POC5_HUMAN
ID POC5_HUMAN Reviewed; 575 AA.
AC Q8NA72; B4DJG7; Q494X7; Q494X9; Q6P085;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Centrosomal protein POC5;
DE AltName: Full=Protein of centriole 5;
DE Short=hPOC5;
GN Name=POC5; Synonyms=C5orf37;
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] (ISOFORMS 1 AND 3), AND VARIANTS
RP ARG-36 AND THR-85.
RC TISSUE=Testis, and Thalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-219 (ISOFORM 1), AND VARIANT ARG-36.
RC TISSUE=Bone marrow;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND SER-109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH CETN2
RP AND CETN3.
RX PubMed=19349582; DOI=10.1083/jcb.200808082;
RA Azimzadeh J., Hergert P., Delouvee A., Euteneuer U., Formstecher E.,
RA Khodjakov A., Bornens M.;
RT "hPOC5 is a centrin-binding protein required for assembly of full-length
RT centrioles.";
RL J. Cell Biol. 185:101-114(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-538, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-109 AND SER-564, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Essential for the assembly of the distal half of centrioles,
CC required for centriole elongation. {ECO:0000269|PubMed:19349582}.
CC -!- SUBUNIT: Interacts with CETN2 and CETN3. {ECO:0000269|PubMed:19349582}.
CC -!- INTERACTION:
CC Q8NA72; Q12798: CETN1; NbExp=6; IntAct=EBI-2561090, EBI-2512818;
CC Q8NA72; P41208: CETN2; NbExp=9; IntAct=EBI-2561090, EBI-1789926;
CC Q8NA72; O15182: CETN3; NbExp=6; IntAct=EBI-2561090, EBI-712959;
CC Q8NA72; Q3B820: FAM161A; NbExp=6; IntAct=EBI-2561090, EBI-719941;
CC Q8NA72; P68366: TUBA4A; NbExp=5; IntAct=EBI-2561090, EBI-351772;
CC Q8NA72-3; Q12798: CETN1; NbExp=4; IntAct=EBI-11751537, EBI-2512818;
CC Q8NA72-3; P41208: CETN2; NbExp=4; IntAct=EBI-11751537, EBI-1789926;
CC Q8NA72-3; O15182: CETN3; NbExp=8; IntAct=EBI-11751537, EBI-712959;
CC Q8NA72-3; Q3B820: FAM161A; NbExp=3; IntAct=EBI-11751537, EBI-719941;
CC Q8NA72-3; P04792: HSPB1; NbExp=3; IntAct=EBI-11751537, EBI-352682;
CC Q8NA72-3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-11751537, EBI-10975473;
CC Q8NA72-3; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-11751537, EBI-396669;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:19349582}. Note=Localized to the distal portion of
CC centrioles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NA72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NA72-2; Sequence=VSP_024098, VSP_024100;
CC Name=3;
CC IsoId=Q8NA72-3; Sequence=VSP_024099;
CC -!- PTM: Hyperphosphorylated during recruitment to procentrioles in G2/M
CC phase.
CC -!- SIMILARITY: Belongs to the POC5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC101328; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 3]:
CC Sequence=BC101328; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK093098; BAC04054.1; -; mRNA.
DR EMBL; AK296071; BAG58829.1; -; mRNA.
DR EMBL; BC065750; AAH65750.1; ALT_TERM; mRNA.
DR EMBL; BC101326; AAI01327.1; -; mRNA.
DR EMBL; BC101325; AAI01326.1; -; mRNA.
DR EMBL; BC101327; AAI01328.1; -; mRNA.
DR EMBL; BC101328; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS47236.1; -. [Q8NA72-1]
DR CCDS; CCDS47237.1; -. [Q8NA72-3]
DR RefSeq; NP_001092741.1; NM_001099271.1. [Q8NA72-1]
DR RefSeq; NP_689621.2; NM_152408.2. [Q8NA72-3]
DR AlphaFoldDB; Q8NA72; -.
DR SMR; Q8NA72; -.
DR BioGRID; 126396; 94.
DR IntAct; Q8NA72; 125.
DR MINT; Q8NA72; -.
DR STRING; 9606.ENSP00000410216; -.
DR GlyGen; Q8NA72; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q8NA72; -.
DR PhosphoSitePlus; Q8NA72; -.
DR BioMuta; POC5; -.
DR DMDM; 143955298; -.
DR EPD; Q8NA72; -.
DR jPOST; Q8NA72; -.
DR MassIVE; Q8NA72; -.
DR MaxQB; Q8NA72; -.
DR PaxDb; Q8NA72; -.
DR PeptideAtlas; Q8NA72; -.
DR PRIDE; Q8NA72; -.
DR ProteomicsDB; 72650; -. [Q8NA72-1]
DR ProteomicsDB; 72651; -. [Q8NA72-2]
DR ProteomicsDB; 72652; -. [Q8NA72-3]
DR Antibodypedia; 49002; 111 antibodies from 17 providers.
DR DNASU; 134359; -.
DR Ensembl; ENST00000428202.7; ENSP00000410216.2; ENSG00000152359.15. [Q8NA72-1]
DR Ensembl; ENST00000446329.6; ENSP00000399481.2; ENSG00000152359.15. [Q8NA72-3]
DR Ensembl; ENST00000510798.5; ENSP00000426796.1; ENSG00000152359.15. [Q8NA72-2]
DR GeneID; 134359; -.
DR KEGG; hsa:134359; -.
DR MANE-Select; ENST00000428202.7; ENSP00000410216.2; NM_001099271.2; NP_001092741.1.
DR UCSC; uc003keg.5; human. [Q8NA72-1]
DR CTD; 134359; -.
DR DisGeNET; 134359; -.
DR GeneCards; POC5; -.
DR HGNC; HGNC:26658; POC5.
DR HPA; ENSG00000152359; Low tissue specificity.
DR MalaCards; POC5; -.
DR MIM; 617880; gene.
DR neXtProt; NX_Q8NA72; -.
DR OpenTargets; ENSG00000152359; -.
DR PharmGKB; PA165660427; -.
DR VEuPathDB; HostDB:ENSG00000152359; -.
DR eggNOG; ENOG502QUKU; Eukaryota.
DR GeneTree; ENSGT00390000004454; -.
DR InParanoid; Q8NA72; -.
DR OMA; AMTMFQN; -.
DR OrthoDB; 1217267at2759; -.
DR PhylomeDB; Q8NA72; -.
DR TreeFam; TF329296; -.
DR PathwayCommons; Q8NA72; -.
DR SignaLink; Q8NA72; -.
DR BioGRID-ORCS; 134359; 19 hits in 1081 CRISPR screens.
DR ChiTaRS; POC5; human.
DR GenomeRNAi; 134359; -.
DR Pharos; Q8NA72; Tbio.
DR PRO; PR:Q8NA72; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8NA72; protein.
DR Bgee; ENSG00000152359; Expressed in secondary oocyte and 154 other tissues.
DR ExpressionAtlas; Q8NA72; baseline and differential.
DR Genevisible; Q8NA72; HS.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR033351; POC5.
DR PANTHER; PTHR28618; PTHR28618; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..575
FT /note="Centrosomal protein POC5"
FT /id="PRO_0000281908"
FT REPEAT 142..173
FT /note="Centrin-binding (CBR) 1"
FT REPEAT 231..262
FT /note="Centrin-binding (CBR) 2"
FT REPEAT 263..295
FT /note="Centrin-binding (CBR) 3"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..222
FT /evidence="ECO:0000255"
FT COILED 316..355
FT /evidence="ECO:0000255"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 538
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024098"
FT VAR_SEQ 1..28
FT /note="MSSDEEKYSLPVVQNDSSRGSSVSSNLQ -> MKW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_024099"
FT VAR_SEQ 470..528
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024100"
FT VARIANT 36
FT /note="H -> R (in dbSNP:rs2307111)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_031324"
FT VARIANT 85
FT /note="I -> T (in dbSNP:rs17672542)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_031325"
FT VARIANT 446
FT /note="A -> T (in dbSNP:rs34678567)"
FT /id="VAR_050778"
FT CONFLICT 41
FT /note="T -> A (in Ref. 2; AAH65750)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="C -> R (in Ref. 1; BAC04054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 63351 MW; 0B544DD102B35D80 CRC64;
MSSDEEKYSL PVVQNDSSRG SSVSSNLQEE YEELLHYAIV TPNIEPCASQ SSHPKGELVP
DVRISTIHDI LHSQGNNSEV RETAIEVGKG CDFHISSHSK TDESSPVLSP RKPSHPVMDF
FSSHLLADSS SPATNSSHTD AHEILVSDFL VSDENLQKME NVLDLWSSGL KTNIISELSK
WRLNFIDWHR MEMRKEKEKH AAHLKQLCNQ INELKELQKT FEISIGRKDE VISSLSHAIG
KQKEKIELMR TFFHWRIGHV RARQDVYEGK LADQYYQRTL LKKVWKVWRS VVQKQWKDVV
ERACQARAEE VCIQISNDYE AKVAMLSGAL ENAKAEIQRM QHEKEHFEDS MKKAFMRGVC
ALNLEAMTIF QNRNDAGIDS TNNKKEEYGP GVQGKEHSAH LDPSAPPMPL PVTSPLLPSP
PAAVGGASAT AVPSAASMTS TRAASASSVH VPVSALGAGS AATAASEEMY VPRVVTSAQQ
KAGRTITARI TGRCDFASKN RISSSLAIMG VSPPMSSVVV EKHHPVTVQT IPQATAAKYP
RTIHPESSTS ASRSLGTRSA HTQSLTSVHS IKVVD
