PITM1_HUMAN - dbPTM
PITM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PITM1_HUMAN
UniProt AC O00562
Protein Name Membrane-associated phosphatidylinositol transfer protein 1
Gene Name PITPNM1
Organism Homo sapiens (Human).
Sequence Length 1244
Subcellular Localization Cytoplasm. Golgi apparatus, Golgi stack membrane
Peripheral membrane protein. Endoplasmic reticulum membrane
Peripheral membrane protein. Lipid droplet . Cleavage furrow . Midbody . Peripheral membrane protein associated with Golgi stacks in inte
Protein Description Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro). May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes (By similarity). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions..
Protein Sequence MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRLYHSVKTGRGPLSDDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELSMADIRALEEETARMLAQRMAKCNTGSEGSEAQPPGKPSTEARSAASNTGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQHGGAVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDSEEVFPKEMTKWNSNDFIDAFASPVEAEGTPEPGAEAAKGIEDGAQAPRDSEGLDGAGELGAEACAVHALFLILHSGNILDSGPGDANSKQADVQTLSSAFEAVTRIHFPEALGHVALRLVPCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTNQAYSAFLRSPEGAGFCGQVALIGDGVGGILGFDALCHSANAGTGSRGSSRRGSMNNELLSPEFGPVRDPLADGVEGLGRGSPEPSALPPQRIPSDMASPEPEGSQNSLQAAPATTSSWEPRRASTAFCPPAASSEAPDGPSSTARLDFKVSGFFLFGSPLGLVLALRKTVMPALEAAQMRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLTVPRYQKFPLGDGSSLLLADTLQTHSSLFLEELEMLVPSTPTSTSGAFWKGSELATDPPAQPAAPSTTSEVVKILERWWGTKRIDYSLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLAECEEPSIYSPAFPREKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLSGRFMYGPLDVVTLTGEKVDVYIMTQPLSGKWIHFGTEVTNSSGRLTFPVPPERALGIGVYPVRMVVRGDHTYAECCLTVVARGTEAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPSQTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHASSGPPRAALGKSSYGVAAPVDFLRKQSQLLRSRGPSQAEREGPGTPPTTLARGKARSISLKLDSEE
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
59PhosphorylationPGGSGQYTHKVYHVG
CCCCCCCEEEEEECC		13.8212225667
166UbiquitinationPRLYHSVKTGRGPLS
CCCCCCCCCCCCCCC		48.56-
280PhosphorylationKPSTEARSAASNTGT
CCCHHHHHHHHCCCC		34.9227251275
283PhosphorylationTEARSAASNTGTPDG
HHHHHHHHCCCCCCC		34.3427251275
285PhosphorylationARSAASNTGTPDGPE
HHHHHHCCCCCCCCC		39.6822199227
287PhosphorylationSAASNTGTPDGPEAP
HHHHCCCCCCCCCCC		19.0322199227
300PhosphorylationAPPGPDASPDASFGK
CCCCCCCCCCCCCCC		30.6028355574
304PhosphorylationPDASPDASFGKQWSS
CCCCCCCCCCCCCCC		41.7428450419
315PhosphorylationQWSSSSRSSYSSQHG
CCCCCCCCCCCCCCC		35.2623663014
316PhosphorylationWSSSSRSSYSSQHGG
CCCCCCCCCCCCCCC		28.1123663014
317PhosphorylationSSSSRSSYSSQHGGA
CCCCCCCCCCCCCCC		17.3723663014
318PhosphorylationSSSRSSYSSQHGGAV
CCCCCCCCCCCCCCC		26.0123663014
319PhosphorylationSSRSSYSSQHGGAVS
CCCCCCCCCCCCCCC		20.2628450419
326PhosphorylationSQHGGAVSPQSLSEW
CCCCCCCCHHHHHHH		19.3828857561
329PhosphorylationGGAVSPQSLSEWRMQ
CCCCCHHHHHHHHHH		36.93-
342PhosphorylationMQNIARDSENSSEEE
HHHHHHCCCCCCHHH		32.88-
345PhosphorylationIARDSENSSEEEFFD
HHHCCCCCCHHHHHH		34.7724461736
346PhosphorylationARDSENSSEEEFFDA
HHCCCCCCHHHHHHC		61.6924461736
358PhosphorylationFDAHEGFSDSEEVFP
HHCCCCCCCCCHHCC		51.5930266825
360PhosphorylationAHEGFSDSEEVFPKE
CCCCCCCCCHHCCHH		34.1630266825
369PhosphorylationEVFPKEMTKWNSNDF
HHCCHHHHCCCCCCC		33.7228450419
373PhosphorylationKEMTKWNSNDFIDAF
HHHHCCCCCCCHHHC		36.3422617229
382PhosphorylationDFIDAFASPVEAEGT
CCHHHCCCCEECCCC		24.0329978859
389PhosphorylationSPVEAEGTPEPGAEA
CCEECCCCCCCCHHH		18.9115125835
505PhosphorylationPYSHDGDSLSRSQDH
CCCCCCCCCCCCCCC		33.5026699800
509PhosphorylationDGDSLSRSQDHIPLA
CCCCCCCCCCCCCHH		36.2620873877
528PhosphorylationLATSSSRYQGAVATV
HHCCCCCCCCCCEEH		17.1622461510
534PhosphorylationRYQGAVATVIARTNQ
CCCCCCEEHHHHCHH		13.0722210691
578PhosphorylationGFDALCHSANAGTGS
CHHHHHCCCCCCCCC		23.4024719451
583PhosphorylationCHSANAGTGSRGSSR
HCCCCCCCCCCCCCC		29.5830301811
585PhosphorylationSANAGTGSRGSSRRG
CCCCCCCCCCCCCCC		33.0530301811
593PhosphorylationRGSSRRGSMNNELLS
CCCCCCCCCCCCCCC		19.2729255136
600PhosphorylationSMNNELLSPEFGPVR
CCCCCCCCCCCCCCC		34.7029255136
621PhosphorylationVEGLGRGSPEPSALP
CCCCCCCCCCCCCCC		25.4030266825
625PhosphorylationGRGSPEPSALPPQRI
CCCCCCCCCCCCCCC		40.5530266825
638PhosphorylationRIPSDMASPEPEGSQ
CCCCCCCCCCCCCCC		24.1415125835
664PhosphorylationSWEPRRASTAFCPPA
CCCCCCCCCCCCCCC		20.6123401153
664O-linked_GlycosylationSWEPRRASTAFCPPA
CCCCCCCCCCCCCCC		20.6130379171
665PhosphorylationWEPRRASTAFCPPAA
CCCCCCCCCCCCCCC		23.8325159151
673PhosphorylationAFCPPAASSEAPDGP
CCCCCCCCCCCCCCC		30.7121964256
673O-linked_GlycosylationAFCPPAASSEAPDGP
CCCCCCCCCCCCCCC		30.7130379171
674PhosphorylationFCPPAASSEAPDGPS
CCCCCCCCCCCCCCC		32.8121964256
747UbiquitinationLEPLLAPKFQAIAPL
CHHHHCCCCEEECCC		44.49-
755PhosphorylationFQAIAPLTVPRYQKF
CEEECCCCCCCCCCC		27.6624719451
794PhosphorylationLEMLVPSTPTSTSGA
HHHHCCCCCCCCCCC		25.2315125835
893PhosphorylationLAECEEPSIYSPAFP
HHCCCCCCCCCCCCC		37.1230108239
895PhosphorylationECEEPSIYSPAFPRE
CCCCCCCCCCCCCHH		16.9728450419
896PhosphorylationCEEPSIYSPAFPREK
CCCCCCCCCCCCHHH		14.2125159151
936PhosphorylationEGRPQVLSGRFMYGP
CCCCEEECCCCCCCC		29.1224719451
1020PhosphorylationLTVVARGTEAVVFSI
EEEEECCCEEEEEEE		18.4123684312
1026PhosphorylationGTEAVVFSIDGSFTA
CCEEEEEEECCCEEE		14.2523684312
1030PhosphorylationVVFSIDGSFTASVSI
EEEEECCCEEEEEEE		18.7123684312
1032PhosphorylationFSIDGSFTASVSIMG
EEECCCEEEEEEECC		21.5223684312
1034PhosphorylationIDGSFTASVSIMGSD
ECCCEEEEEEECCCC		17.2223684312
1036PhosphorylationGSFTASVSIMGSDPK
CCEEEEEEECCCCCC		12.3623684312
1190PhosphorylationPRAALGKSSYGVAAP
CCHHHCCCCCCCHHC		27.3028857561
1191PhosphorylationRAALGKSSYGVAAPV
CHHHCCCCCCCHHCH		29.4128857561
1192PhosphorylationAALGKSSYGVAAPVD
HHHCCCCCCCHHCHH		23.7827642862
1205PhosphorylationVDFLRKQSQLLRSRG
HHHHHHHHHHHHHCC		26.3224719451
1211MethylationQSQLLRSRGPSQAER
HHHHHHHCCCCHHHH		55.3958858943
1214PhosphorylationLLRSRGPSQAEREGP
HHHHCCCCHHHHCCC		44.86-
1218MethylationRGPSQAEREGPGTPP
CCCCHHHHCCCCCCC		58.13-
1223PhosphorylationAEREGPGTPPTTLAR
HHHCCCCCCCCHHHC		29.2715125835
1227PhosphorylationGPGTPPTTLARGKAR
CCCCCCCHHHCCCCC		24.9724719451
1230MethylationTPPTTLARGKARSIS
CCCCHHHCCCCCEEE		50.7082954805
1235PhosphorylationLARGKARSISLKLDS
HHCCCCCEEEEECCC		22.7622617229
1237PhosphorylationRGKARSISLKLDSEE
CCCCCEEEEECCCCC		22.2422617229
1242PhosphorylationSISLKLDSEE-----
EEEEECCCCC-----		54.8022617229
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
287TPhosphorylationKinaseCDK1P06493
Uniprot
382SPhosphorylationKinaseCDK1P06493
Uniprot
794TPhosphorylationKinaseMAPK1P28482
GPS
1223TPhosphorylationKinaseMAPK1P28482
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PITM1_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 PITM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PITM1_HUMAN !!
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 PITM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-896, AND MASSSPECTROMETRY.
"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-593 AND SER-600, ANDMASS SPECTROMETRY.
"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-621, AND MASSSPECTROMETRY.
"Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1provides a docking mechanism for Plk1 and affects cytokinesiscompletion.";
Litvak V., Argov R., Dahan N., Ramachandran S., Amarilio R.,Shainskaya A., Lev S.;
Mol. Cell 14:319-330(2004).
Cited for: PHOSPHORYLATION AT THR-287; SER-382 AND SER-896, MASS SPECTROMETRY,MUTAGENESIS OF THR-287; SER-300; SER-326; SER-382; THR-389; THR-794;SER-896 AND THR-1223, INTERACTION WITH CDK1 AND PLK1, AND SUBCELLULARLOCATION.

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