P63146 (UBE2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cell membrane Membrane Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	canonical Wnt receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB cellular response to insulin stimulus Inferred from electronic annotation. Source: Compara chiasma assembly Inferred from electronic annotation. Source: Compara histone H2A ubiquitination Inferred from mutant phenotype PubMed 18339854. Source: UniProtKB histone lysine demethylation Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara maintenance of chromatin silencing Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of cAMP-mediated signaling Inferred from direct assay PubMed 10373550. Source: UniProtKB negative regulation of histone phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of reciprocal meiotic recombination Inferred from electronic annotation. Source: Compara postreplication repair Inferred from direct assay PubMed 14981545. Source: UniProtKB proteasomal 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 stabilization Inferred from mutant phenotype PubMed 18339854. 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: Compara sperm axoneme assembly Inferred from electronic annotation. Source: Compara spermatogenesis Traceable author statement PubMed 18497339. Source: UniProtKB synaptonemal complex organization Inferred from electronic annotation. Source: Compara
Cellular_component	HULC complex Inferred from direct assay PubMed 19410543. Source: UniProtKB XY body Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay PubMed 18339854. Source: UniProtKB nuclear chromatin Inferred from electronic annotation. Source: Compara 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_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay PubMed 10373550PubMed 19123975Ref.14. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 152

152

Ubiquitin-conjugating enzyme E2 B

PRO_0000082447

Sites

Active site

88

1

Glycyl thioester intermediate By similarity

Experimental info

Sequence conflict

22 – 23

2

VG → C Ref.2

Sequence conflict

41

1

F → I Ref.2

Sequence conflict

54

1

K → R Ref.2

Secondary structure

1

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152

Helix Strand Turn

Details...

Helix

4 – 18

15

Beta strand

24 – 29

6

Beta strand

32 – 41

10

Turn

47 – 50

4

Beta strand

52 – 58

7

Turn

61 – 65

5

Beta strand

69 – 74

6

Beta strand

85 – 87

3

Helix

90 – 92

3

Turn

93 – 95

3

Helix

102 – 113

12

Helix

124 – 132

9

Helix

134 – 147

14

Sequences

	Sequence		Length	Mass (Da)
	P63146 [UniParc]. Last modified September 27, 2004. Version 1. Checksum: CFDEEEE7E06840BE	FASTA	152	17,312
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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

NIEHS-SNPs

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.

IPI

IPI00012060.

PIR

B41222.

RefSeq

NP_003328.1. NM_003337.2.

UniGene

Hs.612096.
Hs.730071.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JAS	NMR	-	A	1-152	[»]
1NXA	model	-	A	1-152	[»]
2Y4W	NMR	-	A	1-152	[»]
2YB6	X-ray	1.50	A	1-152	[»]
2YBF	X-ray	2.00	A	1-152	[»]

ProteinModelPortal

P63146.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29832N.

IntAct

P63146. 16 interactions.

MINT

MINT-97455.

STRING

9606.ENSP00000265339.

Polymorphism databases

DMDM

52783814.

Proteomic databases

PaxDb

P63146.

PRIDE

P63146.

Protocols and materials databases

DNASU

7320.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265339; ENSP00000265339; ENSG00000119048.

GeneID

7320.

KEGG

hsa:7320.

UCSC

uc003kzh.3. human.

Organism-specific databases

CTD

7320.

GeneCards

GC05P133706.

HGNC

HGNC:12473. UBE2B.

MIM

179095. gene.

neXtProt

NX_P63146.

PharmGKB

PA37123.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000233454.

HOVERGEN

HBG063308.

InParanoid

P63146.

KO

K10574.

OMA

VIFGPVG.

OrthoDB

EOG4RJG2S.

PhylomeDB

P63146.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

P63146.

Bgee

P63146.

CleanEx

HS_UBE2B.

Genevestigator

P63146.

GermOnline

ENSG00000119048. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

UBE2B. human.

EvolutionaryTrace

P63146.

GenomeRNAi

7320.

NextBio

28622.

SOURCE

Search...

Entry information

Entry name

UBE2B_HUMAN

Accession

Primary (citable) accession number: P63146
Secondary accession number(s): B2R503 , D3DQA2, P23567, Q4PJ15, Q9D0J6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	September 27, 2004
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.