PITM3_HUMAN - dbPTM
PITM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PITM3_HUMAN
UniProt AC Q9BZ71
Protein Name Membrane-associated phosphatidylinositol transfer protein 3
Gene Name PITPNM3
Organism Homo sapiens (Human).
Sequence Length 974
Subcellular Localization Endomembrane system
Peripheral membrane protein .
Protein Description Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro) (By similarity). Binds calcium ions..
Protein Sequence MAKAGRAGGPPPGGGAPWHLRNVLSDSVESSDDEFFDAREEMAEGKNAILIGMSQWNSNDLVEQIETMGKLDEHQGEGTAPCTSSILQEKQRELYRVSLRRQRFPAQGSIEIHEDSEEGCPQRSCKTHVLLLVLHGGNILDTGAGDPSCKAADIHTFSSVLEKVTRAHFPAALGHILIKFVPCPAICSEAFSLVSHLNPYSHDEGCLSSSQDHVPLAALPLLAISSPQYQDAVATVIERANQVYREFLKSSDGIGFSGQVCLIGDCVGGLLAFDAICYSAGPSGDSPASSSRKGSISSTQDTPVAVEEDCSLASSKRLSKSNIDISSGLEDEEPKRPLPRKQSDSSTYDCEAITQHHAFLSSIHSSVLKDESETPAAGGPQLPEVSLGRFDFDVSDFFLFGSPLGLVLAMRRTVLPGLDGFQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRFPLGDGQSLLLADALHTHSPLFLEGSSRDSPPLLDAPASPPQASRFQRPGRRMSEGSSHSESSESSDSMAPVGASRITAKWWGSKRIDYALYCPDVLTAFPTVALPHLFHASYWESTDVVAFILRQVMRYESVNIKESARLDPAALSPANPREKWLRKRTQVKLRNVTANHRANDVIAAEDGPQVLVGRFMYGPLDMVALTGEKVDILVMAEPSSGRWVHLDTEITNSSGRITYNVPRPRRLGVGVYPVKMVVRGDQTCAMSYLTVLPRGMECVVFSIDGSFAASVSIMGSDPKVRPGAVDVVRHWQDLGYMILYITGRPDMQKQRVVSWLSQHNFPQGMIFFSDGLVHDPLRQKAIFLRNLMQECFIKISAAYGSTKDISVYSVLGLPASQIFIVGRPTKKYQTQCQFLSEGYAAHLAALEASHRSRPKKNNSRMILRKGSFGLHAQPEFLRKRNHLRRTMSVQQPDPPAANPKPERAQSQPESDKDHERPLPALSWARGPPKFESVP
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
25PhosphorylationWHLRNVLSDSVESSD
HHHHHHHHCCCCCCC		24.4527732954
27PhosphorylationLRNVLSDSVESSDDE
HHHHHHCCCCCCCCH		25.1427732954
30PhosphorylationVLSDSVESSDDEFFD
HHHCCCCCCCCHHHH		36.5922617229
30 (in isoform 3)Phosphorylation-36.5929743597
31PhosphorylationLSDSVESSDDEFFDA
HHCCCCCCCCHHHHH		35.2622617229
31 (in isoform 3)Phosphorylation-35.2629743597
58PhosphorylationIGMSQWNSNDLVEQI
EECCCCCCHHHHHHH		28.8528348404
95PhosphorylationQEKQRELYRVSLRRQ
HHHHHHHHHHHHHHC		12.2924719451
98PhosphorylationQRELYRVSLRRQRFP
HHHHHHHHHHHCCCC		13.7324719451
109PhosphorylationQRFPAQGSIEIHEDS
CCCCCCCCEEEECCC		12.6426657352
116PhosphorylationSIEIHEDSEEGCPQR
CEEEECCCCCCCCCC		34.2628102081
124PhosphorylationEEGCPQRSCKTHVLL
CCCCCCCCCCCEEEE		18.08-
295PhosphorylationASSSRKGSISSTQDT
CCCCCCCCCCCCCCC		23.4923927012
297PhosphorylationSSRKGSISSTQDTPV
CCCCCCCCCCCCCCE		29.0923927012
298PhosphorylationSRKGSISSTQDTPVA
CCCCCCCCCCCCCEE		28.5525159151
299PhosphorylationRKGSISSTQDTPVAV
CCCCCCCCCCCCEEH		24.5525159151
302PhosphorylationSISSTQDTPVAVEED
CCCCCCCCCEEHHHC		15.1723927012
319PhosphorylationLASSKRLSKSNIDIS
HHHCCCHHHCCCCCC		37.7626657352
321PhosphorylationSSKRLSKSNIDISSG
HCCCHHHCCCCCCCC		35.3230266825
326PhosphorylationSKSNIDISSGLEDEE
HHCCCCCCCCCCCCC		18.0123927012
327PhosphorylationKSNIDISSGLEDEEP
HCCCCCCCCCCCCCC		47.9723186163
343PhosphorylationRPLPRKQSDSSTYDC
CCCCCCCCCCCCCCH		42.3628348404
345PhosphorylationLPRKQSDSSTYDCEA
CCCCCCCCCCCCHHH		29.8129449344
346PhosphorylationPRKQSDSSTYDCEAI
CCCCCCCCCCCHHHH		35.6629449344
347PhosphorylationRKQSDSSTYDCEAIT
CCCCCCCCCCHHHHH		27.6029449344
348PhosphorylationKQSDSSTYDCEAITQ
CCCCCCCCCHHHHHH		22.1229449344
372PhosphorylationSSVLKDESETPAAGG
HHHCCCCCCCCCCCC		57.8322210691
374PhosphorylationVLKDESETPAAGGPQ
HCCCCCCCCCCCCCC		27.7522210691
413PhosphorylationLVLAMRRTVLPGLDG
HHHHHHHCCCCCCCC		18.9417924679
473PhosphorylationFPLGDGQSLLLADAL
ECCCCCHHEEHHHHH		26.8920873877
482PhosphorylationLLADALHTHSPLFLE
EHHHHHHCCCCEEEC		25.5428348404
484PhosphorylationADALHTHSPLFLEGS
HHHHHCCCCEEECCC		25.1828348404
491PhosphorylationSPLFLEGSSRDSPPL
CCEEECCCCCCCCCC		16.9028348404
492PhosphorylationPLFLEGSSRDSPPLL
CEEECCCCCCCCCCC		51.4628348404
495PhosphorylationLEGSSRDSPPLLDAP
ECCCCCCCCCCCCCC		27.5721815630
504PhosphorylationPLLDAPASPPQASRF
CCCCCCCCCCCCCCC		35.7328355574
509PhosphorylationPASPPQASRFQRPGR
CCCCCCCCCCCCCCC		28.5120873877
519PhosphorylationQRPGRRMSEGSSHSE
CCCCCCCCCCCCCCC		36.6723927012
522PhosphorylationGRRMSEGSSHSESSE
CCCCCCCCCCCCCCC		22.3322210691
523PhosphorylationRRMSEGSSHSESSES
CCCCCCCCCCCCCCC		41.7222210691
525PhosphorylationMSEGSSHSESSESSD
CCCCCCCCCCCCCCC		40.9123090842
527PhosphorylationEGSSHSESSESSDSM
CCCCCCCCCCCCCCC		42.2823090842
528PhosphorylationGSSHSESSESSDSMA
CCCCCCCCCCCCCCC		37.1323927012
530PhosphorylationSHSESSESSDSMAPV
CCCCCCCCCCCCCCC		41.2023090842
531PhosphorylationHSESSESSDSMAPVG
CCCCCCCCCCCCCCC		29.6523090842
612PhosphorylationRLDPAALSPANPREK
CCCHHHCCCCCHHHH		19.7621815630
899PhosphorylationSRPKKNNSRMILRKG
CCCCCCCCCEEECCC		32.4029514088
907PhosphorylationRMILRKGSFGLHAQP
CEEECCCCCCCCCCH		21.1230266825
926PhosphorylationKRNHLRRTMSVQQPD
HCCCHHHCCCCCCCC		13.8328857561
928PhosphorylationNHLRRTMSVQQPDPP
CCHHHCCCCCCCCCC		19.0323911959
946PhosphorylationPKPERAQSQPESDKD
CCHHHHHCCCCCCCC		46.8720873877
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 PITM3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PITM3_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 PITM3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAK2_HUMANPTK2Bphysical
10022914
Drug and Disease Associations
Kegg Disease
OMIM Disease
600977Cone-rod dystrophy 5 (CORD5)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PITM3_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-30; SER-31; SER-907 ANDSER-928, AND MASS 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-413, AND MASSSPECTROMETRY.

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