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P63147 (UBE2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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 B

EC=6.3.2.19
Alternative name(s):
E214K
RAD6 homolog B
Short name=HR6B
Short name=mHR6B
Ubiquitin carrier protein B
Ubiquitin-protein ligase B
Gene names
Name:Ube2b
Synonyms:Rad6b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth By similarity.

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with RAD18, UBR2 and WAC. Ref.4

Subcellular location

Cell membrane By similarity. Nucleus By similarity. Note: In peripheral neurons, expressed both at the plasma membrane and in nuclei By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCell membrane
Membrane
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcanonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 18339854. Source: UniProtKB

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

chiasma assembly

Inferred from mutant phenotype PubMed 12556476. Source: MGI

histone H2A ubiquitination

Inferred from electronic annotation. Source: Ensembl

histone lysine demethylation

Inferred from mutant phenotype PubMed 17488778. Source: MGI

in utero embryonic development

Inferred from genetic interaction PubMed 15169909. Source: MGI

maintenance of chromatin silencing

Inferred from mutant phenotype PubMed 17488778. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 12556476. Source: MGI

negative regulation of cAMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone phosphorylation

Inferred from mutant phenotype PubMed 17488778. Source: MGI

positive regulation of reciprocal meiotic recombination

Inferred from mutant phenotype PubMed 12556476. Source: MGI

postreplication repair

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein K11-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein autoubiquitination

Inferred from electronic annotation. Source: Ensembl

protein monoubiquitination

Inferred from electronic annotation. Source: Ensembl

protein stabilization

Inferred from electronic annotation. Source: Ensembl

regulation of histone modification

Inferred from mutant phenotype PubMed 17488778. Source: MGI

response to UV

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

sperm axoneme assembly

Inferred from mutant phenotype PubMed 12672659. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 9922113. Source: MGI

synaptonemal complex organization

Inferred from mutant phenotype PubMed 12556476PubMed 17488778. Source: MGI

   Cellular_componentHULC complex

Inferred from sequence or structural similarity. Source: UniProtKB

XY body

Inferred from direct assay PubMed 15383616. Source: MGI

chromatin

Inferred from direct assay PubMed 15657431. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from direct assay PubMed 15383616. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

replication fork

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 12509447Ref.4PubMed 17462990. Source: MGI

ubiquitin-protein transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Ubiquitin-conjugating enzyme E2 B
PRO_0000082448

Sites

Active site881Glycyl thioester intermediate By similarity

Experimental info

Sequence conflict71R → E in BAB27570. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P63147 [UniParc].

Last modified September 27, 2004. Version 1.
Checksum: CFDEEEE7E06840BE

FASTA15217,312
        10         20         30         40         50         60 
MSTPARRRLM RDFKRLQEDP PVGVSGAPSE NNIMQWNAVI FGPEGTPFED GTFKLVIEFS 

        70         80         90        100        110        120 
EEYPNKPPTV RFLSKMFHPN VYADGSICLD ILQNRWSPTY DVSSILTSIQ SLLDEPNPNS 

       130        140        150 
PANSQAAQLY QENKREYEKR VSAIVEQSWN DS 

« Hide

References

« Hide 'large scale' references
[1]"Inactivation of the HR6B ubiquitin-conjugating DNA repair enzyme in mice causes male sterility associated with chromatin modification."
Roest H.P., van Klaveren J., de Wit J., van Gurp C.G., Koken M.H.M., Vermey M., van Roijen J.H., Vreeburg J.T.M., Baarends W.M., Bootsma D., Grootegoed J.A., Hoeijmakers J.H.J.
Cell 86:799-810(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Testis.
[2]Varshavsky A., Grigoryev S., Stewart A.E., Kwon Y.T., Arfin S.M., Bradshaw R.A., Jenkins N.A., Copeland N.G.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Strain: C57BL/6J.
Tissue: Amnion and Embryo.
[4]"Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway."
Kwon Y.T., Xia Z., An J.Y., Tasaki T., Davydov I.V., Seo J.W., Sheng J., Xie Y., Varshavsky A.
Mol. Cell. Biol. 23:8255-8271(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBR2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X96859 mRNA. Translation: CAA65602.1.
U57690 mRNA. Translation: AAC52884.1.
AK010432 mRNA. Translation: BAB26934.1.
AK011363 mRNA. Translation: BAB27570.1.
AK147785 mRNA. Translation: BAE28135.1.
AK169229 mRNA. Translation: BAE40998.1.
CCDSCCDS24664.1.
RefSeqNP_033484.3. NM_009458.4.
XP_006533223.1. XM_006533160.1.
UniGeneMm.384918.

3D structure databases

ProteinModelPortalP63147.
SMRP63147. Positions 3-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204415. 1 interaction.

Proteomic databases

PaxDbP63147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020657; ENSMUSP00000020657; ENSMUSG00000020390.
ENSMUST00000109086; ENSMUSP00000104714; ENSMUSG00000020390.
GeneID22210.
KEGGmmu:22210.
UCSCuc007iut.2. mouse.

Organism-specific databases

CTD7320.
MGIMGI:102944. Ube2b.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00730000110565.
HOGENOMHOG000233454.
HOVERGENHBG063308.
InParanoidP63147.
KOK10574.
OMAIVEQSWV.
OrthoDBEOG7M0NTH.
PhylomeDBP63147.
TreeFamTF101128.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressP63147.
BgeeP63147.
GenevestigatorP63147.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2B. mouse.
NextBio28622.
PROP63147.
SOURCESearch...

Entry information

Entry nameUBE2B_MOUSE
AccessionPrimary (citable) accession number: P63147
Secondary accession number(s): P23567, Q3UGS2, Q9D0J6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: July 9, 2014
This is version 97 of the entry and version 1 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