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P61087

- UBE2K_MOUSE

UniProt

P61087 - UBE2K_MOUSE

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Protein

Ubiquitin-conjugating enzyme E2 K

Gene
Ube2k, Hip2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 beta-amyloid neurotoxicity probably by inhibiting proteasome activity; in vitro ubiquitinates CASP12.1 Publication

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Glycyl thioester intermediate By similarity

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin protein ligase binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. ubiquitin-ubiquitin ligase activity Source: Ensembl

GO - Biological processi

  1. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
  2. protein K48-linked ubiquitination Source: UniProtKB
  3. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 K (EC:6.3.2.19)
Alternative name(s):
Huntingtin-interacting protein 2
Short name:
HIP-2
Ubiquitin carrier protein
Ubiquitin-conjugating enzyme E2-25 kDa
Short name:
Ubiquitin-conjugating enzyme E2(25K)
Short name:
Ubiquitin-conjugating enzyme E2-25K
Ubiquitin-protein ligase
Gene namesi
Name:Ube2k
Synonyms:Hip2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1858216. Ube2k.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Neurons are resistant to beta-amyloid neurotoxicity. Significantly lower CASP12 expression in brain.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 200199Ubiquitin-conjugating enzyme E2 KPRO_0000082444Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei14 – 141N6-acetyllysine; alternate By similarity
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Post-translational modificationi

Sumoylation at Lys-14 impairs catalytic activity By similarity.

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP61087.
PaxDbiP61087.
PRIDEiP61087.

2D gel databases

REPRODUCTION-2DPAGEP61087.

PTM databases

PhosphoSiteiP61087.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Expressed at all stages of brain development and increases significantly between postnatal days 7 and 14.1 Publication

Gene expression databases

ArrayExpressiP61087.
BgeeiP61087.
GenevestigatoriP61087.

Interactioni

Subunit structurei

Interacts with RNF138/NARF. Interacts with BRCA1 By similarity.

Protein-protein interaction databases

BioGridi207286. 4 interactions.
IntActiP61087. 1 interaction.
MINTiMINT-4428037.

Structurei

3D structure databases

ProteinModelPortaliP61087.
SMRiP61087. Positions 3-200.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini160 – 20041UBAAdd
BLAST

Sequence similaritiesi

Contains 1 UBA domain.

Phylogenomic databases

eggNOGiCOG5078.
HOVERGENiHBG063308.
InParanoidiP61087.
KOiK04649.
OMAiKHWTNAY.
OrthoDBiEOG7F513F.
PhylomeDBiP61087.
TreeFamiTF101127.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
SMARTiSM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61087-1 [UniParc]FASTAAdd to Basket

« Hide

MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP    50
YEGGRYQLEI KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW 100
AAAMTLRTVL LSLQALLAAA EPDDPQDAVV ANQYKQNPEM FKQTARLWAH 150
VYAGAPVSSP EYTKKIENLC AMGFDRNAVI VALSSKSWDV ETATELLLSN 200
Length:200
Mass (Da):22,407
Last modified:January 23, 2007 - v3
Checksum:iE40668099ED25828
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631T → P in BAA24927. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB011081 mRNA. Translation: BAA24927.1.
BC002013 mRNA. Translation: AAH02013.1.
BC085311 mRNA. Translation: AAH85311.1.
AK006316 mRNA. Translation: BAB24523.1.
CCDSiCCDS39098.1.
RefSeqiNP_058066.2. NM_016786.3.
UniGeneiMm.319512.
Mm.441014.

Genome annotation databases

EnsembliENSMUST00000142407; ENSMUSP00000122471; ENSMUSG00000029203.
GeneIDi53323.
KEGGimmu:53323.
UCSCiuc008xnu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB011081 mRNA. Translation: BAA24927.1 .
BC002013 mRNA. Translation: AAH02013.1 .
BC085311 mRNA. Translation: AAH85311.1 .
AK006316 mRNA. Translation: BAB24523.1 .
CCDSi CCDS39098.1.
RefSeqi NP_058066.2. NM_016786.3.
UniGenei Mm.319512.
Mm.441014.

3D structure databases

ProteinModelPortali P61087.
SMRi P61087. Positions 3-200.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207286. 4 interactions.
IntActi P61087. 1 interaction.
MINTi MINT-4428037.

PTM databases

PhosphoSitei P61087.

2D gel databases

REPRODUCTION-2DPAGE P61087.

Proteomic databases

MaxQBi P61087.
PaxDbi P61087.
PRIDEi P61087.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000142407 ; ENSMUSP00000122471 ; ENSMUSG00000029203 .
GeneIDi 53323.
KEGGi mmu:53323.
UCSCi uc008xnu.1. mouse.

Organism-specific databases

CTDi 3093.
MGIi MGI:1858216. Ube2k.

Phylogenomic databases

eggNOGi COG5078.
HOVERGENi HBG063308.
InParanoidi P61087.
KOi K04649.
OMAi KHWTNAY.
OrthoDBi EOG7F513F.
PhylomeDBi P61087.
TreeFami TF101127.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi UBE2K. mouse.
NextBioi 310133.
PROi P61087.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61087.
Bgeei P61087.
Genevestigatori P61087.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view ]
SMARTi SM00165. UBA. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEi PS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Localization of huntingtin-interacting protein-2 (Hip-2) mRNA in the developing mouse brain."
    Tanno Y., Mori T., Yokoya S., Kanazawa K., Honma Y., Nikaido T., Takeda J., Tojo M., Yamamoto T., Wanaka A.
    J. Chem. Neuroanat. 17:99-107(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone and Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-200.
    Strain: C57BL/6J.
    Tissue: Testis.
  4. Cited for: FUNCTION IN UBIQUITINATION OF CASP12, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiUBE2K_MOUSE
AccessioniPrimary (citable) accession number: P61087
Secondary accession number(s): O54806
, P27924, Q16721, Q9CVV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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