UB2V1_HUMAN
ID UB2V1_HUMAN Reviewed; 147 AA.
AC Q13404; E1P629; Q13403; Q13532; Q5TGE0; Q5TGE3; Q96H34; Q9GZT0; Q9GZW1;
AC Q9H4J3; Q9H4J4; Q9UKL1; Q9UM48; Q9UM49; Q9UM50;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 208.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP 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 the
RT human FOS promoter.";
RL Gene 195:141-149(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION, INDUCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Colon adenocarcinoma;
RX PubMed=9418904; DOI=10.1128/mcb.18.1.576;
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-M6
RT intestinal mucosecretory cells.";
RL Mol. Cell. Biol. 18:576-589(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH TRAF6
RP AND UBE2N, AND IDENTIFICATION BY 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 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., 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., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY 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 project:
RT 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, in
RT 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 CROC-1)
RT define a structurally and functionally conserved Ubc-like protein family.";
RL Nucleic Acids Res. 26:3908-3914(1998).
RN [12]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION OF PESD1-UBE2V1 FUSION 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., Cormand B.,
RA Valeri M., Diaz V.M., Abril J., Burset M., Merino J., Macaya A.,
RA Corominas M., Guigo R.;
RT "Fusion of the human gene for the polyubiquitination coeffector UEV1 with
RT Kua, a newly identified gene.";
RL Genome Res. 10:1743-1756(2000).
RN [13]
RP FUNCTION.
RX PubMed=19825828; DOI=10.1126/scisignal.2000382;
RA Liu C., Qian W., Qian Y., Giltiay N.V., Lu Y., Swaidani S., Misra S.,
RA Deng L., Chen Z.J., Li X.;
RT "Act1, a U-box E3 ubiquitin ligase for IL-17 signaling.";
RL Sci. Signal. 2:ra63-ra63(2009).
RN [14]
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 [15]
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., Albert M.L.,
RA Strambio-De-Castillia C., Mothes W., Pizzato M., Gruetter M.G., Luban J.;
RT "TRIM5 is an innate immune sensor for the retrovirus capsid lattice.";
RL Nature 472:361-365(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP FUNCTION.
RX PubMed=31006531; DOI=10.1016/j.cell.2019.03.017;
RA Cadena C., Ahmad S., Xavier A., Willemsen J., Park S., Park J.W., Oh S.W.,
RA Fujita T., Hou F., Binder M., Hur S.;
RT "Ubiquitin-Dependent and -Independent Roles of E3 Ligase RIPLET in Innate
RT Immunity.";
RL Cell 177:1187-1200(2019).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 8-147 IN COMPLEX WITH STUB1 AND
RP 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).
RN [20] {ECO:0007744|PDB:2HLW}
RP STRUCTURE BY NMR OF 7-147, AND INTERACTION WITH UBE2N.
RX PubMed=16893187; DOI=10.1021/bi060631r;
RA Hau D.D., Lewis M.J., Saltibus L.F., Pastushok L., Xiao W.,
RA Spyracopoulos L.;
RT "Structure and interactions of the ubiquitin-conjugating enzyme variant
RT human Uev1a: implications for enzymatic synthesis of polyubiquitin
RT chains.";
RL Biochemistry 45:9866-9877(2006).
RN [21] {ECO:0007744|PDB:2A4D}
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 7-147.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
CC -!- FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N
CC heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin
CC chains that are linked through Lys-63. This type of poly-ubiquitination
CC activates IKK and does not seem to involve protein degradation by the
CC proteasome. Plays a role in the activation of NF-kappa-B mediated by
CC IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of
CC target genes. Plays a role in the control of progress through the cell
CC cycle and differentiation. Plays a role in the error-free DNA repair
CC pathway and contributes to the survival of cells after DNA damage.
CC Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-
CC UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-
CC linked polyubiquitin chains which activate the MAP3K7/TAK1 complex
CC which in turn results in the induction and expression of NF-kappa-B and
CC MAPK-responsive inflammatory genes. Together with RNF135 and UBE2N,
CC catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of
CC RIG-I/DDX58 to activate the downstream signaling pathway that leads to
CC interferon beta production (PubMed:31006531). UBE2V1-UBE2N together
CC with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked
CC polyubiquitination of TRAF6, a component of IL17A-mediated signaling
CC pathway. {ECO:0000269|PubMed:11057907, ECO:0000269|PubMed:19825828,
CC ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21512573,
CC ECO:0000269|PubMed:31006531, ECO:0000269|PubMed:9305758,
CC ECO:0000269|PubMed:9418904, ECO:0000269|PubMed:9580084,
CC ECO:0000269|PubMed:9705497}.
CC -!- SUBUNIT: Heterodimer with UBE2N (PubMed:11057907, PubMed:16307917,
CC PubMed:16893187). Interacts (UBE2V2-UBE2N heterodimer) with the E3
CC ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-
CC 63'-linked polyubiquitination activity (PubMed:16307917). Interacts
CC with TRAF6 (PubMed:11057907, PubMed:16307917).
CC {ECO:0000269|PubMed:11057907, ECO:0000269|PubMed:16307917,
CC ECO:0000269|PubMed:16893187}.
CC -!- INTERACTION:
CC Q13404; Q92870-2: APBB2; NbExp=3; IntAct=EBI-1050671, EBI-21535880;
CC Q13404; P54253: ATXN1; NbExp=6; IntAct=EBI-1050671, EBI-930964;
CC Q13404; P02489: CRYAA; NbExp=3; IntAct=EBI-1050671, EBI-6875961;
CC Q13404; P78358: CTAG1B; NbExp=3; IntAct=EBI-1050671, EBI-1188472;
CC Q13404; Q15038: DAZAP2; NbExp=3; IntAct=EBI-1050671, EBI-724310;
CC Q13404; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1050671, EBI-10976677;
CC Q13404; Q92567: FAM168A; NbExp=4; IntAct=EBI-1050671, EBI-7957930;
CC Q13404; P22607: FGFR3; NbExp=3; IntAct=EBI-1050671, EBI-348399;
CC Q13404; Q14957: GRIN2C; NbExp=3; IntAct=EBI-1050671, EBI-8285963;
CC Q13404; P06396: GSN; NbExp=3; IntAct=EBI-1050671, EBI-351506;
CC Q13404; P11021: HSPA5; NbExp=3; IntAct=EBI-1050671, EBI-354921;
CC Q13404; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1050671, EBI-10975473;
CC Q13404; Q92876: KLK6; NbExp=3; IntAct=EBI-1050671, EBI-2432309;
CC Q13404; O60260-5: PRKN; NbExp=3; IntAct=EBI-1050671, EBI-21251460;
CC Q13404; Q9Y3C5: RNF11; NbExp=4; IntAct=EBI-1050671, EBI-396669;
CC Q13404; Q6ZNA4: RNF111; NbExp=2; IntAct=EBI-1050671, EBI-2129175;
CC Q13404; Q96DD7: SHISA4; NbExp=3; IntAct=EBI-1050671, EBI-18035902;
CC Q13404; Q13148: TARDBP; NbExp=3; IntAct=EBI-1050671, EBI-372899;
CC Q13404; Q13049: TRIM32; NbExp=4; IntAct=EBI-1050671, EBI-742790;
CC Q13404; P61088: UBE2N; NbExp=18; IntAct=EBI-1050671, EBI-1052908;
CC Q13404; Q9UMX0: UBQLN1; NbExp=9; IntAct=EBI-1050671, EBI-741480;
CC Q13404; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-1050671, EBI-10173939;
CC Q13404; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-1050671, EBI-947187;
CC Q13404; P17861: XBP1; NbExp=3; IntAct=EBI-1050671, EBI-6942961;
CC Q13404; P98170: XIAP; NbExp=3; IntAct=EBI-1050671, EBI-517127;
CC Q13404; Q8ND25: ZNRF1; NbExp=2; IntAct=EBI-1050671, EBI-2129250;
CC Q13404-2; P61088: UBE2N; NbExp=2; IntAct=EBI-15972179, EBI-1052908;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076860,
CC ECO:0000269|PubMed:9305758}. 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 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 -!- TISSUE SPECIFICITY: Highly expressed in thyroid, pancreas, spinal cord,
CC lymph node, trachea, adrenal gland, bone marrow and pancreas. Detected
CC at low levels in heart, breast, placenta, brain, liver, kidney, stomach
CC and lung. {ECO:0000269|PubMed:9418904, ECO:0000269|PubMed:9705497}.
CC -!- INDUCTION: Down-regulated during differentiation of cultured colon
CC adenocarcinoma cells. {ECO:0000269|PubMed:9418904}.
CC -!- MISCELLANEOUS: In human, PESD1/KUA and UBE2V1/UEV1 are adjacent genes
CC which can produce independent proteins and can also be fused to form a
CC PESD1-UBE2V1 hybrid protein.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08944.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS13426.1; -. [Q13404-7]
DR CCDS; CCDS13427.1; -. [Q13404-6]
DR CCDS; CCDS33483.1; -. [Q13404-4]
DR CCDS; CCDS58775.1; -. [Q13404-8]
DR RefSeq; NP_001027459.1; NM_001032288.2. [Q13404-4]
DR RefSeq; NP_001244322.1; NM_001257393.1. [Q13404-7]
DR RefSeq; NP_001244323.1; NM_001257394.1. [Q13404-6]
DR RefSeq; NP_001244325.1; NM_001257396.1. [Q13404-8]
DR RefSeq; NP_068823.2; NM_021988.5. [Q13404-7]
DR RefSeq; NP_071887.1; NM_022442.5. [Q13404-6]
DR RefSeq; NP_954595.1; NM_199144.2. [Q13404-7]
DR RefSeq; NP_954673.1; NM_199203.2.
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 PDB; 6D6I; X-ray; 2.55 A; A/D=8-147.
DR PDBsum; 2A4D; -.
DR PDBsum; 2C2V; -.
DR PDBsum; 2HLW; -.
DR PDBsum; 6D6I; -.
DR AlphaFoldDB; Q13404; -.
DR BMRB; Q13404; -.
DR SMR; Q13404; -.
DR BioGRID; 113183; 105.
DR BioGRID; 132321; 34.
DR ComplexPortal; CPX-485; UBC13-UEV1A ubiquitin-conjugating enzyme E2 complex.
DR CORUM; Q13404; -.
DR DIP; DIP-41911N; -.
DR IntAct; Q13404; 136.
DR MINT; Q13404; -.
DR MoonDB; Q13404; Predicted.
DR GlyGen; Q13404; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13404; -.
DR PhosphoSitePlus; Q13404; -.
DR SwissPalm; Q13404; -.
DR BioMuta; UBE2V1; -.
DR DMDM; 259016163; -.
DR EPD; Q13404; -.
DR jPOST; Q13404; -.
DR MassIVE; Q13404; -.
DR MaxQB; Q13404; -.
DR PaxDb; Q13404; -.
DR PeptideAtlas; Q13404; -.
DR PRIDE; Q13404; -.
DR ProteomicsDB; 59382; -. [Q13404-4]
DR ProteomicsDB; 59383; -. [Q13404-1]
DR ProteomicsDB; 59384; -. [Q13404-2]
DR ProteomicsDB; 59385; -. [Q13404-6]
DR ProteomicsDB; 59386; -. [Q13404-7]
DR ProteomicsDB; 65114; -.
DR TopDownProteomics; Q13404-4; -. [Q13404-4]
DR Antibodypedia; 35021; 273 antibodies from 33 providers.
DR DNASU; 7335; -.
DR Ensembl; ENST00000340309.7; ENSP00000340305.3; ENSG00000244687.13. [Q13404-7]
DR Ensembl; ENST00000371657.9; ENSP00000360720.5; ENSG00000244687.13. [Q13404-8]
DR Ensembl; ENST00000371674.8; ENSP00000360739.4; ENSG00000244687.13. [Q13404-4]
DR Ensembl; ENST00000371677.7; ENSP00000360742.3; ENSG00000244687.13. [Q13404-7]
DR Ensembl; ENST00000415862.6; ENSP00000407770.2; ENSG00000244687.13. [Q13404-6]
DR GeneID; 387522; -.
DR GeneID; 7335; -.
DR KEGG; hsa:387522; -.
DR KEGG; hsa:7335; -.
DR MANE-Select; ENST00000371674.8; ENSP00000360739.4; NM_001032288.3; NP_001027459.1.
DR UCSC; uc002xva.5; human. [Q13404-4]
DR CTD; 387522; -.
DR CTD; 7335; -.
DR DisGeNET; 387522; -.
DR DisGeNET; 7335; -.
DR GeneCards; UBE2V1; -.
DR HGNC; HGNC:12494; UBE2V1.
DR HPA; ENSG00000244687; Low tissue specificity.
DR MIM; 602995; gene.
DR neXtProt; NX_Q13404; -.
DR OpenTargets; ENSG00000244687; -.
DR PharmGKB; PA37142; -.
DR VEuPathDB; HostDB:ENSG00000244687; -.
DR eggNOG; KOG0896; Eukaryota.
DR GeneTree; ENSGT00940000158854; -.
DR HOGENOM; CLU_063065_1_2_1; -.
DR InParanoid; Q13404; -.
DR OMA; NLPCVDQ; -.
DR OrthoDB; 1507995at2759; -.
DR TreeFam; TF316971; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR PathwayCommons; Q13404; -.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
DR Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
DR Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q13404; -.
DR SIGNOR; Q13404; -.
DR BioGRID-ORCS; 387522; 70 hits in 918 CRISPR screens.
DR BioGRID-ORCS; 7335; 223 hits in 1017 CRISPR screens.
DR ChiTaRS; UBE2V1; human.
DR EvolutionaryTrace; Q13404; -.
DR GeneWiki; UBE2V1; -.
DR Pharos; Q13404; Tbio.
DR PRO; PR:Q13404; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q13404; protein.
DR Bgee; ENSG00000244687; Expressed in colonic epithelium and 102 other tissues.
DR ExpressionAtlas; Q13404; baseline and differential.
DR Genevisible; Q13404; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0035370; C:UBC13-UEV1A complex; IDA:UniProtKB.
DR GO; GO:0031371; C:ubiquitin conjugating enzyme complex; IDA:HGNC-UCL.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:HGNC-UCL.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IDA:ComplexPortal.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:HGNC-UCL.
DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006282; P:regulation of DNA repair; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
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; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..147
FT /note="Ubiquitin-conjugating enzyme E2 variant 1"
FT /id="PRO_0000082600"
FT DOMAIN 12..147
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9418904"
FT /id="VSP_038032"
FT VAR_SEQ 1..14
FT /note="MAATTGSGVKVPRN -> MPGEVQASYLKSQSKLSDEGRLEPRKFHCKGSKS
FT PSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9305758,
FT ECO:0000303|PubMed:9418904"
FT /id="VSP_038033"
FT VAR_SEQ 1..7
FT /note="MAATTGS -> MAYKFRTHSPEALEQLYPWECFVFCLIIFGTFTNQIHKWSH
FT TYFGLPRWVTLLQDWHVILPRKHHRIHHVSPHETYFCITT (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9305758, ECO:0000303|PubMed:9418904"
FT /id="VSP_038034"
FT VAR_SEQ 1..7
FT /note="MAATTGS -> MPGEVQASYLKSQSKLSDEGRLEPRKFHCK (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:11057907"
FT /id="VSP_038035"
FT VAR_SEQ 45..57
FT /note="LTRWTGMIIGPPR -> MKEDLNLENFTAK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9418904"
FT /id="VSP_038036"
FT VAR_SEQ 58..99
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044818"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:2A4D"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:2A4D"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:2A4D"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2HLW"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:2A4D"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:2A4D"
FT TURN 73..77
FT /evidence="ECO:0007829|PDB:2A4D"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:2A4D"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2HLW"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2A4D"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2A4D"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:2A4D"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:2A4D"
FT TURN 131..135
FT /evidence="ECO:0007829|PDB:2A4D"
FT CONFLICT Q13404-1:71..81
FT /note="SPHETYFCITT -> WPTSSAQCYSP (in Ref. 2; AAC02755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16495 MW; BA53837F21977B3F CRC64;
MAATTGSGVK VPRNFRLLEE LEEGQKGVGD GTVSWGLEDD EDMTLTRWTG MIIGPPRTIY
ENRIYSLKIE CGPKYPEAPP FVRFVTKINM NGVNSSNGVV DPRAISVLAK WQNSYSIKVV
LQELRRLMMS KENMKLPQPP EGQCYSN
