POC1B_HUMAN - dbPTM
POC1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POC1B_HUMAN
UniProt AC Q8TC44
Protein Name POC1 centriolar protein homolog B
Gene Name POC1B
Organism Homo sapiens (Human).
Sequence Length 478
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. Localizes to the basal body and cent
Protein Description Plays an important role in centriole assembly and/or stability and ciliogenesis. [PubMed: 20008567 Involved in early steps of centriole duplication, as well as in the later steps of centriole length control]
Protein Sequence MASATEDPVLERYFKGHKAAITSLDLSPNGKQLATASWDTFLMLWNFKPHARAYRYVGHKDVVTSVQFSPHGNLLASASRDRTVRLWIPDKRGKFSEFKAHTAPVRSVDFSADGQFLATASEDKSIKVWSMYRQRFLYSLYRHTHWVRCAKFSPDGRLIVSCSEDKTIKIWDTTNKQCVNNFSDSVGFANFVDFNPSGTCIASAGSDQTVKVWDVRVNKLLQHYQVHSGGVNCISFHPSGNYLITASSDGTLKILDLLEGRLIYTLQGHTGPVFTVSFSKGGELFASGGADTQVLLWRTNFDELHCKGLTKRNLKRLHFDSPPHLLDIYPRTPHPHEEKVETVEINPKLEVIDLQISTPPVMDILSFDSTTTTETSGRTLPDKGEEACGYFLNPSLMSPECLPTTTKKKTEDMSDLPCESQRSIPLAVTDALEHIMEQLNVLTQTVSILEQRLTLTEDKLKDCLENQQKLFSAVQQKS
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
3Phosphorylation-----MASATEDPVL
-----CCCCCCCHHH		34.1324719451
22PhosphorylationKGHKAAITSLDLSPN
CCCCEEEEEEECCCC		20.6430622161
23PhosphorylationGHKAAITSLDLSPNG
CCCEEEEEEECCCCC		17.4830622161
27PhosphorylationAITSLDLSPNGKQLA
EEEEEECCCCCCEEE		18.9121815630
91UbiquitinationVRLWIPDKRGKFSEF
EEEECCCCCCCCCCC		58.66-
94UbiquitinationWIPDKRGKFSEFKAH
ECCCCCCCCCCCCCC		50.15-
99MethylationRGKFSEFKAHTAPVR
CCCCCCCCCCCCCEE		34.90115978637
130PhosphorylationDKSIKVWSMYRQRFL
CCCEEHHHHHHHHHH		14.6620860994
132PhosphorylationSIKVWSMYRQRFLYS
CEEHHHHHHHHHHHH		9.7025072903
138PhosphorylationMYRQRFLYSLYRHTH
HHHHHHHHHHHHCCC		8.2325072903
139PhosphorylationYRQRFLYSLYRHTHW
HHHHHHHHHHHCCCE		22.5225072903
141PhosphorylationQRFLYSLYRHTHWVR
HHHHHHHHHCCCEEE		8.3925072903
161PhosphorylationPDGRLIVSCSEDKTI
CCCCEEEEECCCCCE		12.63-
163PhosphorylationGRLIVSCSEDKTIKI
CCEEEEECCCCCEEE		41.13-
277PhosphorylationTGPVFTVSFSKGGEL
CCCEEEEEECCCCEE		22.2724719451
307UbiquitinationNFDELHCKGLTKRNL
CCHHHHCCCCCHHHH		46.32-
321PhosphorylationLKRLHFDSPPHLLDI
HHHCCCCCCCCHHCC		39.1125018096
395PhosphorylationCGYFLNPSLMSPECL
CCCCCCHHHCCCCCC		35.3126074081
398PhosphorylationFLNPSLMSPECLPTT
CCCHHHCCCCCCCCC		23.8825159151
404PhosphorylationMSPECLPTTTKKKTE
CCCCCCCCCCCCCCC		33.8626074081
405PhosphorylationSPECLPTTTKKKTED
CCCCCCCCCCCCCCC		34.3826074081
406PhosphorylationPECLPTTTKKKTEDM
CCCCCCCCCCCCCCC		43.2626074081
408UbiquitinationCLPTTTKKKTEDMSD
CCCCCCCCCCCCCCC		63.94-
409UbiquitinationLPTTTKKKTEDMSDL
CCCCCCCCCCCCCCC		59.72-
410PhosphorylationPTTTKKKTEDMSDLP
CCCCCCCCCCCCCCC		46.20-
414PhosphorylationKKKTEDMSDLPCESQ
CCCCCCCCCCCCCCC		48.6027732954
420PhosphorylationMSDLPCESQRSIPLA
CCCCCCCCCCCCCHH		37.30-
454PhosphorylationSILEQRLTLTEDKLK
HHHHHHHHCCHHHHH		33.55-
469UbiquitinationDCLENQQKLFSAVQQ
HHHHHHHHHHHHHHH		41.56-
477UbiquitinationLFSAVQQKS------
HHHHHHHCC------		40.83-
478PhosphorylationFSAVQQKS-------
HHHHHHCC-------		40.9120860994
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 POC1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POC1B_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 POC1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F161A_HUMANFAM161Aphysical
25018096
BAG2_HUMANBAG2physical
26638075
PYR1_HUMANCADphysical
26638075
TCPB_HUMANCCT2physical
26638075
CDC37_HUMANCDC37physical
26638075
CEP44_HUMANCEP44physical
26638075
CLH1_HUMANCLTCphysical
26638075
CIP2A_HUMANKIAA1524physical
26638075
MIIP_HUMANMIIPphysical
26638075
NUDC_HUMANNUDCphysical
26638075
PELO_HUMANPELOphysical
26638075
PFD1_HUMANPFDN1physical
26638075
PFD2_HUMANPFDN2physical
26638075
PFD4_HUMANPFDN4physical
26638075
PFD5_HUMANPFDN5physical
26638075
PFD6_HUMANPFDN6physical
26638075
POC1A_HUMANPOC1Aphysical
26638075
SRSF2_HUMANSRSF2physical
26638075
SP16H_HUMANSUPT16Hphysical
26638075
TYSY_HUMANTYMSphysical
26638075
UN45A_HUMANUNC45Aphysical
26638075
PFD3_HUMANVBP1physical
26638075
ZN598_HUMANZNF598physical
28514442
SARM1_HUMANSARM1physical
28514442
TACC1_HUMANTACC1physical
28514442
WDR47_HUMANWDR47physical
28514442
HSBP1_HUMANHSBP1physical
28514442
NUDC_HUMANNUDCphysical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
FBX28_HUMANFBXO28physical
28514442
TPM2_HUMANTPM2physical
28514442
BL1S4_HUMANBLOC1S4physical
28514442
TCPG_HUMANCCT3physical
28514442
TCPD_HUMANCCT4physical
28514442
EXOC7_HUMANEXOC7physical
28514442
TCPB_HUMANCCT2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615973Cone-rod dystrophy 20 (CORD20)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of POC1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-321, AND MASSSPECTROMETRY.

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