PITM1_MOUSE - dbPTM
PITM1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PITM1_MOUSE
UniProt AC O35954
Protein Name Membrane-associated phosphatidylinositol transfer protein 1
Gene Name Pitpnm1
Organism Mus musculus (Mouse).
Sequence Length 1243
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 i
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 (By similarity)..
Protein Sequence MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGNGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRIVDTIDIVRDAVAPGEYKAEEDPRLYRSAKTGRGPLADDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWIELSMADIRALEEETARMLAQRMAKCNTGSEGPEAQTPGKSSTEARPGTSTAGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQHGGGVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDSDEVFPKEMTKWNSNDFIDAFASPTEVEGVPDPTVMATKGIEDGARAPRDSEGLDGAGDLVVEACSVHALFLILHSGSILDSGPGDTNSKQADVQTLSTAFEAVTRVHFPEALGHVALRLVPCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTNQAYAAFLRSSEGTGFCGQVVLIGDGVGGILGFDALCHSASAGPGSRGSSRRGSMNNEMLSPEVGPVRDPLADGVEVLGRASPEPSALPAQRTFSDMANPDPDGSQNSLQVASTATSSGEPRRASTASCPPASSEAPDGPTNAARLDFKVSGFFLFGSPLGLVLALRKTVMPALEVAQLRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLAVPRYQKFPLGDGSSLLLADTLQTHSSLFLEELEMMVPSTPTSASGAFWKGSELGNEPASQTAAPSTTSEVVKILDRWWGNKRIDYSLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLTECEEPSIYSPAFPREKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLNGRFMYGPLDVVTLTGEKVDVYVMTQPLSGKWIHFGTEVTNSSGRLTFPVPSERALGIGVYPVRMVVRGDHTYAECCLTVVSRGTEAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPSQTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHAPSGPPRAALAKSSYAVAAPVDFLRKQSQLLRSRGPSQVDREGPGTPPTTLARGKTRSISLKLDSEE
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
59PhosphorylationPGGNGQYTHKVYHVG
CCCCCCEEEEEEECC		13.82-
164PhosphorylationEDPRLYRSAKTGRGP
CCHHHHHHCCCCCCC		22.1430482847
270PhosphorylationSEGPEAQTPGKSSTE
CCCCCCCCCCCCCCC		40.8525521595
274PhosphorylationEAQTPGKSSTEARPG
CCCCCCCCCCCCCCC		48.7025619855
275PhosphorylationAQTPGKSSTEARPGT
CCCCCCCCCCCCCCC		33.4825619855
276PhosphorylationQTPGKSSTEARPGTS
CCCCCCCCCCCCCCC		40.5325619855
282PhosphorylationSTEARPGTSTAGTPD
CCCCCCCCCCCCCCC		26.1125619855
283PhosphorylationTEARPGTSTAGTPDG
CCCCCCCCCCCCCCC		23.3625521595
284PhosphorylationEARPGTSTAGTPDGP
CCCCCCCCCCCCCCC		29.0125619855
287PhosphorylationPGTSTAGTPDGPEAP
CCCCCCCCCCCCCCC		18.7525521595
300PhosphorylationAPPGPDASPDASFGK
CCCCCCCCCCCCCCC		30.6025521595
304PhosphorylationPDASPDASFGKQWSS
CCCCCCCCCCCCCCC		41.7425521595
315PhosphorylationQWSSSSRSSYSSQHG
CCCCCCCCCCCCCCC		35.2619060867
316PhosphorylationWSSSSRSSYSSQHGG
CCCCCCCCCCCCCCC		28.1119060867
317PhosphorylationSSSSRSSYSSQHGGG
CCCCCCCCCCCCCCC		17.3721183079
318PhosphorylationSSSRSSYSSQHGGGV
CCCCCCCCCCCCCCC		26.0120531401
319PhosphorylationSSRSSYSSQHGGGVS
CCCCCCCCCCCCCCC		20.2622817900
326PhosphorylationSQHGGGVSPQSLSEW
CCCCCCCCHHHHHHH		22.0922817900
329PhosphorylationGGGVSPQSLSEWRMQ
CCCCCHHHHHHHHHH		36.9322817900
342PhosphorylationMQNIARDSENSSEEE
HHHHHCCCCCCCHHH		32.8825619855
345PhosphorylationIARDSENSSEEEFFD
HHCCCCCCCHHHHHH		34.7725619855
346PhosphorylationARDSENSSEEEFFDA
HCCCCCCCHHHHHHC		61.6925619855
358PhosphorylationFDAHEGFSDSDEVFP
HHCCCCCCCCCCCCC		47.2425619855
360PhosphorylationAHEGFSDSDEVFPKE
CCCCCCCCCCCCCHH		34.1825619855
369PhosphorylationEVFPKEMTKWNSNDF
CCCCHHHHCCCCCCC		33.7226239621
373PhosphorylationKEMTKWNSNDFIDAF
HHHHCCCCCCCCHHC		36.3424925903
382PhosphorylationDFIDAFASPTEVEGV
CCCHHCCCCCEECCC		26.3826239621
384PhosphorylationIDAFASPTEVEGVPD
CHHCCCCCEECCCCC		50.6026239621
505PhosphorylationPYSHDGDSLSRSQDH
CCCCCCCCCCCCCCC		33.5023737553
509PhosphorylationDGDSLSRSQDHIPLA
CCCCCCCCCCCCCHH		36.2622817900
593PhosphorylationRGSSRRGSMNNEMLS
CCCCCCCCCCCCCCC		19.2725521595
600PhosphorylationSMNNEMLSPEVGPVR
CCCCCCCCCCCCCCC		20.0825177544
621PhosphorylationVEVLGRASPEPSALP
CEEECCCCCCCCCCC		28.5625521595
625PhosphorylationGRASPEPSALPAQRT
CCCCCCCCCCCCCCC		40.5525619855
632PhosphorylationSALPAQRTFSDMANP
CCCCCCCCHHHHCCC		18.5325338131
634PhosphorylationLPAQRTFSDMANPDP
CCCCCCHHHHCCCCC		26.3425338131
664PhosphorylationSGEPRRASTASCPPA
CCCCCCCEECCCCCC		23.7727087446
665PhosphorylationGEPRRASTASCPPAS
CCCCCCEECCCCCCC		22.9325619855
667PhosphorylationPRRASTASCPPASSE
CCCCEECCCCCCCCC		27.5225619855
672PhosphorylationTASCPPASSEAPDGP
ECCCCCCCCCCCCCC		34.1925619855
673PhosphorylationASCPPASSEAPDGPT
CCCCCCCCCCCCCCC		39.6225619855
830MethylationEVVKILDRWWGNKRI
HHHHHHHHHHCCCCE		27.8318959817
886PhosphorylationEKERPQLTECEEPSI
HHHCCCCCCCCCCCC		33.0825777480
892PhosphorylationLTECEEPSIYSPAFP
CCCCCCCCCCCCCCC		37.1228066266
894PhosphorylationECEEPSIYSPAFPRE
CCCCCCCCCCCCCHH		16.9720415495
895PhosphorylationCEEPSIYSPAFPREK
CCCCCCCCCCCCHHH		14.2125521595
1025PhosphorylationGTEAVVFSIDGSFTA
CCEEEEEEECCCEEE		14.2526239621
1029PhosphorylationVVFSIDGSFTASVSI
EEEEECCCEEEEEEE		18.7126239621
1033PhosphorylationIDGSFTASVSIMGSD
ECCCEEEEEEECCCC		17.2226239621
1189PhosphorylationPRAALAKSSYAVAAP
CCHHHHHHHHHHHHC		23.99-
1191PhosphorylationAALAKSSYAVAAPVD
HHHHHHHHHHHHCHH		16.5229514104
1204PhosphorylationVDFLRKQSQLLRSRG
HHHHHHHHHHHHHCC		26.3229899451
1210MethylationQSQLLRSRGPSQVDR
HHHHHHHCCCCCCCC		55.3924129315
1213PhosphorylationLLRSRGPSQVDREGP
HHHHCCCCCCCCCCC		45.7329899451
1217MethylationRGPSQVDREGPGTPP
CCCCCCCCCCCCCCC		52.4924129315
1222PhosphorylationVDREGPGTPPTTLAR
CCCCCCCCCCCCCCC		29.2722807455
1225PhosphorylationEGPGTPPTTLARGKT
CCCCCCCCCCCCCCE		35.3329899451
1232PhosphorylationTTLARGKTRSISLKL
CCCCCCCEEEEEEEE		32.2623984901
1234PhosphorylationLARGKTRSISLKLDS
CCCCCEEEEEEEECC		23.0425266776
1236PhosphorylationRGKTRSISLKLDSEE
CCCEEEEEEEECCCC		22.2426824392
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
382SPhosphorylationKinaseCDK1P11440
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PITM1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PITM1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PITM1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND MASSSPECTROMETRY.

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