dbPTM

SSRA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SSRA_HUMAN
UniProt AC	P43307
Protein Name	Translocon-associated protein subunit alpha
Gene Name	SSR1
Organism	Homo sapiens (Human).
Sequence Length	286
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type I 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. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins..
Protein Sequence	MRLLPRLLLLLLLVFPATVLFRGGPRGLLAVAQDLTEDEETVEDSIIEDEDDEAEVEEDEPTDLVEDKEEEDVSGEPEASPSADTTILFVKGEDFPANNIVKFLVGFTNKGTEDFIVESLDASFRYPQDYQFYIQNFTALPLNTVVPPQRQATFEYSFIPAEPMGGRPFGLVINLNYKDLNGNVFQDAVFNQTVTVIEREDGLDGETIFMYMFLAGLGLLVIVGLHQLLESRKRKRPIQKVEMGTSSQNDVDMSWIPQETLNQINKASPRRLPRKRAQKRSVGSDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
80	Phosphorylation	VSGEPEASPSADTTI CCCCCCCCCCCCCEE	20.09	-
91	Ubiquitination	DTTILFVKGEDFPAN CCEEEEEECCCCCCC	49.61	-
102	Ubiquitination	FPANNIVKFLVGFTN CCCCCCEEHHHCCCC	29.23	21906983
102 (in isoform 1)	Ubiquitination	-	29.23	21906983
110	Ubiquitination	FLVGFTNKGTEDFIV HHHCCCCCCCCCEEE	65.24	-
136	N-linked_Glycosylation	DYQFYIQNFTALPLN CCEEEEEEEEEEECC	27.03	8050590
136	N-linked_Glycosylation	DYQFYIQNFTALPLN CCEEEEEEEEEEECC	27.03	12754519
156	Phosphorylation	QRQATFEYSFIPAEP CCEEEEEEEEEECCC	12.51	-
191	N-linked_Glycosylation	VFQDAVFNQTVTVIE CCCHHHHCCEEEEEE	29.98	8050590
191	N-linked_Glycosylation	VFQDAVFNQTVTVIE CCCHHHHCCEEEEEE	29.98	8050590
239 (in isoform 2)	Ubiquitination	-	46.56	21906983
243	Sulfoxidation	RPIQKVEMGTSSQND CCCCEEECCCCCCCC	8.75	28183972
245	Phosphorylation	IQKVEMGTSSQNDVD CCEEECCCCCCCCCC	24.72	23927012
246	Phosphorylation	QKVEMGTSSQNDVDM CEEECCCCCCCCCCH	24.97	25159151
247	Phosphorylation	KVEMGTSSQNDVDMS EEECCCCCCCCCCHH	32.61	30266825
253	Sulfoxidation	SSQNDVDMSWIPQET CCCCCCCHHHCCHHH	3.43	28183972
254	Phosphorylation	SQNDVDMSWIPQETL CCCCCCHHHCCHHHH	19.86	30266825
260	Phosphorylation	MSWIPQETLNQINKA HHHCCHHHHHHHHHC	26.26	23927012
266	Ubiquitination	ETLNQINKASPRRLP HHHHHHHHCCCCCCC	52.44	2190698
266 (in isoform 1)	Ubiquitination	-	52.44	21906983
268	Phosphorylation	LNQINKASPRRLPRK HHHHHHCCCCCCCCH	22.13	22167270
281	Phosphorylation	RKRAQKRSVGSDE-- CHHHHHCCCCCCC--	37.55	28176443
284	Phosphorylation	AQKRSVGSDE----- HHHCCCCCCC-----	36.09	26074081

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
268	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DKC1_HUMAN	DKC1	physical	16169070
UT14A_HUMAN	UTP14A	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
PTN_HUMAN	PTN	physical	16169070
TCPB_HUMAN	CCT2	physical	22939629
TCPA_HUMAN	TCP1	physical	22939629
TCPE_HUMAN	CCT5	physical	22939629
VATC1_HUMAN	ATP6V1C1	physical	22939629
TCPD_HUMAN	CCT4	physical	22939629
A1AT_HUMAN	SERPINA1	physical	17380188
EDEM1_HUMAN	EDEM1	physical	17380188
GRP78_HUMAN	HSPA5	physical	17380188
ATPG_HUMAN	ATP5C1	physical	26344197
CY1_HUMAN	CYC1	physical	26344197
OST48_HUMAN	DDOST	physical	26344197
PHB_HUMAN	PHB	physical	26344197
SSRD_HUMAN	SSR4	physical	26344197
QCR2_HUMAN	UQCRC2	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 SSRA_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-136 AND ASN-191, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-136.	12754519 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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 THR-260 AND SER-268, ANDMASS SPECTROMETRY.	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-247 AND SER-268, ANDMASS SPECTROMETRY.	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-268, 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-268, AND MASSSPECTROMETRY.	17081983 [Abstract]