Ubiquitin-conjugating enzyme E2 R1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P49427 (UB2R1_HUMAN)

Last modified June 16, 2009. Version 88. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 R1
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase R1
    Ubiquitin-conjugating enzyme E2-32 kDa complementing
    E2-CDC34

Gene names

Name:	CDC34
Synonyms:	UBE2R1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	236 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. May be involved in degradation of katenin. Ref.6
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. Ref.6
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. When phosphorylated, interacts with beta-TrCP (BTRC). Ref.6 Ref.5
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

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Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA replication initiation Ref.1 Non-traceable author statement. Source: UniProtKB G1/S transition of mitotic cell cycle Ref.1 Non-traceable author statement. Source: UniProtKB modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Ref.1 Non-traceable author statement. Source: UniProtKB regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ubiquitin-protein ligase activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPP1CB	P62140	1	EBI-975634,EBI-352350
PPP1CC	P36873-1	1	EBI-975634,EBI-356289

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 236

236

Ubiquitin-conjugating enzyme E2 R1

PRO_0000082451

Regions

Compositional bias

200 – 236

Asp/Glu-rich (acidic)

Sites

Active site

Glycyl thioester intermediate

Amino acid modifications

Modified residue

231

Phosphoserine; by CK2 Probable

Natural variations

Natural variant

227

D → H: dbSNP rs16990650. Ref.3

VAR_021277

Experimental info

Mutagenesis

C → S: Loss of function. Ref.6

Mutagenesis

L → S: Loss of function. Ref.6

Mutagenesis

231

S → A: Abolishes phosphorylation by CK2. Ref.6

Secondary structure

236

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P49427-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 258960666B589DB3
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FASTA

236

26,737

        10         20         30         40         50         60 
MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN TYYEGGYFKA 

        70         80         90        100        110        120 
RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP VDDPQSGELP SERWNPTQNV 

       130        140        150        160        170        180 
RTILLSVISL LNEPNTFSPA NVDASVMYRK WKESKGKDRE YTDIIRKQVL GTKVDAERDG 

       190        200        210        220        230 
VKVPTTLAEY CVKTKAPAPD EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the human homolog of the CDC34 cell cycle gene by complementation in yeast." Plon S.E., Leppig K.A., Do H.N., Groudine M. Proc. Natl. Acad. Sci. U.S.A. 90:10484-10488(1993) [PubMed: 8248134] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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].
[3]	NIEHS SNPs program Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-227.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Lung.
[5]	"SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I kappa B alpha catalyzed by Ubc3 and Ubc4." Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A., Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R., Benfield P., Brizuela L., Rolfe M. Oncogene 19:3529-3536(2000) [PubMed: 10918611] [Abstract] Cited for: INTERACTION WITH SCF COMPLEX.
[6]	"CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation." Semplici F., Meggio F., Pinna L.A., Oliviero S. Oncogene 21:3978-3987(2002) [PubMed: 12037680] [Abstract] Cited for: ENZYME ACTIVITY, FUNCTION, INTERACTION WITH BTRC, PHOSPHORYLATION AT SER-231, MUTAGENESIS OF CYS-93; LEU-97 AND SER-231.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

L22005 mRNA. Translation: AAC37534.1. Different initiation.
BT006659 mRNA. Translation: AAP35305.1.
AY650399 Genomic DNA. Translation: AAT46688.1.
BC009850 mRNA. Translation: AAH09850.1.
BC018143 mRNA. Translation: AAH18143.1.
BC023979 mRNA. Translation: AAH23979.1.

IPI

IPI00027120.

PIR

A49630.

RefSeq

NP_004350.1.

UniGene

Hs.514997

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OB4	X-ray	2.40	A	7-184	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P49427. 3 interactions.

PTM databases

PhosphoSite

P49427.

Proteomic databases

PeptideAtlas

P49427.

PRIDE

P49427.

Genome annotation databases

Ensembl

ENSG00000099804. Homo sapiens. [Contig view]

GeneID

997.

KEGG

hsa:997.

Organism-specific databases

GeneCards

GC19P000482.

H-InvDB

HIX0014554.

HGNC

HGNC:1734. CDC34.

HPA

CAB005109.
HPA002382.

MIM

116948. gene.

PharmGKB

PA142672189.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P49427.

HOVERGEN

P49427.

OMA

P49427. HTHVASS.

Enzyme and pathway databases

BRENDA

6.3.2.19. 247.

Gene expression databases

ArrayExpress

P49427.

Bgee

P49427.

CleanEx

HS_CDC34.

GermOnline

ENSG00000099804. Homo sapiens.

Family and domain databases

InterPro

IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

ProDom

PD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00212. UBCc. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

4188.

SOURCE

Search...

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Entry information

Entry name

UB2R1_HUMAN

Accession

Primary (citable) accession number: P49427

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents