POC5_HUMAN - dbPTM
POC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POC5_HUMAN
UniProt AC Q8NA72
Protein Name Centrosomal protein POC5
Gene Name POC5
Organism Homo sapiens (Human).
Sequence Length 575
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Localized to the distal portion of centrioles.
Protein Description Essential for the assembly of the distal half of centrioles, required for centriole elongation..
Protein Sequence MSSDEEKYSLPVVQNDSSRGSSVSSNLQEEYEELLHYAIVTPNIEPCASQSSHPKGELVPDVRISTIHDILHSQGNNSEVRETAIEVGKGCDFHISSHSKTDESSPVLSPRKPSHPVMDFFSSHLLADSSSPATNSSHTDAHEILVSDFLVSDENLQKMENVLDLWSSGLKTNIISELSKWRLNFIDWHRMEMRKEKEKHAAHLKQLCNQINELKELQKTFEISIGRKDEVISSLSHAIGKQKEKIELMRTFFHWRIGHVRARQDVYEGKLADQYYQRTLLKKVWKVWRSVVQKQWKDVVERACQARAEEVCIQISNDYEAKVAMLSGALENAKAEIQRMQHEKEHFEDSMKKAFMRGVCALNLEAMTIFQNRNDAGIDSTNNKKEEYGPGVQGKEHSAHLDPSAPPMPLPVTSPLLPSPPAAVGGASATAVPSAASMTSTRAASASSVHVPVSALGAGSAATAASEEMYVPRVVTSAQQKAGRTITARITGRCDFASKNRISSSLAIMGVSPPMSSVVVEKHHPVTVQTIPQATAAKYPRTIHPESSTSASRSLGTRSAHTQSLTSVHSIKVVD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSSDEEKYS
------CCCHHHHCC		46.6320873877
3Phosphorylation-----MSSDEEKYSL
-----CCCHHHHCCC		47.9820873877
8PhosphorylationMSSDEEKYSLPVVQN
CCCHHHHCCCCCCCC		20.7920873877
9PhosphorylationSSDEEKYSLPVVQND
CCHHHHCCCCCCCCC		36.9520873877
30UbiquitinationVSSNLQEEYEELLHY
CCCHHHHHHHHHHHH		45.3329967540
31PhosphorylationSSNLQEEYEELLHYA
CCHHHHHHHHHHHHH		17.6027642862
37PhosphorylationEYEELLHYAIVTPNI
HHHHHHHHHHCCCCC		9.6722210691
48PhosphorylationTPNIEPCASQSSHPK
CCCCCCCCCCCCCCC		22.7132142685
51PhosphorylationIEPCASQSSHPKGEL
CCCCCCCCCCCCCCC		28.2822210691
55UbiquitinationASQSSHPKGELVPDV
CCCCCCCCCCCCCCC		60.6429967540
63UbiquitinationGELVPDVRISTIHDI
CCCCCCCCHHHHHHH		25.2323000965
65PhosphorylationLVPDVRISTIHDILH
CCCCCCHHHHHHHHH		15.6720873877
66PhosphorylationVPDVRISTIHDILHS
CCCCCHHHHHHHHHH		21.6920873877
73PhosphorylationTIHDILHSQGNNSEV
HHHHHHHHCCCCHHH		36.0230266825
78PhosphorylationLHSQGNNSEVRETAI
HHHCCCCHHHHHHHH		41.2830266825
83PhosphorylationNNSEVRETAIEVGKG
CCHHHHHHHHHHCCC		23.5230576142
83O-linked_GlycosylationNNSEVRETAIEVGKG
CCHHHHHHHHHHCCC		23.5229351928
96PhosphorylationKGCDFHISSHSKTDE
CCCCEEEECCCCCCC		17.2730576142
97PhosphorylationGCDFHISSHSKTDES
CCCEEEECCCCCCCC		31.0430576142
99PhosphorylationDFHISSHSKTDESSP
CEEEECCCCCCCCCC		38.9230576142
101PhosphorylationHISSHSKTDESSPVL
EEECCCCCCCCCCCC		48.2723927012
104PhosphorylationSHSKTDESSPVLSPR
CCCCCCCCCCCCCCC		42.6329255136
105PhosphorylationHSKTDESSPVLSPRK
CCCCCCCCCCCCCCC		19.5829255136
109PhosphorylationDESSPVLSPRKPSHP
CCCCCCCCCCCCCCC		23.9329255136
114PhosphorylationVLSPRKPSHPVMDFF
CCCCCCCCCCCHHHH		43.3826074081
153 (in isoform 2)Ubiquitination-41.1321906983
155UbiquitinationDFLVSDENLQKMENV
HHHCCHHHHHHHHHH		53.4123000965
172PhosphorylationLWSSGLKTNIISELS
HHHCCHHHHHHHHHH		36.3717924679
176PhosphorylationGLKTNIISELSKWRL
CHHHHHHHHHHHHHH		28.7817924679
179PhosphorylationTNIISELSKWRLNFI
HHHHHHHHHHHHHHH		26.5617924679
180UbiquitinationNIISELSKWRLNFID
HHHHHHHHHHHHHHH		49.2923000965
203UbiquitinationEKEKHAAHLKQLCNQ
HHHHHHHHHHHHHHH		34.0529967540
205UbiquitinationEKHAAHLKQLCNQIN
HHHHHHHHHHHHHHH		31.2129967540
217 (in isoform 2)Ubiquitination-6.3921906983
228UbiquitinationFEISIGRKDEVISSL
HCEECCCHHHHHHHH		53.6929967540
245 (in isoform 3)Ubiquitination-48.8221906983
267PhosphorylationVRARQDVYEGKLADQ
CEECCCHHHCCCHHH		27.53-
270UbiquitinationRQDVYEGKLADQYYQ
CCCHHHCCCHHHHHH		28.6721906983
270 (in isoform 1)Ubiquitination-28.6721906983
297UbiquitinationSVVQKQWKDVVERAC
HHHHHHHHHHHHHHH		37.84-
309UbiquitinationRACQARAEEVCIQIS
HHHHHHHHHHEEEEC		45.4729967540
309 (in isoform 3)Ubiquitination-45.4721906983
334 (in isoform 1)Ubiquitination-59.1221906983
334UbiquitinationSGALENAKAEIQRMQ
HHHHHHHHHHHHHHH		59.122190698
344UbiquitinationIQRMQHEKEHFEDSM
HHHHHHHHHHHHHHH		55.13-
384UbiquitinationGIDSTNNKKEEYGPG
CCCCCCCCCHHCCCC		64.73-
385UbiquitinationIDSTNNKKEEYGPGV
CCCCCCCCHHCCCCC		58.88-
388PhosphorylationTNNKKEEYGPGVQGK
CCCCCHHCCCCCCCC		29.7018083107
413PhosphorylationPPMPLPVTSPLLPSP
CCCCCCCCCCCCCCC		23.7628348404
414PhosphorylationPMPLPVTSPLLPSPP
CCCCCCCCCCCCCCC		17.4928348404
419PhosphorylationVTSPLLPSPPAAVGG
CCCCCCCCCCCCCCC		43.4128348404
428PhosphorylationPAAVGGASATAVPSA
CCCCCCCCCCCCCCC		29.4428348404
430PhosphorylationAVGGASATAVPSAAS
CCCCCCCCCCCCCHH		26.2028348404
445PhosphorylationMTSTRAASASSVHVP
CCCCCCCCCCCCEEE		27.9130108239
447PhosphorylationSTRAASASSVHVPVS
CCCCCCCCCCEEEHH		30.3330108239
448PhosphorylationTRAASASSVHVPVSA
CCCCCCCCCEEEHHH		18.8930108239
454PhosphorylationSSVHVPVSALGAGSA
CCCEEEHHHCCCCHH		16.2330108239
456UbiquitinationVHVPVSALGAGSAAT
CEEEHHHCCCCHHHH		3.6329967540
460PhosphorylationVSALGAGSAATAASE
HHHCCCCHHHHHHCC		17.7530108239
463PhosphorylationLGAGSAATAASEEMY
CCCCHHHHHHCCCCC		23.6025693802
466PhosphorylationGSAATAASEEMYVPR
CHHHHHHCCCCCCCC		31.4629978859
470PhosphorylationTAASEEMYVPRVVTS
HHHCCCCCCCCCCCH		15.5829978859
481UbiquitinationVVTSAQQKAGRTITA
CCCHHHHHCCCEEEE		40.5029967540
498PhosphorylationTGRCDFASKNRISSS
ECCCCHHCCCCCCCC		30.38-
503PhosphorylationFASKNRISSSLAIMG
HHCCCCCCCCEEECC		15.61-
504PhosphorylationASKNRISSSLAIMGV
HCCCCCCCCEEECCC		27.3129523821
505PhosphorylationSKNRISSSLAIMGVS
CCCCCCCCEEECCCC		18.2829523821
512PhosphorylationSLAIMGVSPPMSSVV
CEEECCCCCCCCCEE		19.9827050516
513UbiquitinationLAIMGVSPPMSSVVV
EEECCCCCCCCCEEE		26.6329967540
513AcetylationLAIMGVSPPMSSVVV
EEECCCCCCCCCEEE		26.6319608861
516PhosphorylationMGVSPPMSSVVVEKH
CCCCCCCCCEEEEEC		26.2527251275
517PhosphorylationGVSPPMSSVVVEKHH
CCCCCCCCEEEEECC		16.8129523821
522UbiquitinationMSSVVVEKHHPVTVQ
CCCEEEEECCCCEEE		35.29-
538UbiquitinationIPQATAAKYPRTIHP
CCHHHCCCCCCCCCC		54.0119608861
538AcetylationIPQATAAKYPRTIHP
CCHHHCCCCCCCCCC		54.0119608861
547UbiquitinationPRTIHPESSTSASRS
CCCCCCCCCCCCCHH		43.2829967540
559PhosphorylationSRSLGTRSAHTQSLT
CHHCCCCCHHHCCCC		25.0030576142
562PhosphorylationLGTRSAHTQSLTSVH
CCCCCHHHCCCCEEE		21.4130576142
564PhosphorylationTRSAHTQSLTSVHSI
CCCHHHCCCCEEEEE		34.4730576142
566PhosphorylationSAHTQSLTSVHSIKV
CHHHCCCCEEEEEEE		33.6727732954
567PhosphorylationAHTQSLTSVHSIKVV
HHHCCCCEEEEEEEC		24.1127732954
570PhosphorylationQSLTSVHSIKVVD--
CCCCEEEEEEECC--		23.1927732954
572UbiquitinationLTSVHSIKVVD----
CCEEEEEEECC----		38.9429967540
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of POC5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POC5_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of POC5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABCE1_HUMANABCE1physical
26638075
AGK_HUMANAGKphysical
26638075
AKIP1_HUMANAKIP1physical
26638075
ALMS1_HUMANALMS1physical
26638075
ATD3A_HUMANATAD3Aphysical
26638075
ATP5L_HUMANATP5Lphysical
26638075
CP131_HUMANCEP131physical
26638075
CC138_HUMANCCDC138physical
26638075
CCD14_HUMANCCDC14physical
26638075
CCD18_HUMANCCDC18physical
26638075
CE128_HUMANCEP128physical
26638075
CE152_HUMANCEP152physical
26638075
CEP72_HUMANCEP72physical
26638075
CETN2_HUMANCETN2physical
26638075
CETN3_HUMANCETN3physical
26638075
CHTOP_HUMANCHTOPphysical
26638075
CLH1_HUMANCLTCphysical
26638075
CSPP1_HUMANCSPP1physical
26638075
OST48_HUMANDDOSTphysical
26638075
DDX47_HUMANDDX47physical
26638075
DYHC1_HUMANDYNC1H1physical
26638075
EPIPL_HUMANEPPK1physical
26638075
F161A_HUMANFAM161Aphysical
26638075
GARS_HUMANGARSphysical
26638075
GFPT1_HUMANGFPT1physical
26638075
HAUS1_HUMANHAUS1physical
26638075
HAUS2_HUMANHAUS2physical
26638075
HAUS3_HUMANHAUS3physical
26638075
HAUS4_HUMANHAUS4physical
26638075
HAUS5_HUMANHAUS5physical
26638075
HAUS6_HUMANHAUS6physical
26638075
HAUS7_HUMANHAUS7physical
26638075
HAUS8_HUMANHAUS8physical
26638075
SYIM_HUMANIARS2physical
26638075
IDH3B_HUMANIDH3Bphysical
26638075
IPO8_HUMANIPO8physical
26638075
ERD22_HUMANKDELR2physical
26638075
MOONR_HUMANKIAA0753physical
26638075
K1671_HUMANKIAA1671physical
26638075
MP2K1_HUMANMAP2K1physical
26638075
MCM2_HUMANMCM2physical
26638075
MED4_HUMANMED4physical
26638075
MIB1_HUMANMIB1physical
26638075
MPP9_HUMANMPHOSPH9physical
26638075
NAA15_HUMANNAA15physical
26638075
NIN_HUMANNINphysical
26638075
OFD1_HUMANOFD1physical
26638075
PCM1_HUMANPCM1physical
26638075
PIBF1_HUMANPIBF1physical
26638075
POC1A_HUMANPOC1Aphysical
26638075
POC1B_HUMANPOC1Bphysical
26638075
KAPCA_HUMANPRKACAphysical
26638075
PRPS1_HUMANPRPS1physical
26638075
PSDE_HUMANPSMD14physical
26638075
RAB2A_HUMANRAB2Aphysical
26638075
RAB8A_HUMANRAB8Aphysical
26638075
C560_HUMANSDHCphysical
26638075
SRSF2_HUMANSRSF2physical
26638075
ADIP_HUMANSSX2IPphysical
26638075
TALDO_HUMANTALDO1physical
26638075
TFR1_HUMANTFRCphysical
26638075
TTL12_HUMANTTLL12physical
26638075
TYSY_HUMANTYMSphysical
26638075
QCR1_HUMANUQCRC1physical
26638075
SYVC_HUMANVARSphysical
26638075
F16B1_HUMANFAM160B1physical
28514442
CETN2_HUMANCETN2physical
28514442
HOOK2_HUMANHOOK2physical
28514442
CETN3_HUMANCETN3physical
28514442
CALL3_HUMANCALML3physical
28514442
CATH_HUMANCTSHphysical
28514442
CALL5_HUMANCALML5physical
28514442
SAP3_HUMANGM2Aphysical
28514442
CBPA4_HUMANCPA4physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of POC5_HUMAN

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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-538, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-105 AND SER-109, ANDMASS SPECTROMETRY.
"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-105 AND SER-109, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172; SER-176 ANDSER-179, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND SER-109, ANDMASS SPECTROMETRY.

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