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Ubiquitin-conjugating enzyme E2 K (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme K) (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)

 UBE2K_HUMAN             Reviewed;         200 AA.
P61086; A6NJC1; A8K5Y9; B2RDF8; C9JGP1; O54806; P27924; Q16721;
Q9CVV9; Q9Y2D3;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 159.
RecName: Full=Ubiquitin-conjugating enzyme E2 K;
EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
AltName: Full=E2 ubiquitin-conjugating enzyme K;
AltName: Full=Huntingtin-interacting protein 2;
Short=HIP-2;
AltName: Full=Ubiquitin carrier protein;
AltName: Full=Ubiquitin-conjugating enzyme E2-25 kDa;
Short=Ubiquitin-conjugating enzyme E2(25K);
Short=Ubiquitin-conjugating enzyme E2-25K;
AltName: Full=Ubiquitin-protein ligase;
Name=UBE2K; Synonyms=HIP2, LIG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=8702625; DOI=10.1074/jbc.271.32.19385;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=10634809; DOI=10.1161/01.ATV.20.1.128;
Kikuchi J., Furukawa Y., Kubo N., Tokura A., Hayashi N., Nakamura M.,
Matsuda M., Sakurabayashi I.;
"Induction of ubiquitin-conjugating enzyme by aggregated low density
lipoprotein in human macrophages and its implications for
atherosclerosis.";
Arterioscler. Thromb. Vasc. Biol. 20:128-134(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=10675012;
DOI=10.1002/(SICI)1522-2683(20000101)21:2<338::AID-ELPS338>3.0.CO;2-9;
Furukawa Y., Kubo N., Kikuchi J., Tokura A., Fujita N.,
Sakurabayashi I.;
"Regulation of macrophage-specific gene expression by degenerated
lipoproteins.";
Electrophoresis 21:338-346(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-10; 62-72; 79-97 AND 166-186, FUNCTION,
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RNF138.
PubMed=16714285; DOI=10.1074/jbc.M602089200;
Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K.,
Hyodo-Miura J., Kawachi K., Natsume T., Shibuya H.;
"NARF, an nemo-like kinase (NLK)-associated ring finger protein
regulates the ubiquitylation and degradation of T cell factor/lymphoid
enhancer factor (TCF/LEF).";
J. Biol. Chem. 281:20749-20760(2006).
[10]
PROTEIN SEQUENCE OF 2-8.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[11]
PROTEIN SEQUENCE OF 2-8; 56-72 AND 177-186, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Bilsland A.E., Keith W.N.;
Submitted (JAN-2010) to UniProtKB.
[12]
FUNCTION IN DEGRADATION OF MHC CLASS I HEAVY CHAINS.
PubMed=16868077; DOI=10.1073/pnas.0605215103;
Flierman D., Coleman C.S., Pickart C.M., Rapoport T.A., Chau V.;
"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. 103:11589-11594(2006).
[13]
FUNCTION IN POLYUBIQUITINATION, AND INTERACTION WITH BRCA1.
PubMed=17873885; DOI=10.1038/nsmb1295;
Christensen D.E., Brzovic P.S., Klevit R.E.;
"E2-BRCA1 RING interactions dictate synthesis of mono- or specific
polyubiquitin chain linkages.";
Nat. Struct. Mol. Biol. 14:941-948(2007).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20061386; DOI=10.1074/jbc.M109.089003;
David Y., Ziv T., Admon A., Navon A.;
"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
preferred lysines.";
J. Biol. Chem. 285:8595-8604(2010).
[16]
FUNCTION IN VIRUS-INDUCED DEGRADATION OF RB1.
PubMed=19906396; DOI=10.1016/j.virol.2009.10.018;
Oh K.J., Kalinina A., Bagchi S.;
"Destabilization of Rb by human papillomavirus E7 is cell cycle
dependent: E2-25K is involved in the proteolysis.";
Virology 396:118-124(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
MUTAGENESIS OF ASP-94.
PubMed=21532592; DOI=10.1038/nature09966;
Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E.;
"UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT
hybrids.";
Nature 474:105-108(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
PubMed=19407372; DOI=10.1107/S1744309109011117;
Wilson R.C., Hughes R.C., Flatt J.W., Meehan E.J., Ng J.D.,
Twigg P.D.;
"Structure of full-length ubiquitin-conjugating enzyme E2-25K
(Huntingtin-interacting protein 2).";
Acta Crystallogr. F 65:440-444(2009).
[25]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBE2I.
Structural genomics consortium (SGC);
"A novel and unexpected complex between the SUMO-1-conjugating enzyme
UBC9 and the ubiquitin-conjugating enzyme E2-25 kDA.";
Submitted (FEB-2009) to the PDB data bank.
[26]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Structural genomics consortium (SGC);
"Ubiquitin-conjugating enzyme E2-25 kDA (Huntington-interacting
protein 2).";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. In vitro, in the presence
or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase
complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin
chains. Does not transfer ubiquitin directly to but elongates
monoubiquitinated substrate protein. Mediates the selective
degradation of short-lived and abnormal proteins, such as the
endoplasmic reticulum-associated degradation (ERAD) of misfolded
lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell
formation by the suppression of apoptosis of lipid-bearing
macrophages through ubiquitination and subsequence degradation of
p53/TP53. Proposed to be involved in ubiquitination and
proteolytic processing of NF-kappa-B; in vitro supports
ubiquitination of NFKB1. In case of infection by cytomegaloviruses
may be involved in the US11-dependent degradation of MHC class I
heavy chains following their export from the ER to the cytosol. In
case of viral infections may be involved in the HPV E7 protein-
dependent degradation of RB1. {ECO:0000269|PubMed:10634809,
ECO:0000269|PubMed:10675012, ECO:0000269|PubMed:16714285,
ECO:0000269|PubMed:16868077, ECO:0000269|PubMed:17873885,
ECO:0000269|PubMed:19906396, ECO:0000269|PubMed:20061386,
ECO:0000269|PubMed:8702625}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:20061386}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with RNF138/NARF. Interacts with BRCA1.
{ECO:0000269|PubMed:16714285, ECO:0000269|PubMed:17873885,
ECO:0000269|Ref.25}.
-!- INTERACTION:
P14635:CCNB1; NbExp=2; IntAct=EBI-473850, EBI-495332;
Q8WTU0:DDI1; NbExp=3; IntAct=EBI-473850, EBI-748248;
Q8N9I9:DTX3; NbExp=5; IntAct=EBI-473850, EBI-2340258;
P42858:HTT; NbExp=3; IntAct=EBI-473850, EBI-466029;
Q8TD10:MIPOL1; NbExp=5; IntAct=EBI-473850, EBI-2548751;
Q99PZ6:ospG (xeno); NbExp=2; IntAct=EBI-473850, EBI-9316527;
Q04864:REL; NbExp=3; IntAct=EBI-473850, EBI-307352;
Q8WVD3:RNF138; NbExp=7; IntAct=EBI-473850, EBI-749039;
Q99942:RNF5; NbExp=5; IntAct=EBI-473850, EBI-348482;
Q8IUQ4:SIAH1; NbExp=4; IntAct=EBI-473850, EBI-747107;
P14373:TRIM27; NbExp=10; IntAct=EBI-473850, EBI-719493;
Q9HCM9:TRIM39; NbExp=3; IntAct=EBI-473850, EBI-739510;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61085}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P61086-1; Sequence=Displayed;
Name=2;
IsoId=P61086-2; Sequence=VSP_011798;
Note=May be inactive.;
Name=3;
IsoId=P61086-3; Sequence=VSP_046211;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all tissues tested, including
spleen, thymus, prostate, testis, ovary, small intestine, colon,
peripheral blood leukocytes, T-lymphocytes, monocytes,
granulocytes and bone marrow mononuclear cells. Highly expressed
in brain, with highest levels found in cortex and striatum and at
lower levels in cerebellum and brainstem.
{ECO:0000269|PubMed:10634809, ECO:0000269|PubMed:10675012,
ECO:0000269|PubMed:8702625}.
-!- INDUCTION: By aggregated low-density lipoprotein.
{ECO:0000269|PubMed:10634809, ECO:0000269|PubMed:10675012}.
-!- PTM: Sumoylation at Lys-14 impairs catalytic activity.
{ECO:0000250|UniProtKB:P61085}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
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EMBL; U58522; AAC50633.1; -; mRNA.
EMBL; AB022435; BAA78555.1; -; mRNA.
EMBL; AB022436; BAA78556.1; -; mRNA.
EMBL; BX339118; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK291454; BAF84143.1; -; mRNA.
EMBL; AK315524; BAG37905.1; -; mRNA.
EMBL; AC105287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471069; EAW92948.1; -; Genomic_DNA.
EMBL; BC022804; AAH22804.1; -; mRNA.
EMBL; BC050600; AAH50600.1; -; mRNA.
CCDS; CCDS33976.1; -. [P61086-1]
CCDS; CCDS47043.1; -. [P61086-3]
CCDS; CCDS47044.1; -. [P61086-2]
RefSeq; NP_001104582.1; NM_001111112.1. [P61086-3]
RefSeq; NP_001104583.1; NM_001111113.1. [P61086-2]
RefSeq; NP_005330.1; NM_005339.4. [P61086-1]
UniGene; Hs.50308; -.
PDB; 1YLA; X-ray; 2.40 A; A/B=1-200.
PDB; 2O25; X-ray; 2.60 A; A/B=1-200.
PDB; 3E46; X-ray; 1.86 A; A=1-200.
PDB; 3F92; X-ray; 2.23 A; A=1-200.
PDB; 3K9O; X-ray; 1.80 A; A=1-200.
PDB; 3K9P; X-ray; 2.80 A; A=1-200.
PDB; 5DFL; X-ray; 2.10 A; A=1-200.
PDBsum; 1YLA; -.
PDBsum; 2O25; -.
PDBsum; 3E46; -.
PDBsum; 3F92; -.
PDBsum; 3K9O; -.
PDBsum; 3K9P; -.
PDBsum; 5DFL; -.
ProteinModelPortal; P61086; -.
SMR; P61086; -.
BioGrid; 109340; 95.
DIP; DIP-32524N; -.
IntAct; P61086; 41.
MINT; P61086; -.
STRING; 9606.ENSP00000261427; -.
iPTMnet; P61086; -.
PhosphoSitePlus; P61086; -.
SwissPalm; P61086; -.
BioMuta; UBE2K; -.
DMDM; 46577658; -.
OGP; P27924; -.
EPD; P61086; -.
MaxQB; P61086; -.
PaxDb; P61086; -.
PeptideAtlas; P61086; -.
PRIDE; P61086; -.
TopDownProteomics; P61086-1; -. [P61086-1]
DNASU; 3093; -.
Ensembl; ENST00000261427; ENSP00000261427; ENSG00000078140. [P61086-1]
Ensembl; ENST00000445950; ENSP00000390483; ENSG00000078140. [P61086-3]
Ensembl; ENST00000503368; ENSP00000421203; ENSG00000078140. [P61086-2]
GeneID; 3093; -.
KEGG; hsa:3093; -.
UCSC; uc003gus.5; human. [P61086-1]
CTD; 3093; -.
DisGeNET; 3093; -.
EuPathDB; HostDB:ENSG00000078140.13; -.
GeneCards; UBE2K; -.
HGNC; HGNC:4914; UBE2K.
HPA; CAB033212; -.
HPA; CAB033515; -.
HPA; HPA028869; -.
MIM; 602846; gene.
neXtProt; NX_P61086; -.
OpenTargets; ENSG00000078140; -.
PharmGKB; PA162407874; -.
eggNOG; KOG0418; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00670000098059; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; P61086; -.
KO; K04649; -.
OMA; NKEIADC; -.
OrthoDB; EOG091G0KVW; -.
PhylomeDB; P61086; -.
TreeFam; TF101127; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P61086; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2K; human.
EvolutionaryTrace; P61086; -.
GeneWiki; HIP2; -.
GenomeRNAi; 3093; -.
PRO; PR:P61086; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000078140; -.
CleanEx; HS_UBE2K; -.
ExpressionAtlas; P61086; baseline and differential.
Genevisible; P61086; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; IMP:UniProtKB.
GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00627; UBA; 1.
Pfam; PF00179; UQ_con; 1.
SMART; SM00165; UBA; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS50030; UBA; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:16714285,
ECO:0000269|Ref.11}.
CHAIN 2 200 Ubiquitin-conjugating enzyme E2 K.
/FTId=PRO_0000082443.
DOMAIN 160 200 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
ACT_SITE 92 92 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.11}.
MOD_RES 14 14 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
VAR_SEQ 22 72 Missing (in isoform 2).
{ECO:0000303|PubMed:10634809,
ECO:0000303|PubMed:10675012,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_011798.
VAR_SEQ 134 176 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_046211.
MUTAGEN 94 94 D->E: Decreased lysine reactivity and
impaired formation of free polyubiquitin
chains. {ECO:0000269|PubMed:21532592}.
HELIX 6 17 {ECO:0000244|PDB:3K9O}.
HELIX 20 23 {ECO:0000244|PDB:3K9O}.
STRAND 26 31 {ECO:0000244|PDB:3K9O}.
STRAND 33 35 {ECO:0000244|PDB:2O25}.
STRAND 36 44 {ECO:0000244|PDB:3K9O}.
STRAND 47 49 {ECO:0000244|PDB:1YLA}.
TURN 50 53 {ECO:0000244|PDB:3K9O}.
STRAND 55 61 {ECO:0000244|PDB:3K9O}.
TURN 64 68 {ECO:0000244|PDB:3K9O}.
STRAND 72 77 {ECO:0000244|PDB:3K9O}.
TURN 86 88 {ECO:0000244|PDB:3K9O}.
HELIX 94 96 {ECO:0000244|PDB:3K9O}.
TURN 97 99 {ECO:0000244|PDB:3K9O}.
HELIX 106 118 {ECO:0000244|PDB:3K9O}.
HELIX 128 136 {ECO:0000244|PDB:3K9O}.
HELIX 138 153 {ECO:0000244|PDB:3K9O}.
HELIX 160 170 {ECO:0000244|PDB:3K9O}.
TURN 171 173 {ECO:0000244|PDB:3K9O}.
HELIX 176 185 {ECO:0000244|PDB:3K9O}.
TURN 186 188 {ECO:0000244|PDB:3K9O}.
HELIX 190 199 {ECO:0000244|PDB:3K9O}.
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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