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P61087 (UBE2K_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ube2k
Synonyms:Hip2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 beta-amyloid neurotoxicity probably by inhibiting proteasome activity; in vitro ubiquitinates CASP12. Ref.4

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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

Subcellular location

Cytoplasm By similarity.

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. Ref.1

Developmental stage

Expressed at all stages of brain development and increases significantly between postnatal days 7 and 14. Ref.1

Post-translational modification

Sumoylation at Lys-14 impairs catalytic activity By similarity.

Disruption phenotype

Neurons are resistant to beta-amyloid neurotoxicity. Significantly lower CASP12 expression in brain. Ref.4

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Contains 1 UBA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 200199Ubiquitin-conjugating enzyme E2 K
PRO_0000082444

Regions

Domain160 – 20041UBA

Sites

Active site921Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue141N6-acetyllysine; alternate By similarity
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Experimental info

Sequence conflict1631T → P in BAA24927. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P61087 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E40668099ED25828

FASTA20022,407
        10         20         30         40         50         60 
MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP YEGGRYQLEI 

        70         80         90        100        110        120 
KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW AAAMTLRTVL LSLQALLAAA 

       130        140        150        160        170        180 
EPDDPQDAVV ANQYKQNPEM FKQTARLWAH VYAGAPVSSP EYTKKIENLC AMGFDRNAVI 

       190        200 
VALSSKSWDV ETATELLLSN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"E2-25K/Hip-2 regulates caspase-12 in ER stress-mediated Abeta neurotoxicity."
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.
J. Cell Biol. 182:675-684(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF CASP12, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011081 mRNA. Translation: BAA24927.1.
BC002013 mRNA. Translation: AAH02013.1.
BC085311 mRNA. Translation: AAH85311.1.
AK006316 mRNA. Translation: BAB24523.1.
CCDSCCDS39098.1.
RefSeqNP_058066.2. NM_016786.3.
UniGeneMm.319512.
Mm.441014.

3D structure databases

ProteinModelPortalP61087.
SMRP61087. Positions 3-200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207286. 4 interactions.
IntActP61087. 1 interaction.
MINTMINT-4428037.

PTM databases

PhosphoSiteP61087.

2D gel databases

REPRODUCTION-2DPAGEP61087.

Proteomic databases

MaxQBP61087.
PaxDbP61087.
PRIDEP61087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000142407; ENSMUSP00000122471; ENSMUSG00000029203.
GeneID53323.
KEGGmmu:53323.
UCSCuc008xnu.1. mouse.

Organism-specific databases

CTD3093.
MGIMGI:1858216. Ube2k.

Phylogenomic databases

eggNOGCOG5078.
HOVERGENHBG063308.
InParanoidP61087.
KOK04649.
OMAKHWTNAY.
OrthoDBEOG7F513F.
PhylomeDBP61087.
TreeFamTF101127.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressP61087.
BgeeP61087.
GenevestigatorP61087.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR009060. 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]
PfamPF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
SMARTSM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEPS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2K. mouse.
NextBio310133.
PROP61087.
SOURCESearch...

Entry information

Entry nameUBE2K_MOUSE
AccessionPrimary (citable) accession number: P61087
Secondary accession number(s): O54806 expand/collapse secondary AC list , P27924, Q16721, Q9CVV9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot