dbPTM

SSRG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SSRG_HUMAN
UniProt AC	Q9UNL2
Protein Name	Translocon-associated protein subunit gamma
Gene Name	SSR3
Organism	Homo sapiens (Human).
Sequence Length	185
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein.
Protein Description	TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins..
Protein Sequence	MAPKGSSKQQSEEDLLLQDFSRNLSAKSSALFFGNAFIVSAIPIWLYWRIWHMDLIQSAVLYSVMTLVSTYLVAFAYKNVKFVLKHKVAQKREDAVSKEVTRKLSEADNRKMSRKEKDERILWKKNEVADYEATTFSIFYNNTLFLVVVIVASFFILKNFNPTVNYILSISASSGLIALLSTGSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MAPKGSSK -------CCCCCCCC	15.08	25732826
6	Phosphorylation	--MAPKGSSKQQSEE --CCCCCCCCHHCHH	40.25	23401153
7	Phosphorylation	-MAPKGSSKQQSEED -CCCCCCCCHHCHHH	43.05	28464451
8	Ubiquitination	MAPKGSSKQQSEEDL CCCCCCCCHHCHHHH	54.79	21906983
8	Ubiquitination	MAPKGSSKQQSEEDL CCCCCCCCHHCHHHH	54.79	-
11	Phosphorylation	KGSSKQQSEEDLLLQ CCCCCHHCHHHHHHH	40.22	25159151
21	Phosphorylation	DLLLQDFSRNLSAKS HHHHHHHHHHHCCHH	28.66	23403867
28	Phosphorylation	SRNLSAKSSALFFGN HHHHCCHHHHHHHCC	22.14	24247654
47	Phosphorylation	SAIPIWLYWRIWHMD HHHHHHHHHHHHCHH	4.25	24247654
81	Ubiquitination	AFAYKNVKFVLKHKV HHHHHCHHHHHHHHH	38.87	-
81	Ubiquitination	AFAYKNVKFVLKHKV HHHHHCHHHHHHHHH	38.87	21906983
85	Ubiquitination	KNVKFVLKHKVAQKR HCHHHHHHHHHHHHH	35.76	21906983
85	Ubiquitination	KNVKFVLKHKVAQKR HCHHHHHHHHHHHHH	35.76	-
87	Ubiquitination	VKFVLKHKVAQKRED HHHHHHHHHHHHHHH	37.36	-
98	Acetylation	KREDAVSKEVTRKLS HHHHHHCHHHHHHHH	49.99	26051181
98	Malonylation	KREDAVSKEVTRKLS HHHHHHCHHHHHHHH	49.99	26320211
98	Ubiquitination	KREDAVSKEVTRKLS HHHHHHCHHHHHHHH	49.99	-
98	Ubiquitination	KREDAVSKEVTRKLS HHHHHHCHHHHHHHH	49.99	-
101	Phosphorylation	DAVSKEVTRKLSEAD HHHCHHHHHHHHHHH	24.15	26074081
103	Ubiquitination	VSKEVTRKLSEADNR HCHHHHHHHHHHHHH	47.18	21906983
103	Ubiquitination	VSKEVTRKLSEADNR HCHHHHHHHHHHHHH	47.18	-
103	2-Hydroxyisobutyrylation	VSKEVTRKLSEADNR HCHHHHHHHHHHHHH	47.18	-
103	Acetylation	VSKEVTRKLSEADNR HCHHHHHHHHHHHHH	47.18	20167786
105	Phosphorylation	KEVTRKLSEADNRKM HHHHHHHHHHHHHHC	33.50	30266825
113	Phosphorylation	EADNRKMSRKEKDER HHHHHHCCHHHHHHH	43.14	23882029
115	Acetylation	DNRKMSRKEKDERIL HHHHCCHHHHHHHHH	62.91	20167786
123 (in isoform 2)	Phosphorylation	-	13.75	25159151
124	Ubiquitination	KDERILWKKNEVADY HHHHHHHHHCCCCCC	42.13	-
173	Phosphorylation	YILSISASSGLIALL HHHEEECCCCHHHHH	20.39	-
181	Phosphorylation	SGLIALLSTGSK--- CCHHHHHHCCCC---	31.41	-
182	Phosphorylation	GLIALLSTGSK---- CHHHHHHCCCC----	45.50	-
184	Phosphorylation	IALLSTGSK------ HHHHHCCCC------	34.97	-

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 SSRG_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CLH1_HUMAN	CLTC	physical	26344197
DX39A_HUMAN	DDX39A	physical	26344197
DX39B_HUMAN	DDX39B	physical	26344197
DHB12_HUMAN	HSD17B12	physical	26344197
MAGT1_HUMAN	MAGT1	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RTN4_HUMAN	RTN4	physical	26344197
S61A1_HUMAN	SEC61A1	physical	26344197
SSRA_HUMAN	SSR1	physical	26344197
TMCO1_HUMAN	TMCO1	physical	26344197

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 SSRG_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-11, 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-11, AND MASSSPECTROMETRY.	18691976 [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-105, AND MASSSPECTROMETRY.	17081983 [Abstract]