UB2V1_MOUSE
ID UB2V1_MOUSE Reviewed; 147 AA.
AC Q9CZY3; A2A467; Q8VEB5; Q9ERI7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 1;
DE Short=UEV-1;
DE AltName: Full=CROC-1;
GN Name=Ube2v1; Synonyms=Croc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-147 (ISOFORM 1), FUNCTION, INTERACTION
RP WITH UBE2N, AND TISSUE SPECIFICITY.
RX PubMed=11406273; DOI=10.1016/s0167-4781(01)00223-8;
RA Franko J., Ashley C., Xiao W.;
RT "Molecular cloning and functional characterization of two murine cDNAs
RT which encode Ubc variants involved in DNA repair and mutagenesis.";
RL Biochim. Biophys. Acta 1519:70-77(2001).
RN [5]
RP INTERACTION WITH STUB1 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-UBE2N
CC heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin
CC chains that are linked through 'Lys-63'. This type of poly-
CC ubiquitination activates IKK and does not seem to involve protein
CC degradation by the proteasome. Plays a role in the activation of NF-
CC kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates
CC transcriptional activation of target genes. Plays a role in the control
CC of progress through the cell cycle and differentiation (By similarity).
CC Plays a role in the error-free DNA repair pathway and contributes to
CC the survival of cells after DNA damage. Promotes TRIM5 capsid-specific
CC restriction activity and the UBE2V1-UBE2N heterodimer acts in concert
CC with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which
CC activate the MAP3K7/TAK1 complex which in turn results in the induction
CC and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By
CC similarity). Together with RNF135 and UBE2N, catalyzes the viral RNA-
CC dependent 'Lys-63'-linked polyubiquitination of RIG-I/DDX58 to activate
CC the downstream signaling pathway that leads to interferon beta
CC production (By similarity). UBE2V1-UBE2N together with TRAF3IP2 E3
CC ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a
CC component of IL17A-mediated signaling pathway. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q13404, ECO:0000269|PubMed:11406273}.
CC -!- SUBUNIT: Heterodimer with UBE2N. Interacts (UBE2V2-UBE2N heterodimer)
CC with the E3 ligase STUB1 (via the U-box domain); the complex has a
CC specific 'Lys-63'-linked polyubiquitination activity. Interacts with
CC TRAF6 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the
CC nucleolus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CZY3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZY3-2; Sequence=VSP_011528;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, brain,
CC liver, skeletal msucle, kidney and testis. Detected at lower levels in
CC lung and spleen. {ECO:0000269|PubMed:11406273}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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; AK012021; BAB27978.1; -; mRNA.
DR EMBL; AL589870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003449; AAH03449.1; -; mRNA.
DR EMBL; BC019372; AAH19372.1; -; mRNA.
DR EMBL; AF303829; AAG22085.1; -; mRNA.
DR CCDS; CCDS17103.1; -. [Q9CZY3-1]
DR CCDS; CCDS79869.1; -. [Q9CZY3-2]
DR RefSeq; NP_001298075.1; NM_001311146.1. [Q9CZY3-2]
DR RefSeq; NP_075719.1; NM_023230.2. [Q9CZY3-1]
DR AlphaFoldDB; Q9CZY3; -.
DR SMR; Q9CZY3; -.
DR BioGRID; 211575; 12.
DR ComplexPortal; CPX-616; UBC13-UEV1A ubiquitin-conjugating enzyme E2 complex.
DR IntAct; Q9CZY3; 1.
DR STRING; 10090.ENSMUSP00000104830; -.
DR iPTMnet; Q9CZY3; -.
DR PhosphoSitePlus; Q9CZY3; -.
DR SwissPalm; Q9CZY3; -.
DR EPD; Q9CZY3; -.
DR jPOST; Q9CZY3; -.
DR MaxQB; Q9CZY3; -.
DR PaxDb; Q9CZY3; -.
DR PeptideAtlas; Q9CZY3; -.
DR PRIDE; Q9CZY3; -.
DR ProteomicsDB; 297692; -. [Q9CZY3-1]
DR ProteomicsDB; 297693; -. [Q9CZY3-2]
DR DNASU; 66589; -.
DR Ensembl; ENSMUST00000060645; ENSMUSP00000053109; ENSMUSG00000078923. [Q9CZY3-2]
DR Ensembl; ENSMUST00000109207; ENSMUSP00000104830; ENSMUSG00000078923. [Q9CZY3-1]
DR GeneID; 66589; -.
DR KEGG; mmu:66589; -.
DR UCSC; uc008oaa.1; mouse. [Q9CZY3-1]
DR UCSC; uc008oab.1; mouse. [Q9CZY3-2]
DR CTD; 7335; -.
DR MGI; MGI:1913839; Ube2v1.
DR VEuPathDB; HostDB:ENSMUSG00000078923; -.
DR eggNOG; KOG0896; Eukaryota.
DR GeneTree; ENSGT00940000158854; -.
DR HOGENOM; CLU_063065_3_0_1; -.
DR InParanoid; Q9CZY3; -.
DR OMA; NLPCVDQ; -.
DR PhylomeDB; Q9CZY3; -.
DR TreeFam; TF316971; -.
DR Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-937039; IRAK1 recruits IKK complex.
DR Reactome; R-MMU-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR Reactome; R-MMU-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 66589; 6 hits in 91 CRISPR screens.
DR ChiTaRS; Ube2v1; mouse.
DR PRO; PR:Q9CZY3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CZY3; protein.
DR Bgee; ENSMUSG00000078923; Expressed in embryonic post-anal tail and 60 other tissues.
DR ExpressionAtlas; Q9CZY3; baseline and differential.
DR Genevisible; Q9CZY3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035370; C:UBC13-UEV1A complex; ISS:UniProtKB.
DR GO; GO:0031371; C:ubiquitin conjugating enzyme complex; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:MGI.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IGI:MGI.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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 Acetylation; Alternative splicing; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13404"
FT CHAIN 2..147
FT /note="Ubiquitin-conjugating enzyme E2 variant 1"
FT /id="PRO_0000082601"
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:0000250|UniProtKB:Q13404"
FT VAR_SEQ 58..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011528"
FT CONFLICT 59
FT /note="I -> M (in Ref. 4; AAG22085)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="S -> G (in Ref. 4; AAG22085)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="A -> P (in Ref. 4; AAG22085)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="V -> M (in Ref. 4; AAG22085)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="L -> P (in Ref. 3; AAH19372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16355 MW; E66E83EEE9D08E92 CRC64;
MAATTGSGVK VPRNFRLLEE LEEGQKGVGD GTVSWGLEDD EDMTLTRWTG MIIGPPRTIY
ENRIYSLKIE CGPKYPEAPP SVRFVTRVNM SGVSSSNGVV DPRATAVLAK WQNSHSIKVI
LQELRRLMMS KENMKLPQPP EGQCYSN
