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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_MOUSE             Reviewed;         200 AA.
P61087; O54806; P27924; Q16721; Q9CVV9;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 145.
RecName: Full=Ubiquitin-conjugating enzyme E2 K;
EC=2.3.2.23;
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Brain;
PubMed=10585161; DOI=10.1016/S0891-0618(99)00030-7;
Tanno Y., Mori T., Yokoya S., Kanazawa K., Honma Y., Nikaido T.,
Takeda J., Tojo M., Yamamoto T., Wanaka A.;
"Localization of huntingtin-interacting protein-2 (Hip-2) mRNA in the
developing mouse brain.";
J. Chem. Neuroanat. 17:99-107(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone, and Mammary tumor;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-200.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
FUNCTION IN UBIQUITINATION OF CASP12, AND DISRUPTION PHENOTYPE.
PubMed=18710920; DOI=10.1083/jcb.200711066;
Song S., Lee H., Kam T.I., Tai M.L., Lee J.Y., Noh J.Y., Shim S.M.,
Seo S.J., Kong Y.Y., Nakagawa T., Chung C.W., Choi D.Y., Oubrahim H.,
Jung Y.K.;
"E2-25K/Hip-2 regulates caspase-12 in ER stress-mediated Abeta
neurotoxicity.";
J. Cell Biol. 182:675-684(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. Involved in stabilization of CASP12
during ER stress-mediated amyloid-beta neurotoxicity probably by
inhibiting proteasome activity; in vitro ubiquitinates CASP12.
{ECO:0000269|PubMed:18710920}.
-!- 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}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with RNF138/NARF. Interacts with BRCA1.
{ECO:0000250|UniProtKB:P61086}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61085}.
-!- TISSUE SPECIFICITY: Expressed in the brain, with highest levels
found in the mitral cells of the olfactory bulb, the pyramidal
cell layer of the hippocampus and the Purkinje cells of the
cerebellar cortex. {ECO:0000269|PubMed:10585161}.
-!- DEVELOPMENTAL STAGE: Expressed at all stages of brain development
and increases significantly between postnatal days 7 and 14.
{ECO:0000269|PubMed:10585161}.
-!- PTM: Sumoylation at Lys-14 impairs catalytic activity.
{ECO:0000250|UniProtKB:P61085}.
-!- DISRUPTION PHENOTYPE: Neurons are resistant to amyloid-beta
neurotoxicity. Significantly lower CASP12 expression in brain.
{ECO:0000269|PubMed:18710920}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB011081; BAA24927.1; -; mRNA.
EMBL; BC002013; AAH02013.1; -; mRNA.
EMBL; BC085311; AAH85311.1; -; mRNA.
EMBL; AK006316; BAB24523.1; -; mRNA.
CCDS; CCDS39098.1; -.
RefSeq; NP_058066.2; NM_016786.4.
UniGene; Mm.319512; -.
UniGene; Mm.441014; -.
ProteinModelPortal; P61087; -.
SMR; P61087; -.
BioGrid; 207286; 19.
IntAct; P61087; 14.
MINT; P61087; -.
STRING; 10090.ENSMUSP00000122471; -.
iPTMnet; P61087; -.
PhosphoSitePlus; P61087; -.
SwissPalm; P61087; -.
REPRODUCTION-2DPAGE; P61087; -.
EPD; P61087; -.
PaxDb; P61087; -.
PeptideAtlas; P61087; -.
PRIDE; P61087; -.
Ensembl; ENSMUST00000142407; ENSMUSP00000122471; ENSMUSG00000029203.
GeneID; 53323; -.
KEGG; mmu:53323; -.
UCSC; uc008xnu.1; mouse.
CTD; 3093; -.
MGI; MGI:1858216; Ube2k.
eggNOG; KOG0418; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00670000098059; -.
HOVERGEN; HBG063308; -.
InParanoid; P61087; -.
KO; K04649; -.
OMA; NKEIADC; -.
OrthoDB; EOG091G0KVW; -.
PhylomeDB; P61087; -.
TreeFam; TF101127; -.
Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Ube2k; mouse.
PRO; PR:P61087; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029203; Expressed in 321 organ(s), highest expression level in primary oocyte.
ExpressionAtlas; P61087; baseline and differential.
Genevisible; P61087; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0032433; C:filopodium tip; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISO:MGI.
GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
GO; GO:0010994; P:free ubiquitin chain polymerization; ISO:MGI.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:MGI.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISO:MGI.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:MGI.
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;
Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Isopeptide bond; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P61086}.
CHAIN 2 200 Ubiquitin-conjugating enzyme E2 K.
/FTId=PRO_0000082444.
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:0000250|UniProtKB:P61086}.
MOD_RES 14 14 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P61086}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000250|UniProtKB:P61086}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:P61085}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P61086}.
CONFLICT 163 163 T -> P (in Ref. 1; BAA24927).
{ECO:0000305}.
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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