Kua-UEV

PEDS1-UBE2V1
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2A4D, 2C2V, 2HLW
Identifiers
Aliases	PEDS1-UBE2V1 , CROC-1B, CROC1B, KUA-UEV, Kua-UEV, TMEM189-UBE2V1 readthrough, PEDS1-UBE2V1 readthrough, TMEM189-UBE2V1
External IDs	HomoloGene: 100008 GeneCards: PEDS1-UBE2V1
Gene location (Human) Chr. Chromosome 20 (human) [1] Band 20q13.13 Start 50,081,124 bp [1] End 50,153,637 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium placenta prefrontal cortex right coronary artery right lung gastrocnemius muscle superior frontal gyrus monocyte vagina popliteal artery n/a More reference expression data BioGPS n/a
Gene ontology Molecular function ubiquitin protein ligase binding ubiquitin protein ligase activity protein binding ubiquitin conjugating enzyme activity Cellular component cytoplasm integral component of membrane endoplasmic reticulum membrane membrane endoplasmic reticulum cytosol ubiquitin conjugating enzyme complex UBC13-UEV1A complex ubiquitin ligase complex extracellular exosome nucleus nucleoplasm protein-containing complex Biological process protein ubiquitination 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 Species Human Mouse Entrez 387522 n/a Ensembl ENSG00000124208 n/a UniProt Q13404 n/a RefSeq (mRNA) NM_003349 NM_199203 n/a RefSeq (protein) NP_001155977 NP_954580 NP_954673 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 n/a Location (UCSC) Chr 20: 50.08 – 50.15 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

Ubiquitin-conjugating enzyme E2 variant 1, also known as Kua-UEV, is a human gene. ^[3]

The Kua-UEV mRNA is an infrequent but naturally occurring co-transcribed product of the neighboring Kua and UBE2V1 genes. ^[4] 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. Two alternative transcripts encoding different isoforms have been described. The proteins produced by these transcripts have UEV1 B domains but the proteins are localized to the cytoplasm rather than to the nucleus. The significance of these co-transcribed mRNAs and the function of their protein products have not yet been determined. ^[3]

References

1. GRCh38: Ensembl release 89: ENSG00000124208 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Entrez Gene: Kua-UEV ubiquitin-conjugating enzyme E2 variant 1".
4. Thomson TM, Lozano JJ, Loukili N, Carrió R, Serras F, Cormand B, et al. (November 2000). "Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene". Genome Research. 10 (11): 1743–56. doi:10.1101/gr.gr-1405r. PMC   310942 . PMID   11076860.

Further reading

• Long M (November 2000). "A new function evolved from gene fusion". Genome Research. 10 (11): 1655–7. doi: 10.1101/gr.165700 . PMID   11076848.
• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi: 10.1101/gr.6.9.791 . PMID   8889548.
• Rothofsky ML, Lin SL (August 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.
• Sancho E, Vilá MR, Sánchez-Pulido L, Lozano JJ, Paciucci R, Nadal M, et al. (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". Molecular and Cellular Biology. 18 (1): 576–89. doi:10.1128/mcb.18.1.576. PMC   121525 . PMID   9418904.
• Xiao W, Lin SL, Broomfield S, Chow BL, Wei YF (September 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 Research. 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 (September 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.
• Hofmann RM, Pickart CM (March 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, et al. (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.
• Thomson TM, Lozano JJ, Loukili N, Carrió R, Serras F, Cormand B, et al. (November 2000). "Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene". Genome Research. 10 (11): 1743–56. doi:10.1101/gr.GR-1405R. PMC   310942 . PMID   11076860.
• Dias DC, Dolios G, Wang R, Pan ZQ (December 2002). "CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16601–6. doi: 10.1073/pnas.252646399 . PMC   139190 . PMID   12481031.
• Guo D, Han J, Adam BL, Colburn NH, Wang MH, Dong Z, et al. (December 2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical Research Communications. 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID   16236267.