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Q9UJX6

- ANC2_HUMAN

UniProt

Q9UJX6 - ANC2_HUMAN

Protein

Anaphase-promoting complex subunit 2

Gene

ANAPC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic differentiation.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. ubiquitin-protein transferase activity Source: ProtInc

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. cyclin catabolic process Source: ProtInc
    3. mitotic cell cycle Source: Reactome
    4. mitotic nuclear division Source: UniProtKB-KW
    5. mitotic spindle assembly checkpoint Source: Reactome
    6. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    7. positive regulation of axon extension Source: Ensembl
    8. positive regulation of dendrite morphogenesis Source: Ensembl
    9. positive regulation of synapse maturation Source: UniProtKB
    10. positive regulation of synaptic plasticity Source: UniProtKB
    11. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    12. protein K11-linked ubiquitination Source: UniProtKB
    13. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
    14. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. ubiquitin-dependent protein catabolic process Source: ProtInc

    Keywords - Biological processi

    Cell cycle, Cell division, Differentiation, Mitosis, Neurogenesis, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ9UJX6.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anaphase-promoting complex subunit 2
    Short name:
    APC2
    Alternative name(s):
    Cyclosome subunit 2
    Gene namesi
    Name:ANAPC2
    Synonyms:APC2, KIAA1406
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:19989. ANAPC2.

    Subcellular locationi

    GO - Cellular componenti

    1. anaphase-promoting complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134884359.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 822822Anaphase-promoting complex subunit 2PRO_0000119811Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei218 – 2181Phosphoserine3 Publications
    Modified residuei314 – 3141Phosphoserine2 Publications
    Modified residuei470 – 4701Phosphoserine2 Publications
    Modified residuei534 – 5341Phosphoserine2 Publications
    Modified residuei810 – 8101PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UJX6.
    PaxDbiQ9UJX6.
    PRIDEiQ9UJX6.

    PTM databases

    PhosphoSiteiQ9UJX6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UJX6.
    BgeeiQ9UJX6.
    CleanExiHS_ANAPC2.
    HS_APC2.
    GenevestigatoriQ9UJX6.

    Organism-specific databases

    HPAiCAB018692.

    Interactioni

    Subunit structurei

    Interacts with NEUROD2 By similarity. The APC/C is composed of at least 12 subunits. Interacts through the cullin domain with ANAPC11 and with UBCH10.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi118937. 52 interactions.
    DIPiDIP-32957N.
    IntActiQ9UJX6. 20 interactions.
    MINTiMINT-1196367.
    STRINGi9606.ENSP00000314004.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UJX6.
    SMRiQ9UJX6. Positions 508-696.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5647.
    HOGENOMiHOG000033936.
    HOVERGENiHBG045327.
    InParanoidiQ9UJX6.
    KOiK03349.
    OMAiELLVAWN.
    OrthoDBiEOG76MK7Q.
    PhylomeDBiQ9UJX6.
    TreeFamiTF105442.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR014786. APC_su2_C.
    IPR016158. Cullin_homology.
    IPR001373. Cullin_N.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF08672. APC2. 1 hit.
    PF00888. Cullin. 1 hit.
    [Graphical view]
    SMARTiSM01013. APC2. 1 hit.
    SM00182. CULLIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF75632. SSF75632. 1 hit.
    PROSITEiPS50069. CULLIN_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UJX6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP    50
    KEEELRAAVE VLRGHGLHSV LEEWFVEVLQ NDLQANISPE FWNAISQCEN 100
    SADEPQCLLL LLDAFGLLES RLDPYLRSLE LLEKWTRLGL LMGTGAQGLR 150
    EEVHTMLRGV LFFSTPRTFQ EMIQRLYGCF LRVYMQSKRK GEGGTDPELE 200
    GELDSRYARR RYYRLLQSPL CAGCSSDKQQ CWCRQALEQF HQLSQVLHRL 250
    SLLERVSAEA VTTTLHQVTR ERMEDRCRGE YERSFLREFH KWIERVVGWL 300
    GKVFLQDGPA RPASPEAGNT LRRWRCHVQR FFYRIYASLR IEELFSIVRD 350
    FPDSRPAIED LKYCLERTDQ RQQLLVSLKA ALETRLLHPG VNTCDIITLY 400
    ISAIKALRVL DPSMVILEVA CEPIRRYLRT REDTVRQIVA GLTGDSDGTG 450
    DLAVELSKTD PASLETGQDS EDDSGEPEDW VPDPVDADPG KSSSKRRSSD 500
    IISLLVSIYG SKDLFINEYR SLLADRLLHQ FSFSPEREIR NVELLKLRFG 550
    EAPMHFCEVM LKDMADSRRI NANIREEDEK RPAEEQPPFG VYAVILSSEF 600
    WPPFKDEKLE VPEDIRAALE AYCKKYEQLK AMRTLSWKHT LGLVTMDVEL 650
    ADRTLSVAVT PVQAVILLYF QDQASWTLEE LSKAVKMPVA LLRRRMSVWL 700
    QQGVLREEPP GTFSVIEEER PQDRDNMVLI DSDDESDSGM ASQADQKEEE 750
    LLLFWTYIQA MLTNLESLSL DRIYNMLRMF VVTGPALAEI DLQELQGYLQ 800
    KKVRDQQLVY SAGVYRLPKN CS 822
    Length:822
    Mass (Da):93,828
    Last modified:May 1, 2000 - v1
    Checksum:i94A2B1D015805573
    GO
    Isoform 2 (identifier: Q9UJX6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         350-352: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:819
    Mass (Da):93,469
    Checksum:iE3FC0627ECE9C324
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei350 – 3523Missing in isoform 2. 1 PublicationVSP_008463

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191337 mRNA. Translation: AAF05751.1.
    AL929554 Genomic DNA. Translation: CAH72881.1.
    BC032503 mRNA. Translation: AAH32503.1.
    BC001579 mRNA. Translation: AAH01579.1.
    BC009487 mRNA. Translation: AAH09487.2. Sequence problems.
    AB037827 mRNA. Translation: BAA92644.1.
    CCDSiCCDS7033.1. [Q9UJX6-1]
    RefSeqiNP_037498.1. NM_013366.3. [Q9UJX6-1]
    UniGeneiHs.533262.

    Genome annotation databases

    EnsembliENST00000323927; ENSP00000314004; ENSG00000176248. [Q9UJX6-1]
    GeneIDi29882.
    KEGGihsa:29882.
    UCSCiuc004clq.1. human. [Q9UJX6-2]
    uc004clr.1. human. [Q9UJX6-1]

    Polymorphism databases

    DMDMi37537863.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191337 mRNA. Translation: AAF05751.1 .
    AL929554 Genomic DNA. Translation: CAH72881.1 .
    BC032503 mRNA. Translation: AAH32503.1 .
    BC001579 mRNA. Translation: AAH01579.1 .
    BC009487 mRNA. Translation: AAH09487.2 . Sequence problems.
    AB037827 mRNA. Translation: BAA92644.1 .
    CCDSi CCDS7033.1. [Q9UJX6-1 ]
    RefSeqi NP_037498.1. NM_013366.3. [Q9UJX6-1 ]
    UniGenei Hs.533262.

    3D structure databases

    ProteinModelPortali Q9UJX6.
    SMRi Q9UJX6. Positions 508-696.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118937. 52 interactions.
    DIPi DIP-32957N.
    IntActi Q9UJX6. 20 interactions.
    MINTi MINT-1196367.
    STRINGi 9606.ENSP00000314004.

    PTM databases

    PhosphoSitei Q9UJX6.

    Polymorphism databases

    DMDMi 37537863.

    Proteomic databases

    MaxQBi Q9UJX6.
    PaxDbi Q9UJX6.
    PRIDEi Q9UJX6.

    Protocols and materials databases

    DNASUi 29882.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323927 ; ENSP00000314004 ; ENSG00000176248 . [Q9UJX6-1 ]
    GeneIDi 29882.
    KEGGi hsa:29882.
    UCSCi uc004clq.1. human. [Q9UJX6-2 ]
    uc004clr.1. human. [Q9UJX6-1 ]

    Organism-specific databases

    CTDi 29882.
    GeneCardsi GC09M140069.
    HGNCi HGNC:19989. ANAPC2.
    HPAi CAB018692.
    MIMi 606946. gene.
    neXtProti NX_Q9UJX6.
    PharmGKBi PA134884359.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5647.
    HOGENOMi HOG000033936.
    HOVERGENi HBG045327.
    InParanoidi Q9UJX6.
    KOi K03349.
    OMAi ELLVAWN.
    OrthoDBi EOG76MK7Q.
    PhylomeDBi Q9UJX6.
    TreeFami TF105442.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q9UJX6.

    Miscellaneous databases

    GeneWikii ANAPC2.
    GenomeRNAii 29882.
    NextBioi 52411.
    PROi Q9UJX6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJX6.
    Bgeei Q9UJX6.
    CleanExi HS_ANAPC2.
    HS_APC2.
    Genevestigatori Q9UJX6.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR014786. APC_su2_C.
    IPR016158. Cullin_homology.
    IPR001373. Cullin_N.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF08672. APC2. 1 hit.
    PF00888. Cullin. 1 hit.
    [Graphical view ]
    SMARTi SM01013. APC2. 1 hit.
    SM00182. CULLIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF75632. SSF75632. 1 hit.
    PROSITEi PS50069. CULLIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a cullin homology region in a subunit of the anaphase-promoting complex."
      Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.
      Science 279:1219-1222(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT.
    2. "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].
    3. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 243-822 (ISOFORM 2).
      Tissue: Brain, Cervix and Ovary.
    4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-822 (ISOFORM 1).
      Tissue: Brain.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. "APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex."
      Tang Z., Li B., Bharadwaj R., Zhu H., Oezkan E., Hakala K., Deisenhofer J., Yu H.
      Mol. Biol. Cell 12:3839-3851(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ANAPC11 AND UBCH10.
    7. "Mitotic regulation of the human anaphase-promoting complex by phosphorylation."
      Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M.
      EMBO J. 22:6598-6609(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-314 AND SER-534.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex."
      Jin L., Williamson A., Banerjee S., Philipp I., Rape M.
      Cell 133:653-665(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE APC/C.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-470 AND SER-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C."
      Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A., Engel A., Peters J.-M., Stark H.
      Mol. Cell 20:867-879(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ELECTRON MICROSCOPY OF THE APC/C.

    Entry informationi

    Entry nameiANC2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJX6
    Secondary accession number(s): Q5VSG1
    , Q96DG5, Q96GG4, Q9P2E1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 129 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