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Q9UJX4

- APC5_HUMAN

UniProt

Q9UJX4 - APC5_HUMAN

Protein

Anaphase-promoting complex subunit 5

Gene

ANAPC5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      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.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. protein phosphatase binding Source: BHF-UCL
    2. ubiquitin-protein transferase activity Source: ProtInc

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. G2/M transition of mitotic cell cycle Source: ProtInc
    3. mitotic anaphase Source: ProtInc
    4. mitotic cell cycle Source: Reactome
    5. mitotic nuclear division Source: UniProtKB-KW
    6. mitotic spindle assembly checkpoint Source: Reactome
    7. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    8. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    9. protein K11-linked ubiquitination Source: UniProtKB
    10. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    11. ubiquitin-dependent protein catabolic process Source: ProtInc

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, 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.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anaphase-promoting complex subunit 5
    Short name:
    APC5
    Alternative name(s):
    Cyclosome subunit 5
    Gene namesi
    Name:ANAPC5
    Synonyms:APC5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:15713. ANAPC5.

    Subcellular locationi

    GO - Cellular componenti

    1. anaphase-promoting complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: BHF-UCL

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24788.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 755755Anaphase-promoting complex subunit 5PRO_0000064597Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei195 – 1951Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UJX4.
    PaxDbiQ9UJX4.
    PeptideAtlasiQ9UJX4.
    PRIDEiQ9UJX4.

    PTM databases

    PhosphoSiteiQ9UJX4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UJX4.
    BgeeiQ9UJX4.
    CleanExiHS_ANAPC5.
    GenevestigatoriQ9UJX4.

    Organism-specific databases

    HPAiHPA039457.

    Interactioni

    Subunit structurei

    The APC/C is composed of at least 12 subunits.1 Publication

    Protein-protein interaction databases

    BioGridi119537. 53 interactions.
    DIPiDIP-32945N.
    IntActiQ9UJX4. 28 interactions.
    MINTiMINT-1391095.
    STRINGi9606.ENSP00000261819.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UJX4.
    SMRiQ9UJX4. Positions 472-498, 545-608, 618-648.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati301 – 33434TPR 1Add
    BLAST
    Repeati522 – 55534TPR 2Add
    BLAST
    Repeati581 – 61434TPR 3Add
    BLAST
    Repeati678 – 71134TPR 4Add
    BLAST

    Sequence similaritiesi

    Belongs to the APC5 family.Curated
    Contains 4 TPR repeats.Curated

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiNOG320252.
    HOGENOMiHOG000033988.
    HOVERGENiHBG001285.
    InParanoidiQ9UJX4.
    KOiK03352.
    OMAiLYWRSSC.
    OrthoDBiEOG7T7GSR.
    PhylomeDBiQ9UJX4.
    TreeFamiTF105444.

    Family and domain databases

    Gene3Di1.25.40.10. 4 hits.
    InterProiIPR026000. Apc5/TPR19_dom.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PfamiPF12862. Apc5. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UJX4-1) [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

    MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG    50
    AVSLMERRRL NQLLLPLLQG PDITLSKLYK LIEESCPQLA NSVQIRIKLM 100
    AEGELKDMEQ FFDDLSDSFS GTEPEVHKTS VVGLFLRHMI LAYSKLSFSQ 150
    VFKLYTALQQ YFQNGEKKTV EDADMELTSR DEGERKMEKE ELDVSVREEE 200
    VSCSGPLSQK QAEFFLSQQA SLLKNDETKA LTPASLQKEL NNLLKFNPDF 250
    AEAHYLSYLN NLRVQDVFSS THSLLHYFDR LILTGAESKS NGEEGYGRSL 300
    RYAALNLAAL HCRFGHYQQA ELALQEAIRI AQESNDHVCL QHCLSWLYVL 350
    GQKRSDSYVL LEHSVKKAVH FGLPYLASLG IQSLVQQRAF AGKTANKLMD 400
    ALKDSDLLHW KHSLSELIDI SIAQKTAIWR LYGRSTMALQ QAQMLLSMNS 450
    LEAVNAGVQQ NNTESFAVAL CHLAELHAEQ GCFAAASEVL KHLKERFPPN 500
    SQHAQLWMLC DQKIQFDRAM NDGKYHLADS LVTGITALNS IEGVYRKAVV 550
    LQAQNQMSEA HKLLQKLLVH CQKLKNTEMV ISVLLSVAEL YWRSSSPTIA 600
    LPMLLQALAL SKEYRLQYLA SETVLNLAFA QLILGIPEQA LSLLHMAIEP 650
    ILADGAILDK GRAMFLVAKC QVASAASYDQ PKKAEALEAA IENLNEAKNY 700
    FAKVDCKERI RDVVYFQARL YHTLGKTQER NRCAMLFRQL HQELPSHGVP 750
    LINHL 755
    Length:755
    Mass (Da):85,077
    Last modified:October 3, 2003 - v2
    Checksum:i174F68EAB44760EB
    GO
    Isoform 2 (identifier: Q9UJX4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-121: Missing.
         122-131: TEPEVHKTSV → MLSPCLSSYF
         318-340: QQAELALQEAIRIAQESNDHVCL → TSPPWEYSPLFNRELLLGRRQTS
         341-755: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:219
    Mass (Da):25,147
    Checksum:iE74D54AFF6C8744E
    GO
    Isoform 3 (identifier: Q9UJX4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-99: Missing.
         375-387: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:643
    Mass (Da):72,526
    Checksum:i6245611F5812F7CC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241F → L in AAF05753. (PubMed:9469815)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti617 – 6171Q → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035793

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 121121Missing in isoform 2. 1 PublicationVSP_008466Add
    BLAST
    Alternative sequencei1 – 9999Missing in isoform 3. 1 PublicationVSP_044878Add
    BLAST
    Alternative sequencei122 – 13110TEPEVHKTSV → MLSPCLSSYF in isoform 2. 1 PublicationVSP_008467
    Alternative sequencei318 – 34023QQAEL…DHVCL → TSPPWEYSPLFNRELLLGRR QTS in isoform 2. 1 PublicationVSP_008468Add
    BLAST
    Alternative sequencei341 – 755415Missing in isoform 2. 1 PublicationVSP_008469Add
    BLAST
    Alternative sequencei375 – 38713Missing in isoform 3. 1 PublicationVSP_044879Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191339 mRNA. Translation: AAF05753.1.
    AK025614 mRNA. No translation available.
    BX537687 mRNA. Translation: CAD97812.1.
    AC048337 Genomic DNA. No translation available.
    AC069209 Genomic DNA. No translation available.
    BC001081 mRNA. Translation: AAH01081.1.
    BC001950 mRNA. Translation: AAH01950.1.
    BC006301 mRNA. Translation: AAH06301.1.
    BC034243 mRNA. Translation: AAH34243.1.
    CCDSiCCDS45000.1. [Q9UJX4-3]
    CCDS9220.1. [Q9UJX4-1]
    RefSeqiNP_001131031.1. NM_001137559.1. [Q9UJX4-3]
    NP_057321.2. NM_016237.4. [Q9UJX4-1]
    UniGeneiHs.7101.

    Genome annotation databases

    EnsembliENST00000261819; ENSP00000261819; ENSG00000089053. [Q9UJX4-1]
    ENST00000441917; ENSP00000415061; ENSG00000089053. [Q9UJX4-3]
    GeneIDi51433.
    KEGGihsa:51433.
    UCSCiuc001uag.3. human. [Q9UJX4-1]
    uc001uah.3. human.

    Polymorphism databases

    DMDMi37537861.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191339 mRNA. Translation: AAF05753.1 .
    AK025614 mRNA. No translation available.
    BX537687 mRNA. Translation: CAD97812.1 .
    AC048337 Genomic DNA. No translation available.
    AC069209 Genomic DNA. No translation available.
    BC001081 mRNA. Translation: AAH01081.1 .
    BC001950 mRNA. Translation: AAH01950.1 .
    BC006301 mRNA. Translation: AAH06301.1 .
    BC034243 mRNA. Translation: AAH34243.1 .
    CCDSi CCDS45000.1. [Q9UJX4-3 ]
    CCDS9220.1. [Q9UJX4-1 ]
    RefSeqi NP_001131031.1. NM_001137559.1. [Q9UJX4-3 ]
    NP_057321.2. NM_016237.4. [Q9UJX4-1 ]
    UniGenei Hs.7101.

    3D structure databases

    ProteinModelPortali Q9UJX4.
    SMRi Q9UJX4. Positions 472-498, 545-608, 618-648.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119537. 53 interactions.
    DIPi DIP-32945N.
    IntActi Q9UJX4. 28 interactions.
    MINTi MINT-1391095.
    STRINGi 9606.ENSP00000261819.

    PTM databases

    PhosphoSitei Q9UJX4.

    Polymorphism databases

    DMDMi 37537861.

    Proteomic databases

    MaxQBi Q9UJX4.
    PaxDbi Q9UJX4.
    PeptideAtlasi Q9UJX4.
    PRIDEi Q9UJX4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261819 ; ENSP00000261819 ; ENSG00000089053 . [Q9UJX4-1 ]
    ENST00000441917 ; ENSP00000415061 ; ENSG00000089053 . [Q9UJX4-3 ]
    GeneIDi 51433.
    KEGGi hsa:51433.
    UCSCi uc001uag.3. human. [Q9UJX4-1 ]
    uc001uah.3. human.

    Organism-specific databases

    CTDi 51433.
    GeneCardsi GC12M121746.
    HGNCi HGNC:15713. ANAPC5.
    HPAi HPA039457.
    MIMi 606948. gene.
    neXtProti NX_Q9UJX4.
    PharmGKBi PA24788.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320252.
    HOGENOMi HOG000033988.
    HOVERGENi HBG001285.
    InParanoidi Q9UJX4.
    KOi K03352.
    OMAi LYWRSSC.
    OrthoDBi EOG7T7GSR.
    PhylomeDBi Q9UJX4.
    TreeFami TF105444.

    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.

    Miscellaneous databases

    ChiTaRSi ANAPC5. human.
    GeneWikii ANAPC5.
    GenomeRNAii 51433.
    NextBioi 55001.
    PROi Q9UJX4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJX4.
    Bgeei Q9UJX4.
    CleanExi HS_ANAPC5.
    Genevestigatori Q9UJX4.

    Family and domain databases

    Gene3Di 1.25.40.10. 4 hits.
    InterProi IPR026000. Apc5/TPR19_dom.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    Pfami PF12862. Apc5. 2 hits.
    [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. "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] (ISOFORM 3).
      Tissue: Hepatoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Esophagus.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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).
      Tissue: Brain, Cervix and Lung.
    6. "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-195.
    7. "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.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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.
    11. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-617.

    Entry informationi

    Entry nameiAPC5_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJX4
    Secondary accession number(s): E9PFB2, Q8N4H7, Q9BQD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3