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Centrosomal protein of 72 kDa (Cep72)

 CEP72_HUMAN             Reviewed;         647 AA.
Q9P209; B4DR26; Q9BV03; Q9BWM3; Q9NVR4;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
22-NOV-2017, entry version 138.
RecName: Full=Centrosomal protein of 72 kDa;
Short=Cep72;
Name=CEP72; Synonyms=KIAA1519;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-509.
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[2]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 93-647 (ISOFORM 1).
TISSUE=Teratocarcinoma;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Placenta;
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).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, 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).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIZ.
PubMed=19536135; DOI=10.1038/emboj.2009.161;
Oshimori N., Li X., Ohsugi M., Yamamoto T.;
"Cep72 regulates the localization of key centrosomal proteins and
proper bipolar spindle formation.";
EMBO J. 28:2066-2076(2009).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-382 AND
SER-404, 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).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDK5RAP2 AND
PCM1.
PubMed=26297806; DOI=10.7554/eLife.07519;
Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L.,
Al-Gazali L., Sztriha L., Partlow J.N., Kim H., Krup A.L.,
Dammermann A., Krogan N., Walsh C.A., Reiter J.F.;
"Centriolar satellites assemble centrosomal microcephaly proteins to
recruit CDK2 and promote centriole duplication.";
Elife 4:0-0(2015).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Involved in the recruitment of key centrosomal proteins
to the centrosome. Provides centrosomal microtubule-nucleation
activity on the gamma-tubulin ring complexes (gamma-TuRCs) and has
critical roles in forming a focused bipolar spindle, which is
needed for proper tension generation between sister chromatids.
Required for localization of KIZ, AKAP9 and gamma-tubulin ring
complexes (gamma-TuRCs) (PubMed:19536135). Involved in centriole
duplication. Required for CDK5RAP22, CEP152, WDR62 and CEP63
centrosomal localization and promotes the centrosomal localization
of CDK2 (PubMed:26297806). {ECO:0000269|PubMed:19536135,
ECO:0000269|PubMed:26297806}.
-!- SUBUNIT: Interacts with KIZ, PCM1 and CDK5RAP2.
{ECO:0000269|PubMed:19536135, ECO:0000269|PubMed:26297806}.
-!- INTERACTION:
O15265:ATXN7; NbExp=2; IntAct=EBI-739498, EBI-708350;
Q7Z7H3:CATIP; NbExp=5; IntAct=EBI-739498, EBI-10258233;
Q96SN8:CDK5RAP2; NbExp=3; IntAct=EBI-739498, EBI-308374;
Q86YD7:FAM90A1; NbExp=3; IntAct=EBI-739498, EBI-6658203;
Q2M2Z5:KIZ; NbExp=3; IntAct=EBI-739498, EBI-2554344;
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-739498, EBI-739832;
Q9Y5B8:NME7; NbExp=8; IntAct=EBI-739498, EBI-744782;
Q15154:PCM1; NbExp=6; IntAct=EBI-739498, EBI-741421;
Q9Y237:PIN4; NbExp=3; IntAct=EBI-739498, EBI-714599;
P25786:PSMA1; NbExp=5; IntAct=EBI-739498, EBI-359352;
Q6NXQ0:SFRS2; NbExp=3; IntAct=EBI-739498, EBI-10251550;
Q96R06:SPAG5; NbExp=2; IntAct=EBI-739498, EBI-413317;
Q86W54:SPATA24; NbExp=3; IntAct=EBI-739498, EBI-3916986;
Q96FJ0:STAMBPL1; NbExp=9; IntAct=EBI-739498, EBI-745021;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:14654843,
ECO:0000269|PubMed:19536135}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriolar satellite
{ECO:0000269|PubMed:26297806}. Note=Localizes to the centrosome
and centrosome-surrounding particles throughout the cell cycle.
These particles disappear after microtubules are depolymerized
using nocodazole, suggesting that CEP72-associating particles
localize in a microtubule- dependent manner.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9P209-1; Sequence=Displayed;
Name=2;
IsoId=Q9P209-2; Sequence=VSP_037835, VSP_037836;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the CEP72 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91685.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA96043.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB040952; BAA96043.1; ALT_INIT; mRNA.
EMBL; AK001427; BAA91685.1; ALT_INIT; mRNA.
EMBL; AK299072; BAG61138.1; -; mRNA.
EMBL; BC000132; AAH00132.1; -; mRNA.
EMBL; BC001750; AAH01750.2; -; mRNA.
CCDS; CCDS34126.1; -. [Q9P209-1]
RefSeq; NP_060610.2; NM_018140.3. [Q9P209-1]
RefSeq; XP_011512365.1; XM_011514063.1. [Q9P209-1]
UniGene; Hs.591741; -.
ProteinModelPortal; Q9P209; -.
SMR; Q9P209; -.
BioGrid; 120844; 99.
DIP; DIP-54272N; -.
IntAct; Q9P209; 86.
MINT; MINT-1442378; -.
STRING; 9606.ENSP00000264935; -.
iPTMnet; Q9P209; -.
PhosphoSitePlus; Q9P209; -.
BioMuta; CEP72; -.
DMDM; 62901504; -.
EPD; Q9P209; -.
MaxQB; Q9P209; -.
PaxDb; Q9P209; -.
PeptideAtlas; Q9P209; -.
PRIDE; Q9P209; -.
Ensembl; ENST00000264935; ENSP00000264935; ENSG00000112877. [Q9P209-1]
GeneID; 55722; -.
KEGG; hsa:55722; -.
UCSC; uc003jbf.4; human. [Q9P209-1]
CTD; 55722; -.
DisGeNET; 55722; -.
EuPathDB; HostDB:ENSG00000112877.7; -.
GeneCards; CEP72; -.
HGNC; HGNC:25547; CEP72.
HPA; HPA058235; -.
HPA; HPA074879; -.
MIM; 616475; gene.
neXtProt; NX_Q9P209; -.
OpenTargets; ENSG00000112877; -.
PharmGKB; PA142672125; -.
eggNOG; ENOG410IH75; Eukaryota.
eggNOG; ENOG4111P3A; LUCA.
GeneTree; ENSGT00530000063884; -.
HOGENOM; HOG000111549; -.
HOVERGEN; HBG050900; -.
InParanoid; Q9P209; -.
KO; K16532; -.
OMA; IAECEWD; -.
OrthoDB; EOG091G04WS; -.
PhylomeDB; Q9P209; -.
TreeFam; TF338646; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
GeneWiki; CEP72; -.
GenomeRNAi; 55722; -.
PRO; PR:Q9P209; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000112877; -.
CleanEx; HS_CEP72; -.
Genevisible; Q9P209; HS.
GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0033566; P:gamma-tubulin complex localization; IMP:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:1904779; P:regulation of protein localization to centrosome; IMP:UniProtKB.
GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR003603; U2A'_phosphoprotein32A_C.
SMART; SM00369; LRR_TYP; 2.
SMART; SM00446; LRRcap; 1.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS51450; LRR; 2.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Leucine-rich repeat; Phosphoprotein; Polymorphism;
Reference proteome; Repeat.
CHAIN 1 647 Centrosomal protein of 72 kDa.
/FTId=PRO_0000089499.
REPEAT 29 50 LRR 1.
REPEAT 55 76 LRR 2.
REPEAT 77 98 LRR 3.
DOMAIN 111 150 LRRCT.
COILED 476 620 {ECO:0000255}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 404 404 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 172 193 PHHPRAKCTEALAKQSLVMDAD -> IQTSVEPAVGTVPVW
GLWEAGP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037835.
VAR_SEQ 194 647 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037836.
VARIANT 238 238 P -> L (in dbSNP:rs869955).
/FTId=VAR_050798.
VARIANT 412 412 P -> T (in dbSNP:rs12522955).
/FTId=VAR_050799.
VARIANT 509 509 T -> A (in dbSNP:rs868649).
{ECO:0000269|PubMed:10819331}.
/FTId=VAR_050800.
CONFLICT 566 566 G -> V (in Ref. 2; BAA91685).
{ECO:0000305}.
SEQUENCE 647 AA; 71718 MW; 9F45C88511311460 CRC64;
MARAGPRLVL SEEAVRAKSG LGPHRDLAEL QSLSIPGTYQ EKITHLGHSL MSLTGLKSLD
LSRNSLVSLE GIQYLTALES LNLYYNCISS LAEVFRLHAL TELVDVDFRL NPVVKVEPDY
RLFVVHLLPK LQQLDDRPVR ASERKASRLH FASEDSLDSK ESVPASLKEG RPHHPRAKCT
EALAKQSLVM DADDEAVLNL IAECEWDLGR PPGSTSFSQK GREADSRGSQ ESRHLLSPQL
VQYQCGDSGK QGRETRRSSC RGCCLEKMPW SQLCGELPPL YGAEPEASRA PRPHTYFTPH
PDSMDTEDSA SSQKLDLSGE MVPGPLPAPG KCRKRRMPVG RFQTFSDQEG LGCPERTHGS
SVPKESLSRQ DSSESRNGRT LSQPEASETE EQRSRGVTDT REPSPGSHSA LPGKKTALQA
ALLETLLDLV DRSWGGCRSL HSNEAFLAQA RHILSSVEEF TAAQDSSAMV GEDVGSLALE
SKSLQSRLAE QQQQHAREMS EVTAELHHTH KELDDLRQHL DKSLEENSRL KSLLLSMKKE
VKSADTAATL NLQIAGLQTS VKRLCGEIVE LKQHLEHYDK IQELTQMLQE SHSSLVSTNE
HLLQELSQVR AQHRAEVEQM HWSYQELKKT MALFPHSSAS HGGCQAC


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