Full text data of UBE2K
UBE2K
(HIP2, LIG)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-conjugating enzyme E2 K; 6.3.2.19 (Huntingtin-interacting protein 2; HIP-2; Ubiquitin carrier protein; Ubiquitin-conjugating enzyme E2-25 kDa; Ubiquitin-conjugating enzyme E2(25K); Ubiquitin-conjugating enzyme E2-25K; Ubiquitin-protein ligase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-conjugating enzyme E2 K; 6.3.2.19 (Huntingtin-interacting protein 2; HIP-2; Ubiquitin carrier protein; Ubiquitin-conjugating enzyme E2-25 kDa; Ubiquitin-conjugating enzyme E2(25K); Ubiquitin-conjugating enzyme E2-25K; Ubiquitin-protein ligase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61086
ID UBE2K_HUMAN Reviewed; 200 AA.
AC P61086; A6NJC1; A8K5Y9; B2RDF8; C9JGP1; O54806; P27924; Q16721;
read moreAC Q9CVV9; Q9Y2D3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 K;
DE EC=6.3.2.19;
DE AltName: Full=Huntingtin-interacting protein 2;
DE Short=HIP-2;
DE AltName: Full=Ubiquitin carrier protein;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-25 kDa;
DE Short=Ubiquitin-conjugating enzyme E2(25K);
DE Short=Ubiquitin-conjugating enzyme E2-25K;
DE AltName: Full=Ubiquitin-protein ligase;
GN Name=UBE2K; Synonyms=HIP2, LIG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8702625; DOI=10.1074/jbc.271.32.19385;
RA Kalchman M.A., Graham R.K., Xia G., Koide H.B., Hodgson J.G.,
RA Graham K.C., Goldberg Y.P., Gietz R.D., Pickart C.M., Hayden M.R.;
RT "Huntingtin is ubiquitinated and interacts with a specific ubiquitin-
RT conjugating enzyme.";
RL J. Biol. Chem. 271:19385-19394(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=10634809;
RA Kikuchi J., Furukawa Y., Kubo N., Tokura A., Hayashi N., Nakamura M.,
RA Matsuda M., Sakurabayashi I.;
RT "Induction of ubiquitin-conjugating enzyme by aggregated low density
RT lipoprotein in human macrophages and its implications for
RT atherosclerosis.";
RL Arterioscler. Thromb. Vasc. Biol. 20:128-134(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=10675012;
RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<338::AID-ELPS338>3.0.CO;2-9;
RA Furukawa Y., Kubo N., Kikuchi J., Tokura A., Fujita N.,
RA Sakurabayashi I.;
RT "Regulation of macrophage-specific gene expression by degenerated
RT lipoproteins.";
RL Electrophoresis 21:338-346(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-10; 62-72; 79-97 AND 166-186, FUNCTION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RNF138.
RX PubMed=16714285; DOI=10.1074/jbc.M602089200;
RA Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K.,
RA Hyodo-Miura J., Kawachi K., Natsume T., Shibuya H.;
RT "NARF, an nemo-like kinase (NLK)-associated ring finger protein
RT regulates the ubiquitylation and degradation of T cell factor/lymphoid
RT enhancer factor (TCF/LEF).";
RL J. Biol. Chem. 281:20749-20760(2006).
RN [10]
RP PROTEIN SEQUENCE OF 2-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP PROTEIN SEQUENCE OF 2-8; 56-72 AND 177-186, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL Submitted (JAN-2010) to UniProtKB.
RN [12]
RP FUNCTION IN DEGRADATION OF MHC CLASS I HEAVY CHAINS.
RX PubMed=16868077; DOI=10.1073/pnas.0605215103;
RA Flierman D., Coleman C.S., Pickart C.M., Rapoport T.A., Chau V.;
RT "E2-25K mediates US11-triggered retro-translocation of MHC class I
RT heavy chains in a permeabilized cell system.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11589-11594(2006).
RN [13]
RP FUNCTION IN POLYUBIQUITINATION, AND INTERACTION WITH BRCA1.
RX PubMed=17873885; DOI=10.1038/nsmb1295;
RA Christensen D.E., Brzovic P.S., Klevit R.E.;
RT "E2-BRCA1 RING interactions dictate synthesis of mono- or specific
RT polyubiquitin chain linkages.";
RL Nat. Struct. Mol. Biol. 14:941-948(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP FUNCTION.
RX PubMed=20061386; DOI=10.1074/jbc.M109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [16]
RP FUNCTION IN VIRUS-INDUCED DEGRADATION OF RB1.
RX PubMed=19906396; DOI=10.1016/j.virol.2009.10.018;
RA Oh K.J., Kalinina A., Bagchi S.;
RT "Destabilization of Rb by human papillomavirus E7 is cell cycle
RT dependent: E2-25K is involved in the proteolysis.";
RL Virology 396:118-124(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP MUTAGENESIS OF ASP-94.
RX PubMed=21532592; DOI=10.1038/nature09966;
RA Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E.;
RT "UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT
RT hybrids.";
RL Nature 474:105-108(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
RX PubMed=19407372; DOI=10.1107/S1744309109011117;
RA Wilson R.C., Hughes R.C., Flatt J.W., Meehan E.J., Ng J.D.,
RA Twigg P.D.;
RT "Structure of full-length ubiquitin-conjugating enzyme E2-25K
RT (Huntingtin-interacting protein 2).";
RL Acta Crystallogr. F 65:440-444(2009).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBE2I.
RG Structural genomics consortium (SGC);
RT "A novel and unexpected complex between the SUMO-1-conjugating enzyme
RT UBC9 and the ubiquitin-conjugating enzyme E2-25 kDA.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "Ubiquitin-conjugating enzyme E2-25 kDA (Huntington-interacting
RT protein 2).";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro, in the presence
CC or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase
CC complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin
CC chains. Does not transfer ubiquitin directly to but elongates
CC monoubiquitinated substrate protein. Mediates the selective
CC degradation of short-lived and abnormal proteins, such as the
CC endoplasmic reticulum-associated degradation (ERAD) of misfolded
CC lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell
CC formation by the suppression of apoptosis of lipid-bearing
CC macrophages through ubiquitination and subsequence degradation of
CC p53/TP53. Proposed to be involved in ubiquitination and
CC proteolytic processing of NF-kappa-B; in vitro supports
CC ubiquitination of NFKB1. In case of infection by cytomegaloviruses
CC may be involved in the US11-dependent degradation of MHC class I
CC heavy chains following their export from the ER to the cytosol. In
CC case of viral infections may be involved in the HPV E7 protein-
CC dependent degradation of RB1.
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RNF138/NARF. Interacts with BRCA1.
CC -!- INTERACTION:
CC P14635:CCNB1; NbExp=2; IntAct=EBI-473850, EBI-495332;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P61086-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61086-2; Sequence=VSP_011798;
CC Note=May be inactive;
CC Name=3;
CC IsoId=P61086-3; Sequence=VSP_046211;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including
CC spleen, thymus, prostate, testis, ovary, small intestine, colon,
CC peripheral blood leukocytes, T-lymphocytes, monocytes,
CC granulocytes and bone marrow mononuclear cells. Highly expressed
CC in brain, with highest levels found in cortex and striatum and at
CC lower levels in cerebellum and brainstem.
CC -!- INDUCTION: By aggregated low-density lipoprotein.
CC -!- PTM: Sumoylation at Lys-14 impairs catalytic activity (By
CC similarity).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U58522; AAC50633.1; -; mRNA.
DR EMBL; AB022435; BAA78555.1; -; mRNA.
DR EMBL; AB022436; BAA78556.1; -; mRNA.
DR EMBL; BX339118; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK291454; BAF84143.1; -; mRNA.
DR EMBL; AK315524; BAG37905.1; -; mRNA.
DR EMBL; AC105287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471069; EAW92948.1; -; Genomic_DNA.
DR EMBL; BC022804; AAH22804.1; -; mRNA.
DR EMBL; BC050600; AAH50600.1; -; mRNA.
DR RefSeq; NP_001104582.1; NM_001111112.1.
DR RefSeq; NP_001104583.1; NM_001111113.1.
DR RefSeq; NP_005330.1; NM_005339.4.
DR UniGene; Hs.50308; -.
DR PDB; 1YLA; X-ray; 2.40 A; A/B=1-200.
DR PDB; 2O25; X-ray; 2.60 A; A/B=1-200.
DR PDB; 3E46; X-ray; 1.86 A; A=1-200.
DR PDB; 3F92; X-ray; 2.23 A; A=1-200.
DR PDB; 3K9O; X-ray; 1.80 A; A=1-200.
DR PDB; 3K9P; X-ray; 2.80 A; A=1-200.
DR PDBsum; 1YLA; -.
DR PDBsum; 2O25; -.
DR PDBsum; 3E46; -.
DR PDBsum; 3F92; -.
DR PDBsum; 3K9O; -.
DR PDBsum; 3K9P; -.
DR ProteinModelPortal; P61086; -.
DR SMR; P61086; 3-200.
DR IntAct; P61086; 11.
DR MINT; MINT-5000019; -.
DR PhosphoSite; P61086; -.
DR DMDM; 46577658; -.
DR OGP; P27924; -.
DR PaxDb; P61086; -.
DR PeptideAtlas; P61086; -.
DR PRIDE; P61086; -.
DR DNASU; 3093; -.
DR Ensembl; ENST00000261427; ENSP00000261427; ENSG00000078140.
DR Ensembl; ENST00000445950; ENSP00000390483; ENSG00000078140.
DR Ensembl; ENST00000503368; ENSP00000421203; ENSG00000078140.
DR GeneID; 3093; -.
DR KEGG; hsa:3093; -.
DR UCSC; uc003gus.4; human.
DR CTD; 3093; -.
DR GeneCards; GC04P039700; -.
DR HGNC; HGNC:4914; UBE2K.
DR HPA; CAB033212; -.
DR HPA; CAB033515; -.
DR HPA; HPA028869; -.
DR MIM; 602846; gene.
DR neXtProt; NX_P61086; -.
DR PharmGKB; PA162407874; -.
DR eggNOG; COG5078; -.
DR HOVERGEN; HBG063308; -.
DR InParanoid; P61086; -.
DR KO; K04649; -.
DR OMA; KHWTNAY; -.
DR OrthoDB; EOG7F513F; -.
DR Reactome; REACT_107772; Immune System.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P61086; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P61086; -.
DR GeneWiki; HIP2; -.
DR GenomeRNAi; 3093; -.
DR NextBio; 12275; -.
DR PRO; PR:P61086; -.
DR ArrayExpress; P61086; -.
DR Bgee; P61086; -.
DR CleanEx; HS_UBE2K; -.
DR Genevestigator; P61086; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 200 Ubiquitin-conjugating enzyme E2 K.
FT /FTId=PRO_0000082443.
FT DOMAIN 160 200 UBA.
FT ACT_SITE 92 92 Glycyl thioester intermediate (By
FT similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 14 14 N6-acetyllysine; alternate.
FT CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO);
FT alternate (By similarity).
FT VAR_SEQ 22 72 Missing (in isoform 2).
FT /FTId=VSP_011798.
FT VAR_SEQ 134 176 Missing (in isoform 3).
FT /FTId=VSP_046211.
FT MUTAGEN 94 94 D->E: Decreased lysine reactivity and
FT impaired formation of free polyubiquitin
FT chains.
FT HELIX 6 17
FT HELIX 20 23
FT STRAND 26 31
FT STRAND 33 35
FT STRAND 36 44
FT STRAND 47 49
FT TURN 50 53
FT STRAND 55 61
FT TURN 64 68
FT STRAND 72 77
FT TURN 86 88
FT HELIX 94 96
FT TURN 97 99
FT HELIX 106 118
FT HELIX 128 136
FT HELIX 138 153
FT HELIX 160 170
FT TURN 171 173
FT HELIX 176 185
FT TURN 186 188
FT HELIX 190 199
SQ SEQUENCE 200 AA; 22407 MW; E40668099ED25828 CRC64;
MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP YEGGRYQLEI
KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW AAAMTLRTVL LSLQALLAAA
EPDDPQDAVV ANQYKQNPEM FKQTARLWAH VYAGAPVSSP EYTKKIENLC AMGFDRNAVI
VALSSKSWDV ETATELLLSN
//
ID UBE2K_HUMAN Reviewed; 200 AA.
AC P61086; A6NJC1; A8K5Y9; B2RDF8; C9JGP1; O54806; P27924; Q16721;
read moreAC Q9CVV9; Q9Y2D3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 K;
DE EC=6.3.2.19;
DE AltName: Full=Huntingtin-interacting protein 2;
DE Short=HIP-2;
DE AltName: Full=Ubiquitin carrier protein;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-25 kDa;
DE Short=Ubiquitin-conjugating enzyme E2(25K);
DE Short=Ubiquitin-conjugating enzyme E2-25K;
DE AltName: Full=Ubiquitin-protein ligase;
GN Name=UBE2K; Synonyms=HIP2, LIG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8702625; DOI=10.1074/jbc.271.32.19385;
RA Kalchman M.A., Graham R.K., Xia G., Koide H.B., Hodgson J.G.,
RA Graham K.C., Goldberg Y.P., Gietz R.D., Pickart C.M., Hayden M.R.;
RT "Huntingtin is ubiquitinated and interacts with a specific ubiquitin-
RT conjugating enzyme.";
RL J. Biol. Chem. 271:19385-19394(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=10634809;
RA Kikuchi J., Furukawa Y., Kubo N., Tokura A., Hayashi N., Nakamura M.,
RA Matsuda M., Sakurabayashi I.;
RT "Induction of ubiquitin-conjugating enzyme by aggregated low density
RT lipoprotein in human macrophages and its implications for
RT atherosclerosis.";
RL Arterioscler. Thromb. Vasc. Biol. 20:128-134(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=10675012;
RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<338::AID-ELPS338>3.0.CO;2-9;
RA Furukawa Y., Kubo N., Kikuchi J., Tokura A., Fujita N.,
RA Sakurabayashi I.;
RT "Regulation of macrophage-specific gene expression by degenerated
RT lipoproteins.";
RL Electrophoresis 21:338-346(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-10; 62-72; 79-97 AND 166-186, FUNCTION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RNF138.
RX PubMed=16714285; DOI=10.1074/jbc.M602089200;
RA Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K.,
RA Hyodo-Miura J., Kawachi K., Natsume T., Shibuya H.;
RT "NARF, an nemo-like kinase (NLK)-associated ring finger protein
RT regulates the ubiquitylation and degradation of T cell factor/lymphoid
RT enhancer factor (TCF/LEF).";
RL J. Biol. Chem. 281:20749-20760(2006).
RN [10]
RP PROTEIN SEQUENCE OF 2-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP PROTEIN SEQUENCE OF 2-8; 56-72 AND 177-186, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL Submitted (JAN-2010) to UniProtKB.
RN [12]
RP FUNCTION IN DEGRADATION OF MHC CLASS I HEAVY CHAINS.
RX PubMed=16868077; DOI=10.1073/pnas.0605215103;
RA Flierman D., Coleman C.S., Pickart C.M., Rapoport T.A., Chau V.;
RT "E2-25K mediates US11-triggered retro-translocation of MHC class I
RT heavy chains in a permeabilized cell system.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11589-11594(2006).
RN [13]
RP FUNCTION IN POLYUBIQUITINATION, AND INTERACTION WITH BRCA1.
RX PubMed=17873885; DOI=10.1038/nsmb1295;
RA Christensen D.E., Brzovic P.S., Klevit R.E.;
RT "E2-BRCA1 RING interactions dictate synthesis of mono- or specific
RT polyubiquitin chain linkages.";
RL Nat. Struct. Mol. Biol. 14:941-948(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP FUNCTION.
RX PubMed=20061386; DOI=10.1074/jbc.M109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [16]
RP FUNCTION IN VIRUS-INDUCED DEGRADATION OF RB1.
RX PubMed=19906396; DOI=10.1016/j.virol.2009.10.018;
RA Oh K.J., Kalinina A., Bagchi S.;
RT "Destabilization of Rb by human papillomavirus E7 is cell cycle
RT dependent: E2-25K is involved in the proteolysis.";
RL Virology 396:118-124(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP MUTAGENESIS OF ASP-94.
RX PubMed=21532592; DOI=10.1038/nature09966;
RA Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E.;
RT "UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT
RT hybrids.";
RL Nature 474:105-108(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
RX PubMed=19407372; DOI=10.1107/S1744309109011117;
RA Wilson R.C., Hughes R.C., Flatt J.W., Meehan E.J., Ng J.D.,
RA Twigg P.D.;
RT "Structure of full-length ubiquitin-conjugating enzyme E2-25K
RT (Huntingtin-interacting protein 2).";
RL Acta Crystallogr. F 65:440-444(2009).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBE2I.
RG Structural genomics consortium (SGC);
RT "A novel and unexpected complex between the SUMO-1-conjugating enzyme
RT UBC9 and the ubiquitin-conjugating enzyme E2-25 kDA.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "Ubiquitin-conjugating enzyme E2-25 kDA (Huntington-interacting
RT protein 2).";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro, in the presence
CC or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase
CC complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin
CC chains. Does not transfer ubiquitin directly to but elongates
CC monoubiquitinated substrate protein. Mediates the selective
CC degradation of short-lived and abnormal proteins, such as the
CC endoplasmic reticulum-associated degradation (ERAD) of misfolded
CC lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell
CC formation by the suppression of apoptosis of lipid-bearing
CC macrophages through ubiquitination and subsequence degradation of
CC p53/TP53. Proposed to be involved in ubiquitination and
CC proteolytic processing of NF-kappa-B; in vitro supports
CC ubiquitination of NFKB1. In case of infection by cytomegaloviruses
CC may be involved in the US11-dependent degradation of MHC class I
CC heavy chains following their export from the ER to the cytosol. In
CC case of viral infections may be involved in the HPV E7 protein-
CC dependent degradation of RB1.
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RNF138/NARF. Interacts with BRCA1.
CC -!- INTERACTION:
CC P14635:CCNB1; NbExp=2; IntAct=EBI-473850, EBI-495332;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P61086-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61086-2; Sequence=VSP_011798;
CC Note=May be inactive;
CC Name=3;
CC IsoId=P61086-3; Sequence=VSP_046211;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including
CC spleen, thymus, prostate, testis, ovary, small intestine, colon,
CC peripheral blood leukocytes, T-lymphocytes, monocytes,
CC granulocytes and bone marrow mononuclear cells. Highly expressed
CC in brain, with highest levels found in cortex and striatum and at
CC lower levels in cerebellum and brainstem.
CC -!- INDUCTION: By aggregated low-density lipoprotein.
CC -!- PTM: Sumoylation at Lys-14 impairs catalytic activity (By
CC similarity).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U58522; AAC50633.1; -; mRNA.
DR EMBL; AB022435; BAA78555.1; -; mRNA.
DR EMBL; AB022436; BAA78556.1; -; mRNA.
DR EMBL; BX339118; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK291454; BAF84143.1; -; mRNA.
DR EMBL; AK315524; BAG37905.1; -; mRNA.
DR EMBL; AC105287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471069; EAW92948.1; -; Genomic_DNA.
DR EMBL; BC022804; AAH22804.1; -; mRNA.
DR EMBL; BC050600; AAH50600.1; -; mRNA.
DR RefSeq; NP_001104582.1; NM_001111112.1.
DR RefSeq; NP_001104583.1; NM_001111113.1.
DR RefSeq; NP_005330.1; NM_005339.4.
DR UniGene; Hs.50308; -.
DR PDB; 1YLA; X-ray; 2.40 A; A/B=1-200.
DR PDB; 2O25; X-ray; 2.60 A; A/B=1-200.
DR PDB; 3E46; X-ray; 1.86 A; A=1-200.
DR PDB; 3F92; X-ray; 2.23 A; A=1-200.
DR PDB; 3K9O; X-ray; 1.80 A; A=1-200.
DR PDB; 3K9P; X-ray; 2.80 A; A=1-200.
DR PDBsum; 1YLA; -.
DR PDBsum; 2O25; -.
DR PDBsum; 3E46; -.
DR PDBsum; 3F92; -.
DR PDBsum; 3K9O; -.
DR PDBsum; 3K9P; -.
DR ProteinModelPortal; P61086; -.
DR SMR; P61086; 3-200.
DR IntAct; P61086; 11.
DR MINT; MINT-5000019; -.
DR PhosphoSite; P61086; -.
DR DMDM; 46577658; -.
DR OGP; P27924; -.
DR PaxDb; P61086; -.
DR PeptideAtlas; P61086; -.
DR PRIDE; P61086; -.
DR DNASU; 3093; -.
DR Ensembl; ENST00000261427; ENSP00000261427; ENSG00000078140.
DR Ensembl; ENST00000445950; ENSP00000390483; ENSG00000078140.
DR Ensembl; ENST00000503368; ENSP00000421203; ENSG00000078140.
DR GeneID; 3093; -.
DR KEGG; hsa:3093; -.
DR UCSC; uc003gus.4; human.
DR CTD; 3093; -.
DR GeneCards; GC04P039700; -.
DR HGNC; HGNC:4914; UBE2K.
DR HPA; CAB033212; -.
DR HPA; CAB033515; -.
DR HPA; HPA028869; -.
DR MIM; 602846; gene.
DR neXtProt; NX_P61086; -.
DR PharmGKB; PA162407874; -.
DR eggNOG; COG5078; -.
DR HOVERGEN; HBG063308; -.
DR InParanoid; P61086; -.
DR KO; K04649; -.
DR OMA; KHWTNAY; -.
DR OrthoDB; EOG7F513F; -.
DR Reactome; REACT_107772; Immune System.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P61086; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P61086; -.
DR GeneWiki; HIP2; -.
DR GenomeRNAi; 3093; -.
DR NextBio; 12275; -.
DR PRO; PR:P61086; -.
DR ArrayExpress; P61086; -.
DR Bgee; P61086; -.
DR CleanEx; HS_UBE2K; -.
DR Genevestigator; P61086; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 200 Ubiquitin-conjugating enzyme E2 K.
FT /FTId=PRO_0000082443.
FT DOMAIN 160 200 UBA.
FT ACT_SITE 92 92 Glycyl thioester intermediate (By
FT similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 14 14 N6-acetyllysine; alternate.
FT CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO);
FT alternate (By similarity).
FT VAR_SEQ 22 72 Missing (in isoform 2).
FT /FTId=VSP_011798.
FT VAR_SEQ 134 176 Missing (in isoform 3).
FT /FTId=VSP_046211.
FT MUTAGEN 94 94 D->E: Decreased lysine reactivity and
FT impaired formation of free polyubiquitin
FT chains.
FT HELIX 6 17
FT HELIX 20 23
FT STRAND 26 31
FT STRAND 33 35
FT STRAND 36 44
FT STRAND 47 49
FT TURN 50 53
FT STRAND 55 61
FT TURN 64 68
FT STRAND 72 77
FT TURN 86 88
FT HELIX 94 96
FT TURN 97 99
FT HELIX 106 118
FT HELIX 128 136
FT HELIX 138 153
FT HELIX 160 170
FT TURN 171 173
FT HELIX 176 185
FT TURN 186 188
FT HELIX 190 199
SQ SEQUENCE 200 AA; 22407 MW; E40668099ED25828 CRC64;
MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP YEGGRYQLEI
KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW AAAMTLRTVL LSLQALLAAA
EPDDPQDAVV ANQYKQNPEM FKQTARLWAH VYAGAPVSSP EYTKKIENLC AMGFDRNAVI
VALSSKSWDV ETATELLLSN
//
MIM
602846
*RECORD*
*FIELD* NO
602846
*FIELD* TI
*602846 HUNTINGTIN-INTERACTING PROTEIN 2; HIP2
;;UBIQUITIN-CONJUGATING ENZYME E2-25K
read more*FIELD* TX
DESCRIPTION
Huntington disease (HD; 143100) may be caused by a toxic
gain-of-function due to abnormal protein-protein interactions. Protein
that interact with huntingtin (HTT; 613004) include the glycolytic
enzyme GAPD (138400), huntingtin-associated protein (600947), and
huntingtin-interacting protein-1 (HIP1; 601767).
CLONING
Kalchman et al. (1996) used the yeast 2-hybrid system to identify the
HIP2 protein. The 200-amino acid HIP2 protein sequence was identical to
that of bovine ubiquitin-conjugating enzyme E2-25K. Assays of the
interaction of HIP2 with huntingtin revealed that HIP2 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.
Northern blot analysis revealed that HIP2 is transcribed as 1.2 and
1.4-kb mRNAs in all human tissues studied. Western blot analysis
detected protein bands of 25, 28, and 45 kD; the 28-kD band appeared to
be selective for tissues of the central nervous system. Kalchman et al.
(1996) showed that huntingtin is ubiquitinated in peripheral cells,
suggesting a role for HIP2 in the degradation of huntingtin.
MAPPING
Kalchman et al. (1996) used fluorescence in situ hybridization to map
the HIP2 gene to human chromosome 4p14.
*FIELD* RF
1. Kalchman, M. A.; Graham, R. K.; Xia, G.; Koide, H. B.; Hodgson,
J. G.; Graham, K. C.; Goldberg, Y. P.; Gietz, R. D.; Pickart, C. M.;
Hayden, M. R.: Huntingtin is ubiquitinated and interacts with a specific
ubiquitin-conjugating enzyme. J. Biol. Chem. 271: 19385-19394, 1996.
*FIELD* CD
Jennifer P. Macke: 7/14/1998
*FIELD* ED
wwang: 09/15/2009
alopez: 7/14/1998
*RECORD*
*FIELD* NO
602846
*FIELD* TI
*602846 HUNTINGTIN-INTERACTING PROTEIN 2; HIP2
;;UBIQUITIN-CONJUGATING ENZYME E2-25K
read more*FIELD* TX
DESCRIPTION
Huntington disease (HD; 143100) may be caused by a toxic
gain-of-function due to abnormal protein-protein interactions. Protein
that interact with huntingtin (HTT; 613004) include the glycolytic
enzyme GAPD (138400), huntingtin-associated protein (600947), and
huntingtin-interacting protein-1 (HIP1; 601767).
CLONING
Kalchman et al. (1996) used the yeast 2-hybrid system to identify the
HIP2 protein. The 200-amino acid HIP2 protein sequence was identical to
that of bovine ubiquitin-conjugating enzyme E2-25K. Assays of the
interaction of HIP2 with huntingtin revealed that HIP2 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.
Northern blot analysis revealed that HIP2 is transcribed as 1.2 and
1.4-kb mRNAs in all human tissues studied. Western blot analysis
detected protein bands of 25, 28, and 45 kD; the 28-kD band appeared to
be selective for tissues of the central nervous system. Kalchman et al.
(1996) showed that huntingtin is ubiquitinated in peripheral cells,
suggesting a role for HIP2 in the degradation of huntingtin.
MAPPING
Kalchman et al. (1996) used fluorescence in situ hybridization to map
the HIP2 gene to human chromosome 4p14.
*FIELD* RF
1. Kalchman, M. A.; Graham, R. K.; Xia, G.; Koide, H. B.; Hodgson,
J. G.; Graham, K. C.; Goldberg, Y. P.; Gietz, R. D.; Pickart, C. M.;
Hayden, M. R.: Huntingtin is ubiquitinated and interacts with a specific
ubiquitin-conjugating enzyme. J. Biol. Chem. 271: 19385-19394, 1996.
*FIELD* CD
Jennifer P. Macke: 7/14/1998
*FIELD* ED
wwang: 09/15/2009
alopez: 7/14/1998