HIP2

Ubiquitin-conjugating enzyme E2 K is a protein that in humans is encoded by the UBE2K gene.[5][6][7]

UBE2K
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1YLA, 2O25, 3E46, 3F92, 3K9O, 3K9P, 5DFL
Identifiers
Aliases	UBE2K, E2-25K, HIP2, HYPG, LIG, UBC1, ubiquitin conjugating enzyme E2 K
External IDs	OMIM: 602846 MGI: 1858216 HomoloGene: 3903 GeneCards: UBE2K
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4p14 Start 39,698,109 bp[1] End 39,782,792 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 C3.1|5 33.72 cM Start 65,537,233 bp[2] End 65,598,988 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • ubiquitin-protein transferase activity • transferase activity • nucleotide binding • ubiquitin-ubiquitin ligase activity • GO:0001948 protein binding • ATP binding • ubiquitin protein ligase binding • ubiquitin conjugating enzyme activity Cellular component • cytoplasm • filopodium tip • cell nucleus • cytosol Biological process • protein K48-linked ubiquitination • positive regulation of type I interferon-mediated signaling pathway • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress • free ubiquitin chain polymerization • positive regulation of peptidyl-threonine phosphorylation • ubiquitin-dependent protein catabolic process • cellular response to interferon-beta • proteasome-mediated ubiquitin-dependent protein catabolic process • regulation of proteasomal ubiquitin-dependent protein catabolic process • protein ubiquitination Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3093	53323
Ensembl	ENSG00000078140	ENSMUSG00000029203
UniProt	P61086	P61087
RefSeq (mRNA)	NM_005339 NM_001111112 NM_001111113 NM_001312646 NM_001312647 NM_001312648	NM_016786 NM_001310618 NM_001310619
RefSeq (protein)	NP_001104582 NP_001104583 NP_001299575 NP_001299576 NP_001299577 NP_005330	NP_001297547 NP_001297548 NP_058066
Location (UCSC)	Chr 4: 39.7 – 39.78 Mb	Chr 5: 65.54 – 65.6 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene belongs to the ubiquitin-conjugating enzyme family. It binds selectively to a large region at the N terminus of huntingtin. This interaction is not influenced by the length of the huntingtin polyglutamine tract. This protein has been implicated in the degradation of huntingtin and suppression of apoptosis.[7]

Interactions

HIP2 has been shown to interact with Huntingtin[5][8] and RNF2.[9]

References

1. GRCh38: Ensembl release 89: ENSG00000078140 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029203 - 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. Kalchman MA, Graham RK, Xia G, Koide HB, Hodgson JG, Graham KC, Goldberg YP, Gietz RD, Pickart CM, Hayden MR (Sep 1996). "Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme". J Biol Chem. 271 (32): 19385–94. doi:10.1074/jbc.271.32.19385. PMID 8702625.
6. Christensen DE, Brzovic PS, Klevit RE (Oct 2007). "E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages". Nat Struct Mol Biol. 14 (10): 941–8. doi:10.1038/nsmb1295. PMID 17873885.
7. "Entrez Gene: HIP2 huntingtin interacting protein 2".
8. Faber PW, Barnes GT, Srinidhi J, Chen J, Gusella JF, MacDonald ME (Sep 1998). "Huntingtin interacts with a family of WW domain proteins". Hum. Mol. Genet. 7 (9): 1463–74. doi:10.1093/hmg/7.9.1463. PMID 9700202.
9. Lee SJ, Choi JY, Sung YM, Park H, Rhim H, Kang S (Aug 2001). "E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme". FEBS Lett. 503 (1): 61–4. doi:10.1016/S0014-5793(01)02689-8. PMID 11513855.

Further reading

• Petersén A, Mani K, Brundin P (1999). "Recent advances on the pathogenesis of Huntington's disease". Exp. Neurol. 157 (1): 1–18. doi:10.1006/exnr.1998.7006. PMID 10222105.
• Coux O, Goldberg AL (1998). "Enzymes catalyzing ubiquitination and proteolytic processing of the p105 precursor of nuclear factor kappaB1". J. Biol. Chem. 273 (15): 8820–8. doi:10.1074/jbc.273.15.8820. PMID 9535861.
• Whitby FG, Xia G, Pickart CM, Hill CP (1999). "Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes". J. Biol. Chem. 273 (52): 34983–91. doi:10.1074/jbc.273.52.34983. PMID 9857030.
• Kikuchi J, Furukawa Y, Kubo N, Tokura A, Hayashi N, Nakamura M, Matsuda M, Sakurabayashi I (2000). "Induction of ubiquitin-conjugating enzyme by aggregated low density lipoprotein in human macrophages and its implications for atherosclerosis". Arterioscler. Thromb. Vasc. Biol. 20 (1): 128–34. doi:10.1161/01.ATV.20.1.128. PMID 10634809.
• Furukawa Y, Kubo N, Kikuchi J, Tokura A, Fujita N, Sakurabayashi I (2000). "Regulation of macrophage-specific gene expression by degenerated lipoproteins". Electrophoresis. 21 (2): 338–46. doi:10.1002/(SICI)1522-2683(20000101)21:2<338::AID-ELPS338>3.0.CO;2-9. PMID 10675012.
• Lee SJ, Choi JY, Sung YM, Park H, Rhim H, Kang S (2001). "E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme". FEBS Lett. 503 (1): 61–4. doi:10.1016/S0014-5793(01)02689-8. PMID 11513855.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Goehler H, Lalowski M, Stelzl U, Waelter S, Stroedicke M, Worm U, Droege A, Lindenberg KS, Knoblich M, Haenig C, Herbst M, Suopanki J, Scherzinger E, Abraham C, Bauer B, Hasenbank R, Fritzsche A, Ludewig AH, Büssow K, Buessow K, Coleman SH, Gutekunst CA, Landwehrmeyer BG, Lehrach H, Wanker EE (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Mol. Cell. 15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Flierman D, Coleman CS, Pickart CM, Rapoport TA, Chau V (2006). "E2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell system". Proc. Natl. Acad. Sci. U.S.A. 103 (31): 11589–94. doi:10.1073/pnas.0605215103. PMC 1520313. PMID 16868077.
• de Pril R, Fischer DF, Roos RA, van Leeuwen FW (2007). "Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases". Mol. Cell. Neurosci. 34 (1): 10–9. doi:10.1016/j.mcn.2006.09.006. PMID 17092742.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.