Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ubiquitin-conjugating enzyme E2 R2

Gene

Ube2r2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 (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 sitei93 – 931Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding 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
  4. protein polyubiquitination Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1914865. Ube2r2.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Ubiquitin-conjugating enzyme E2 R2PRO_0000280514Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei233 – 2331Phosphoserine; by CK2By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6ZWZ2.
PaxDbiQ6ZWZ2.
PRIDEiQ6ZWZ2.

PTM databases

PhosphoSiteiQ6ZWZ2.

Expressioni

Gene expression databases

BgeeiQ6ZWZ2.
CleanExiMM_UBE2R2.
GenevestigatoriQ6ZWZ2.

Interactioni

Subunit structurei

When phosphorylated, interacts with beta-TrCP (BTRC).By similarity

Protein-protein interaction databases

BioGridi212312. 1 interaction.
IntActiQ6ZWZ2. 4 interactions.
MINTiMINT-4609410.

Structurei

3D structure databases

ProteinModelPortaliQ6ZWZ2.
SMRiQ6ZWZ2. 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.
InParanoidiQ6ZWZ2.
KOiK02207.
OMAiNQDDSGN.
OrthoDBiEOG7VB2HT.
PhylomeDBiQ6ZWZ2.
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.

Q6ZWZ2-1 [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 conflicti16 – 161E → D in BAC35899. (PubMed:16141072)Curated
Sequence conflicti29 – 291R → L in BAC35899. (PubMed:16141072)Curated
Sequence conflicti33 – 331V → L in BAC35899. (PubMed:16141072)Curated
Sequence conflicti35 – 351E → Y in BAC35899. (PubMed:16141072)Curated
Sequence conflicti37 – 371D → Y in BAC35899. (PubMed:16141072)Curated
Sequence conflicti149 – 1491R → T in CAC80335. (PubMed:12037680)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ240086 mRNA. Translation: CAC80335.1.
AK003550 mRNA. Translation: BAB22850.1.
AK007517 mRNA. Translation: BAB25085.1.
AK075703 mRNA. Translation: BAC35899.1.
AK075714 mRNA. Translation: BAC35904.1.
AL807823, AL954379 Genomic DNA. Translation: CAM20979.1.
AL807823, AL954379 Genomic DNA. Translation: CAM27658.1.
BC011112 mRNA. Translation: AAH11112.1.
CCDSiCCDS18057.1.
RefSeqiNP_080551.1. NM_026275.4.
UniGeneiMm.389540.

Genome annotation databases

EnsembliENSMUST00000040008; ENSMUSP00000038813; ENSMUSG00000036241.
GeneIDi67615.
KEGGimmu:67615.
UCSCiuc008sij.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ240086 mRNA. Translation: CAC80335.1.
AK003550 mRNA. Translation: BAB22850.1.
AK007517 mRNA. Translation: BAB25085.1.
AK075703 mRNA. Translation: BAC35899.1.
AK075714 mRNA. Translation: BAC35904.1.
AL807823, AL954379 Genomic DNA. Translation: CAM20979.1.
AL807823, AL954379 Genomic DNA. Translation: CAM27658.1.
BC011112 mRNA. Translation: AAH11112.1.
CCDSiCCDS18057.1.
RefSeqiNP_080551.1. NM_026275.4.
UniGeneiMm.389540.

3D structure databases

ProteinModelPortaliQ6ZWZ2.
SMRiQ6ZWZ2. Positions 8-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212312. 1 interaction.
IntActiQ6ZWZ2. 4 interactions.
MINTiMINT-4609410.

PTM databases

PhosphoSiteiQ6ZWZ2.

Proteomic databases

MaxQBiQ6ZWZ2.
PaxDbiQ6ZWZ2.
PRIDEiQ6ZWZ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040008; ENSMUSP00000038813; ENSMUSG00000036241.
GeneIDi67615.
KEGGimmu:67615.
UCSCiuc008sij.1. mouse.

Organism-specific databases

CTDi54926.
MGIiMGI:1914865. Ube2r2.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110436.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiQ6ZWZ2.
KOiK02207.
OMAiNQDDSGN.
OrthoDBiEOG7VB2HT.
PhylomeDBiQ6ZWZ2.
TreeFamiTF101107.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiUbe2r2. mouse.
NextBioi325049.
PROiQ6ZWZ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZWZ2.
CleanExiMM_UBE2R2.
GenevestigatoriQ6ZWZ2.

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].
  2. "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: Liver, Lung and Pancreas.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiUB2R2_MOUSE
AccessioniPrimary (citable) accession number: Q6ZWZ2
Secondary accession number(s): Q8BW18, Q8VDE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: February 4, 2015
This is version 95 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.