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Protein

Ubiquitin-conjugating enzyme E2 K

Gene

Ube2k

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. small conjugating protein transferase activity Source: GO_Central
  4. ubiquitin conjugating enzyme activity Source: MGI
  5. ubiquitin protein ligase activity Source: GO_Central
  6. ubiquitin protein ligase binding Source: UniProtKB
  7. ubiquitin-protein transferase activity Source: UniProtKB
  8. ubiquitin-ubiquitin ligase activity Source: MGI

GO - Biological processi

  1. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: MGI
  2. protein K48-linked ubiquitination Source: UniProtKB
  3. protein polyubiquitination Source: GO_Central
  4. 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. actin cytoskeleton Source: MGI
  2. cytoplasm Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. filopodium tip Source: MGI
  5. intermediate filament cytoskeleton Source: MGI
  6. nucleus Source: MGI
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 – 11RemovedBy similarity
Chaini2 – 200199Ubiquitin-conjugating enzyme E2 KPRO_0000082444Add
BLAST

Amino acid modifications

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

BgeeiP61087.
ExpressionAtlasiP61087. baseline and differential.
GenevestigatoriP61087.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi207286. 5 interactions.
IntActiP61087. 1 interaction.
MINTiMINT-4428037.

Structurei

3D structure databases

ProteinModelPortaliP61087.
SMRiP61087. Positions 3-200.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini160 – 20041UBAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
HOVERGENiHBG063308.
InParanoidiP61087.
KOiK04649.
OMAiHEMFILT.
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

        10         20         30         40         50
MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP
60 70 80 90 100
YEGGRYQLEI KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW
110 120 130 140 150
AAAMTLRTVL LSLQALLAAA EPDDPQDAVV ANQYKQNPEM FKQTARLWAH
160 170 180 190 200
VYAGAPVSSP EYTKKIENLC AMGFDRNAVI VALSSKSWDV ETATELLLSN
Length:200
Mass (Da):22,407
Last modified:January 23, 2007 - v3
Checksum:iE40668099ED25828
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631T → P in BAA24927 (PubMed:10585161).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP61087.
SMRiP61087. Positions 3-200.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207286. 5 interactions.
IntActiP61087. 1 interaction.
MINTiMINT-4428037.

PTM databases

PhosphoSiteiP61087.

2D gel databases

REPRODUCTION-2DPAGEP61087.

Proteomic databases

MaxQBiP61087.
PaxDbiP61087.
PRIDEiP61087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3093.
MGIiMGI:1858216. Ube2k.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiUbe2k. mouse.
NextBioi310133.
PROiP61087.
SOURCEiSearch...

Gene expression databases

BgeeiP61087.
ExpressionAtlasiP61087. baseline and differential.
GenevestigatoriP61087.

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]
ProtoNetiSearch...

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: March 4, 2015
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.