PTSS1_HUMAN - dbPTM
PTSS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTSS1_HUMAN
UniProt AC P48651
Protein Name Phosphatidylserine synthase 1
Gene Name PTDSS1
Organism Homo sapiens (Human).
Sequence Length 473
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. Highly enriched in the mitochondria-associated membrane (MAM)..
Protein Description Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. In membranes, PTDSS1 catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine..
Protein Sequence MASCVGSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTRDDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLFLNFEQVKSLMYWLDPNLRYATREADVMEYAVNCHVITWERIISHFDIFAFGHFWGWAMKALLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFLEMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLTELNTFFLKHIFVFQASHPLSWGRILFIGGITAPTVRQYYAYLTDTQCKRVGTQCWVFGVIGFLEAIVCIKFGQDLFSKTQILYVVLWLLCVAFTTFLCLYGMIWYAEHYGHREKTYSECEDGTYSPEISWHHRKGTKGSEDSPPKHAGNNESHSSRRRNRHSKSKVTNGVGKK
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
2Acetylation------MASCVGSRT
------CCCCCCCCC		16.1925944712
3Phosphorylation-----MASCVGSRTL
-----CCCCCCCCCC		14.19-
7Phosphorylation-MASCVGSRTLSKDD
-CCCCCCCCCCCHHH		11.1625159151
9PhosphorylationASCVGSRTLSKDDVN
CCCCCCCCCCHHHCC		36.7619691289
11PhosphorylationCVGSRTLSKDDVNYK
CCCCCCCCHHHCCHH		33.1623401153
12UbiquitinationVGSRTLSKDDVNYKM
CCCCCCCHHHCCHHE		62.1521906983
122-HydroxyisobutyrylationVGSRTLSKDDVNYKM
CCCCCCCHHHCCHHE		62.15-
12AcetylationVGSRTLSKDDVNYKM
CCCCCCCHHHCCHHE		62.1526051181
17PhosphorylationLSKDDVNYKMHFRMI
CCHHHCCHHEEEEEC		14.9922817900
18UbiquitinationSKDDVNYKMHFRMIN
CHHHCCHHEEEEECC		22.2427667366
18AcetylationSKDDVNYKMHFRMIN
CHHHCCHHEEEEECC		22.2427452117
48UbiquitinationHTITLLSFTIVSLMY
CHHHHHHHHHHHHHH		5.6521890473
56UbiquitinationTIVSLMYFAFTRDDS
HHHHHHHHHHCCCCC		2.54-
58UbiquitinationVSLMYFAFTRDDSVP
HHHHHHHHCCCCCCC		4.06-
78UbiquitinationRGILSVIFFFLIISV
HHHHHHHHHHHHHHH		3.1221890473
105UbiquitinationPALWRMVFGLSVLYF
HHHHHHHHHHHHHHH		6.2721890473
105UbiquitinationPALWRMVFGLSVLYF
HHHHHHHHHHHHHHH		6.2721890473
113UbiquitinationGLSVLYFLFLVFLLF
HHHHHHHHHHHHHHH		1.7321963094
115UbiquitinationSVLYFLFLVFLLFLN
HHHHHHHHHHHHHCC		2.6421963094
130SulfoxidationFEQVKSLMYWLDPNL
HHHHHHHHHHHCCCC		2.6628183972
135UbiquitinationSLMYWLDPNLRYATR
HHHHHHCCCCCHHCC		39.3221890473
135UbiquitinationSLMYWLDPNLRYATR
HHHHHHCCCCCHHCC		39.3221890473
145UbiquitinationRYATREADVMEYAVN
CHHCCHHHHHHHHHH		35.2321890473
157PhosphorylationAVNCHVITWERIISH
HHHCEEEEHHHHHHH		21.8620068231
202UbiquitinationTWELTELFFMHLLPN
HHHHHHHHHHHHCCC		4.0921890473
202UbiquitinationTWELTELFFMHLLPN
HHHHHHHHHHHHCCC		4.0921890473
239 (in isoform 3)Phosphorylation-5.9925056879
249PhosphorylationMRTYHWASFKDIHTT
HHHCEEHHCCCHHCC		27.8627080861
251UbiquitinationTYHWASFKDIHTTTG
HCEEHHCCCHHCCCC		53.9621906983
255PhosphorylationASFKDIHTTTGKIKR
HHCCCHHCCCCCCCC		26.79-
256PhosphorylationSFKDIHTTTGKIKRA
HCCCHHCCCCCCCCH		21.27-
257PhosphorylationFKDIHTTTGKIKRAV
CCCHHCCCCCCCCHH		37.32-
2592-HydroxyisobutyrylationDIHTTTGKIKRAVLQ
CHHCCCCCCCCHHHH		42.85-
259UbiquitinationDIHTTTGKIKRAVLQ
CHHCCCCCCCCHHHH		42.8521906983
261UbiquitinationHTTTGKIKRAVLQFT
HCCCCCCCCHHHHHC		37.4821906983
271PhosphorylationVLQFTPASWTYVRWF
HHHHCCCCEEEEEEC		22.5832142685
274PhosphorylationFTPASWTYVRWFDPK
HCCCCEEEEEECCCC		5.0320068231
281UbiquitinationYVRWFDPKSSFQRVA
EEEECCCCCHHHHHH		61.6521906983
296PhosphorylationGVYLFMIIWQLTELN
HHHHHHHHHHHHHHH		0.9832645325
327UbiquitinationSWGRILFIGGITAPT
CCCCEEEECCCCCCH		4.4124816145
348UbiquitinationYLTDTQCKRVGTQCW
HHCHHCCCCCCCCHH		40.0621906983
377PhosphorylationKFGQDLFSKTQILYV
HHCCCCCCHHHHHHH		41.9326074081
379PhosphorylationGQDLFSKTQILYVVL
CCCCCCHHHHHHHHH		21.4626074081
383PhosphorylationFSKTQILYVVLWLLC
CCHHHHHHHHHHHHH		7.0826074081
415PhosphorylationHYGHREKTYSECEDG
HHCCCCCCCHHCCCC		27.7722167270
416PhosphorylationYGHREKTYSECEDGT
HCCCCCCCHHCCCCC		17.3422167270
417PhosphorylationGHREKTYSECEDGTY
CCCCCCCHHCCCCCC		40.7922167270
423PhosphorylationYSECEDGTYSPEISW
CHHCCCCCCCCCEEE		32.9022167270
424PhosphorylationSECEDGTYSPEISWH
HHCCCCCCCCCEEEE		27.9722167270
425PhosphorylationECEDGTYSPEISWHH
HCCCCCCCCCEEEEC		18.8523401153
429PhosphorylationGTYSPEISWHHRKGT
CCCCCCEEEECCCCC		20.7823401153
436PhosphorylationSWHHRKGTKGSEDSP
EEECCCCCCCCCCCC		34.9630576142
439PhosphorylationHRKGTKGSEDSPPKH
CCCCCCCCCCCCCCC		39.5230278072
442PhosphorylationGTKGSEDSPPKHAGN
CCCCCCCCCCCCCCC		38.7629255136
452PhosphorylationKHAGNNESHSSRRRN
CCCCCCCCCHHHHHC		30.6928176443
454PhosphorylationAGNNESHSSRRRNRH
CCCCCCCHHHHHCHH		34.5228176443
455PhosphorylationGNNESHSSRRRNRHS
CCCCCCHHHHHCHHC		25.1226055452
462PhosphorylationSRRRNRHSKSKVTNG
HHHHCHHCCCCCCCC		35.07-
473UbiquitinationVTNGVGKK-------
CCCCCCCC-------		60.6924816145
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 PTSS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTSS1_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 PTSS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STOM_HUMANSTOMphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
151050Lenz-Majewski hyperostotic dwarfism (LMHD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00144Phosphatidylserine
Regulatory Network of PTSS1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-425, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND MASSSPECTROMETRY.
"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 TYR-424 AND SER-425, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND MASSSPECTROMETRY.

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