Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Pericentriolar material 1 protein  

UniProtKB / Swiss-Prot ID :  PCM1_HUMAN

Gene Name (Synonyms) : 
PCM1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, centrosome. Cytoplasmic granule. Note=Localizes to cytoplasmic granules which are enriched around the centrosome. This centrosomal enrichment requires microtubules and dynein. The majority of the protein  

Protein Function :  Required for centrosome assembly and function. Essential for the correct localization of several centrosomal proteins including CEP250, CETN3, PCNT and NEK2. Required to anchor microtubules to the centrosome. Involved in the biogenesis of cilia. 

Protein Sequence MATGGGPFEDGMNDQDLPNWSNENVDDRLNNMDWGAQQKKANRSSEKNKKKFGVESDKRVTNDISPESSP...
Predicted Secondary Structure CCCCCCCHHHCCCCCCCCCCCCCCHHHHHCCCCCCCCCCCCCCHHHHHHHHHCCHHHHHHHCCCCCCCCC...
Protein Variant
LocationDescription
159S -> N (in dbSNP:rs412750). VAR_030164
159S -> R (in dbSNP:rs412750). VAR_062172
176A -> D (in dbSNP:rs2285302). VAR_030165
597M -> V (in dbSNP:rs208753). VAR_030166
600S -> P (in dbSNP:rs34325017). VAR_047381
691A -> S (in dbSNP:rs17635381). VAR_030167
871G -> V (in dbSNP:rs7009117). VAR_030168
1251R -> H (in dbSNP:rs17514547). VAR_030169
1326E -> D (in dbSNP:rs34932823). VAR_047382
1543T -> I (in dbSNP:rs370429). VAR_030170
1701K -> N (in dbSNP:rs36113670). VAR_047383
1865N -> D (in dbSNP:rs35789133). VAR_047384
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
61PhosphothreonineDKRVTNDIS
HHHHHCCCC
31.07HPRD
Link-
61Phosphothreonine.DKRVTNDIS
HHHHHCCCC
31.07UniProtKB
Link-
65PhosphoserineTNDISPESS
HCCCCCCCC
26.02HPRD
Link-
65PhosphoserineTNDISPESS
HCCCCCCCC
26.02PhosphoELM
Link-
65PhosphoserineTNDISPESS
HCCCCCCCC
26.02SysPTM
Link-
65Phosphoserine.TNDISPESS
HCCCCCCCC
26.02UniProtKB
Link-
68PhosphoserineISPESSPGV
CCCCCCCCC
45.26HPRD
Link-
68PhosphoserineISPESSPGV
CCCCCCCCC
45.26PhosphoELM
Link-
68Phosphoserine.ISPESSPGV
CCCCCCCCC
45.26UniProtKB
Link-
69PhosphoserineSPESSPGVG
CCCCCCCCC
24.82HPRD
Link-
69PhosphoserineSPESSPGVG
CCCCCCCCC
24.82PhosphoELM
Link-
69PhosphoserineSPESSPGVG
CCCCCCCCC
24.82SysPTM
Link-
69Phosphoserine.SPESSPGVG
CCCCCCCCC
24.82UniProtKB
Link-
88PhosphotyrosinePHSRYMSQM
CCHHHHHHC
12.25HPRD
Link-
93PhosphoserineMSQMSVPEQ
HHHCCCCCH
27.21HPRD
Link-
93Phosphoserine.MSQMSVPEQ
HHHCCCCCH
27.21UniProtKB
Link-
110PhosphoserineRINFSDLDQ
HCCHHHCCC
32.54HPRD
Link-
110PhosphoserineRINFSDLDQ
HCCHHHCCC
32.54PhosphoELM
Link-
110Phosphoserine.RINFSDLDQ
HCCHHHCCC
32.54UniProtKB
Link-
116PhosphoserineLDQRSIGSD
CCCHHCCCC
26.18HPRD
Link-
116Phosphoserine.LDQRSIGSD
CCCHHCCCC
26.18UniProtKB
Link-
119PhosphoserineRSIGSDSQG
HHCCCCCCC
32.21HPRD
Link-
119Phosphoserine.RSIGSDSQG
HHCCCCCCC
32.21UniProtKB
Link-
158PhosphothreonineKDASTSPPN
CCCCCCCCC
47.15HPRD
Link-
159PhosphoserineDASTSPPNR
CCCCCCCCC
35.55HPRD
Link-
159Phosphoserine.DASTSPPNR
CCCCCCCCC
35.55UniProtKB
Link-
356PhosphoserineQLRDSQPPA
HHCCCCCCC
37.85HPRD
Link-
356PhosphoserineQLRDSQPPA
HHCCCCCCC
37.85PhosphoELM
Link-
356Phosphoserine.QLRDSQPPA
HHCCCCCCC
37.85UniProtKB
Link-
372PhosphoserineAESLSLTRE
HHHHHHHHH
36.65HPRD
Link-
372Phosphoserine.AESLSLTRE
HHHHHHHHH
36.65UniProtKB
Link-
374PhosphothreonineSLSLTREVS
HHHHHHHHH
22.77HPRD
Link-
384PhosphoserineSRKPSASER
CCCCCCCCC
47.68HPRD
Link-
384PhosphoserineSRKPSASER
CCCCCCCCC
47.68PhosphoELM
Link-
386PhosphoserineKPSASERLP
CCCCCCCCC
27.82HPRD
Link-
386PhosphoserineKPSASERLP
CCCCCCCCC
27.82PhosphoELM
Link-
399N6-acetyllysineELFSKMRVL
HHHHHHHHH
24.32HPRD
Link-
399N6-acetyllysine.ELFSKMRVL
HHHHHHHHH
24.32UniProtKB
Link-
430PhosphoserineNNSSSSPQR
CCCCCCCCC
45.95HPRD
Link-
431PhosphoserineNSSSSPQRS
CCCCCCCCC
27.31HPRD
Link-
431PhosphoserineNSSSSPQRS
CCCCCCCCC
27.31HPRD
Link-
431PhosphoserineNSSSSPQRS
CCCCCCCCC
27.31PhosphoELM
Link-
431Phosphoserine.NSSSSPQRS
CCCCCCCCC
27.31UniProtKB
Link-
530PhosphothreonineKDEETEESE
CHHHHHHCC
42.90HPRD
Link-
533PhosphoserineETEESEYDS
HHHHCCCCC
34.91HPRD
Link-
535PhosphotyrosineEESEYDSEH
HHCCCCCCC
33.76HPRD
Link-
537PhosphoserineSEYDSEHEN
CCCCCCCCC
39.69HPRD
Link-
542PhosphoserineEHENSEPVT
CCCCCCCCC
40.05HPRD
Link-
720PhosphothreonineNANKTQKDT
CHHHHHHHH
40.43HPRD
Link-
724PhosphothreonineTQKDTGVNE
HHHHHCCCH
50.49HPRD
Link-
776PhosphoserineDLQLSAASV
CCEECCCCC
14.61HPRD
Link-
779PhosphoserineLSAASVGNC
ECCCCCCCC
30.21HPRD
Link-
795PhosphothreonineAVTSTPTVN
CCCCCCCCC
17.39HPRD
Link-
804PhosphoserineQHETSTSKS
CCCCCCCCC
27.91HPRD
Link-
816PhosphoserinePEDSSIVDN
CCCCCCCCH
38.66HPRD
Link-
861PhosphoserineAETASPVAV
HHHCCCEEE
27.59HPRD
Link-
861PhosphoserineAETASPVAV
HHHCCCEEE
27.59PhosphoELM
Link-
861Phosphoserine.AETASPVAV
HHHCCCEEE
27.59UniProtKB
Link-
866PhosphoserinePVAVSLRSD
CEEEEEECC
14.34HPRD
Link-
866Phosphoserine.PVAVSLRSD
CEEEEEECC
14.34UniProtKB
Link-
869PhosphoserineVSLRSDGSE
EEEECCCCH
52.17HPRD
Link-
869Phosphoserine.VSLRSDGSE
EEEECCCCH
52.17UniProtKB
Link-
872PhosphoserineRSDGSENLC
ECCCCHHHC
28.44HPRD
Link-
872Phosphoserine.RSDGSENLC
ECCCCHHHC
28.44UniProtKB
Link-
877PhosphothreonineENLCTPQQS
HHHCCCHHH
27.57HPRD
Link-
877PhosphothreonineENLCTPQQS
HHHCCCHHH
27.57PhosphoELM
Link-
877Phosphothreonine.ENLCTPQQS
HHHCCCHHH
27.57UniProtKB
Link-
960PhosphoserineNCPFSADEN
CCCCCCCCC
21.69HPRD
Link-
960Phosphoserine.NCPFSADEN
CCCCCCCCC
21.69UniProtKB
Link-
991PhosphoserineVSELSYVEE
HHHHHHHHH
24.07HPRD
Link-
991PhosphoserineVSELSYVEE
HHHHHHHHH
24.07PhosphoELM
Link-
991PhosphoserineVSELSYVEE
HHHHHHHHH
24.07SysPTM
Link-
991Phosphoserine.VSELSYVEE
HHHHHHHHH
24.07UniProtKB
Link-
1185PhosphoserineKPFESSSSI
CCCCCCCCC
35.58HPRD
Link-
1185Phosphoserine.KPFESSSSI
CCCCCCCCC
35.58UniProtKB
Link-
1187PhosphoserineFESSSSIGA
CCCCCCCCC
34.94HPRD
Link-
1187Phosphoserine.FESSSSIGA
CCCCCCCCC
34.94UniProtKB
Link-
1188PhosphoserineESSSSIGAE
CCCCCCCCC
27.30HPRD
Link-
1188Phosphoserine.ESSSSIGAE
CCCCCCCCC
27.30UniProtKB
Link-
1231PhosphoserineGFSVSVEKS
CCCCCCCCC
24.30HPRD
Link-
1231Phosphoserine.GFSVSVEKS
CCCCCCCCC
24.30UniProtKB
Link-
1257PhosphoserineFDEESLESF
HHHCHHHHH
35.08HPRD
Link-
1257PhosphoserineFDEESLESF
HHHCHHHHH
35.08PhosphoELM
Link-
1257Phosphoserine.FDEESLESF
HHHCHHHHH
35.08UniProtKB
Link-
1260PhosphoserineESLESFSSM
CHHHHHCCC
35.40HPRD
Link-
1260PhosphoserineESLESFSSM
CHHHHHCCC
35.40PhosphoELM
Link-
1260Phosphoserine.ESLESFSSM
CHHHHHCCC
35.40UniProtKB
Link-
1262PhosphoserineLESFSSMPD
HHHHCCCCC
34.70HPRD
Link-
1262Phosphoserine.LESFSSMPD
HHHHCCCCC
34.70UniProtKB
Link-
1263PhosphoserineESFSSMPDP
HHHCCCCCC
32.12HPRD
Link-
1271PhosphothreoninePVDPTTVTK
CCCCCCCCC
29.45HPRD
Link-
1272PhosphothreonineVDPTTVTKT
CCCCCCCCH
31.40HPRD
Link-
1274PhosphothreoninePTTVTKTFK
CCCCCCHHH
23.44HPRD
Link-
1283PhosphoserineTRKASAQAS
HHHCHHHHH
24.77HPRD
Link-
1373Phosphoserine.SETGSDFSM
HCCCCHHHH
42.79UniProtKB
Link-
1435PhosphoserineSRHISESHE
HHHCCCCCC
27.24HPRD
Link-
1494PhosphoserineADNASVLSV
CCCEEEEEC
29.82HPRD
Link-
1494PhosphoserineADNASVLSV
CCCEEEEEC
29.82PhosphoELM
Link-
1497PhosphoserineASVLSVSSN
EEEEECCCC
20.14HPRD
Link-
1497PhosphoserineASVLSVSSN
EEEEECCCC
20.14PhosphoELM
Link-
1499PhosphoserineVLSVSSNFE
EEECCCCCC
19.05HPRD
Link-
1499PhosphoserineVLSVSSNFE
EEECCCCCC
19.05PhosphoELM
Link-
1499PhosphoserineVLSVSSNFE
EEECCCCCC
19.05PhosphoELM
Link-
1697Phosphoserine.LDNNSITVK
CCCCEEECH
26.37UniProtKB
Link-
1699PhosphothreonineNNSITVKQR
CCEEECHHH
22.82HPRD
Link-
1730PhosphoserineEDHGSPAGE
CCCCCCCCC
14.25HPRD
Link-
1730PhosphoserineEDHGSPAGE
CCCCCCCCC
14.25PhosphoELM
Link-
1730Phosphoserine.EDHGSPAGE
CCCCCCCCC
14.25UniProtKB
Link-
1765PhosphoserineKNVRSDISD
CCCCCCCCC
34.71HPRD
Link-
1765PhosphoserineKNVRSDISD
CCCCCCCCC
34.71PhosphoELM
Link-
1765Phosphoserine.KNVRSDISD
CCCCCCCCC
34.71UniProtKB
Link-
1768PhosphoserineRSDISDQEE
CCCCCCCCC
37.93HPRD
Link-
1768PhosphoserineRSDISDQEE
CCCCCCCCC
37.93PhosphoELM
Link-
1768Phosphoserine.RSDISDQEE
CCCCCCCCC
37.93UniProtKB
Link-
1776PhosphoserineEDEESEGCP
CCCCCCCCC
36.92HPRD
Link-
1776Phosphoserine.EDEESEGCP
CCCCCCCCC
36.92UniProtKB
Link-
1958PhosphoserineISQKSDEED
CCCCCCHHH
42.49HPRD
Link-
1977Phosphoserine.LTIYSEADL
CCCHHHHHH
23.58UniProtKB
Link-
2023PhosphoserineVGAQSI
CCCCC
29.72HPRD
Link-
2023Phosphoserine.VGAQSI
CCCCC
29.72UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
GSK3B_HUMANcolocalizationMINT-4049759MINT17139249
1433Z_HUMANphysical interactionMINT-3295217MINT15161933
CCD53_HUMANphysical interactionEBI-756409
intact16189514
ECM29_HUMANphysical interactionEBI-754222
intact16189514
ABI2_HUMANphysical interactionEBI-756796
intact16189514
EXOC8_HUMANphysical interactionEBI-756907
intact16189514
CEP72_HUMANphysical interactionEBI-759601
intact16189514
ABI2_HUMANyeast 2-hybridHPRD:02624HPRD16189514
CEP72_HUMANyeast 2-hybridHPRD:02624HPRD16189514
EXOC8_HUMANyeast 2-hybridHPRD:02624HPRD16189514
CCD53_HUMANyeast 2-hybridHPRD:02624HPRD16189514
ING5_HUMANyeast 2-hybridHPRD:02624HPRD16189514
BBS4_HUMANENSP00000327077STRING
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Disease Reference
Kegg disease
OMIM disease
188550Thyroid papillary carcinoma (TPC)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-399, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69;SER-110; SER-431; SER-861; SER-866; SER-869; SER-872; SER-1730;SER-1765; SER-1768 AND SER-1776, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69 ANDTHR-877, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-69 AND SER-991,AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69;SER-93; SER-110; SER-960; SER-1231; SER-1257; SER-1260; SER-1262;SER-1730; SER-1765; SER-1768 AND SER-1776, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61; SER-65; SER-68;SER-69; SER-110; SER-159; SER-861; SER-872; SER-1185; SER-1187;SER-1188; SER-1765; SER-1768; SER-1776 AND SER-2023, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69;SER-93; SER-110; SER-116; SER-119; SER-1185; SER-1257; SER-1373;SER-1697; SER-1765; SER-1768; SER-1776 AND SER-1977, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures