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Q712K3

- UB2R2_HUMAN

UniProt

Q712K3 - UB2R2_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 R2

Gene

UBE2R2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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.1 PublicationPROSITE-ProRule annotation

    Pathwayi

    Sites

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

    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

    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.

    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.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi120266. 26 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.
    HOGENOMiHOG000233454.
    HOVERGENiHBG063308.
    InParanoidiQ712K3.
    KOiK02207.
    OMAiNSEETAM.
    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

    MAQQQMTSSQ KALMLELKSL QEEPVEGFRI TLVDESDLYN WEVAIFGPPN    50
    TLYEGGYFKA HIKFPIDYPY SPPTFRFLTK MWHPNIYENG DVCISILHPP 100
    VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMFRK 150
    WRDSKGKDKE YAEIIRKQVS ATKAEAEKDG VKVPTTLAEY CIKTKVPSND 200
    NSSDLLYDDL YDDDIDDEDE EEEDADCYDD DDSGNEES 238
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6546.1.
    RefSeqi NP_060281.2. NM_017811.3.
    UniGenei Hs.643648.

    3D structure databases

    ProteinModelPortali Q712K3.
    SMRi Q712K3. Positions 8-184.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120266. 26 interactions.
    IntActi Q712K3. 11 interactions.
    MINTi MINT-4828298.
    STRINGi 9606.ENSP00000263228.

    PTM databases

    PhosphoSitei Q712K3.

    Polymorphism databases

    DMDMi 74749761.

    Proteomic databases

    MaxQBi Q712K3.
    PaxDbi Q712K3.
    PeptideAtlasi Q712K3.
    PRIDEi Q712K3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263228 ; ENSP00000263228 ; ENSG00000107341 .
    GeneIDi 54926.
    KEGGi hsa:54926.
    UCSCi uc003ztm.3. human.

    Organism-specific databases

    CTDi 54926.
    GeneCardsi GC09P033817.
    HGNCi HGNC:19907. UBE2R2.
    HPAi CAB019438.
    MIMi 612506. gene.
    neXtProti NX_Q712K3.
    PharmGKBi PA134946881.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233454.
    HOVERGENi HBG063308.
    InParanoidi Q712K3.
    KOi K02207.
    OMAi NSEETAM.
    OrthoDBi EOG7VB2HT.
    PhylomeDBi Q712K3.
    TreeFami TF101107.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q712K3.

    Miscellaneous databases

    ChiTaRSi UBE2R2. human.
    GeneWikii UBE2R2.
    GenomeRNAii 54926.
    NextBioi 58015.
    PROi Q712K3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q712K3.
    CleanExi HS_UBE2R2.
    Genevestigatori Q712K3.

    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

    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: October 1, 2014
    This is version 108 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