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Protein

Ubiquitin-conjugating enzyme E2 R2

Gene

UBE2R2

Organism
Homo sapiens (Human)
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 vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin.2 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei93 – 931Glycyl thioester intermediate

GO - Molecular functioni

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

GO - Biological processi

  1. proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  2. protein K48-linked ubiquitination Source: UniProtKB
  3. protein monoubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ712K3.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 R2 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein R2
Ubiquitin-conjugating enzyme E2-CDC34B
Ubiquitin-protein ligase R2
Gene namesi
Name:UBE2R2
Synonyms:CDC34B, UBC3B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:19907. UBE2R2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi93 – 931C → S: Loss of function. 1 Publication
Mutagenesisi97 – 971L → S: Loss of function. 1 Publication
Mutagenesisi233 – 2331S → A: Abolishes phosphorylation by CK2. 1 Publication

Organism-specific databases

PharmGKBiPA134946881.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Ubiquitin-conjugating enzyme E2 R2PRO_0000280513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei233 – 2331Phosphoserine; by CK22 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ712K3.
PaxDbiQ712K3.
PeptideAtlasiQ712K3.
PRIDEiQ712K3.

PTM databases

PhosphoSiteiQ712K3.

Expressioni

Gene expression databases

BgeeiQ712K3.
CleanExiHS_UBE2R2.
GenevestigatoriQ712K3.

Organism-specific databases

HPAiCAB019438.
HPA061000.

Interactioni

Subunit structurei

When phosphorylated, interacts with beta-TrCP (BTRC).1 Publication

Protein-protein interaction databases

BioGridi120266. 29 interactions.
IntActiQ712K3. 11 interactions.
MINTiMINT-4828298.
STRINGi9606.ENSP00000263228.

Structurei

3D structure databases

ProteinModelPortaliQ712K3.
SMRiQ712K3. Positions 8-184.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi200 – 23839Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110436.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiQ712K3.
KOiK02207.
OMAiNQDDSGN.
OrthoDBiEOG7VB2HT.
PhylomeDBiQ712K3.
TreeFamiTF101107.

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.

Q712K3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQQQMTSSQ KALMLELKSL QEEPVEGFRI TLVDESDLYN WEVAIFGPPN
60 70 80 90 100
TLYEGGYFKA HIKFPIDYPY SPPTFRFLTK MWHPNIYENG DVCISILHPP
110 120 130 140 150
VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMFRK
160 170 180 190 200
WRDSKGKDKE YAEIIRKQVS ATKAEAEKDG VKVPTTLAEY CIKTKVPSND
210 220 230
NSSDLLYDDL YDDDIDDEDE EEEDADCYDD DDSGNEES
Length:238
Mass (Da):27,166
Last modified:July 5, 2004 - v1
Checksum:iE896CF0116A56308
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391Y → H in BAA91156 (PubMed:14702039).Curated
Sequence conflicti127 – 1271V → A in BAA91156 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ240087 mRNA. Translation: CAC80336.1.
AK000426 mRNA. Translation: BAA91156.1.
CR457233 mRNA. Translation: CAG33514.1.
AL139113 Genomic DNA. Translation: CAI39656.1.
CH471071 Genomic DNA. Translation: EAW58479.1.
CH471071 Genomic DNA. Translation: EAW58480.1.
BC004862 mRNA. Translation: AAH04862.1.
BC047584 mRNA. Translation: AAH47584.1.
CCDSiCCDS6546.1.
RefSeqiNP_060281.2. NM_017811.3.
UniGeneiHs.643648.

Genome annotation databases

EnsembliENST00000263228; ENSP00000263228; ENSG00000107341.
GeneIDi54926.
KEGGihsa:54926.
UCSCiuc003ztm.3. human.

Polymorphism databases

DMDMi74749761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ240087 mRNA. Translation: CAC80336.1.
AK000426 mRNA. Translation: BAA91156.1.
CR457233 mRNA. Translation: CAG33514.1.
AL139113 Genomic DNA. Translation: CAI39656.1.
CH471071 Genomic DNA. Translation: EAW58479.1.
CH471071 Genomic DNA. Translation: EAW58480.1.
BC004862 mRNA. Translation: AAH04862.1.
BC047584 mRNA. Translation: AAH47584.1.
CCDSiCCDS6546.1.
RefSeqiNP_060281.2. NM_017811.3.
UniGeneiHs.643648.

3D structure databases

ProteinModelPortaliQ712K3.
SMRiQ712K3. Positions 8-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120266. 29 interactions.
IntActiQ712K3. 11 interactions.
MINTiMINT-4828298.
STRINGi9606.ENSP00000263228.

PTM databases

PhosphoSiteiQ712K3.

Polymorphism databases

DMDMi74749761.

Proteomic databases

MaxQBiQ712K3.
PaxDbiQ712K3.
PeptideAtlasiQ712K3.
PRIDEiQ712K3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263228; ENSP00000263228; ENSG00000107341.
GeneIDi54926.
KEGGihsa:54926.
UCSCiuc003ztm.3. human.

Organism-specific databases

CTDi54926.
GeneCardsiGC09P033817.
HGNCiHGNC:19907. UBE2R2.
HPAiCAB019438.
HPA061000.
MIMi612506. gene.
neXtProtiNX_Q712K3.
PharmGKBiPA134946881.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110436.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiQ712K3.
KOiK02207.
OMAiNQDDSGN.
OrthoDBiEOG7VB2HT.
PhylomeDBiQ712K3.
TreeFamiTF101107.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ712K3.

Miscellaneous databases

ChiTaRSiUBE2R2. human.
GeneWikiiUBE2R2.
GenomeRNAii54926.
NextBioi58015.
PROiQ712K3.
SOURCEiSearch...

Gene expression databases

BgeeiQ712K3.
CleanExiHS_UBE2R2.
GenevestigatoriQ712K3.

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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, INTERACTION WITH BTRC, PHOSPHORYLATION AT SER-233, MUTAGENESIS OF CYS-93; LEU-97 AND SER-233.
  2. "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: Carcinoma.
  3. "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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Ovary and Testis.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUB2R2_HUMAN
AccessioniPrimary (citable) accession number: Q712K3
Secondary accession number(s): D3DRL5, Q9NX64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 5, 2004
Last modified: March 4, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.