIGPPRTIY
ENRIYSLKIE CGPKYPEAPP FVRFVTKINM NGVNSSNGVV DPRAISVLAK WQNSYSIKVV
LQELRRLMMS KENMKLPQPP EGQCYSN
//
ID UB2V1_HUMAN Reviewed; 147 AA.
AC Q13404; E1P629; Q13403; Q13532; Q5TGE0; Q5TGE3; Q96H34; Q9GZT0;
read moreAC Q9GZW1; Q9H4J3; Q9H4J4; Q9UKL1; Q9UM48; Q9UM49; Q9UM50;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 139.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 1;
DE Short=UEV-1;
DE AltName: Full=CROC-1;
DE AltName: Full=TRAF6-regulated IKK activator 1 beta Uev1A;
GN Name=UBE2V1; Synonyms=CROC1, UBE2V, UEV1; ORFNames=P/OKcl.19;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9305758; DOI=10.1016/S0378-1119(97)00097-8;
RA Rothofsky M.L., Lin S.L.;
RT "CROC-1 encodes a protein which mediates transcriptional activation of
RT the human FOS promoter.";
RL Gene 195:141-149(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION, INDUCTION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Colon adenocarcinoma;
RX PubMed=9418904;
RA Sancho E., Vila M.R., Sanchez-Pulido L., Lozano J.J., Paciucci R.,
RA Nadal M., Fox M., Harvey C., Bercovich B., Loukili N., Ciechanover A.,
RA Lin S.L., Sanz F., Estivill X., Valencia A., Thomson T.M.;
RT "Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating
RT enzymes, in in vitro differentiation and cell cycle behavior of HT-29-
RT M6 intestinal mucosecretory cells.";
RL Mol. Cell. Biol. 18:576-589(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH
RP TRAF6 AND UBE2N, AND MASS SPECTROMETRY.
RX PubMed=11057907; DOI=10.1016/S0092-8674(00)00126-4;
RA Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C.,
RA Pickart C., Chen Z.J.;
RT "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric
RT ubiquitin-conjugating enzyme complex and a unique polyubiquitin
RT chain.";
RL Cell 103:351-361(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 2-13 (ISOFORM 3), CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung fibroblast;
RA Bienvenut W.V., Pchelintsev N., Adams P.D.;
RL Submitted (JUL-2009) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-147 (ISOFORMS 1 AND 3).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP FUNCTION.
RX PubMed=9580084; DOI=10.1016/S0014-5793(98)00060-X;
RA Thomson T.M., Khalid H., Lozano J.J., Sancho E., Arino J.;
RT "Role of UEV-1A, a homologue of the tumor suppressor protein TSG101,
RT in protection from DNA damage.";
RL FEBS Lett. 423:49-52(1998).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9705497; DOI=10.1093/nar/26.17.3908;
RA Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.-F.;
RT "The products of the yeast MMS2 and two human homologs (hMMS2 and
RT CROC-1) define a structurally and functionally conserved Ubc-like
RT protein family.";
RL Nucleic Acids Res. 26:3908-3914(1998).
RN [12]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION OF TMEM189-UBE2V1 FUSION
RP PROTEIN.
RC TISSUE=Colon cancer;
RX PubMed=11076860; DOI=10.1101/gr.GR-1405R;
RA Thomson T.M., Lozano J.J., Loukili N., Carrio R., Serras F.,
RA Cormand B., Valeri M., Diaz V.M., Abril J., Burset M., Merino J.,
RA Macaya A., Corominas M., Guigo R.;
RT "Fusion of the human gene for the polyubiquitination coeffector UEV1
RT with Kua, a newly identified gene.";
RL Genome Res. 10:1743-1756(2000).
RN [13]
RP FUNCTION.
RX PubMed=20061386; DOI=10.1074/jbc.M109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [14]
RP FUNCTION.
RX PubMed=21512573; DOI=10.1038/nature09976;
RA Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J.,
RA Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A.,
RA Albert M.L., Strambio-De-Castillia C., Mothes W., Pizzato M.,
RA Gruetter M.G., Luban J.;
RT "TRIM5 is an innate immune sensor for the retrovirus capsid lattice.";
RL Nature 472:361-365(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 8-147 IN COMPLEX WITH STUB1
RP AND UBE2N.
RX PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
RA Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
RA Pearl L.H.;
RT "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
RT ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
RL Mol. Cell 20:525-538(2005).
CC -!- FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V1-
CC UBE2N heterodimer catalyzes the synthesis of non-canonical poly-
CC ubiquitin chains that are linked through Lys-63. This type of
CC poly-ubiquitination activates IKK and does not seem to involve
CC protein degradation by the proteasome. Plays a role in the
CC activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2.
CC Mediates transcriptional activation of target genes. Plays a role
CC in the control of progress through the cell cycle and
CC differentiation. Plays a role in the error-free DNA repair pathway
CC and contributes to the survival of cells after DNA damage.
CC Promotes TRIM5 capsid-specific restriction activity and the
CC UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate
CC 'Lys-63'-linked polyubiquitin chains which activate the
CC MAP3K7/TAK1 complex which in turn results in the induction and
CC expression of NF-kappa-B and MAPK-responsive inflammatory genes.
CC -!- SUBUNIT: Heterodimer with UBE2N. Interacts (UBE2V2-UBE2N
CC heterodimer) with the E3 ligase STUB1 (via the U-box domain); the
CC complex has a specific 'Lys-63'-linked polyubiquitination
CC activity. Interacts with TRAF6.
CC -!- INTERACTION:
CC P61088:UBE2N; NbExp=9; IntAct=EBI-1050671, EBI-1052908;
CC P98170:XIAP; NbExp=2; IntAct=EBI-1050671, EBI-517127;
CC Q8ND25:ZNRF1; NbExp=2; IntAct=EBI-1050671, EBI-2129250;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Excluded from the nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist;
CC Name=3; Synonyms=Isoform 2;
CC IsoId=Q13404-4; Sequence=Displayed;
CC Name=1; Synonyms=CROC-1B, UEV-1B, Isoform 4;
CC IsoId=Q13404-1; Sequence=VSP_038034;
CC Note=Ref.2 (AAC02755) sequence is in conflict in positions:
CC 71:SPHETYFCITT->WPTSSAQCYSP;
CC Name=2; Synonyms=CROC-1A, UEV-1A;
CC IsoId=Q13404-2; Sequence=VSP_038033;
CC Name=4; Synonyms=UEV-1As;
CC IsoId=Q13404-6; Sequence=VSP_038032, VSP_038036;
CC Name=5; Synonyms=Isoform 3;
CC IsoId=Q13404-7; Sequence=VSP_038035;
CC Name=6;
CC IsoId=Q13404-8; Sequence=VSP_044818;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in thyroid, pancreas, spinal
CC cord, lymph node, trachea, adrenal gland, bone marrow and
CC pancreas. Detected at low levels in heart, breast, placenta,
CC brain, liver, kidney, stomach and lung.
CC -!- INDUCTION: Down-regulated during differentiation of cultured colon
CC adenocarcinoma cells.
CC -!- MISCELLANEOUS: In human, TMEM189/KUA and UBE2V1/UEV1 are adjacent
CC genes which can produce independent proteins and can also be fused
CC to form a TMEM189-UBE2V1 hybrid protein.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08944.2; Type=Erroneous initiation;
CC Sequence=CAC16955.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; U39360; AAB72015.1; -; mRNA.
DR EMBL; U39361; AAB72016.1; -; mRNA.
DR EMBL; U49278; AAC02757.1; -; mRNA.
DR EMBL; U97279; AAC02780.1; -; mRNA.
DR EMBL; U97280; AAC02755.1; -; mRNA.
DR EMBL; U97281; AAC02756.1; -; mRNA.
DR EMBL; AY008273; AAG24229.1; -; mRNA.
DR EMBL; BT007382; AAP36046.1; -; mRNA.
DR EMBL; DA580976; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL034423; CAB76864.1; -; Genomic_DNA.
DR EMBL; AL034423; CAB76865.1; -; Genomic_DNA.
DR EMBL; AL034423; CAC16954.1; -; Genomic_DNA.
DR EMBL; AL034423; CAC16955.2; ALT_INIT; Genomic_DNA.
DR EMBL; AL034423; CAI19382.1; -; Genomic_DNA.
DR EMBL; AL034423; CAI19383.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75635.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75634.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75636.1; -; Genomic_DNA.
DR EMBL; BC000468; AAH00468.1; -; mRNA.
DR EMBL; BC008944; AAH08944.2; ALT_INIT; mRNA.
DR RefSeq; NP_001027459.1; NM_001032288.2.
DR RefSeq; NP_001244322.1; NM_001257393.1.
DR RefSeq; NP_001244323.1; NM_001257394.1.
DR RefSeq; NP_001244325.1; NM_001257396.1.
DR RefSeq; NP_068823.2; NM_021988.5.
DR RefSeq; NP_071887.1; NM_022442.5.
DR RefSeq; NP_954595.1; NM_199144.2.
DR RefSeq; NP_954673.1; NM_199203.2.
DR UniGene; Hs.420529; -.
DR UniGene; Hs.744839; -.
DR PDB; 2A4D; X-ray; 1.69 A; A=8-147.
DR PDB; 2C2V; X-ray; 2.90 A; C/F/I/L=8-147.
DR PDB; 2HLW; NMR; -; A=8-147.
DR PDBsum; 2A4D; -.
DR PDBsum; 2C2V; -.
DR PDBsum; 2HLW; -.
DR ProteinModelPortal; Q13404; -.
DR SMR; Q13404; 8-146.
DR DIP; DIP-41911N; -.
DR IntAct; Q13404; 27.
DR MINT; MINT-5002796; -.
DR DMDM; 259016163; -.
DR PaxDb; Q13404; -.
DR PRIDE; Q13404; -.
DR DNASU; 387522; -.
DR DNASU; 7335; -.
DR Ensembl; ENST00000340309; ENSP00000340305; ENSG00000244687.
DR Ensembl; ENST00000371657; ENSP00000360720; ENSG00000244687.
DR Ensembl; ENST00000371674; ENSP00000360739; ENSG00000244687.
DR Ensembl; ENST00000371677; ENSP00000360742; ENSG00000244687.
DR Ensembl; ENST00000415862; ENSP00000407770; ENSG00000244687.
DR Ensembl; ENST00000420027; ENSP00000395264; ENSG00000244687.
DR GeneID; 387522; -.
DR GeneID; 7335; -.
DR KEGG; hsa:387522; -.
DR KEGG; hsa:7335; -.
DR UCSC; uc002xva.4; human.
DR CTD; 387522; -.
DR CTD; 7335; -.
DR GeneCards; GC20M048698; -.
DR HGNC; HGNC:12494; UBE2V1.
DR MIM; 602995; gene.
DR neXtProt; NX_Q13404; -.
DR PharmGKB; PA37142; -.
DR eggNOG; NOG119330; -.
DR HOVERGEN; HBG054552; -.
DR InParanoid; Q13404; -.
DR KO; K10704; -.
DR OMA; TVHENRI; -.
DR OrthoDB; EOG77M8R5; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q13404; -.
DR ChiTaRS; UBE2V1; human.
DR EvolutionaryTrace; Q13404; -.
DR GeneWiki; UBE2V1; -.
DR NextBio; 101372; -.
DR PRO; PR:Q13404; -.
DR ArrayExpress; Q13404; -.
DR Bgee; Q13404; -.
DR Genevestigator; Q13404; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0035370; C:UBC13-UEV1A complex; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:HGNC.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:HGNC.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; TAS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; TAS:ProtInc.
DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 147 Ubiquitin-conjugating enzyme E2 variant
FT 1.
FT /FTId=PRO_0000082600.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 44 Missing (in isoform 4).
FT /FTId=VSP_038032.
FT VAR_SEQ 1 14 MAATTGSGVKVPRN -> MPGEVQASYLKSQSKLSDEGRLE
FT PRKFHCKGSKSPSQ (in isoform 2).
FT /FTId=VSP_038033.
FT VAR_SEQ 1 7 MAATTGS -> MAYKFRTHSPEALEQLYPWECFVFCLIIFG
FT TFTNQIHKWSHTYFGLPRWVTLLQDWHVILPRKHHRIHHVS
FT PHETYFCITT (in isoform 1).
FT /FTId=VSP_038034.
FT VAR_SEQ 1 7 MAATTGS -> MPGEVQASYLKSQSKLSDEGRLEPRKFHCK
FT (in isoform 5).
FT /FTId=VSP_038035.
FT VAR_SEQ 45 57 LTRWTGMIIGPPR -> MKEDLNLENFTAK (in
FT isoform 4).
FT /FTId=VSP_038036.
FT VAR_SEQ 58 99 Missing (in isoform 6).
FT /FTId=VSP_044818.
FT HELIX 11 25
FT STRAND 31 39
FT STRAND 47 53
FT STRAND 56 58
FT TURN 59 62
FT STRAND 64 70
FT TURN 73 77
FT STRAND 81 86
FT STRAND 91 93
FT TURN 95 97
FT HELIX 102 104
FT HELIX 106 109
FT HELIX 117 128
FT TURN 131 135
SQ SEQUENCE 147 AA; 16495 MW; BA53837F21977B3F CRC64;
MAATTGSGVK VPRNFRLLEE LEEGQKGVGD GTVSWGLEDD EDMTLTRWTG MIIGPPRTIY
ENRIYSLKIE CGPKYPEAPP FVRFVTKINM NGVNSSNGVV DPRAISVLAK WQNSYSIKVV
LQELRRLMMS KENMKLPQPP EGQCYSN
//
MIM
602995
*RECORD*
*FIELD* NO
602995
*FIELD* TI
*602995 UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 1; UBE2V1
;;UEV1; UEV1A;;
CROC1
*FIELD* TX
read more
CLONING
Rothofsky and Lin (1997) isolated human brain cDNAs encoding UBE2V1,
which they called CROC1. They identified 2 alternative 5-prime CROC1
cDNA sequences that result in predicted 221- and 170-amino acid
proteins, designated CROC1B and CROC1A, respectively, with different
N-terminal ends. The CROC1 isoforms have an acidic domain and a
C-terminal basic domain. They show sequence similarity to
ubiquitin-conjugating enzymes (UBCs, or E2s, e.g., UBE2D1; 602961), but
they lack the conserved cysteine critical for E2 catalytic activity. The
CROC1 C-terminal domain has 42% sequence identity with the potential
DNA-binding domain of TAFII250 (TAF2A; 313650). Immunofluorescence
microscopy localized recombinant CROC1 to the nucleus, excluding the
nucleolar organizer regions. Northern blot analysis detected 2.1- and
2.5-kb CROC1 transcripts in all human tissues examined, with highest
levels in brain, skeletal muscle, and kidney.
Sancho et al. (1998) isolated partial human intestinal epithelial cell
cDNAs containing the 3-prime coding sequence and 3-prime UTR of UBE2V1,
which they called UEV1. RT-PCR identified 4 alternatively spliced UEV1
transcripts encoding proteins with identical 90-amino acid C-terminal
sequences, including the region homologous to the conserved Ubc domain
of E2 enzymes, but unique N-terminal sequences. The 140-amino acid C
terminus of the deduced 221- and 170-amino acid UEV1 isoforms identified
by Rothofsky and Lin (1997), which Sancho et al. (1998) called UEV1B and
UEV1A, respectively, is 90% identical to UEV2 (UBE2V2; 603001) and 18%,
24%, and 22% identical to the Ubc domain of human UBE2I (601661), S.
cerevisiae UBC4 and UBC7, and A. thaliana UBC1, respectively.
Thomson et al. (2000) determined that the 5-prime UEV1 splice variant
identified as CROC1B by Rothofsky and Lin (1997) and UEV1B by Sancho et
al. (1998) is a fusion transcripts resulting from splicing of the first
5 exons of the KUA gene (610994) with the last 3 exons of the UEV1 gene.
The last exon of KUA and the first exon of UEV1 are skipped. The deduced
protein contains an N-terminal KUA domain and a C-terminal UEV1 domain.
See 610994 for further information on the KUA/UEV1 fusion transcript.
GENE FUNCTION
Rothofsky and Lin (1997) demonstrated that CROC1 can cause
transcriptional activation of the human FOS (164810) promoter.
Sancho et al. (1998) showed that UEV1 does not have
ubiquitin-conjugating activity in vitro. UEV1 transcripts were
downregulated upon differentiation of a colon carcinoma cell line.
Constitutive expression of exogenous UEV1 protein in these colon
carcinoma cells inhibited their capacity to differentiate upon
confluence and induced changes in their cell cycle behavior, which was
associated with an inhibition of the mitotic kinase CDK1 (see CDC2;
116940).
Deng et al. (2000) purified a heterodimeric protein complex that links
TRAF6 (602355) to IKK (see 600664) activation. Peptide mass
fingerprinting analysis revealed that this complex is composed of the
ubiquitin conjugating enzyme UBC13 (603679) and the UBC-like protein
UBE2V1, which the authors called UEV1A. They found that TRAF6, a RING
domain protein, functions together with UBC13/UEV1A to catalyze the
synthesis of unique polyubiquitin chains linked through lysine-63 (K63)
of ubiquitin. Blockade of this polyubiquitin chain synthesis, but not
inhibition of the proteasome, prevents the activation of IKK by TRAF6.
These results unveil a new regulatory function for ubiquitin, in which
IKK is activated through the assembly of K63-linked polyubiquitin
chains.
Pertel et al. (2011) demonstrated that TRIM5 (608487) promotes innate
immune signaling and that this activity is amplified by retroviral
infection and interaction with the capsid lattice. Acting with the
heterodimeric, ubiquitin-conjugating enzyme UBC13-UEV1A, TRIM5 catalyzes
the synthesis of unattached K63-linked ubiquitin chains that activate
the TAK1 (602614) kinase complex and stimulate AP1 (see 165160) and
NF-kappa-B (see 164011) signaling. Interaction with the HIV-1 capsid
lattice greatly enhanced the UBC13-UEV1A-dependent E3 activity of TRIM5,
and challenge with retroviruses induced the transcription of AP1- and
NF-kappa-B-dependent factors with a magnitude that tracked with TRIM5
avidity for the invading capsid. Finally, TAK1 and UBC13-UEV1A
contribute to capsid-specific restriction by TRIM5. Pertel et al. (2011)
concluded that the retroviral restriction factor TRIM5 has 2 additional
activities that are linked to restriction: it constitutively promotes
innate immune signaling, and it acts as a pattern recognition receptor
specific for the retrovirus capsid lattice.
GENE STRUCTURE
Sancho et al. (1998) determined that the UEV1 gene contains at least 6
exons and has at least 3 alternative polyadenylation sites in the
3-prime UTR. However, Thomson et al. (2000) determined that UBE2V1 gene
contains 4 exons. The most 5-prime UBE2V1 exon described by Sancho et
al. (1998) originates from exons 4 and 5 of the upstream KUA gene.
MAPPING
By fluorescence in situ hybridization, Sancho et al. (1998) mapped the
human UEV1 gene to chromosome 20q13.2.
*FIELD* RF
1. Deng, L.; Wang, C.; Spencer, E.; Yang, L.; Braun, A.; You, J.;
Slaughter, C.; Pickart, C.; Chen, Z. J.: Activation of the I-kappa-B
complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex
and a unique polyubiquitin chain. Cell 103: 351-361, 2000.
2. Pertel, T.; Hausmann, S.; Morger, D.; Zuger, S.; Guerra, J.; Lascano,
J.; Reinhard, C.; Santoni, F. A.; Uchil, P. D.; Chatel, L.; Bisiaux,
A.; Albert, M. L.; Strambio-De-Castillia, C.; Mothes, W.; Pizzato,
M.; Grutter, M. G.; Luban, J.: TRIM5 is an innate immune sensor for
the retrovirus capsid lattice. Nature 472: 361-365, 2011.
3. Rothofsky, M. L.; Lin, S. L.: CROC-1 encodes a protein which mediates
transcriptional activation of the human FOS promoter. Gene 195:
141-149, 1997.
4. Sancho, E.; Vila, M. R.; Sanchez-Pulido, L.; Lozano, J. J.; Paciucci,
R.; Nadal, M.; Fox, M.; Harvey, C.; Bercovich, B.; Loukili, N.; Ciechanover,
A.; Lin, S. L.; Sanz, F.; Estivill, X.; Valencia, A.; Thomson, T.
M.: Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating
enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6
intestinal mucosecretory cells. Molec. Cell. Biol. 18: 576-589,
1998.
5. Thomson, T. M.; Lozano, J. J.; Loukili, N.; Carrio, R.; Serras,
F.; Cormand, B.; Valeri, M.; Diaz, V. M.; Abril, J.; Burset, M.; Merino,
J.; Macaya, A.; Corominas, M.; Guigo, R.: Fusion of the human gene
for the polyubiquitination coeffector UEV1 with Kua, a newly identified
gene. Genome Res. 10: 1743-1756, 2000.
*FIELD* CN
Ada Hamosh - updated: 7/8/2011
Patricia A. Hartz - updated: 3/14/2007
Stylianos E. Antonarakis - updated: 10/24/2000
Stylianos E. Antonarakis - updated: 3/25/1999
*FIELD* CD
Patti M. Sherman: 8/21/1998
*FIELD* ED
alopez: 07/12/2011
terry: 7/8/2011
mgross: 5/7/2007
terry: 3/14/2007
carol: 10/24/2000
mgross: 3/31/1999
mgross: 3/29/1999
terry: 3/25/1999
alopez: 9/22/1998
*RECORD*
*FIELD* NO
602995
*FIELD* TI
*602995 UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 1; UBE2V1
;;UEV1; UEV1A;;
CROC1
*FIELD* TX
read more
CLONING
Rothofsky and Lin (1997) isolated human brain cDNAs encoding UBE2V1,
which they called CROC1. They identified 2 alternative 5-prime CROC1
cDNA sequences that result in predicted 221- and 170-amino acid
proteins, designated CROC1B and CROC1A, respectively, with different
N-terminal ends. The CROC1 isoforms have an acidic domain and a
C-terminal basic domain. They show sequence similarity to
ubiquitin-conjugating enzymes (UBCs, or E2s, e.g., UBE2D1; 602961), but
they lack the conserved cysteine critical for E2 catalytic activity. The
CROC1 C-terminal domain has 42% sequence identity with the potential
DNA-binding domain of TAFII250 (TAF2A; 313650). Immunofluorescence
microscopy localized recombinant CROC1 to the nucleus, excluding the
nucleolar organizer regions. Northern blot analysis detected 2.1- and
2.5-kb CROC1 transcripts in all human tissues examined, with highest
levels in brain, skeletal muscle, and kidney.
Sancho et al. (1998) isolated partial human intestinal epithelial cell
cDNAs containing the 3-prime coding sequence and 3-prime UTR of UBE2V1,
which they called UEV1. RT-PCR identified 4 alternatively spliced UEV1
transcripts encoding proteins with identical 90-amino acid C-terminal
sequences, including the region homologous to the conserved Ubc domain
of E2 enzymes, but unique N-terminal sequences. The 140-amino acid C
terminus of the deduced 221- and 170-amino acid UEV1 isoforms identified
by Rothofsky and Lin (1997), which Sancho et al. (1998) called UEV1B and
UEV1A, respectively, is 90% identical to UEV2 (UBE2V2; 603001) and 18%,
24%, and 22% identical to the Ubc domain of human UBE2I (601661), S.
cerevisiae UBC4 and UBC7, and A. thaliana UBC1, respectively.
Thomson et al. (2000) determined that the 5-prime UEV1 splice variant
identified as CROC1B by Rothofsky and Lin (1997) and UEV1B by Sancho et
al. (1998) is a fusion transcripts resulting from splicing of the first
5 exons of the KUA gene (610994) with the last 3 exons of the UEV1 gene.
The last exon of KUA and the first exon of UEV1 are skipped. The deduced
protein contains an N-terminal KUA domain and a C-terminal UEV1 domain.
See 610994 for further information on the KUA/UEV1 fusion transcript.
GENE FUNCTION
Rothofsky and Lin (1997) demonstrated that CROC1 can cause
transcriptional activation of the human FOS (164810) promoter.
Sancho et al. (1998) showed that UEV1 does not have
ubiquitin-conjugating activity in vitro. UEV1 transcripts were
downregulated upon differentiation of a colon carcinoma cell line.
Constitutive expression of exogenous UEV1 protein in these colon
carcinoma cells inhibited their capacity to differentiate upon
confluence and induced changes in their cell cycle behavior, which was
associated with an inhibition of the mitotic kinase CDK1 (see CDC2;
116940).
Deng et al. (2000) purified a heterodimeric protein complex that links
TRAF6 (602355) to IKK (see 600664) activation. Peptide mass
fingerprinting analysis revealed that this complex is composed of the
ubiquitin conjugating enzyme UBC13 (603679) and the UBC-like protein
UBE2V1, which the authors called UEV1A. They found that TRAF6, a RING
domain protein, functions together with UBC13/UEV1A to catalyze the
synthesis of unique polyubiquitin chains linked through lysine-63 (K63)
of ubiquitin. Blockade of this polyubiquitin chain synthesis, but not
inhibition of the proteasome, prevents the activation of IKK by TRAF6.
These results unveil a new regulatory function for ubiquitin, in which
IKK is activated through the assembly of K63-linked polyubiquitin
chains.
Pertel et al. (2011) demonstrated that TRIM5 (608487) promotes innate
immune signaling and that this activity is amplified by retroviral
infection and interaction with the capsid lattice. Acting with the
heterodimeric, ubiquitin-conjugating enzyme UBC13-UEV1A, TRIM5 catalyzes
the synthesis of unattached K63-linked ubiquitin chains that activate
the TAK1 (602614) kinase complex and stimulate AP1 (see 165160) and
NF-kappa-B (see 164011) signaling. Interaction with the HIV-1 capsid
lattice greatly enhanced the UBC13-UEV1A-dependent E3 activity of TRIM5,
and challenge with retroviruses induced the transcription of AP1- and
NF-kappa-B-dependent factors with a magnitude that tracked with TRIM5
avidity for the invading capsid. Finally, TAK1 and UBC13-UEV1A
contribute to capsid-specific restriction by TRIM5. Pertel et al. (2011)
concluded that the retroviral restriction factor TRIM5 has 2 additional
activities that are linked to restriction: it constitutively promotes
innate immune signaling, and it acts as a pattern recognition receptor
specific for the retrovirus capsid lattice.
GENE STRUCTURE
Sancho et al. (1998) determined that the UEV1 gene contains at least 6
exons and has at least 3 alternative polyadenylation sites in the
3-prime UTR. However, Thomson et al. (2000) determined that UBE2V1 gene
contains 4 exons. The most 5-prime UBE2V1 exon described by Sancho et
al. (1998) originates from exons 4 and 5 of the upstream KUA gene.
MAPPING
By fluorescence in situ hybridization, Sancho et al. (1998) mapped the
human UEV1 gene to chromosome 20q13.2.
*FIELD* RF
1. Deng, L.; Wang, C.; Spencer, E.; Yang, L.; Braun, A.; You, J.;
Slaughter, C.; Pickart, C.; Chen, Z. J.: Activation of the I-kappa-B
complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex
and a unique polyubiquitin chain. Cell 103: 351-361, 2000.
2. Pertel, T.; Hausmann, S.; Morger, D.; Zuger, S.; Guerra, J.; Lascano,
J.; Reinhard, C.; Santoni, F. A.; Uchil, P. D.; Chatel, L.; Bisiaux,
A.; Albert, M. L.; Strambio-De-Castillia, C.; Mothes, W.; Pizzato,
M.; Grutter, M. G.; Luban, J.: TRIM5 is an innate immune sensor for
the retrovirus capsid lattice. Nature 472: 361-365, 2011.
3. Rothofsky, M. L.; Lin, S. L.: CROC-1 encodes a protein which mediates
transcriptional activation of the human FOS promoter. Gene 195:
141-149, 1997.
4. Sancho, E.; Vila, M. R.; Sanchez-Pulido, L.; Lozano, J. J.; Paciucci,
R.; Nadal, M.; Fox, M.; Harvey, C.; Bercovich, B.; Loukili, N.; Ciechanover,
A.; Lin, S. L.; Sanz, F.; Estivill, X.; Valencia, A.; Thomson, T.
M.: Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating
enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6
intestinal mucosecretory cells. Molec. Cell. Biol. 18: 576-589,
1998.
5. Thomson, T. M.; Lozano, J. J.; Loukili, N.; Carrio, R.; Serras,
F.; Cormand, B.; Valeri, M.; Diaz, V. M.; Abril, J.; Burset, M.; Merino,
J.; Macaya, A.; Corominas, M.; Guigo, R.: Fusion of the human gene
for the polyubiquitination coeffector UEV1 with Kua, a newly identified
gene. Genome Res. 10: 1743-1756, 2000.
*FIELD* CN
Ada Hamosh - updated: 7/8/2011
Patricia A. Hartz - updated: 3/14/2007
Stylianos E. Antonarakis - updated: 10/24/2000
Stylianos E. Antonarakis - updated: 3/25/1999
*FIELD* CD
Patti M. Sherman: 8/21/1998
*FIELD* ED
alopez: 07/12/2011
terry: 7/8/2011
mgross: 5/7/2007
terry: 3/14/2007
carol: 10/24/2000
mgross: 3/31/1999
mgross: 3/29/1999
terry: 3/25/1999
alopez: 9/22/1998