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P63146 (UBE2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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):
RAD6 homolog B
Short name=HR6B
Short name=hHR6B
Ubiquitin carrier protein B
Ubiquitin-conjugating enzyme E2-17 kDa
Ubiquitin-protein ligase B
Gene names
Name:UBE2B
Synonyms:RAD6B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.3 Ref.11 Ref.12 Ref.13 Ref.14

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.10 Ref.15

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 term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from genetic interaction Ref.3. Source: UniProtKB

canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 14981545. Source: UniProtKB

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

chiasma assembly

Inferred from electronic annotation. Source: Ensembl

histone H2A ubiquitination

Inferred from mutant phenotype PubMed 18339854. Source: UniProtKB

histone lysine demethylation

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

maintenance of chromatin silencing

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cAMP-mediated signaling

Inferred from direct assay PubMed 10373550. Source: UniProtKB

negative regulation of histone phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of reciprocal meiotic recombination

Inferred from electronic annotation. Source: Ensembl

postreplication repair

Inferred from direct assay PubMed 14981545. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 10373550. Source: UniProtKB

protein K11-linked ubiquitination

Inferred from direct assay Ref.14. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from direct assay Ref.14. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from direct assay Ref.14. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay PubMed 19123975. Source: UniProtKB

protein monoubiquitination

Inferred from mutant phenotype PubMed 18339854. Source: UniProtKB

protein polyubiquitination

Inferred from mutant phenotype PubMed 18339854. Source: UniProtKB

protein stabilization

Inferred from mutant phenotype PubMed 18339854. Source: UniProtKB

protein ubiquitination

Inferred from direct assay PubMed 10373550PubMed 19123975. Source: UniProtKB

response to UV

Inferred from genetic interaction Ref.3. Source: UniProtKB

response to drug

Inferred from direct assay PubMed 14981545. Source: UniProtKB

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

sperm axoneme assembly

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Traceable author statement PubMed 18497339. Source: UniProtKB

synaptonemal complex organization

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 10373550. Source: UniProtKB

   Cellular_componentHULC complex

Inferred from direct assay PubMed 19410543. Source: UniProtKB

XY body

Inferred from electronic annotation. Source: Ensembl

chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 18339854. Source: UniProtKB

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 18339854. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

replication fork

Inferred from direct assay PubMed 18363965. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin protein ligase binding

Inferred from physical interaction Ref.10PubMed 18363965. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 10373550PubMed 19123975Ref.14. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Ubiquitin-conjugating enzyme E2 B
PRO_0000082447

Sites

Active site881Glycyl thioester intermediate By similarity

Experimental info

Sequence conflict22 – 232VG → C Ref.2
Sequence conflict411F → I Ref.2
Sequence conflict541K → R Ref.2

Secondary structure

.......................... 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63146 [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]"The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to the yeast DNA repair gene RAD6."
Schneider R., Eckerskorn C., Lottspeich F., Schweiger M.
EMBO J. 9:1431-1435(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Placenta.
[2]"Mammalian mRNAs encoding protein closely related to ubiquitin-conjugating enzyme encoded by yeast DNA repair gene RAD6."
Woffendin C., Chen Z.Y., Staskus K., Retzel E.F., Plagemann P.G.
Biochim. Biophys. Acta 1090:81-85(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6."
Koken M.H.M., Reynolds P., Jaspers-Dekker I., Prakash L., Prakash S., Bootsma D., Hoeijmakers J.H.J.
Proc. Natl. Acad. Sci. U.S.A. 88:8865-8869(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]NIEHS SNPs program
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 marrow and Brain.
[10]"The human RAD18 gene product interacts with HHR6A and HHR6B."
Xin H., Lin W., Sumanasekera W., Zhang Y., Wu X., Wang Z.
Nucleic Acids Res. 28:2847-2854(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAD18.
[11]"The human homolog of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions."
Kim J., Hake S.B., Roeder R.G.
Mol. Cell 20:759-770(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination."
Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.
J. Cell Biol. 175:703-708(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen."
Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., Hurwitz J., Prakash L., Prakash S., Haracska L.
Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
David Y., Ziv T., Admon A., Navon A.
J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription."
Zhang F., Yu X.
Mol. Cell 41:384-397(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WAC.
[16]"The NMR structure of the class I human ubiquitin-conjugating enzyme 2b."
Miura T., Klaus W., Ross A., Guntert P., Senn H.
J. Biomol. NMR 22:89-92(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74525 mRNA. Translation: AAA35982.1.
X53251 mRNA. Translation: CAA37339.1.
BT007071 mRNA. Translation: AAP35734.1.
CR407634 mRNA. Translation: CAG28562.1.
DQ090910 Genomic DNA. Translation: AAY68224.1.
AK312012 mRNA. Translation: BAG34950.1.
CH471062 Genomic DNA. Translation: EAW62257.1.
CH471062 Genomic DNA. Translation: EAW62258.1.
BC005979 mRNA. Translation: AAH05979.1.
BC008404 mRNA. Translation: AAH08404.1.
BC008470 mRNA. Translation: AAH08470.1.
PIRB41222.
RefSeqNP_003328.1. NM_003337.2.
UniGeneHs.612096.
Hs.730071.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JASNMR-A1-152[»]
1NXAmodel-A1-152[»]
2Y4WNMR-A1-152[»]
2YB6X-ray1.50A1-152[»]
2YBFX-ray2.00A1-152[»]
ProteinModelPortalP63146.
SMRP63146. Positions 3-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113168. 56 interactions.
DIPDIP-29832N.
IntActP63146. 16 interactions.
MINTMINT-97455.
STRING9606.ENSP00000265339.

Polymorphism databases

DMDM52783814.

Proteomic databases

PaxDbP63146.
PRIDEP63146.

Protocols and materials databases

DNASU7320.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265339; ENSP00000265339; ENSG00000119048.
GeneID7320.
KEGGhsa:7320.
UCSCuc003kzh.3. human.

Organism-specific databases

CTD7320.
GeneCardsGC05P133706.
HGNCHGNC:12473. UBE2B.
MIM179095. gene.
neXtProtNX_P63146.
PharmGKBPA37123.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233454.
HOVERGENHBG063308.
InParanoidP63146.
KOK10574.
OMAIVEQSWV.
OrthoDBEOG7M0NTH.
PhylomeDBP63146.
TreeFamTF101128.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP63146.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP63146.
BgeeP63146.
CleanExHS_UBE2B.
GenevestigatorP63146.

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. human.
EvolutionaryTraceP63146.
GeneWikiUBE2B.
GenomeRNAi7320.
NextBio28622.
PROP63146.
SOURCESearch...

Entry information

Entry nameUBE2B_HUMAN
AccessionPrimary (citable) accession number: P63146
Secondary accession number(s): B2R503 expand/collapse secondary AC list , D3DQA2, P23567, Q4PJ15, Q9D0J6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM