UBE2V1

Protein-coding gene in the species Homo sapiens
UBE2V1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2A4D, 2C2V, 2HLW

Identifiers
AliasesUBE2V1, CIR1, CROC-1, CROC1, UBE2V, UEV-1, UEV1, UEV1A, ubiquitin conjugating enzyme E2 V1
External IDsOMIM: 602995; MGI: 1913839; HomoloGene: 81888; GeneCards: UBE2V1; OMA:UBE2V1 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for UBE2V1
Genomic location for UBE2V1
Band20q13.13Start50,081,124 bp[1]
End50,115,959 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for UBE2V1
Genomic location for UBE2V1
Band2 H3|2 87.44 cMStart167,449,558 bp[2]
End167,474,015 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • epithelium of colon

  • superior frontal gyrus

  • tonsil

  • smooth muscle tissue

  • placenta

  • ganglionic eminence

  • primary visual cortex

  • bone marrow cells

  • skin of leg

  • monocyte
Top expressed in
  • tail of embryo

  • epiblast

  • Cortex of frontal lobe

  • dentate gyrus of hippocampal formation granule cell

  • superior frontal gyrus

  • striatum of neuraxis

  • neural tube

  • urinary bladder

  • ventricular zone

  • primary visual cortex
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein binding
  • ubiquitin protein ligase activity
  • ubiquitin protein ligase binding
  • ubiquitin conjugating enzyme activity
Cellular component
  • cytoplasm
  • cytosol
  • ubiquitin conjugating enzyme complex
  • UBC13-UEV1A complex
  • ubiquitin ligase complex
  • extracellular exosome
  • nucleus
  • nucleoplasm
  • protein-containing complex
Biological process
  • protein polyubiquitination
  • Fc-epsilon receptor signaling pathway
  • protein K63-linked ubiquitination
  • nucleotide-binding oligomerization domain containing signaling pathway
  • positive regulation of transcription, DNA-templated
  • stimulatory C-type lectin receptor signaling pathway
  • regulation of DNA repair
  • regulation of transcription, DNA-templated
  • T cell receptor signaling pathway
  • cell differentiation
  • postreplication repair
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • JNK cascade
  • positive regulation of NF-kappaB transcription factor activity
  • interleukin-1-mediated signaling pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7335

66589

Ensembl

ENSG00000244687

ENSMUSG00000078923

UniProt

Q13404

Q9CZY3

RefSeq (mRNA)
NM_001032288
NM_001257393
NM_001257394
NM_001257395
NM_001257396

NM_001257397
NM_001257398
NM_001257399
NM_001282575
NM_001282576
NM_001282577
NM_001282578
NM_001282579
NM_001282580
NM_021988
NM_022442
NM_199144

NM_023230
NM_001311131
NM_001311146

RefSeq (protein)
NP_001027459
NP_001244322
NP_001244323
NP_001244324
NP_001244325

NP_001244326
NP_001244327
NP_001244328
NP_001269504
NP_001269505
NP_001269506
NP_001269507
NP_001269508
NP_001269509
NP_068823
NP_071887
NP_954595
NP_954673

NP_001298060
NP_001298075
NP_075719

Location (UCSC)Chr 20: 50.08 – 50.12 MbChr 2: 167.45 – 167.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ubiquitin-conjugating enzyme E2 variant 1 is a protein that in humans is encoded by the UBE2V1 gene.[5][6][7]

Function

Ubiquitin-conjugating E2 enzyme variant proteins constitute a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of E2s. The protein encoded by this gene is located in the nucleus and can cause transcriptional activation of the human FOS proto-oncogene. It is thought to be involved in the control of differentiation by altering cell cycle behavior. Multiple alternatively spliced transcripts encoding different isoforms have been described for this gene. A pseudogene has been identified which is also located on chromosome 20. Co-transcription of this gene and the neighboring upstream gene generates a rare transcript (Kua-UEV), which encodes a fusion protein consisting of sequence sharing identity with each individual gene product.[7]

Interactions

UBE2V1 has been shown to interact with UBE2N.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000244687 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000078923 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Sancho E, Vilá MR, Sánchez-Pulido L, Lozano JJ, Paciucci R, Nadal M, Fox M, Harvey C, Bercovich B, Loukili N, Ciechanover A, Lin SL, Sanz F, Estivill X, Valencia A, Thomson TM (January 1998). "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". Mol Cell Biol. 18 (1): 576–89. doi:10.1128/mcb.18.1.576. PMC 121525. PMID 9418904.
  6. ^ Rothofsky ML, Lin SL (October 1997). "CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter". Gene. 195 (2): 141–9. doi:10.1016/S0378-1119(97)00097-8. PMID 9305758.
  7. ^ a b "Entrez Gene: UBE2V1 ubiquitin-conjugating enzyme E2 variant 1".
  8. ^ Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (October 2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell. 103 (2): 351–61. doi:10.1016/S0092-8674(00)00126-4. PMID 11057907. S2CID 18154645.

Further reading

  • Long M (2001). "A new function evolved from gene fusion". Genome Res. 10 (11): 1655–7. doi:10.1101/gr.165700. PMID 11076848.
  • Thomson TM, Khalid H, Lozano JJ, Sancho E, Ariño J (1998). "Role of UEV-1A, a homologue of the tumor suppressor protein TSG101, in protection from DNA damage". FEBS Lett. 423 (1): 49–52. Bibcode:1998FEBSL.423...49T. doi:10.1016/S0014-5793(98)00060-X. PMID 9580084. S2CID 28536857.
  • Xiao W, Lin SL, Broomfield S, Chow BL, Wei YF (1998). "The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family". Nucleic Acids Res. 26 (17): 3908–14. doi:10.1093/nar/26.17.3908. PMC 147796. PMID 9705497.
  • Ma L, Broomfield S, Lavery C, Lin SL, Xiao W, Bacchetti S (1998). "Up-regulation of CIR1/CROC1 expression upon cell immortalization and in tumor-derived human cell lines". Oncogene. 17 (10): 1321–6. doi:10.1038/sj.onc.1202058. PMID 9771976. S2CID 9281963.
  • Hofmann RM, Pickart CM (1999). "Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair". Cell. 96 (5): 645–53. doi:10.1016/S0092-8674(00)80575-9. PMID 10089880. S2CID 17117789.
  • Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell. 103 (2): 351–61. doi:10.1016/S0092-8674(00)00126-4. PMID 11057907. S2CID 18154645.
  • Thomson TM, Lozano JJ, Loukili N, Carrió R, Serras F, Cormand B, Valeri M, Díaz VM, Abril J, Burset M, Merino J, Macaya A, Corominas M, Guigó R (2001). "Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene". Genome Res. 10 (11): 1743–56. doi:10.1101/gr.GR-1405R. PMC 310942. PMID 11076860.
  • Ito M, Shichijo S, Tsuda N, Ochi M, Harashima N, Saito N, Itoh K (2001). "Molecular basis of T cell-mediated recognition of pancreatic cancer cells". Cancer Res. 61 (5): 2038–46. PMID 11280764.
  • Andersen PL, Zhou H, Pastushok L, Moraes T, McKenna S, Ziola B, Ellison MJ, Dixit VM, Xiao W (2005). "Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A". J. Cell Biol. 170 (5): 745–55. doi:10.1083/jcb.200502113. PMC 2171356. PMID 16129784.
  • Hau DD, Lewis MJ, Saltibus LF, Pastushok L, Xiao W, Spyracopoulos L (2006). "Structure and interactions of the ubiquitin-conjugating enzyme variant human Uev1a: implications for enzymatic synthesis of polyubiquitin chains". Biochemistry. 45 (32): 9866–77. doi:10.1021/bi060631r. PMID 16893187.
  • Syed NA, Andersen PL, Warrington RC, Xiao W (2007). "Uev1A, a ubiquitin conjugating enzyme variant, inhibits stress-induced apoptosis through NF-kappaB activation". Apoptosis. 11 (12): 2147–57. doi:10.1007/s10495-006-0197-3. PMID 17041755. S2CID 6078250.
  • Petroski MD, Zhou X, Dong G, Daniel-Issakani S, Payan DG, Huang J (2007). "Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme". J. Biol. Chem. 282 (41): 29936–45. doi:10.1074/jbc.M703911200. PMID 17709375.
  • v
  • t
  • e
  • 1j74: Crystal Structure of Mms2
    1j74: Crystal Structure of Mms2
  • 1j7d: Crystal Structure of hMms2-hUbc13
    1j7d: Crystal Structure of hMms2-hUbc13
  • 1zgu: Solution structure of the human Mms2-Ubiquitin complex
    1zgu: Solution structure of the human Mms2-Ubiquitin complex
  • 2a4d: Structure of the human ubiquitin-conjugating enzyme E2 variant 1 (UEV-1)
    2a4d: Structure of the human ubiquitin-conjugating enzyme E2 variant 1 (UEV-1)
  • 2c2v: CRYSTAL STRUCTURE OF THE CHIP-UBC13-UEV1A COMPLEX
    2c2v: CRYSTAL STRUCTURE OF THE CHIP-UBC13-UEV1A COMPLEX
  • 2hlw: Solution Structure of the Human Ubiquitin-conjugating Enzyme Variant Uev1a
    2hlw: Solution Structure of the Human Ubiquitin-conjugating Enzyme Variant Uev1a
  • v
  • t
  • e
Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
(ubiquitylation)
Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other


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