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Protein

Ubiquitin-conjugating enzyme E2 B

Gene

Ube2b

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 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).By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. canonical Wnt signaling pathway Source: UniProtKB
  2. cellular response to DNA damage stimulus Source: MGI
  3. cellular response to insulin stimulus Source: Ensembl
  4. chiasma assembly Source: MGI
  5. DNA repair Source: MGI
  6. histone H2A ubiquitination Source: MGI
  7. histone lysine demethylation Source: MGI
  8. histone ubiquitination Source: GO_Central
  9. in utero embryonic development Source: MGI
  10. maintenance of chromatin silencing Source: MGI
  11. negative regulation of apoptotic process Source: MGI
  12. negative regulation of cAMP-mediated signaling Source: MGI
  13. negative regulation of histone phosphorylation Source: MGI
  14. positive regulation of reciprocal meiotic recombination Source: MGI
  15. postreplication repair Source: MGI
  16. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  17. protein autoubiquitination Source: MGI
  18. protein K11-linked ubiquitination Source: UniProtKB
  19. protein K48-linked ubiquitination Source: UniProtKB
  20. protein K63-linked ubiquitination Source: UniProtKB
  21. protein monoubiquitination Source: MGI
  22. protein polyubiquitination Source: MGI
  23. protein stabilization Source: MGI
  24. protein ubiquitination Source: MGI
  25. regulation of histone modification Source: MGI
  26. response to drug Source: MGI
  27. response to hypoxia Source: Ensembl
  28. response to UV Source: MGI
  29. spermatogenesis Source: MGI
  30. sperm axoneme assembly Source: MGI
  31. synaptonemal complex organization Source: MGI
  32. ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ube2b
Synonyms:Rad6b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:102944. Ube2b.

Subcellular locationi

  1. Cell membrane By similarity
  2. Nucleus By similarity

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

GO - Cellular componenti

  1. chromatin Source: MGI
  2. cytoplasm Source: MGI
  3. HULC complex Source: UniProtKB
  4. nuclear chromatin Source: MGI
  5. nucleus Source: MGI
  6. plasma membrane Source: UniProtKB-SubCell
  7. replication fork Source: MGI
  8. XY body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Ubiquitin-conjugating enzyme E2 BPRO_0000082448Add
BLAST

Proteomic databases

MaxQBiP63147.
PaxDbiP63147.

Expressioni

Gene expression databases

BgeeiP63147.
ExpressionAtlasiP63147. baseline and differential.
GenevestigatoriP63147.

Interactioni

Subunit structurei

Interacts with RAD18, UBR2 and WAC.1 Publication

Protein-protein interaction databases

BioGridi204415. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP63147.
SMRiP63147. Positions 3-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63147.
KOiK10574.
OMAiIVEQSWV.
OrthoDBiEOG7M0NTH.
PhylomeDBiP63147.
TreeFamiTF101128.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63147-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPARRRLM RDFKRLQEDP PVGVSGAPSE NNIMQWNAVI FGPEGTPFED
60 70 80 90 100
GTFKLVIEFS EEYPNKPPTV RFLSKMFHPN VYADGSICLD ILQNRWSPTY
110 120 130 140 150
DVSSILTSIQ SLLDEPNPNS PANSQAAQLY QENKREYEKR VSAIVEQSWN

DS
Length:152
Mass (Da):17,312
Last modified:September 27, 2004 - v1
Checksum:iCFDEEEE7E06840BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71R → E in BAB27570 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS24664.1.
RefSeqiNP_033484.3. NM_009458.4.
XP_006533223.1. XM_006533160.2.
UniGeneiMm.384918.

Genome annotation databases

EnsembliENSMUST00000020657; ENSMUSP00000020657; ENSMUSG00000020390.
ENSMUST00000109086; ENSMUSP00000104714; ENSMUSG00000020390.
GeneIDi22210.
KEGGimmu:22210.
UCSCiuc007iut.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS24664.1.
RefSeqiNP_033484.3. NM_009458.4.
XP_006533223.1. XM_006533160.2.
UniGeneiMm.384918.

3D structure databases

ProteinModelPortaliP63147.
SMRiP63147. Positions 3-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204415. 1 interaction.

Proteomic databases

MaxQBiP63147.
PaxDbiP63147.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020657; ENSMUSP00000020657; ENSMUSG00000020390.
ENSMUST00000109086; ENSMUSP00000104714; ENSMUSG00000020390.
GeneIDi22210.
KEGGimmu:22210.
UCSCiuc007iut.2. mouse.

Organism-specific databases

CTDi7320.
MGIiMGI:102944. Ube2b.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63147.
KOiK10574.
OMAiIVEQSWV.
OrthoDBiEOG7M0NTH.
PhylomeDBiP63147.
TreeFamiTF101128.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiUbe2b. mouse.
NextBioi28622.
PROiP63147.
SOURCEiSearch...

Gene expression databases

BgeeiP63147.
ExpressionAtlasiP63147. baseline and differential.
GenevestigatoriP63147.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiUBE2B_MOUSE
AccessioniPrimary (citable) accession number: P63147
Secondary accession number(s): P23567, Q3UGS2, Q9D0J6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: April 1, 2015
This is version 105 of the entry and version 1 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.