Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9D1C1

- UBE2C_MOUSE

UniProt

Q9D1C1 - UBE2C_MOUSE

Protein

Ubiquitin-conjugating enzyme E2 C

Gene

Ube2c

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit 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 sitei114 – 1141Glycyl 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. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    2. cyclin catabolic process Source: Ensembl
    3. exit from mitosis Source: UniProtKB
    4. free ubiquitin chain polymerization Source: UniProtKB
    5. positive regulation of exit from mitosis Source: Ensembl
    6. protein K11-linked ubiquitination Source: UniProtKB
    7. protein K48-linked ubiquitination Source: UniProtKB
    8. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_205250. Phosphorylation of the APC/C.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_207679. Separation of Sister Chromatids.
    REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
    REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 C (EC:6.3.2.19)
    Alternative name(s):
    UbcH10
    Ubiquitin carrier protein C
    Ubiquitin-protein ligase C
    Gene namesi
    Name:Ube2c
    Synonyms:Ubch10
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1915862. Ube2c.

    Subcellular locationi

    GO - Cellular componenti

    1. anaphase-promoting complex Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 179178Ubiquitin-conjugating enzyme E2 CPRO_0000082561Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei3 – 31PhosphoserineBy similarity

    Post-translational modificationi

    Autoubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Its degradation plays a central role in APC/C regulation, allowing cyclin-A accumulation before S phase entry. APC/C substrates inhibit the autoubiquitination of UBE2C/UBCH10 but not its E2 function, hence APC/C remaining active until its substrates have been destroyed By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9D1C1.
    PaxDbiQ9D1C1.
    PRIDEiQ9D1C1.

    PTM databases

    PhosphoSiteiQ9D1C1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9D1C1.
    BgeeiQ9D1C1.
    CleanExiMM_UBE2C.
    GenevestigatoriQ9D1C1.

    Interactioni

    Subunit structurei

    Component of the APC/C complex.By similarity

    Protein-protein interaction databases

    BioGridi212952. 4 interactions.
    STRINGi10090.ENSMUSP00000085581.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D1C1.
    SMRiQ9D1C1. Positions 30-175.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110854.
    HOGENOMiHOG000233454.
    HOVERGENiHBG063308.
    InParanoidiQ9D1C1.
    KOiK06688.
    OMAiAELWDKD.
    OrthoDBiEOG7M0NTH.
    PhylomeDBiQ9D1C1.
    TreeFamiTF101116.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9D1C1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASQNRDPAA ASVAAVRKGA EPCGGAARGP VGKRLQQELM ILMTSGDKGI    50
    SAFPESDNLF KWVGTIHGAA GTVYEDLRYK LSLEFPSGYP YNAPTVKFLT 100
    PCYHPNVDTQ GNICLDILKD KWSALYDVRT ILLSIQSLLG EPNIDSPLNT 150
    HAAELWKNPT AFKKYLQETY SKQVSSQDP 179
    Length:179
    Mass (Da):19,606
    Last modified:June 1, 2001 - v1
    Checksum:i1FE2F36EB69B117C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK003722 mRNA. Translation: BAB22959.1.
    AK160740 mRNA. Translation: BAE35981.1.
    CCDSiCCDS17055.1.
    RefSeqiNP_081061.1. NM_026785.2.
    UniGeneiMm.89830.

    Genome annotation databases

    EnsembliENSMUST00000088248; ENSMUSP00000085581; ENSMUSG00000001403.
    GeneIDi68612.
    KEGGimmu:68612.
    UCSCiuc008nvy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK003722 mRNA. Translation: BAB22959.1 .
    AK160740 mRNA. Translation: BAE35981.1 .
    CCDSi CCDS17055.1.
    RefSeqi NP_081061.1. NM_026785.2.
    UniGenei Mm.89830.

    3D structure databases

    ProteinModelPortali Q9D1C1.
    SMRi Q9D1C1. Positions 30-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212952. 4 interactions.
    STRINGi 10090.ENSMUSP00000085581.

    PTM databases

    PhosphoSitei Q9D1C1.

    Proteomic databases

    MaxQBi Q9D1C1.
    PaxDbi Q9D1C1.
    PRIDEi Q9D1C1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000088248 ; ENSMUSP00000085581 ; ENSMUSG00000001403 .
    GeneIDi 68612.
    KEGGi mmu:68612.
    UCSCi uc008nvy.1. mouse.

    Organism-specific databases

    CTDi 11065.
    MGIi MGI:1915862. Ube2c.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00730000110854.
    HOGENOMi HOG000233454.
    HOVERGENi HBG063308.
    InParanoidi Q9D1C1.
    KOi K06688.
    OMAi AELWDKD.
    OrthoDBi EOG7M0NTH.
    PhylomeDBi Q9D1C1.
    TreeFami TF101116.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_205250. Phosphorylation of the APC/C.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_207679. Separation of Sister Chromatids.
    REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
    REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

    Miscellaneous databases

    NextBioi 327556.
    PROi Q9D1C1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D1C1.
    Bgeei Q9D1C1.
    CleanExi MM_UBE2C.
    Genevestigatori Q9D1C1.

    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. "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: Embryo and Head.

    Entry informationi

    Entry nameiUBE2C_MOUSE
    AccessioniPrimary (citable) accession number: Q9D1C1
    Secondary accession number(s): Q3TUJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 102 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