APC15_HUMAN
ID APC15_HUMAN Reviewed; 121 AA.
AC P60006; G3V1Q3; Q9CXK2; Q9Y269;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Anaphase-promoting complex subunit 15;
DE Short=APC15;
GN Name=ANAPC15; Synonyms=C11orf51; ORFNames=HSPC020;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Smooth muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE APC/C COMPLEX.
RX PubMed=21926987; DOI=10.1038/ncb2347;
RA Mansfeld J., Collin P., Collins M.O., Choudhary J.S., Pines J.;
RT "APC15 drives the turnover of MCC-CDC20 to make the spindle assembly
RT checkpoint responsive to kinetochore attachment.";
RL Nat. Cell Biol. 13:1234-1243(2011).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, AND SUBUNIT.
RX PubMed=25043029; DOI=10.1038/nature13543;
RA Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT "Molecular architecture and mechanism of the anaphase-promoting complex.";
RL Nature 513:388-393(2014).
RN [9] {ECO:0007744|PDB:4UI9, ECO:0007744|PDB:5A31}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF APC/C, AND SUBUNIT.
RX PubMed=26083744; DOI=10.1038/nature14471;
RA Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT "Atomic structure of the APC/C and its mechanism of protein
RT ubiquitination.";
RL Nature 522:450-454(2015).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle. In the
CC complex, plays a role in the release of the mitotic checkpoint complex
CC (MCC) from the APC/C: not required for APC/C activity itself, but
CC promotes the turnover of CDC20 and MCC on the APC/C, thereby
CC participating in the responsiveness of the spindle assembly checkpoint.
CC Also required for degradation of CDC20. {ECO:0000269|PubMed:21926987}.
CC -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC ANAPC16 that assemble into a complex of at least 19 chains with a
CC combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC and FBXO5. {ECO:0000269|PubMed:21926987, ECO:0000269|PubMed:25043029,
CC ECO:0000269|PubMed:26083744}.
CC -!- INTERACTION:
CC P60006; Q96LK0: CEP19; NbExp=3; IntAct=EBI-8787535, EBI-741885;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60006-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60006-2; Sequence=VSP_055048;
CC -!- SIMILARITY: Belongs to the APC15 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW74842.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF077206; AAD27001.1; -; mRNA.
DR EMBL; AL080071; CAB45698.1; -; mRNA.
DR EMBL; AK222622; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AP000812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74842.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC005156; AAH05156.1; -; mRNA.
DR EMBL; BC005393; AAH05393.1; -; mRNA.
DR CCDS; CCDS60880.1; -. [P60006-2]
DR CCDS; CCDS8210.1; -. [P60006-1]
DR PIR; T12467; T12467.
DR RefSeq; NP_001265414.1; NM_001278485.1. [P60006-2]
DR RefSeq; NP_001265415.1; NM_001278486.1. [P60006-2]
DR RefSeq; NP_001265416.1; NM_001278487.1. [P60006-1]
DR RefSeq; NP_001265417.1; NM_001278488.1. [P60006-1]
DR RefSeq; NP_001265418.1; NM_001278489.1. [P60006-1]
DR RefSeq; NP_001265419.1; NM_001278490.1. [P60006-1]
DR RefSeq; NP_001265420.1; NM_001278491.1. [P60006-1]
DR RefSeq; NP_001265421.1; NM_001278492.1. [P60006-1]
DR RefSeq; NP_001265422.1; NM_001278493.1. [P60006-1]
DR RefSeq; NP_001265423.1; NM_001278494.1. [P60006-1]
DR RefSeq; NP_054761.1; NM_014042.2. [P60006-1]
DR RefSeq; XP_016872985.1; XM_017017496.1. [P60006-1]
DR RefSeq; XP_016872986.1; XM_017017497.1. [P60006-1]
DR PDB; 4UI9; EM; 3.60 A; D=1-121.
DR PDB; 5A31; EM; 4.30 A; D=6-121.
DR PDB; 5G04; EM; 4.00 A; D=1-121.
DR PDB; 5G05; EM; 3.40 A; D=1-121.
DR PDB; 5L9T; EM; 6.40 A; D=1-121.
DR PDB; 5L9U; EM; 6.40 A; D=1-121.
DR PDB; 5LCW; EM; 4.00 A; D=1-121.
DR PDB; 6Q6G; EM; 3.20 A; D=1-121.
DR PDB; 6Q6H; EM; 3.20 A; D=1-121.
DR PDB; 6TLJ; EM; 3.80 A; D=1-121.
DR PDB; 6TM5; EM; 3.90 A; D=1-121.
DR PDB; 6TNT; EM; 3.78 A; D=1-121.
DR PDB; 7QE7; EM; 2.90 A; D=1-121.
DR PDBsum; 4UI9; -.
DR PDBsum; 5A31; -.
DR PDBsum; 5G04; -.
DR PDBsum; 5G05; -.
DR PDBsum; 5L9T; -.
DR PDBsum; 5L9U; -.
DR PDBsum; 5LCW; -.
DR PDBsum; 6Q6G; -.
DR PDBsum; 6Q6H; -.
DR PDBsum; 6TLJ; -.
DR PDBsum; 6TM5; -.
DR PDBsum; 6TNT; -.
DR PDBsum; 7QE7; -.
DR AlphaFoldDB; P60006; -.
DR SMR; P60006; -.
DR BioGRID; 117412; 131.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR DIP; DIP-61021N; -.
DR IntAct; P60006; 47.
DR STRING; 9606.ENSP00000439403; -.
DR BioMuta; ANAPC15; -.
DR DMDM; 38372627; -.
DR EPD; P60006; -.
DR MassIVE; P60006; -.
DR MaxQB; P60006; -.
DR PaxDb; P60006; -.
DR PeptideAtlas; P60006; -.
DR PRIDE; P60006; -.
DR ProteomicsDB; 57178; -. [P60006-1]
DR Antibodypedia; 44861; 36 antibodies from 16 providers.
DR DNASU; 25906; -.
DR Ensembl; ENST00000227618.9; ENSP00000227618.4; ENSG00000110200.9. [P60006-1]
DR Ensembl; ENST00000535234.5; ENSP00000446412.1; ENSG00000110200.9. [P60006-1]
DR Ensembl; ENST00000535503.5; ENSP00000443383.1; ENSG00000110200.9. [P60006-1]
DR Ensembl; ENST00000538393.5; ENSP00000440002.1; ENSG00000110200.9. [P60006-1]
DR Ensembl; ENST00000538919.5; ENSP00000440983.1; ENSG00000110200.9. [P60006-1]
DR Ensembl; ENST00000542531.5; ENSP00000443911.1; ENSG00000110200.9. [P60006-1]
DR Ensembl; ENST00000543587.5; ENSP00000439403.1; ENSG00000110200.9. [P60006-2]
DR Ensembl; ENST00000545680.5; ENSP00000443645.1; ENSG00000110200.9. [P60006-2]
DR Ensembl; ENST00000545944.5; ENSP00000446383.1; ENSG00000110200.9. [P60006-1]
DR GeneID; 25906; -.
DR KEGG; hsa:25906; -.
DR MANE-Select; ENST00000227618.9; ENSP00000227618.4; NM_014042.3; NP_054761.1.
DR UCSC; uc001orv.5; human. [P60006-1]
DR CTD; 25906; -.
DR DisGeNET; 25906; -.
DR GeneCards; ANAPC15; -.
DR HGNC; HGNC:24531; ANAPC15.
DR HPA; ENSG00000110200; Low tissue specificity.
DR MIM; 614717; gene.
DR neXtProt; NX_P60006; -.
DR OpenTargets; ENSG00000110200; -.
DR PharmGKB; PA143485346; -.
DR VEuPathDB; HostDB:ENSG00000110200; -.
DR eggNOG; ENOG502RZUK; Eukaryota.
DR GeneTree; ENSGT00390000000938; -.
DR HOGENOM; CLU_142923_0_0_1; -.
DR InParanoid; P60006; -.
DR OMA; EGTDQDQ; -.
DR PhylomeDB; P60006; -.
DR PathwayCommons; P60006; -.
DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-HSA-176412; Phosphorylation of the APC/C.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR SignaLink; P60006; -.
DR BioGRID-ORCS; 25906; 412 hits in 1081 CRISPR screens.
DR ChiTaRS; ANAPC15; human.
DR GenomeRNAi; 25906; -.
DR Pharos; P60006; Tdark.
DR PRO; PR:P60006; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P60006; protein.
DR Bgee; ENSG00000110200; Expressed in apex of heart and 193 other tissues.
DR ExpressionAtlas; P60006; baseline and differential.
DR Genevisible; P60006; HS.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IC:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
DR DisProt; DP01454; -.
DR InterPro; IPR026182; ANAPC15.
DR PANTHER; PTHR22526; PTHR22526; 1.
DR Pfam; PF15243; ANAPC15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Mitosis;
KW Reference proteome.
FT CHAIN 1..121
FT /note="Anaphase-promoting complex subunit 15"
FT /id="PRO_0000084072"
FT REGION 46..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 106
FT /note="E -> EPPLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055048"
FT CONFLICT 73
FT /note="D -> G (in Ref. 3; AK222622)"
FT /evidence="ECO:0000305"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 26..45
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:5G05"
SQ SEQUENCE 121 AA; 14281 MW; 2C889607C3013A82 CRC64;
MSTLFPSLFP RVTETLWFNL DRPCVEETEL QQQEQQHQAW LQSIAEKDNN LVPIGKPASE
HYDDEEEEDD EDDEDSEEDS EDDEDMQDMD EMNDYNESPD DGEVNEVDME GNEQDQDQWM
I
