CPTP_HUMAN - dbPTM
CPTP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPTP_HUMAN
UniProt AC Q5TA50
Protein Name Ceramide-1-phosphate transfer protein {ECO:0000303|PubMed:23863933, ECO:0000305}
Gene Name CPTP {ECO:0000312|HGNC:HGNC:28116}
Organism Homo sapiens (Human).
Sequence Length 214
Subcellular Localization Cytoplasm, cytosol . Golgi apparatus, trans-Golgi network membrane
Peripheral membrane protein . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Endosome membrane
Peripheral membrane protein . Nucleus outer membrane
Peripheral membr
Protein Description Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1-phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles. [PubMed: 28011644 Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis]
Protein Sequence MDDSETGFNLKVVLVSFKQCLDEKEEVLLDPYIASWKGLVRFLNSLGTIFSFISKDVVSKLRIMERLRGGPQSEHYRSLQAMVAHELSNRLVDLERRSHHPESGCRTVLRLHRALHWLQLFLEGLRTSPEDARTSALCADSYNASLAAYHPWVVRRAVTVAFCTLPTREVFLEAMNVGPPEQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
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
4Phosphorylation----MDDSETGFNLK
----CCCCCCCCCCE
20068231
6Phosphorylation--MDDSETGFNLKVV
--CCCCCCCCCCEEE
20068231
24UbiquitinationFKQCLDEKEEVLLDP
HHHHCCCCHHHHCCH
-
35PhosphorylationLLDPYIASWKGLVRF
HCCHHHHCHHHHHHH
24719451
78PhosphorylationPQSEHYRSLQAMVAH
CCCHHHHHHHHHHHH
22210691
88PhosphorylationAMVAHELSNRLVDLE
HHHHHHHHHHHHCHH
22210691
205PhosphorylationYNVSQKLYAEHSLLD
HCHHHHHHHHHHCCC
25693802
209PhosphorylationQKLYAEHSLLDLP--
HHHHHHHHCCCCC--
30622161

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 CPTP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPTP_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 CPTP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN451_HUMANZNF451physical
21988832
SMAD3_HUMANSMAD3physical
21988832
ELOC_HUMANTCEB1physical
21988832
INP5K_HUMANINPP5Kphysical
21988832
PHF13_HUMANPHF13physical
21988832

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 CPTP_HUMAN

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Related Literatures of Post-Translational Modification

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