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Q6ZWZ2

- UB2R2_MOUSE

UniProt

Q6ZWZ2 - UB2R2_MOUSE

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Protein

Ubiquitin-conjugating enzyme E2 R2

Gene

Ube2r2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. protein K48-linked ubiquitination Source: UniProtKB
  2. 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

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.

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. 1 interaction.
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.
OMAiNSEETAM.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18057.1.
RefSeqi NP_080551.1. NM_026275.4.
UniGenei Mm.389540.

3D structure databases

ProteinModelPortali Q6ZWZ2.
SMRi Q6ZWZ2. Positions 8-184.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212312. 1 interaction.
IntActi Q6ZWZ2. 1 interaction.
MINTi MINT-4609410.

PTM databases

PhosphoSitei Q6ZWZ2.

Proteomic databases

MaxQBi Q6ZWZ2.
PaxDbi Q6ZWZ2.
PRIDEi Q6ZWZ2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000040008 ; ENSMUSP00000038813 ; ENSMUSG00000036241 .
GeneIDi 67615.
KEGGi mmu:67615.
UCSCi uc008sij.1. mouse.

Organism-specific databases

CTDi 54926.
MGIi MGI:1914865. Ube2r2.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00730000110436.
HOGENOMi HOG000233454.
HOVERGENi HBG063308.
InParanoidi Q6ZWZ2.
KOi K02207.
OMAi NSEETAM.
OrthoDBi EOG7VB2HT.
PhylomeDBi Q6ZWZ2.
TreeFami TF101107.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi UBE2R2. mouse.
NextBioi 325049.
PROi Q6ZWZ2.
SOURCEi Search...

Gene expression databases

Bgeei Q6ZWZ2.
CleanExi MM_UBE2R2.
Genevestigatori Q6ZWZ2.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 1, 2014
This is version 92 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