Q13404 (UB2V1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 variant 1
Short name=UEV-1

Alternative name(s):
CROC-1
TRAF6-regulated IKK activator 1 beta Uev1A

Gene names

Name:	UBE2V1
Synonyms:	CROC1, UBE2V, UEV1
ORF Names:	P/OKcl.19

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. Ref.1 Ref.2 Ref.3 Ref.10 Ref.11 Ref.13 Ref.14
Subunit structure	Heterodimer with UBE2N. Interacts (UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with TRAF6. Ref.3
Subcellular location	Nucleus. Note: Excluded from the nucleolus. Ref.1 Ref.12
Tissue specificity	Highly expressed in thyroid, pancreas, spinal cord, lymph node, trachea, adrenal gland, bone marrow and pancreas. Detected at low levels in heart, breast, placenta, brain, liver, kidney, stomach and lung. Ref.2 Ref.11
Induction	Down-regulated during differentiation of cultured colon adenocarcinoma cells. Ref.2
Miscellaneous	In human, TMEM189/KUA and UBE2V1/UEV1 are adjacent genes which can produce independent proteins and can also be fused to form a TMEM189-UBE2V1 hybrid protein.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.
Sequence caution	The sequence AAH08944.2 differs from that shown. Reason: Erroneous initiation. The sequence CAC16955.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome T cell receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome cell differentiation Non-traceable author statement Ref.2. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome nucleotide-binding oligomerization domain containing signaling pathway Traceable author statement. Source: Reactome positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 16129784. Source: HGNC positive regulation of NF-kappaB transcription factor activity Inferred from mutant phenotype PubMed 16129784. Source: HGNC positive regulation of transcription, DNA-dependent Traceable author statement Ref.1. Source: UniProtKB protein K63-linked ubiquitination Inferred from direct assay Ref.15Ref.14. Source: UniProtKB regulation of DNA repair Traceable author statement PubMed 10089880. Source: ProtInc toll-like receptor 1 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome
Cellular_component	UBC13-UEV1A complex Inferred from direct assay Ref.15. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleus Traceable author statement Ref.1. Source: UniProtKB ubiquitin ligase complex Inferred from direct assay Ref.15. Source: UniProtKB
Molecular_function	acid-amino acid ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
UBE2N	P61088	9	EBI-1050671,EBI-1052908
XIAP	P98170	2	EBI-1050671,EBI-517127
ZNRF1	Q8ND25	2	EBI-1050671,EBI-2129250

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 3 (identifier: Q13404-4)

Also known as: Isoform 2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: Q13404-1)

Also known as: CROC-1B; UEV-1B; Isoform 4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MAATTGS → MAYKFRTHSP...PHETYFCITT

Isoform 2 (identifier: Q13404-2)

Also known as: CROC-1A; UEV-1A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MAATTGSGVKVPRN → MPGEVQASYLKSQSKLSDEGRLEPRKFHCKGSKSPSQ

Isoform 4 (identifier: Q13404-6)

Also known as: UEV-1As;

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-57: LTRWTGMIIGPPR → MKEDLNLENFTAK

Isoform 5 (identifier: Q13404-7)

Also known as: Isoform 3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MAATTGS → MPGEVQASYLKSQSKLSDEGRLEPRKFHCK

Isoform 6 (identifier: Q13404-8)

The sequence of this isoform differs from the canonical sequence as follows:
     58-99: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 147

146

Ubiquitin-conjugating enzyme E2 variant 1

PRO_0000082600

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8

Natural variations

Alternative sequence

1 – 44

44

Missing in isoform 4.

VSP_038032

Alternative sequence

1 – 14

14

MAATT…KVPRN → MPGEVQASYLKSQSKLSDEG RLEPRKFHCKGSKSPSQ in isoform 2.

VSP_038033

Alternative sequence

1 – 7

7

MAATTGS → MAYKFRTHSPEALEQLYPWE CFVFCLIIFGTFTNQIHKWS HTYFGLPRWVTLLQDWHVIL PRKHHRIHHVSPHETYFCIT T in isoform 1.

VSP_038034

Alternative sequence

1 – 7

7

MAATTGS → MPGEVQASYLKSQSKLSDEG RLEPRKFHCK in isoform 5.

VSP_038035

Alternative sequence

45 – 57

13

LTRWT…IGPPR → MKEDLNLENFTAK in isoform 4.

VSP_038036

Alternative sequence

58 – 99

42

Missing in isoform 6.

VSP_044818

Experimental info

Isoform 1:

Sequence conflict

71 – 81

11

SPHETYFCITT → WPTSSAQCYSP in AAC02755. Ref.2

Secondary structure

1

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147

Helix Strand Turn

Details...

Helix

11 – 25

15

Beta strand

31 – 39

9

Beta strand

47 – 53

7

Beta strand

56 – 58

3

Turn

59 – 62

4

Beta strand

64 – 70

7

Turn

73 – 77

5

Beta strand

81 – 86

6

Beta strand

91 – 93

3

Turn

95 – 97

3

Helix

102 – 104

3

Helix

106 – 109

4

Helix

117 – 128

12

Turn

131 – 135

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 (Isoform 2) [UniParc]. Last modified September 22, 2009. Version 2. Checksum: BA53837F21977B3F	FASTA	147	16,495
	10 20 30 40 50 60 MAATTGSGVK VPRNFRLLEE LEEGQKGVGD GTVSWGLEDD EDMTLTRWTG MIIGPPRTIY 70 80 90 100 110 120 ENRIYSLKIE CGPKYPEAPP FVRFVTKINM NGVNSSNGVV DPRAISVLAK WQNSYSIKVV 130 140 LQELRRLMMS KENMKLPQPP EGQCYSN
	Isoform 1 (CROC-1B) (UEV-1B) (Isoform 4) [UniParc]. Checksum: 6EE5C0FCC8CBBEE6	FASTA	221	25,797
	10 20 30 40 50 60 MAYKFRTHSP EALEQLYPWE CFVFCLIIFG TFTNQIHKWS HTYFGLPRWV TLLQDWHVIL 70 80 90 100 110 120 PRKHHRIHHV SPHETYFCIT TGVKVPRNFR LLEELEEGQK GVGDGTVSWG LEDDEDMTLT 130 140 150 160 170 180 RWTGMIIGPP RTIYENRIYS LKIECGPKYP EAPPFVRFVT KINMNGVNSS NGVVDPRAIS 190 200 210 220 VLAKWQNSYS IKVVLQELRR LMMSKENMKL PQPPEGQCYS N
	Isoform 2 (CROC-1A) (UEV-1A) [UniParc]. Checksum: 9D3A8AC1EBEB22A6	FASTA	170	19,228
	10 20 30 40 50 60 MPGEVQASYL KSQSKLSDEG RLEPRKFHCK GSKSPSQFRL LEELEEGQKG VGDGTVSWGL 70 80 90 100 110 120 EDDEDMTLTR WTGMIIGPPR TIYENRIYSL KIECGPKYPE APPFVRFVTK INMNGVNSSN 130 140 150 160 170 GVVDPRAISV LAKWQNSYSI KVVLQELRRL MMSKENMKLP QPPEGQCYSN
	Isoform 4 (UEV-1As) [UniParc]. Checksum: 76C152A73DE9AC40	FASTA	103	11,842
	10 20 30 40 50 60 MKEDLNLENF TAKTIYENRI YSLKIECGPK YPEAPPFVRF VTKINMNGVN SSNGVVDPRA 70 80 90 100 ISVLAKWQNS YSIKVVLQEL RRLMMSKENM KLPQPPEGQC YSN
	Isoform 5 (Isoform 3) [UniParc]. Checksum: 5B2E8C6FFDF51510	FASTA	170	19,307
	10 20 30 40 50 60 MPGEVQASYL KSQSKLSDEG RLEPRKFHCK GVKVPRNFRL LEELEEGQKG VGDGTVSWGL 70 80 90 100 110 120 EDDEDMTLTR WTGMIIGPPR TIYENRIYSL KIECGPKYPE APPFVRFVTK INMNGVNSSN 130 140 150 160 170 GVVDPRAISV LAKWQNSYSI KVVLQELRRL MMSKENMKLP QPPEGQCYSN
	Isoform 6 [UniParc]. Checksum: D7C2659FBA3FC719	FASTA	105	11,766
	10 20 30 40 50 60 MAATTGSGVK VPRNFRLLEE LEEGQKGVGD GTVSWGLEDD EDMTLTRWTG MIIGPPRVDP 70 80 90 100 RAISVLAKWQ NSYSIKVVLQ ELRRLMMSKE NMKLPQPPEG QCYSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter." Rothofsky M.L., Lin S.L. Gene 195:141-149(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION. Tissue: Brain.
[2]	"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." 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. Mol. Cell. Biol. 18:576-589(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION, INDUCTION, TISSUE SPECIFICITY. Tissue: Colon adenocarcinoma.
[3]	"Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain." Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C., Pickart C., Chen Z.J. Cell 103:351-361(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH TRAF6 AND UBE2N, MASS SPECTROMETRY.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Tissue: Lung.
[6]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Bienvenut W.V., Pchelintsev N., Adams P.D. Submitted (JUL-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13 (ISOFORM 3), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Lung fibroblast.
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-147 (ISOFORMS 1 AND 3). Tissue: Muscle.
[10]	"Role of UEV-1A, a homologue of the tumor suppressor protein TSG101, in protection from DNA damage." Thomson T.M., Khalid H., Lozano J.J., Sancho E., Arino J. FEBS Lett. 423:49-52(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family." Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.-F. Nucleic Acids Res. 26:3908-3914(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]	"Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene." 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. Genome Res. 10:1743-1756(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION OF TMEM189-UBE2V1 FUSION PROTEIN. Tissue: Colon cancer.
[13]	"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines." David Y., Ziv T., Admon A., Navon A. J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"TRIM5 is an innate immune sensor for the retrovirus capsid lattice." Pertel T., Hausmann S., Morger D., Zueger 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., Gruetter M.G., Luban J. Nature 472:361-365(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex." Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H. Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 8-147 IN COMPLEX WITH STUB1 AND UBE2N.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U39360 mRNA. Translation: AAB72015.1.
U39361 mRNA. Translation: AAB72016.1.
U49278 mRNA. Translation: AAC02757.1.
U97279 mRNA. Translation: AAC02780.1.
U97280 mRNA. Translation: AAC02755.1.
U97281 mRNA. Translation: AAC02756.1.
AY008273 mRNA. Translation: AAG24229.1.
BT007382 mRNA. Translation: AAP36046.1.
DA580976 mRNA. No translation available.
AL034423 Genomic DNA. Translation: CAB76864.1.
AL034423 Genomic DNA. Translation: CAB76865.1.
AL034423 Genomic DNA. Translation: CAC16954.1.
AL034423 Genomic DNA. Translation: CAC16955.2. Different initiation.
AL034423 Genomic DNA. Translation: CAI19382.1.
AL034423 Genomic DNA. Translation: CAI19383.1.
CH471077 Genomic DNA. Translation: EAW75635.1.
CH471077 Genomic DNA. Translation: EAW75634.1.
CH471077 Genomic DNA. Translation: EAW75636.1.
BC000468 mRNA. Translation: AAH00468.1.
BC008944 mRNA. Translation: AAH08944.2. Different initiation.

IPI

IPI00007847.
IPI00019599.
IPI00030962.
IPI00447356.
IPI00472498.
IPI00514724.

RefSeq

NP_001027459.1. NM_001032288.2.
NP_001244322.1. NM_001257393.1.
NP_001244323.1. NM_001257394.1.
NP_001244325.1. NM_001257396.1.
NP_068823.2. NM_021988.5.
NP_071887.1. NM_022442.5.
NP_954595.1. NM_199144.2.
NP_954673.1. NM_199203.2.

UniGene

Hs.420529.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A4D	X-ray	1.69	A	8-147	[»]
2C2V	X-ray	2.90	C/F/I/L	8-147	[»]
2HLW	NMR	-	A	8-147	[»]

ProteinModelPortal

Q13404.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41911N.

IntAct

Q13404. 27 interactions.

MINT

MINT-5002796.

Polymorphism databases

DMDM

259016163.

Proteomic databases

PaxDb

Q13404.

PRIDE

Q13404.

Protocols and materials databases

DNASU

387522.
7335.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000340309; ENSP00000340305; ENSG00000244687.
ENST00000371657; ENSP00000360720; ENSG00000244687.
ENST00000371674; ENSP00000360739; ENSG00000244687.
ENST00000371677; ENSP00000360742; ENSG00000244687.
ENST00000415862; ENSP00000407770; ENSG00000244687.
ENST00000420027; ENSP00000395264; ENSG00000244687.

GeneID

387522.
7335.

KEGG

hsa:387522.
hsa:7335.

UCSC

uc002xva.3. human.
uc002xvc.3. human.
uc002xvd.3. human.
uc002xvf.3. human.

Organism-specific databases

CTD

387522.
7335.

GeneCards

GC20M048697.
GC20M048698.

HGNC

HGNC:12494. UBE2V1.

MIM

602995. gene.

neXtProt

NX_Q13404.

PharmGKB

PA37142.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG119330.

HOVERGEN

HBG054552.

InParanoid

Q13404.

KO

K10704.

OMA

IECGERY.

OrthoDB

EOG4VHK75.

Enzyme and pathway databases

Pathway_Interaction_DB

il1pathway. IL1-mediated signaling events.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q13404.

Bgee

Q13404.

Genevestigator

Q13404.

GermOnline

ENSG00000124208. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5234.

ChiTaRS

UBE2V1. human.

EvolutionaryTrace

Q13404.

GenomeRNAi

7335.

NextBio

101372.

SOURCE

Search...

Entry information

Entry name

UB2V1_HUMAN

Accession

Primary (citable) accession number: Q13404
Secondary accession number(s): E1P629 , Q13403, Q13532, Q5TGE0, Q5TGE3, Q96H34, Q9GZT0, Q9GZW1, Q9H4J3, Q9H4J4, Q9UKL1, Q9UM48, Q9UM49, Q9UM50

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	September 22, 2009
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.