dbPTM

PTSS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTSS2_HUMAN
UniProt AC	Q9BVG9
Protein Name	Phosphatidylserine synthase 2
Gene Name	PTDSS2
Organism	Homo sapiens (Human).
Sequence Length	487
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. PTDSS2 is specific for phosphatatidylethanolamine and does not act on phosphatidylcholine..
Protein Sequence	MRRGERRDAGGPRPESPVPAGRASLEEPPDGPSAGQATGPGEGRRSTESEVYDDGTNTFFWRAHTLTVLFILTCTLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPKLGVPLPERDYGGNCLIYDPDNETDPFHNIWDKLDGFVPAHFLGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLVCNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSWVRFEWKPASSLRRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGVAMREIYDFMDDPKPHKKLGPQAWLVAAITATELLIVVKYDPHTLTLSLPFYISQCWTLGSVLALTWTVWRFFLRDITLRYKETRWQKWQNKDDQGSTVGNGDQHPLGLDEDLLGPGVAEGEGAPTPN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Phosphorylation	AGGPRPESPVPAGRA CCCCCCCCCCCCCCC	33.60	29255136
24	Phosphorylation	PVPAGRASLEEPPDG CCCCCCCCCCCCCCC	34.65	28355574
33	Phosphorylation	EEPPDGPSAGQATGP CCCCCCCCCCCCCCC	51.03	23927012
46	Phosphorylation	GPGEGRRSTESEVYD CCCCCCCCCCEEEEE	34.86	-
47	Phosphorylation	PGEGRRSTESEVYDD CCCCCCCCCEEEEEC	41.54	-
156	Phosphorylation	DGRQFLKYVDPKLGV HHHHHHHHCCCCCCC	16.54	-
160	2-Hydroxyisobutyrylation	FLKYVDPKLGVPLPE HHHHCCCCCCCCCCC	54.10	-
160	Ubiquitination	FLKYVDPKLGVPLPE HHHHCCCCCCCCCCC	54.10	21890473
181	N-linked_Glycosylation	CLIYDPDNETDPFHN EEEECCCCCCCCCCC	60.50	19159218
205	Phosphorylation	PAHFLGWYLKTLMIR HHHHHHHHHHHHHHH	9.12	-
271	Ubiquitination	TLEWLSLKTYKWQGL HHHHHHCCEEEECCC	46.57	21890473
274	Ubiquitination	WLSLKTYKWQGLWNI HHHCCEEEECCCCCC	37.97	21890473
285	Ubiquitination	LWNIPTYKGKMKRIA CCCCCCCCCCEEEEE	55.31	21890473
309	Phosphorylation	RFEWKPASSLRRWLA EEEEECHHHHHHHHH	38.13	23898821
310	Phosphorylation	FEWKPASSLRRWLAV EEEECHHHHHHHHHH	28.18	23898821
366	Phosphorylation	GVAMREIYDFMDDPK CHHHHHHHHHCCCCC	9.81	-
447	Ubiquitination	YKETRWQKWQNKDDQ CHHHHHHHCCCCCCC	43.73	21890473
485	Phosphorylation	AEGEGAPTPN----- CCCCCCCCCC-----	34.62	17192257

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 PTSS2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PTSS2_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 PTSS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
STOM_HUMAN	STOM	physical	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
DB00144	Phosphatidylserine

Regulatory Network of PTSS2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181, AND MASSSPECTROMETRY.	19159218 [Abstract]
Phosphorylation
Reference	PubMed
"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-16, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-16, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-16 AND THR-485, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY.	18088087 [Abstract]
"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-16, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY.	17081983 [Abstract]