PITC1_HUMAN - dbPTM
PITC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PITC1_HUMAN
UniProt AC Q9UKF7
Protein Name Cytoplasmic phosphatidylinositol transfer protein 1
Gene Name PITPNC1
Organism Homo sapiens (Human).
Sequence Length 332
Subcellular Localization Cytoplasm .
Protein Description Phosphatidylinositol transfer proteins mediate the monomeric transport of lipids by shielding a lipid from the aqueous environment and binding the lipid in a hydrophobic cavity. Able to transfer phosphatidylinositol in vitro..
Protein Sequence MLLKEYRICMPLTVDEYKIGQLYMISKHSHEQSDRGEGVEVVQNEPFEDPHHGNGQFTEKRVYLNSKLPSWARAVVPKIFYVTEKAWNYYPYTITEYTCSFLPKFSIHIETKYEDNKGSNDTIFDNEAKDVEREVCFIDIACDEIPERYYKESEDPKHFKSEKTGRGQLREGWRDSHQPIMCSYKLVTVKFEVWGLQTRVEQFVHKVVRDILLIGHRQAFAWVDEWYDMTMDEVREFERATQEATNKKIGIFPPAISISSIPLLPSSVRSAPSSAPSTPLSTDAPEFLSVPKDRPRKKSAPETLTLPDPEKKATLNLPGMHSSDKPCRPKSE
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
4Sumoylation----MLLKEYRICMP
----CCCCEEEEEEE
49.06-
4Sumoylation----MLLKEYRICMP
----CCCCEEEEEEE
49.06-
119PhosphorylationKYEDNKGSNDTIFDN
ECCCCCCCCCCCCCC
32.8925307156
122PhosphorylationDNKGSNDTIFDNEAK
CCCCCCCCCCCCCHH
28.0025307156
129UbiquitinationTIFDNEAKDVEREVC
CCCCCCHHHHCEEEE
57.01-
254 (in isoform 2)Phosphorylation-31.3228270605
255 (in isoform 2)Phosphorylation-14.3828450419
266 (in isoform 2)Phosphorylation-41.2428450419
267 (in isoform 2)Phosphorylation-21.4328450419
268 (in isoform 2)Phosphorylation-7.0428450419
270PhosphorylationLLPSSVRSAPSSAPS
CCCCCCCCCCCCCCC
42.2329255136
273PhosphorylationSSVRSAPSSAPSTPL
CCCCCCCCCCCCCCC
38.5629255136
274PhosphorylationSVRSAPSSAPSTPLS
CCCCCCCCCCCCCCC
43.0429255136
277PhosphorylationSAPSSAPSTPLSTDA
CCCCCCCCCCCCCCC
42.2329255136
278PhosphorylationAPSSAPSTPLSTDAP
CCCCCCCCCCCCCCC
27.4729255136
281PhosphorylationSAPSTPLSTDAPEFL
CCCCCCCCCCCCCHH
25.9929255136
282PhosphorylationAPSTPLSTDAPEFLS
CCCCCCCCCCCCHHC
43.8129255136
289PhosphorylationTDAPEFLSVPKDRPR
CCCCCHHCCCCCCCC
41.5129255136
299PhosphorylationKDRPRKKSAPETLTL
CCCCCCCCCCCCCCC
52.6819664994
303PhosphorylationRKKSAPETLTLPDPE
CCCCCCCCCCCCCHH
24.8030266825
305PhosphorylationKSAPETLTLPDPEKK
CCCCCCCCCCCHHHC
43.6030266825

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
274SPhosphorylationKinasePKCAP17252
PSP
299SPhosphorylationKinasePKCAP17252
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PITC1_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 PITC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATRAP_HUMANAGTRAPphysical
16189514
ATRAP_MOUSEAgtrapphysical
21728994
ATRAP_HUMANAGTRAPphysical
19060904
ATRAP_HUMANAGTRAPphysical
25416956
CKLF5_HUMANCMTM5physical
25416956

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 PITC1_HUMAN

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Related Literatures of Post-Translational Modification

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