PRIC3_HUMAN - dbPTM
PRIC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRIC3_HUMAN
UniProt AC O43900
Protein Name Prickle planar cell polarity protein 3 {ECO:0000312|HGNC:HGNC:6645}
Gene Name PRICKLE3 {ECO:0000312|HGNC:HGNC:6645}
Organism Homo sapiens (Human).
Sequence Length 615
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Recruited by VANGL2 to anterior cell borders. This polarity is controlled by Wnt proteins (By similarity). WTIP is involved in the recruitment of PRICKLE3 to the basal body
Protein Description Involved in the planar cell polarity (PCP) pathway that is essential for the polarization of epithelial cells during morphogenetic processes, including gastrulation and neurulation (By similarity). PCP is maintained by two molecular modules, the global and the core modules, PRICKLE3 being part of the core module (By similarity). Distinct complexes of the core module segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (By similarity). Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity)..
Protein Sequence MFARGSRRRRSGRAPPEAEDPDRGQPCNSCREQCPGFLLHGWRKICQHCKCPREEHAVHAVPVDLERIMCRLISDFQRHSISDDDSGCASEEYAWVPPGLKPEQVYQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSEAQYCTALEEEEKKELRAFSQQRKRENLGRGIVRIFPVTITGAICEECGKQIGGGDIAVFASRAGLGACWHPQCFVCTTCQELLVDLIYFYHVGKVYCGRHHAECLRPRCQACDEIIFSPECTEAEGRHWHMDHFCCFECEASLGGQRYVMRQSRPHCCACYEARHAEYCDGCGEHIGLDQGQMAYEGQHWHASDRCFCCSRCGRALLGRPFLPRRGLIFCSRACSLGSEPTAPGPSRRSWSAGPVTAPLAASTASFSAVKGASETTTKGTSTELAPATGPEEPSRFLRGAPHRHSMPELGLRSVPEPPPESPGQPNLRPDDSAFGRQSTPRVSFRDPLVSEGGPRRTLSAPPAQRRRPRSPPPRAPSRRRHHHHNHHHHHNRHPSRRRHYQCDAGSGSDSESCSSSPSSSSSESSEDDGFFLGERIPLPPHLCRPMPAQDTAMETFNSPSLSLPRDSRAGMPRQARDKNCIVA
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
4Methylation----MFARGSRRRRS
----CCCCCCCCCCC		32.14115482191
74PhosphorylationRIMCRLISDFQRHSI
HHHHHHHHHHHHHCC		36.6428555341
80PhosphorylationISDFQRHSISDDDSG
HHHHHHHCCCCCCCC		26.4424275569
122PhosphorylationDKVPYVNSPGEKYRI
CCCCCCCCCCHHHHH		25.0025159151
126UbiquitinationYVNSPGEKYRIKQLL
CCCCCCHHHHHHHHH		45.8221890473
130UbiquitinationPGEKYRIKQLLHQLP
CCHHHHHHHHHHHCC		26.37-
182PhosphorylationRIFPVTITGAICEEC
EEEEEEEEHHHHHHH		15.9322210691
303PhosphorylationRPHCCACYEARHAEY
CCCEEEEHHHHCHHC		8.2925839225
329UbiquitinationQGQMAYEGQHWHASD
CCCCCCCCCCCCCCC		16.3921890473
367PhosphorylationIFCSRACSLGSEPTA
EEEECCCCCCCCCCC		34.4816964243
370PhosphorylationSRACSLGSEPTAPGP
ECCCCCCCCCCCCCC		45.7716964243
378PhosphorylationEPTAPGPSRRSWSAG
CCCCCCCCCCCCCCC		46.3616964243
381PhosphorylationAPGPSRRSWSAGPVT
CCCCCCCCCCCCCCC		25.0322617229
383PhosphorylationGPSRRSWSAGPVTAP
CCCCCCCCCCCCCCC		25.2921712546
388PhosphorylationSWSAGPVTAPLAAST
CCCCCCCCCCHHHHC		26.2026074081
394PhosphorylationVTAPLAASTASFSAV
CCCCHHHHCCCEECC		20.9226074081
395PhosphorylationTAPLAASTASFSAVK
CCCHHHHCCCEECCC		22.9226074081
397PhosphorylationPLAASTASFSAVKGA
CHHHHCCCEECCCCC		21.5926074081
405PhosphorylationFSAVKGASETTTKGT
EECCCCCCCCCCCCC		44.1122210691
407PhosphorylationAVKGASETTTKGTST
CCCCCCCCCCCCCCC		36.9530576142
408PhosphorylationVKGASETTTKGTSTE
CCCCCCCCCCCCCCC		23.5822210691
409PhosphorylationKGASETTTKGTSTEL
CCCCCCCCCCCCCCC		34.5923312004
410UbiquitinationGASETTTKGTSTELA
CCCCCCCCCCCCCCC		59.0921890473
412PhosphorylationSETTTKGTSTELAPA
CCCCCCCCCCCCCCC		33.7530266825
413PhosphorylationETTTKGTSTELAPAT
CCCCCCCCCCCCCCC		28.6630266825
414PhosphorylationTTTKGTSTELAPATG
CCCCCCCCCCCCCCC		34.5530266825
437PhosphorylationRGAPHRHSMPELGLR
CCCCCCCCCCCCCCC		35.6730266825
445PhosphorylationMPELGLRSVPEPPPE
CCCCCCCCCCCCCCC		47.2529978859
453PhosphorylationVPEPPPESPGQPNLR
CCCCCCCCCCCCCCC		39.8526657352
464PhosphorylationPNLRPDDSAFGRQST
CCCCCCCCCCCCCCC		32.6430576142
470PhosphorylationDSAFGRQSTPRVSFR
CCCCCCCCCCCEECC		38.7323186163
471PhosphorylationSAFGRQSTPRVSFRD
CCCCCCCCCCEECCC		13.5323186163
475PhosphorylationRQSTPRVSFRDPLVS
CCCCCCEECCCCCCC		18.8230266825
482PhosphorylationSFRDPLVSEGGPRRT
ECCCCCCCCCCCCCC		37.9030266825
489PhosphorylationSEGGPRRTLSAPPAQ
CCCCCCCCCCCCHHH		26.7526657352
491PhosphorylationGGPRRTLSAPPAQRR
CCCCCCCCCCHHHHC		37.8130266825
502PhosphorylationAQRRRPRSPPPRAPS
HHHCCCCCCCCCCCC		44.4326329039
538PhosphorylationHYQCDAGSGSDSESC
EEECCCCCCCCCCCC		36.5230576142
542PhosphorylationDAGSGSDSESCSSSP
CCCCCCCCCCCCCCC		32.86-
553PhosphorylationSSSPSSSSSESSEDD
CCCCCCCCCCCCCCC		39.8230576142
590PhosphorylationTAMETFNSPSLSLPR
CHHHHHCCCCCCCCC		16.2125850435
592PhosphorylationMETFNSPSLSLPRDS
HHHHCCCCCCCCCCC		30.3429978859
594PhosphorylationTFNSPSLSLPRDSRA
HHCCCCCCCCCCCCC		40.4424719451
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 PRIC3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRIC3_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 PRIC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI29_HUMANTRIM29physical
20211142
ST2B1_HUMANSULT2B1physical
25416956
GLGB_HUMANGBE1physical
26496610
TWF1_HUMANTWF1physical
26496610
TBG1_HUMANTUBG1physical
26496610
1433E_HUMANYWHAEphysical
26496610
UBL4A_HUMANUBL4Aphysical
26496610
CHD9_HUMANCHD9physical
26496610
RN170_HUMANRNF170physical
26496610
MET18_HUMANMETTL18physical
28514442
PLCD3_HUMANPLCD3physical
28514442
E41L1_HUMANEPB41L1physical
28514442
PRD10_HUMANPRDM10physical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
E41L5_HUMANEPB41L5physical
28514442
SIAH2_HUMANSIAH2physical
28514442
GCP4_HUMANTUBGCP4physical
28514442
ARMC8_HUMANARMC8physical
28514442
1433E_HUMANYWHAEphysical
28514442
ZBT10_HUMANZBTB10physical
28514442
PDLI7_HUMANPDLIM7physical
28514442
FBW1A_HUMANBTRCphysical
28514442
1433Z_HUMANYWHAZphysical
28514442
WDR26_HUMANWDR26physical
28514442
NDK7_HUMANNME7physical
28514442
RBP10_HUMANRANBP10physical
28514442
PI42B_HUMANPIP4K2Bphysical
28514442
HIC2_HUMANHIC2physical
28514442
AFAD_HUMANMLLT4physical
28514442
ZBT21_HUMANZBTB21physical
28514442
E41L3_HUMANEPB41L3physical
28514442
MAEA_HUMANMAEAphysical
28514442
1433G_HUMANYWHAGphysical
28514442
RMD5A_HUMANRMND5Aphysical
28514442
1433F_HUMANYWHAHphysical
28514442
PP1R7_HUMANPPP1R7physical
28514442
FBW1B_HUMANFBXW11physical
28514442
FARP2_HUMANFARP2physical
28514442
PI42A_HUMANPIP4K2Aphysical
28514442
1433B_HUMANYWHABphysical
28514442
TSR3_HUMANTSR3physical
28514442
VANG1_HUMANVANGL1physical
28514442
GID8_HUMANGID8physical
28514442
ZN460_HUMANZNF460physical
28514442
CAMKV_HUMANCAMKVphysical
28514442
OSBL3_HUMANOSBPL3physical
28514442
GID4_HUMANGID4physical
28514442
RN138_HUMANRNF138physical
28514442
TOP1_HUMANTOP1physical
28514442
ZN852_HUMANZNF852physical
28514442
SLIT2_HUMANSLIT2physical
28514442
GCP6_HUMANTUBGCP6physical
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 PRIC3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-502, AND MASSSPECTROMETRY.
"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-502, AND MASSSPECTROMETRY.

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