POC1A_HUMAN - dbPTM
POC1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POC1A_HUMAN
UniProt AC Q8NBT0
Protein Name POC1 centriolar protein homolog A
Gene Name POC1A
Organism Homo sapiens (Human).
Sequence Length 407
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, spindle pole. Component of both mother and daughter centrioles.
Protein Description Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. Acts in concert with POC1B to ensure centriole integrity and proper mitotic spindle formation..
Protein Sequence MAAPCAEDPSLERHFKGHRDAVTCVDFSINTKQLASGSMDSCLMVWHMKPQSRAYRFTGHKDAVTCVNFSPSGHLLASGSRDKTVRIWVPNVKGESTVFRAHTATVRSVHFCSDGQSFVTASDDKTVKVWATHRQKFLFSLSQHINWVRCAKFSPDGRLIVSASDDKTVKLWDKSSRECVHSYCEHGGFVTYVDFHPSGTCIAAAGMDNTVKVWDVRTHRLLQHYQLHSAAVNGLSFHPSGNYLITASSDSTLKILDLMEGRLLYTLHGHQGPATTVAFSRTGEYFASGGSDEQVMVWKSNFDIVDHGEVTKVPRPPATLASSMGNLPEVDFPVPPGRGRSVESVQSQPQEPVSVPQTLTSTLEHIVGQLDVLTQTVSILEQRLTLTEDKLKQCLENQQLIMQRATP
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
28PhosphorylationAVTCVDFSINTKQLA
CCEEEECEECHHHHH
15.5124505115
61UbiquitinationAYRFTGHKDAVTCVN
CCCCCCCCCCEEEEE
49.04-
65PhosphorylationTGHKDAVTCVNFSPS
CCCCCCEEEEEECCC
16.6825850435
70PhosphorylationAVTCVNFSPSGHLLA
CEEEEEECCCCCEEE
16.9825850435
72PhosphorylationTCVNFSPSGHLLASG
EEEEECCCCCEEECC
37.3325850435
78PhosphorylationPSGHLLASGSRDKTV
CCCCEEECCCCCCEE
36.9525850435
80PhosphorylationGHLLASGSRDKTVRI
CCEEECCCCCCEEEE
34.5125850435
90UbiquitinationKTVRIWVPNVKGEST
CEEEEEECCCCCCCC
25.5429967540
93UbiquitinationRIWVPNVKGESTVFR
EEEECCCCCCCCEEE
64.70-
97PhosphorylationPNVKGESTVFRAHTA
CCCCCCCCEEEEEEC
21.2524719451
128UbiquitinationASDDKTVKVWATHRQ
CCCCCEEEEEEECHH
36.9729967540
129UbiquitinationSDDKTVKVWATHRQK
CCCCEEEEEEECHHH
3.5029967540
132UbiquitinationKTVKVWATHRQKFLF
CEEEEEEECHHHHHH
11.2429967540
167UbiquitinationIVSASDDKTVKLWDK
EEECCCCCCEEEECC
61.2729967540
170UbiquitinationASDDKTVKLWDKSSR
CCCCCCEEEECCCCH
49.4429967540
174UbiquitinationKTVKLWDKSSRECVH
CCEEEECCCCHHHHH
38.46-
252PhosphorylationITASSDSTLKILDLM
EEECCCCCEEEEHHH
36.74-
319PhosphorylationKVPRPPATLASSMGN
CCCCCCHHHHHCCCC
28.7325693802
319 (in isoform 2)Phosphorylation-28.7324719451
322 (in isoform 2)Phosphorylation-24.7824043423
322PhosphorylationRPPATLASSMGNLPE
CCCHHHHHCCCCCCC
24.7825693802
323 (in isoform 2)Phosphorylation-25.7124043423
323PhosphorylationPPATLASSMGNLPEV
CCHHHHHCCCCCCCC
25.7125693802
328 (in isoform 2)Phosphorylation-43.4924043423
330 (in isoform 2)Phosphorylation-9.6824043423
337 (in isoform 2)Phosphorylation-38.3124719451
339 (in isoform 2)Phosphorylation-31.9324719451
341PhosphorylationVPPGRGRSVESVQSQ
CCCCCCCCHHHHCCC
32.8227251275
344UbiquitinationGRGRSVESVQSQPQE
CCCCCHHHHCCCCCC
24.2529967540
344PhosphorylationGRGRSVESVQSQPQE
CCCCCHHHHCCCCCC
24.2527251275
347PhosphorylationRSVESVQSQPQEPVS
CCHHHHCCCCCCCCC
41.4927251275
354UbiquitinationSQPQEPVSVPQTLTS
CCCCCCCCCCHHHHH
38.5029967540
354PhosphorylationSQPQEPVSVPQTLTS
CCCCCCCCCCHHHHH
38.5027251275
374PhosphorylationVGQLDVLTQTVSILE
HHHHHHHHHHHHHHH
23.2627251275
376PhosphorylationQLDVLTQTVSILEQR
HHHHHHHHHHHHHHH
15.8127251275
378PhosphorylationDVLTQTVSILEQRLT
HHHHHHHHHHHHHHC
25.5027251275
385PhosphorylationSILEQRLTLTEDKLK
HHHHHHHCCCHHHHH
33.55-
387PhosphorylationLEQRLTLTEDKLKQC
HHHHHCCCHHHHHHH
36.58-
392UbiquitinationTLTEDKLKQCLENQQ
CCCHHHHHHHHHHHH
44.7129967540
406PhosphorylationQLIMQRATP------
HHHHHHCCC------
31.5526074081

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 POC1A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POC1A_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 POC1A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPH_HUMANCCT7physical
26186194
TCPD_HUMANCCT4physical
26186194
HSP7C_HUMANHSPA8physical
26186194
HSP76_HUMANHSPA6physical
26186194
HS71L_HUMANHSPA1Lphysical
26186194
TCPZ_HUMANCCT6Aphysical
26186194
TCPQ_HUMANCCT8physical
26186194
TCPG_HUMANCCT3physical
26186194
TCPA_HUMANTCP1physical
26186194
POC1B_HUMANPOC1Bphysical
26186194
TCPE_HUMANCCT5physical
26186194
TCPB_HUMANCCT2physical
26186194
PHLP_HUMANPDCLphysical
26186194
TXND9_HUMANTXNDC9physical
26186194
COR1A_HUMANCORO1Aphysical
26186194
SAHH2_HUMANAHCYL1physical
26638075
AKIP1_HUMANAKIP1physical
26638075
AP4B1_HUMANAP4B1physical
26638075
ATG2B_HUMANATG2Bphysical
26638075
BTF3_HUMANBTF3physical
26638075
R3HCL_HUMANR3HCC1Lphysical
26638075
CAMP1_HUMANCAMSAP1physical
26638075
CCD66_HUMANCCDC66physical
26638075
TCPB_HUMANCCT2physical
26638075
TCPG_HUMANCCT3physical
26638075
TCPD_HUMANCCT4physical
26638075
TCPE_HUMANCCT5physical
26638075
TCPZ_HUMANCCT6Aphysical
26638075
TCPH_HUMANCCT7physical
26638075
TCPQ_HUMANCCT8physical
26638075
CENPH_HUMANCENPHphysical
26638075
CEP44_HUMANCEP44physical
26638075
CKAP2_HUMANCKAP2physical
26638075
KCRB_HUMANCKBphysical
26638075
COMD2_HUMANCOMMD2physical
26638075
COMD4_HUMANCOMMD4physical
26638075
CRBG3_HUMANCRYBG3physical
26638075
DDX3Y_HUMANDDX3Yphysical
26638075
KTU_HUMANDNAAF2physical
26638075
DNJA2_HUMANDNAJA2physical
26638075
ECD_HUMANECDphysical
26638075
ENOG_HUMANENO2physical
26638075
F161A_HUMANFAM161Aphysical
26638075
FKBP4_HUMANFKBP4physical
26638075
GTSE1_HUMANGTSE1physical
26638075
HAUS4_HUMANHAUS4physical
26638075
IBTK_HUMANIBTKphysical
26638075
LAR1B_HUMANLARP1Bphysical
26638075
LTV1_HUMANLTV1physical
26638075
LUZP1_HUMANLUZP1physical
26638075
MA7D1_HUMANMAP7D1physical
26638075
MA7D3_HUMANMAP7D3physical
26638075
MARE2_HUMANMAPRE2physical
26638075
MIIP_HUMANMIIPphysical
26638075
MTUS1_HUMANMTUS1physical
26638075
CND2_HUMANNCAPHphysical
26638075
NOB1_HUMANNOB1physical
26638075
NUDC_HUMANNUDCphysical
26638075
PHLP_HUMANPDCLphysical
26638075
PDCL3_HUMANPDCL3physical
26638075
PELO_HUMANPELOphysical
26638075
PFD1_HUMANPFDN1physical
26638075
PFD2_HUMANPFDN2physical
26638075
PFD4_HUMANPFDN4physical
26638075
PFD5_HUMANPFDN5physical
26638075
PFD6_HUMANPFDN6physical
26638075
PKHA5_HUMANPLEKHA5physical
26638075
POC1B_HUMANPOC1Bphysical
26638075
POC5_HUMANPOC5physical
26638075
RIOK1_HUMANRIOK1physical
26638075
RPAP3_HUMANRPAP3physical
26638075
RIR2_HUMANRRM2physical
26638075
SKA3_HUMANSKA3physical
26638075
SLAI2_HUMANSLAIN2physical
26638075
SGT1_HUMANSUGT1physical
26638075
TAF2_HUMANTAF2physical
26638075
TCHP_HUMANTCHPphysical
26638075
TCPA_HUMANTCP1physical
26638075
TDRD3_HUMANTDRD3physical
26638075
TOP3B_HUMANTOP3Bphysical
26638075
TTK_HUMANTTKphysical
26638075
TXND9_HUMANTXNDC9physical
26638075
UN45A_HUMANUNC45Aphysical
26638075
PFD3_HUMANVBP1physical
26638075
WIPI4_HUMANWDR45physical
26638075
XRN1_HUMANXRN1physical
26638075
POC1B_HUMANPOC1Bphysical
28514442
COR1A_HUMANCORO1Aphysical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPB_HUMANCCT2physical
28514442
TCPD_HUMANCCT4physical
28514442
TCPH_HUMANCCT7physical
28514442
TCPA_HUMANTCP1physical
28514442
TCPG_HUMANCCT3physical
28514442
TCPQ_HUMANCCT8physical
28514442
TCPE_HUMANCCT5physical
28514442
HSP7C_HUMANHSPA8physical
28514442
HSP76_HUMANHSPA6physical
28514442
POTEF_HUMANPOTEFphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of POC1A_HUMAN

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Related Literatures of Post-Translational Modification

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