PISD_HUMAN - dbPTM
PISD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PISD_HUMAN
UniProt AC Q9UG56
Protein Name Phosphatidylserine decarboxylase proenzyme, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03208}
Gene Name PISD {ECO:0000255|HAMAP-Rule:MF_03208}
Organism Homo sapiens (Human).
Sequence Length 409
Subcellular Localization Phosphatidylserine decarboxylase beta chain: Mitochondrion inner membrane
Single-pass membrane protein
Intermembrane side .
Phosphatidylserine decarboxylase alpha chain: Mitochondrion inner membrane
Peripheral membrane protein
Intermembrane side
Protein Description Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine..
Protein Sequence MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL
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
5 (in isoform 2)Phosphorylation-6.9529083192
37 (in isoform 2)Phosphorylation-39.1522210691
112UbiquitinationHWEVALYKSVPTRLL
CEEEEEEECCCHHHH
45.91-
166PhosphorylationLHHYRNLSEFFRRKL
HHHHCCHHHHHHHHC
35.5928857561
201UbiquitinationILNFGQVKNCEVEQV
EEECCEEECCEEEEE
48.25-
209UbiquitinationNCEVEQVKGVTYSLE
CCEEEEEECEEEEHH
47.56-
217PhosphorylationGVTYSLESFLGPRMC
CEEEEHHHHHCCCCC
30.9428857561
240UbiquitinationAASCDSFKNQLVTRE
CCCCHHHHCEEEECC
47.97-
262 (in isoform 2)Ubiquitination-29.0121890473
262UbiquitinationVIYLAPGDYHCFHSP
EEEECCCCCCEECCC
29.0121890473
295 (in isoform 3)Ubiquitination-1.7521890473
296UbiquitinationPGMARWIKELFCHNE
HHHHHHHHHHHCCCC
41.2121890473
312 (in isoform 2)Ubiquitination-38.2921890473
312UbiquitinationVVLTGDWKHGFFSLT
EEEECCCCCCEEEEE
38.2921890473
314PhosphorylationLTGDWKHGFFSLTAV
EECCCCCCEEEEEEE
22.9027251275
339PhosphorylationYFDRDLHTNSPRHSK
EECCCCCCCCCCCCC
44.6929214152
341PhosphorylationDRDLHTNSPRHSKGS
CCCCCCCCCCCCCCC
25.1929214152
345 (in isoform 3)Ubiquitination-39.7421890473
345PhosphorylationHTNSPRHSKGSYNDF
CCCCCCCCCCCCCCC
39.7429214152
346UbiquitinationTNSPRHSKGSYNDFS
CCCCCCCCCCCCCCE
45.832189047
348PhosphorylationSPRHSKGSYNDFSFV
CCCCCCCCCCCCEEE
25.2130108239
349PhosphorylationPRHSKGSYNDFSFVT
CCCCCCCCCCCEEEE
27.6730108239
353PhosphorylationKGSYNDFSFVTHTNR
CCCCCCCEEEEEECC
22.9828857561
378PyruvateLGEFNLGSTIVLIFE
CCCCCCCCEEEEEEE
20.37-
378Pyruvic acid (Ser)LGEFNLGSTIVLIFE
CCCCCCCCEEEEEEE
20.37-
395UbiquitinationKDFNFQLKTGQKIRF
CCCCCEECCCCEEEE
39.56-

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 PISD_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PISD_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 PISD_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHX29_HUMANDHX29physical
16169070
DGLB_HUMANDAGLBphysical
16169070
IF140_HUMANIFT140physical
27173435
WDR19_HUMANWDR19physical
27173435

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
DB00144Phosphatidylserine
Regulatory Network of PISD_HUMAN

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Related Literatures of Post-Translational Modification

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