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Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Cyclosome subunit 8)

 CDC23_HUMAN             Reviewed;         597 AA.
Q9UJX2; A8K6E5; B4E3A2; B7WP05; D3DQB7; O75433; Q53FN2; Q9BS73;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 3.
12-AUG-2020, entry version 195.
RecName: Full=Cell division cycle protein 23 homolog;
AltName: Full=Anaphase-promoting complex subunit 8;
Short=APC8;
AltName: Full=Cyclosome subunit 8;
Name=CDC23; Synonyms=ANAPC8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Oyamatsu T., Kotani S., Todokoro K.;
"Human CDC23 gene.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Placenta, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-78.
NIEHS SNPs program;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Gastric mucosa;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 5-597 (ISOFORM 1).
TISSUE=Brain, Duodenum, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-597 (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=9790767; DOI=10.1006/geno.1998.5473;
Zhao N., Lai F., Fernald A.A., Eisenbart J.D., Espinosa R., Wang P.W.,
Le Beau M.M.;
"Human CDC23: cDNA cloning, mapping to 5q31, genomic structure, and
evaluation as a candidate tumor suppressor gene in myeloid leukemias.";
Genomics 53:184-190(1998).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-597 (ISOFORM 1), AND SUBUNIT.
PubMed=9469815; DOI=10.1126/science.279.5354.1219;
Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.;
"Identification of a cullin homology region in a subunit of the anaphase-
promoting complex.";
Science 279:1219-1222(1998).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-597 (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[11]
PHOSPHORYLATION AT TYR-273; THR-562 AND THR-565.
PubMed=14657031; DOI=10.1093/emboj/cdg627;
Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,
Peters J.-M.;
"Mitotic regulation of the human anaphase-promoting complex by
phosphorylation.";
EMBO J. 22:6598-6609(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
FUNCTION OF THE APC/C.
PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
"Mechanism of ubiquitin-chain formation by the human anaphase-promoting
complex.";
Cell 133:653-665(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562; THR-582; SER-588;
SER-593 AND THR-596, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; THR-582; SER-588 AND
THR-596, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-467, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
TPR REPEATS.
PubMed=21307936; DOI=10.1038/nature09756;
Schreiber A., Stengel F., Zhang Z., Enchev R.I., Kong E.H., Morris E.P.,
Robinson C.V., da Fonseca P.C., Barford D.;
"Structural basis for the subunit assembly of the anaphase-promoting
complex.";
Nature 470:227-232(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; SER-588; SER-593 AND
THR-596, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[27]
STRUCTURE BY ELECTRON MICROSCOPY OF THE APC/C.
PubMed=16364912; DOI=10.1016/j.molcel.2005.11.008;
Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A.,
Engel A., Peters J.-M., Stark H.;
"Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a
cryo-electron microscopy model of vertebrate APC/C.";
Mol. Cell 20:867-879(2005).
[28]
STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, AND SUBUNIT.
PubMed=25043029; DOI=10.1038/nature13543;
Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
"Molecular architecture and mechanism of the anaphase-promoting complex.";
Nature 513:388-393(2014).
[29] {ECO:0000244|PDB:4UI9, ECO:0000244|PDB:5A31}
STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 7-597 OF APC/C,
SUBUNIT, AND MUTAGENESIS OF ASN-339 AND GLU-374.
PubMed=26083744; DOI=10.1038/nature14471;
Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
"Atomic structure of the APC/C and its mechanism of protein
ubiquitination.";
Nature 522:450-454(2015).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:18485873}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
ANAPC16 that assemble into a complex of at least 19 chains with a
combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
and FBXO5. {ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744,
ECO:0000269|PubMed:9469815}.
-!- INTERACTION:
Q9UJX2; A8K3Z6: ANAPC13; NbExp=3; IntAct=EBI-396137, EBI-10322710;
Q9UJX2; Q9BS18: ANAPC13; NbExp=7; IntAct=EBI-396137, EBI-2555953;
Q9UJX2; X5D778: ANKRD11; NbExp=3; IntAct=EBI-396137, EBI-17183751;
Q9UJX2; O14791: APOL1; NbExp=3; IntAct=EBI-396137, EBI-1221934;
Q9UJX2; Q8WXE1: ATRIP; NbExp=3; IntAct=EBI-396137, EBI-747353;
Q9UJX2; Q9H6U6: BCAS3; NbExp=3; IntAct=EBI-396137, EBI-6083685;
Q9UJX2; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-396137, EBI-742722;
Q9UJX2; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-396137, EBI-11519926;
Q9UJX2; Q13895: BYSL; NbExp=5; IntAct=EBI-396137, EBI-358049;
Q9UJX2; Q8NA61: CBY2; NbExp=3; IntAct=EBI-396137, EBI-741724;
Q9UJX2; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-396137, EBI-11977221;
Q9UJX2; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-396137, EBI-1104933;
Q9UJX2; Q8IYA8: CCDC36; NbExp=6; IntAct=EBI-396137, EBI-8638439;
Q9UJX2; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-396137, EBI-744115;
Q9UJX2; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-396137, EBI-12261896;
Q9UJX2; P38432: COIL; NbExp=3; IntAct=EBI-396137, EBI-945751;
Q9UJX2; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-396137, EBI-739773;
Q9UJX2; Q53ET0: CRTC2; NbExp=3; IntAct=EBI-396137, EBI-1181987;
Q9UJX2; Q6BCY4: CYB5R2; NbExp=3; IntAct=EBI-396137, EBI-744761;
Q9UJX2; O15075-2: DCLK1; NbExp=3; IntAct=EBI-396137, EBI-12324841;
Q9UJX2; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-396137, EBI-11988027;
Q9UJX2; Q9GZV4: EIF5A2; NbExp=3; IntAct=EBI-396137, EBI-748028;
Q9UJX2; Q9NYK6-3: EURL; NbExp=3; IntAct=EBI-396137, EBI-13371226;
Q9UJX2; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-396137, EBI-10175124;
Q9UJX2; A4D1I3: FLJ34048; NbExp=3; IntAct=EBI-396137, EBI-10173415;
Q9UJX2; O15353: FOXN1; NbExp=3; IntAct=EBI-396137, EBI-11319000;
Q9UJX2; O95073: FSBP; NbExp=3; IntAct=EBI-396137, EBI-1059030;
Q9UJX2; Q9H8Y8: GORASP2; NbExp=9; IntAct=EBI-396137, EBI-739467;
Q9UJX2; Q8N3Z3: GTPBP8; NbExp=3; IntAct=EBI-396137, EBI-6912536;
Q9UJX2; Q9Y5R4: HEMK1; NbExp=3; IntAct=EBI-396137, EBI-10329202;
Q9UJX2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-396137, EBI-6509505;
Q9UJX2; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-396137, EBI-769401;
Q9UJX2; Q15735: INPP5J; NbExp=3; IntAct=EBI-396137, EBI-10236940;
Q9UJX2; Q8NC69: KCTD6; NbExp=6; IntAct=EBI-396137, EBI-2511344;
Q9UJX2; O76013-2: KRT36; NbExp=3; IntAct=EBI-396137, EBI-11958506;
Q9UJX2; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-396137, EBI-12039345;
Q9UJX2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-396137, EBI-1216080;
Q9UJX2; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-396137, EBI-741037;
Q9UJX2; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-396137, EBI-716006;
Q9UJX2; Q15742: NAB2; NbExp=3; IntAct=EBI-396137, EBI-8641936;
Q9UJX2; Q96F24: NRBF2; NbExp=3; IntAct=EBI-396137, EBI-2362014;
Q9UJX2; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-396137, EBI-741048;
Q9UJX2; Q96CV9: OPTN; NbExp=8; IntAct=EBI-396137, EBI-748974;
Q9UJX2; Q16877: PFKFB4; NbExp=3; IntAct=EBI-396137, EBI-764534;
Q9UJX2; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-396137, EBI-10232538;
Q9UJX2; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-396137, EBI-10171633;
Q9UJX2; P78424: POU6F2; NbExp=3; IntAct=EBI-396137, EBI-12029004;
Q9UJX2; Q2NL68: PROSER3; NbExp=3; IntAct=EBI-396137, EBI-11336487;
Q9UJX2; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-396137, EBI-1567797;
Q9UJX2; P63000: RAC1; NbExp=3; IntAct=EBI-396137, EBI-413628;
Q9UJX2; Q8NDT2-2: RBM15B; NbExp=3; IntAct=EBI-396137, EBI-10269922;
Q9UJX2; P10745: RBP3; NbExp=3; IntAct=EBI-396137, EBI-12806054;
Q9UJX2; Q93062: RBPMS; NbExp=4; IntAct=EBI-396137, EBI-740322;
Q9UJX2; Q9UHA3: RSL24D1; NbExp=3; IntAct=EBI-396137, EBI-749321;
Q9UJX2; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-396137, EBI-11984663;
Q9UJX2; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-396137, EBI-747107;
Q9UJX2; Q9HAB3: SLC52A2; NbExp=3; IntAct=EBI-396137, EBI-10309896;
Q9UJX2; Q53HV7: SMUG1; NbExp=3; IntAct=EBI-396137, EBI-749970;
Q9UJX2; O60504: SORBS3; NbExp=3; IntAct=EBI-396137, EBI-741237;
Q9UJX2; P35711: SOX5; NbExp=3; IntAct=EBI-396137, EBI-3505701;
Q9UJX2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-396137, EBI-11959123;
Q9UJX2; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-396137, EBI-2212028;
Q9UJX2; P32856-2: STX2; NbExp=3; IntAct=EBI-396137, EBI-11956649;
Q9UJX2; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-396137, EBI-11139477;
Q9UJX2; Q15025: TNIP1; NbExp=3; IntAct=EBI-396137, EBI-357849;
Q9UJX2; P14373: TRIM27; NbExp=4; IntAct=EBI-396137, EBI-719493;
Q9UJX2; Q9Y3Q8: TSC22D4; NbExp=4; IntAct=EBI-396137, EBI-739485;
Q9UJX2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-396137, EBI-11975223;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9UJX2-1; Sequence=Displayed;
Name=2;
IsoId=Q9UJX2-2; Sequence=VSP_008429, VSP_008430;
Name=3;
IsoId=Q9UJX2-3; Sequence=VSP_037678;
-!- PTM: Phosphorylated. Phosphorylation on Thr-562 occurs specifically
during mitosis. {ECO:0000269|PubMed:14657031}.
-!- SIMILARITY: Belongs to the APC8/CDC23 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC70920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH05258.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH10944.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH17713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAS99353.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA75628.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD96970.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAF84299.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc23/";
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AB011472; BAA75628.1; ALT_INIT; mRNA.
EMBL; AK291610; BAF84299.1; ALT_INIT; mRNA.
EMBL; AK304635; BAG65414.1; -; mRNA.
EMBL; AY603103; AAS99353.1; ALT_INIT; Genomic_DNA.
EMBL; AK223250; BAD96970.1; ALT_INIT; mRNA.
EMBL; AC106752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW62155.1; -; Genomic_DNA.
EMBL; CH471062; EAW62154.1; -; Genomic_DNA.
EMBL; CH471062; EAW62156.1; -; Genomic_DNA.
EMBL; BC005258; AAH05258.1; ALT_INIT; mRNA.
EMBL; BC010944; AAH10944.1; ALT_INIT; mRNA.
EMBL; BC017713; AAH17713.1; ALT_INIT; mRNA.
EMBL; AF053977; AAC70920.1; ALT_INIT; mRNA.
EMBL; AF191341; AAF05755.1; -; mRNA.
EMBL; BT009810; AAP88812.1; -; mRNA.
CCDS; CCDS4200.2; -. [Q9UJX2-1]
PIR; T51168; T51168.
RefSeq; NP_004652.2; NM_004661.3. [Q9UJX2-1]
PDB; 4UI9; EM; 3.60 A; C/P=7-597.
PDB; 5A31; EM; 4.30 A; C/P=1-597.
PDB; 5G04; EM; 4.00 A; C/P=1-597.
PDB; 5G05; EM; 3.40 A; C/P=1-597.
PDB; 5KHR; EM; 6.10 A; C/P=1-597.
PDB; 5KHU; EM; 4.80 A; C/P=1-597.
PDB; 5L9T; EM; 6.40 A; C/P=1-597.
PDB; 5L9U; EM; 6.40 A; C/P=1-597.
PDB; 5LCW; EM; 4.00 A; C/P=1-597.
PDB; 6Q6G; EM; 3.20 A; U/V=1-597.
PDB; 6Q6H; EM; 3.20 A; U/V=1-597.
PDB; 6TLJ; EM; 3.80 A; C/P=1-597.
PDB; 6TM5; EM; 3.90 A; C/P=1-597.
PDBsum; 4UI9; -.
PDBsum; 5A31; -.
PDBsum; 5G04; -.
PDBsum; 5G05; -.
PDBsum; 5KHR; -.
PDBsum; 5KHU; -.
PDBsum; 5L9T; -.
PDBsum; 5L9U; -.
PDBsum; 5LCW; -.
PDBsum; 6Q6G; -.
PDBsum; 6Q6H; -.
PDBsum; 6TLJ; -.
PDBsum; 6TM5; -.
SMR; Q9UJX2; -.
BioGRID; 114242; 161.
CORUM; Q9UJX2; -.
DIP; DIP-32959N; -.
ELM; Q9UJX2; -.
IntAct; Q9UJX2; 156.
MINT; Q9UJX2; -.
STRING; 9606.ENSP00000378350; -.
iPTMnet; Q9UJX2; -.
PhosphoSitePlus; Q9UJX2; -.
BioMuta; CDC23; -.
DMDM; 254763423; -.
EPD; Q9UJX2; -.
jPOST; Q9UJX2; -.
MassIVE; Q9UJX2; -.
PaxDb; Q9UJX2; -.
PeptideAtlas; Q9UJX2; -.
PRIDE; Q9UJX2; -.
ProteomicsDB; 84679; -. [Q9UJX2-1]
ProteomicsDB; 84680; -. [Q9UJX2-2]
ProteomicsDB; 84681; -. [Q9UJX2-3]
Antibodypedia; 14882; 281 antibodies.
DNASU; 8697; -.
Ensembl; ENST00000394884; ENSP00000378348; ENSG00000094880. [Q9UJX2-2]
Ensembl; ENST00000394886; ENSP00000378350; ENSG00000094880. [Q9UJX2-1]
GeneID; 8697; -.
KEGG; hsa:8697; -.
UCSC; uc003lcl.3; human. [Q9UJX2-1]
CTD; 8697; -.
DisGeNET; 8697; -.
EuPathDB; HostDB:ENSG00000094880.10; -.
GeneCards; CDC23; -.
HGNC; HGNC:1724; CDC23.
HPA; ENSG00000094880; Low tissue specificity.
MIM; 603462; gene.
neXtProt; NX_Q9UJX2; -.
OpenTargets; ENSG00000094880; -.
PharmGKB; PA26258; -.
eggNOG; KOG1155; Eukaryota.
GeneTree; ENSGT00950000182950; -.
HOGENOM; CLU_018320_3_0_1; -.
InParanoid; Q9UJX2; -.
KO; K03355; -.
OMA; EYDRCAA; -.
OrthoDB; 761109at2759; -.
PhylomeDB; Q9UJX2; -.
TreeFam; TF101055; -.
PathwayCommons; Q9UJX2; -.
Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
Reactome; R-HSA-176412; Phosphorylation of the APC/C.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q9UJX2; -.
UniPathway; UPA00143; -.
BioGRID-ORCS; 8697; 748 hits in 878 CRISPR screens.
ChiTaRS; CDC23; human.
GeneWiki; CDC23; -.
GenomeRNAi; 8697; -.
Pharos; Q9UJX2; Tbio.
PRO; PR:Q9UJX2; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; Q9UJX2; protein.
Bgee; ENSG00000094880; Expressed in female gonad and 235 other tissues.
ExpressionAtlas; Q9UJX2; baseline and differential.
Genevisible; Q9UJX2; HS.
GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
GO; GO:0051301; P:cell division; IBA:GO_Central.
GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
GO; GO:0007080; P:mitotic metaphase plate congression; IDA:UniProtKB.
GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
GO; GO:0007096; P:regulation of exit from mitosis; TAS:ProtInc.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:Reactome.
DisProt; DP01240; -.
Gene3D; 1.25.40.10; -; 2.
InterPro; IPR007192; APC8.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
Pfam; PF04049; ANAPC8; 1.
Pfam; PF13181; TPR_8; 1.
SMART; SM00028; TPR; 7.
SUPFAM; SSF48452; SSF48452; 2.
PROSITE; PS50005; TPR; 6.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
Isopeptide bond; Mitosis; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; TPR repeat; Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000244|PubMed:22814378"
CHAIN 2..597
/note="Cell division cycle protein 23 homolog"
/id="PRO_0000106270"
REPEAT 27..63
/note="TPR 1"
REPEAT 73..112
/note="TPR 2"
REPEAT 114..144
/note="TPR 3"
REPEAT 169..200
/note="TPR 4"
REPEAT 229..259
/note="TPR 5"
REPEAT 263..293
/note="TPR 6"
REPEAT 297..327
/note="TPR 7"
REPEAT 331..361
/note="TPR 8"
REPEAT 366..395
/note="TPR 9"
REPEAT 400..432
/note="TPR 10"
REPEAT 433..466
/note="TPR 11"
REPEAT 468..500
/note="TPR 12"
REPEAT 504..540
/note="TPR 13"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000244|PubMed:22814378"
MOD_RES 273
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:14657031"
MOD_RES 467
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 562
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:14657031"
MOD_RES 565
/note="Phosphothreonine"
/evidence="ECO:0000269|PubMed:14657031"
MOD_RES 578
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163"
MOD_RES 582
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332"
MOD_RES 588
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 593
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163"
MOD_RES 596
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
CROSSLNK 147
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
VAR_SEQ 1..118
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_037678"
VAR_SEQ 125..151
/note="SGEKKKDDETVDSLGPLEKGQVKNEAL -> VRAILKCHSAFSETSIFRTNG
KVKSFK (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_008429"
VAR_SEQ 152..597
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_008430"
VARIANT 9
/note="P -> L (in dbSNP:rs2231471)"
/id="VAR_024675"
VARIANT 78
/note="E -> Q (in dbSNP:rs17228304)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_019232"
MUTAGEN 339
/note="N->A: Inhibits APC/FZR1 E3 ubiquitin-protein ligase
complex activity; when associated with A-374."
/evidence="ECO:0000269|PubMed:26083744"
MUTAGEN 374
/note="E->A: Inhibits APC/FZR1 E3 ubiquitin-protein ligase
complex activity; when associated with A-339."
/evidence="ECO:0000269|PubMed:26083744"
CONFLICT 83
/note="D -> E (in Ref. 4; BAD96970)"
/evidence="ECO:0000305"
CONFLICT 105
/note="F -> S (in Ref. 4; BAD96970)"
/evidence="ECO:0000305"
CONFLICT 527
/note="D -> G (in Ref. 2; BAG65414)"
/evidence="ECO:0000305"
CONFLICT 588
/note="S -> F (in Ref. 9; AAF05755)"
/evidence="ECO:0000305"
HELIX 29..45
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 49..61
/evidence="ECO:0000244|PDB:6Q6G"
TURN 67..69
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 78..81
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 84..95
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 99..105
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 112..133
/evidence="ECO:0000244|PDB:6Q6G"
STRAND 137..139
/evidence="ECO:0000244|PDB:6Q6H"
TURN 140..142
/evidence="ECO:0000244|PDB:5G05"
STRAND 143..145
/evidence="ECO:0000244|PDB:5G05"
HELIX 149..163
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 170..181
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 185..198
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 203..210
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 216..221
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 229..240
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 244..257
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 259..261
/evidence="ECO:0000244|PDB:5G05"
HELIX 263..276
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 279..292
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 300..308
/evidence="ECO:0000244|PDB:6Q6G"
TURN 309..311
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 313..326
/evidence="ECO:0000244|PDB:6Q6G"
STRAND 328..330
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 331..343
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 347..360
/evidence="ECO:0000244|PDB:6Q6G"
STRAND 361..363
/evidence="ECO:0000244|PDB:5G05"
HELIX 365..377
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 381..394
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 399..411
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 415..428
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 434..445
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 449..461
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 469..479
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 484..499
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 513..516
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 519..522
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 527..532
/evidence="ECO:0000244|PDB:6Q6G"
TURN 533..538
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 543..553
/evidence="ECO:0000244|PDB:6Q6G"
SEQUENCE 597 AA; 68834 MW; 358F2B8745DB9D32 CRC64;
MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF
SLPALPLAEL QPPPPITEED AQDMDAYTLA KAYFDVKEYD RAAHFLHGCN SKKAYFLYMY
SRYLSGEKKK DDETVDSLGP LEKGQVKNEA LRELRVELSK KHQARELDGF GLYLYGVVLR
KLDLVKEAID VFVEATHVLP LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE
LQLIEEALQK YQNLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM
DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA ALYFQRALKL
NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR AWYGLGQTYE ILKMPFYCLY
YYRRAHQLRP NDSRMLVALG ECYEKLNQLV EAKKCYWRAY AVGDVEKMAL VKLAKLHEQL
TESEQAAQCY IKYIQDIYSC GEIVEHLEES TAFRYLAQYY FKCKLWDEAS TCAQKCCAFN
DTREEGKALL RQILQLRNQG ETPTTEVPAP FFLPASLSAN NTPTRRVSPL NLSSVTP


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EIAAB06426 Anaphase-promoting complex subunit CDC26,Cdc26,Cell division cycle protein 26 homolog,Mouse,Mus musculus
EIAAB06432 ANAPC3,Anaphase-promoting complex subunit 3,APC3,CDC27,CDC27 homolog,CDC27Hs,Cell division cycle protein 27 homolog,D0S1430E,D17S978E,H-NUC,Homo sapiens,Human
EIAAB06429 Anaphase-promoting complex subunit CDC26,Cdc26,Cell division cycle protein 26 homolog,Protein BWK-2,Rat,Rattus norvegicus
29-605 The anaphase-promoting complex (APC) consists of at least 8 protein subunits, including APC5, CDC27 (APC3), CDC16 (APC6), and CDC23 (APC8).The anaphase-promoting complex (APC) consists of at least 8 p 0.05 mg
CSB-RP051044h Recombinant human Anaphase-promoting complex subunit 5 protein 500ug
PE051044h Recombinant human Anaphase-promoting complex subunit 5 protein 5mg
PE051044h Recombinant human Anaphase-promoting complex subunit 5 protein 50ug
PE051044h Recombinant human Anaphase-promoting complex subunit 5 protein 1mg
PE051044h Recombinant human Anaphase-promoting complex subunit 5 protein 200ug
CSB-RP051044h Recombinant human Anaphase-promoting complex subunit 5 protein Source: E.coli 1mg
ANAPC13-1919H Protein: Recombinant Human Anaphase Promoting Complex Subunit 13, T7-tagged 50ug
CSB-RP051044h Recombinant human Anaphase-promoting complex subunit 5 protein Source: E.coli 200ug
Pathways :
WP1566: Citrate cycle (TCA cycle)
WP414: Cell Cycle and Cell Division
WP2272: Pathogenic Escherichia coli infection
WP1694: Pyrimidine metabolism
WP1693: Purine metabolism
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1644: DNA replication
WP2292: Chemokine signaling pathway
WP348: G1 to S cell cycle control
WP964: Cell cycle
WP1200: Cell cycle
WP844: Cell cycle
WP1083: Cell cycle
WP31: Cell cycle
WP190: Cell cycle
WP1775: Cell Cycle Checkpoints
WP1626: Benzoate degradation via CoA ligation
WP1792: Cell Cycle, Mitotic
WP1393: Cell cycle
WP959: G1 to S cell cycle control
WP1195: G1 to S cell cycle control
WP413: G1 to S cell cycle control
WP840: G1 to S cell cycle control
WP1078: G1 to S cell cycle control

Related Genes :
[mat-3 apc-8 cdc-23 pod-4 vex-2 F10C5.1] Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Metaphase-to-anaphase transition defect protein 3)
[APC8 CDC23 At3g48150 T24C20.30] Anaphase-promoting complex subunit 8 (Cell division cycle protein 23 homolog) (CDC23 homolog) (Cyclosome subunit 8)
[APC2 At2g04660 F28I8.30] Anaphase-promoting complex subunit 2 (Cyclosome subunit 2)
[ANAPC7 APC7] Anaphase-promoting complex subunit 7 (APC7) (Cyclosome subunit 7)
[APC6 CDC16 At1g78770 F9K20.19] Anaphase-promoting complex subunit 6 (Cell division cycle protein 16 homolog) (CDC16 homolog) (Cyclosome subunit 6) (Protein NOMEGA)
[nuc2 apc3 SPAC17C9.01c SPAC1851.01] Anaphase-promoting complex subunit 3 (20S cyclosome/APC complex protein apc3) (Nuclear alteration protein 2) (Nuclear scaffold-like protein p76)
[cut4 apc1 SPBC106.09] Anaphase-promoting complex subunit 1 (20S cyclosome/APC complex protein apc1) (Cell untimely torn protein 4)
[cut20 apc4 lid1 SPAC19G12.01c SPAPJ698.04c] Anaphase-promoting complex subunit 4 (20S cyclosome/APC complex protein apc4) (Cell untimely torn protein 20)
[mat-2 apc-1 evl-22 pod-3 W10C6.1] Anaphase-promoting complex subunit 1 (APC1) (Metaphase-to-anaphase transition protein 2)
[cdc-48.2 C41C4.8] Transitional endoplasmic reticulum ATPase homolog 2 (EC 3.6.4.6) (Cell division cycle-related protein 48.2) (p97/CDC48 homolog 2)
[apc11 SPAC343.03] Anaphase-promoting complex subunit 11 (20S cyclosome/APC complex protein apc11)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[CDC43 CAL1 YGL155W G1864] Geranylgeranyl transferase type-1 subunit beta (GGTase-I-beta) (EC 2.5.1.59) (Cell division cycle protein 43) (Geranylgeranyl transferase type I subunit beta) (RAS proteins geranylgeranyltransferase subunit beta) (Type I protein geranyl-geranyltransferase subunit beta) (PGGTase I beta)
[lin-35 C32F10.2] Retinoblastoma-like protein homolog lin-35 (Abnormal cell lineage protein 35) (Synthetic multivulva protein lin-35)
[APC10 At2g18290 T30D6.20] Anaphase-promoting complex subunit 10 (APC10) (Cyclosome subunit 10)
[apc-11 F35G12.9] Anaphase-promoting complex subunit 11 (APC11)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdk8 CG10572] Cyclin-dependent kinase 8 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 8) (DmCdk8) (Mediator complex subunit Cdk8) (Mediator of RNA polymerase II transcription subunit Cdk8)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDC14A] Dual specificity protein phosphatase CDC14A (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog A)
[CDCA8 PESCRG3] Borealin (Cell division cycle-associated protein 8) (Dasra-B) (hDasra-B) (Pluripotent embryonic stem cell-related gene 3 protein)
[cdc-48.1 C06A1.1] Transitional endoplasmic reticulum ATPase homolog 1 (EC 3.6.4.6) (Cell division cycle-related protein 48.1) (p97/CDC48 homolog 1)
[Cdk1 cdc2 CG5363] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK8] Cyclin-dependent kinase 8 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 8) (Mediator complex subunit CDK8) (Mediator of RNA polymerase II transcription subunit CDK8) (Protein kinase K35)
[fes-1 NCU06606] Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 5) (Complex III subunit V) (Rieske iron-sulfur protein) (RISP) (Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit) (Ubiquinol-cytochrome c reductase complex 25 kDa protein)
[INTS13 ASUN C12orf11 GCT1] Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Germ cell tumor 1) (Protein asunder homolog) (Sarcoma antigen NY-SAR-95)
[CDK7 CAK CAK1 CDKN7 MO15 STK1] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (p39 Mo15) (CDK-activating kinase 1) (Cell division protein kinase 7) (Serine/threonine-protein kinase 1) (TFIIH basal transcription factor complex kinase subunit)
[CDK13 CDC2L CDC2L5 CHED KIAA1791] Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)
[Cdca8] Borealin (Cell division cycle-associated protein 8) (MESrg)
[Cdk8] Cyclin-dependent kinase 8 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 8) (Mediator complex subunit CDK8) (Mediator of RNA polymerase II transcription subunit CDK8)

Bibliography :
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