GenomeNet

Database: UniProt
Entry: P61086
LinkDB: P61086
Original site: P61086 
ID   UBE2K_HUMAN             Reviewed;         200 AA.
AC   P61086; A6NJC1; A8K5Y9; B2RDF8; C9JGP1; O54806; P27924; Q16721; Q9CVV9;
AC   Q9Y2D3;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   29-SEP-2021, entry version 184.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 K;
DE            EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
DE   AltName: Full=E2 ubiquitin-conjugating enzyme K;
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE 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., Graham K.C.,
RA   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; DOI=10.1161/01.atv.20.1.128;
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., 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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., 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., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., 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., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   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., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 project:
RT   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., Hyodo-Miura J.,
RA   Kawachi K., Natsume T., Shibuya H.;
RT   "NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates
RT   the ubiquitylation and degradation of T cell factor/lymphoid enhancer
RT   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., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   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 IDENTIFICATION BY 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 heavy
RT   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 IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   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, AND CATALYTIC ACTIVITY.
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 dependent:
RT   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., Buerckstuemmer T.,
RA   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, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [22]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [24]
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., Twigg P.D.;
RT   "Structure of full-length ubiquitin-conjugating enzyme E2-25K (Huntingtin-
RT   interacting protein 2).";
RL   Acta Crystallogr. F 65:440-444(2009).
RN   [25]
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 UBC9
RT   and the ubiquitin-conjugating enzyme E2-25 kDA.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RG   Structural genomics consortium (SGC);
RT   "Ubiquitin-conjugating enzyme E2-25 kDA (Huntington-interacting protein
RT   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 or in
CC       the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex,
CC       catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does
CC       not transfer ubiquitin directly to but elongates monoubiquitinated
CC       substrate protein. Mediates the selective degradation of short-lived
CC       and abnormal proteins, such as the endoplasmic reticulum-associated
CC       degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates
CC       huntingtin. May mediate foam cell formation by the suppression of
CC       apoptosis of lipid-bearing macrophages through ubiquitination and
CC       subsequence degradation of p53/TP53. Proposed to be involved in
CC       ubiquitination and proteolytic processing of NF-kappa-B; in vitro
CC       supports ubiquitination of NFKB1. In case of infection by
CC       cytomegaloviruses may be involved in the US11-dependent degradation of
CC       MHC class I heavy chains following their export from the ER to the
CC       cytosol. In case of viral infections may be involved in the HPV E7
CC       protein-dependent degradation of RB1. {ECO:0000269|PubMed:10634809,
CC       ECO:0000269|PubMed:10675012, ECO:0000269|PubMed:16714285,
CC       ECO:0000269|PubMed:16868077, ECO:0000269|PubMed:17873885,
CC       ECO:0000269|PubMed:19906396, ECO:0000269|PubMed:20061386,
CC       ECO:0000269|PubMed:8702625}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC         ProRule:PRU10133, ECO:0000269|PubMed:20061386};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with RNF138/NARF. Interacts with BRCA1.
CC       {ECO:0000269|PubMed:16714285, ECO:0000269|PubMed:17873885,
CC       ECO:0000269|Ref.25}.
CC   -!- INTERACTION:
CC       P61086; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-473850, EBI-18899653;
CC       P61086; Q9NZS9: BFAR; NbExp=6; IntAct=EBI-473850, EBI-2130199;
CC       P61086; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-473850, EBI-517623;
CC       P61086; Q6PIA0: BIRC8; NbExp=3; IntAct=EBI-473850, EBI-2129837;
CC       P61086; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-473850, EBI-2837444;
CC       P61086; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-473850, EBI-1383687;
CC       P61086; Q9ULV8: CBLC; NbExp=3; IntAct=EBI-473850, EBI-2341018;
CC       P61086; P14635: CCNB1; NbExp=2; IntAct=EBI-473850, EBI-495332;
CC       P61086; P24863: CCNC; NbExp=3; IntAct=EBI-473850, EBI-395261;
CC       P61086; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-473850, EBI-744045;
CC       P61086; Q8WTU0: DDI1; NbExp=3; IntAct=EBI-473850, EBI-748248;
CC       P61086; Q9NX09: DDIT4; NbExp=3; IntAct=EBI-473850, EBI-715104;
CC       P61086; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-473850, EBI-25847826;
CC       P61086; Q8N9I9: DTX3; NbExp=10; IntAct=EBI-473850, EBI-2340258;
CC       P61086; Q8TDB6: DTX3L; NbExp=3; IntAct=EBI-473850, EBI-2340392;
CC       P61086; Q15024: EXOSC7; NbExp=3; IntAct=EBI-473850, EBI-371841;
CC       P61086; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-473850, EBI-11793142;
CC       P61086; Q7L8L6: FASTKD5; NbExp=3; IntAct=EBI-473850, EBI-747570;
CC       P61086; Q4G1C9-2: GLIPR1L2; NbExp=3; IntAct=EBI-473850, EBI-20835942;
CC       P61086; P62879: GNB2; NbExp=3; IntAct=EBI-473850, EBI-356942;
CC       P61086; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-473850, EBI-3957665;
CC       P61086; P42858: HTT; NbExp=24; IntAct=EBI-473850, EBI-466029;
CC       P61086; O00522: KRIT1; NbExp=3; IntAct=EBI-473850, EBI-1573121;
CC       P61086; Q6IAA8: LAMTOR1; NbExp=3; IntAct=EBI-473850, EBI-715385;
CC       P61086; Q86UD3: MARCHF3; NbExp=3; IntAct=EBI-473850, EBI-2341065;
CC       P61086; Q9H992: MARCHF7; NbExp=3; IntAct=EBI-473850, EBI-949983;
CC       P61086; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-473850, EBI-16439278;
CC       P61086; O15344: MID1; NbExp=3; IntAct=EBI-473850, EBI-2340316;
CC       P61086; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-473850, EBI-10172526;
CC       P61086; Q8TD10: MIPOL1; NbExp=6; IntAct=EBI-473850, EBI-2548751;
CC       P61086; Q13064: MKRN3; NbExp=3; IntAct=EBI-473850, EBI-2340269;
CC       P61086; Q15843: NEDD8; NbExp=3; IntAct=EBI-473850, EBI-716247;
CC       P61086; P26367: PAX6; NbExp=3; IntAct=EBI-473850, EBI-747278;
CC       P61086; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-473850, EBI-79165;
CC       P61086; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-473850, EBI-25830870;
CC       P61086; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-473850, EBI-2340624;
CC       P61086; Q9BYM8-4: RBCK1; NbExp=3; IntAct=EBI-473850, EBI-25867896;
CC       P61086; Q04864: REL; NbExp=3; IntAct=EBI-473850, EBI-307352;
CC       P61086; Q06587: RING1; NbExp=9; IntAct=EBI-473850, EBI-752313;
CC       P61086; Q6ZNA4-2: RNF111; NbExp=3; IntAct=EBI-473850, EBI-21535400;
CC       P61086; Q9Y508: RNF114; NbExp=3; IntAct=EBI-473850, EBI-723587;
CC       P61086; Q8WVD3: RNF138; NbExp=11; IntAct=EBI-473850, EBI-749039;
CC       P61086; Q96A37: RNF166; NbExp=3; IntAct=EBI-473850, EBI-2130320;
CC       P61086; Q9H6Y7: RNF167; NbExp=3; IntAct=EBI-473850, EBI-1055214;
CC       P61086; Q8N6D2: RNF182; NbExp=3; IntAct=EBI-473850, EBI-2130099;
CC       P61086; Q96D59: RNF183; NbExp=3; IntAct=EBI-473850, EBI-743938;
CC       P61086; Q96GF1: RNF185; NbExp=3; IntAct=EBI-473850, EBI-2340249;
CC       P61086; Q99496: RNF2; NbExp=3; IntAct=EBI-473850, EBI-722416;
CC       P61086; Q9H0A6-4: RNF32; NbExp=3; IntAct=EBI-473850, EBI-25868153;
CC       P61086; Q9H4P4: RNF41; NbExp=3; IntAct=EBI-473850, EBI-2130266;
CC       P61086; Q99942: RNF5; NbExp=11; IntAct=EBI-473850, EBI-348482;
CC       P61086; O00560: SDCBP; NbExp=3; IntAct=EBI-473850, EBI-727004;
CC       P61086; Q8IUQ4: SIAH1; NbExp=4; IntAct=EBI-473850, EBI-747107;
CC       P61086; Q8IUQ4-2: SIAH1; NbExp=6; IntAct=EBI-473850, EBI-11522811;
CC       P61086; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-473850, EBI-2659201;
CC       P61086; Q99619: SPSB2; NbExp=3; IntAct=EBI-473850, EBI-2323209;
CC       P61086; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-473850, EBI-11123832;
CC       P61086; O15273: TCAP; NbExp=3; IntAct=EBI-473850, EBI-954089;
CC       P61086; Q12888: TP53BP1; NbExp=3; IntAct=EBI-473850, EBI-396540;
CC       P61086; Q9BWF2: TRAIP; NbExp=3; IntAct=EBI-473850, EBI-1756205;
CC       P61086; Q9C040: TRIM2; NbExp=3; IntAct=EBI-473850, EBI-749840;
CC       P61086; P14373: TRIM27; NbExp=12; IntAct=EBI-473850, EBI-719493;
CC       P61086; Q9BZY9: TRIM31; NbExp=11; IntAct=EBI-473850, EBI-747544;
CC       P61086; Q9UPQ4-2: TRIM35; NbExp=6; IntAct=EBI-473850, EBI-17716262;
CC       P61086; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-473850, EBI-739510;
CC       P61086; Q9HCM9-2: TRIM39; NbExp=8; IntAct=EBI-473850, EBI-11523450;
CC       P61086; Q96BQ3: TRIM43; NbExp=3; IntAct=EBI-473850, EBI-2129899;
CC       P61086; Q9C035-3: TRIM5; NbExp=6; IntAct=EBI-473850, EBI-12840050;
CC       P61086; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-473850, EBI-9867283;
CC       P61086; Q15631: TSN; NbExp=3; IntAct=EBI-473850, EBI-1044160;
CC       P61086; P09936: UCHL1; NbExp=3; IntAct=EBI-473850, EBI-714860;
CC       P61086; P40337-2: VHL; NbExp=3; IntAct=EBI-473850, EBI-12157263;
CC       P61086; Q9H270: VPS11; NbExp=3; IntAct=EBI-473850, EBI-373380;
CC       P61086; O76024: WFS1; NbExp=3; IntAct=EBI-473850, EBI-720609;
CC       P61086; Q99PZ6: ospG; Xeno; NbExp=2; IntAct=EBI-473850, EBI-9316527;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61085}.
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       Name=3;
CC         IsoId=P61086-3; Sequence=VSP_046211;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including spleen,
CC       thymus, prostate, testis, ovary, small intestine, colon, peripheral
CC       blood leukocytes, T-lymphocytes, monocytes, granulocytes and bone
CC       marrow mononuclear cells. Highly expressed in brain, with highest
CC       levels found in cortex and striatum and at lower levels in cerebellum
CC       and brainstem. {ECO:0000269|PubMed:10634809,
CC       ECO:0000269|PubMed:10675012, ECO:0000269|PubMed:8702625}.
CC   -!- INDUCTION: By aggregated low-density lipoprotein.
CC       {ECO:0000269|PubMed:10634809, ECO:0000269|PubMed:10675012}.
CC   -!- PTM: Sumoylation at Lys-14 impairs catalytic activity.
CC       {ECO:0000250|UniProtKB:P61085}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be inactive. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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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   CCDS; CCDS33976.1; -. [P61086-1]
DR   CCDS; CCDS47043.1; -. [P61086-3]
DR   CCDS; CCDS47044.1; -. [P61086-2]
DR   RefSeq; NP_001104582.1; NM_001111112.1. [P61086-3]
DR   RefSeq; NP_001104583.1; NM_001111113.1. [P61086-2]
DR   RefSeq; NP_005330.1; NM_005339.4. [P61086-1]
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   PDB; 5DFL; X-ray; 2.10 A; A=1-200.
DR   PDB; 6IF1; X-ray; 2.47 A; A/B=1-199.
DR   PDB; 6JB6; X-ray; 2.70 A; A=1-200.
DR   PDB; 6JB7; X-ray; 2.10 A; A=1-200.
DR   PDBsum; 1YLA; -.
DR   PDBsum; 2O25; -.
DR   PDBsum; 3E46; -.
DR   PDBsum; 3F92; -.
DR   PDBsum; 3K9O; -.
DR   PDBsum; 3K9P; -.
DR   PDBsum; 5DFL; -.
DR   PDBsum; 6IF1; -.
DR   PDBsum; 6JB6; -.
DR   PDBsum; 6JB7; -.
DR   BMRB; P61086; -.
DR   SMR; P61086; -.
DR   BioGRID; 109340; 124.
DR   DIP; DIP-32524N; -.
DR   IntAct; P61086; 88.
DR   STRING; 9606.ENSP00000261427; -.
DR   ChEMBL; CHEMBL4105835; -.
DR   MoonDB; P61086; Predicted.
DR   GlyGen; P61086; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61086; -.
DR   MetOSite; P61086; -.
DR   PhosphoSitePlus; P61086; -.
DR   SwissPalm; P61086; -.
DR   BioMuta; UBE2K; -.
DR   DMDM; 46577658; -.
DR   OGP; P27924; -.
DR   EPD; P61086; -.
DR   jPOST; P61086; -.
DR   MassIVE; P61086; -.
DR   MaxQB; P61086; -.
DR   PaxDb; P61086; -.
DR   PeptideAtlas; P61086; -.
DR   PRIDE; P61086; -.
DR   ProteomicsDB; 10126; -.
DR   ProteomicsDB; 57262; -. [P61086-1]
DR   ProteomicsDB; 57263; -. [P61086-2]
DR   TopDownProteomics; P61086-1; -. [P61086-1]
DR   Antibodypedia; 11733; 427 antibodies.
DR   DNASU; 3093; -.
DR   Ensembl; ENST00000261427; ENSP00000261427; ENSG00000078140. [P61086-1]
DR   Ensembl; ENST00000445950; ENSP00000390483; ENSG00000078140. [P61086-3]
DR   Ensembl; ENST00000503368; ENSP00000421203; ENSG00000078140. [P61086-2]
DR   GeneID; 3093; -.
DR   KEGG; hsa:3093; -.
DR   UCSC; uc003gus.5; human. [P61086-1]
DR   CTD; 3093; -.
DR   DisGeNET; 3093; -.
DR   GeneCards; UBE2K; -.
DR   HGNC; HGNC:4914; UBE2K.
DR   HPA; ENSG00000078140; Low tissue specificity.
DR   MIM; 602846; gene.
DR   neXtProt; NX_P61086; -.
DR   OpenTargets; ENSG00000078140; -.
DR   PharmGKB; PA162407874; -.
DR   VEuPathDB; HostDB:ENSG00000078140; -.
DR   eggNOG; KOG0418; Eukaryota.
DR   GeneTree; ENSGT00670000098059; -.
DR   HOGENOM; CLU_030988_13_1_1; -.
DR   InParanoid; P61086; -.
DR   OMA; HHLKGSF; -.
DR   OrthoDB; 1418652at2759; -.
DR   PhylomeDB; P61086; -.
DR   TreeFam; TF101127; -.
DR   BRENDA; 2.3.2.24; 2681.
DR   PathwayCommons; P61086; -.
DR   Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; P61086; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 3093; 74 hits in 1024 CRISPR screens.
DR   ChiTaRS; UBE2K; human.
DR   EvolutionaryTrace; P61086; -.
DR   GeneWiki; HIP2; -.
DR   GenomeRNAi; 3093; -.
DR   Pharos; P61086; Tbio.
DR   PRO; PR:P61086; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P61086; protein.
DR   Bgee; ENSG00000078140; Expressed in postcentral gyrus and 239 other tissues.
DR   ExpressionAtlas; P61086; baseline and differential.
DR   Genevisible; P61086; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:UniProtKB.
DR   GO; GO:0035458; P:cellular response to interferon-beta; IMP:UniProtKB.
DR   GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB.
DR   GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR   GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IMP:FlyBase.
DR   GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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   CDD; cd14390; UBA_II_E2_UBE2K; 1.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR042599; UBE2K_UBA.
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; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Isopeptide bond; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0000269|PubMed:16714285, ECO:0000269|Ref.11,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..200
FT                   /note="Ubiquitin-conjugating enzyme E2 K"
FT                   /id="PRO_0000082443"
FT   DOMAIN          4..154
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   DOMAIN          160..200
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   ACT_SITE        92
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.11, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        14
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   VAR_SEQ         22..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10634809,
FT                   ECO:0000303|PubMed:10675012, ECO:0000303|PubMed:14702039"
FT                   /id="VSP_011798"
FT   VAR_SEQ         134..176
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_046211"
FT   MUTAGEN         94
FT                   /note="D->E: Decreased lysine reactivity and impaired
FT                   formation of free polyubiquitin chains."
FT                   /evidence="ECO:0000269|PubMed:21532592"
FT   HELIX           6..17
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   STRAND          26..31
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:2O25"
FT   STRAND          36..44
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:1YLA"
FT   TURN            50..53
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   TURN            64..68
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   STRAND          72..77
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   HELIX           106..118
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   HELIX           138..153
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   HELIX           160..170
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   HELIX           176..185
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   TURN            186..188
FT                   /evidence="ECO:0007829|PDB:3K9O"
FT   HELIX           190..199
FT                   /evidence="ECO:0007829|PDB:3K9O"
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
//
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