TRAM1_HUMAN - dbPTM
TRAM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRAM1_HUMAN
UniProt AC Q15629
Protein Name Translocating chain-associated membrane protein 1
Gene Name TRAM1
Organism Homo sapiens (Human).
Sequence Length 374
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Stimulatory or required for the translocation of secretory proteins across the ER membrane..
Protein Sequence MAIRKKSTKSPPVLSHEFVLQNHADIVSCVAMVFLLGLMFEITAKASIIFVTLQYNVTLPATEEQATESVSLYYYGIKDLATVFFYMLVAIIIHAVIQEYMLDKINRRMHFSKTKHSKFNESGQLSAFYLFACVWGTFILISENYISDPTILWRAYPHNLMTFQMKFFYISQLAYWLHAFPELYFQKTKKEDIPRQLVYIGLYLFHIAGAYLLNLNHLGLVLLVLHYFVEFLFHISRLFYFSNEKYQKGFSLWAVLFVLGRLLTLILSVLTVGFGLARAENQKLDFSTGNFNVLAVRIAVLASICVTQAFMMWKFINFQLRRWREHSAFQAPAVKKKPTVTKGRSSKKGTENGVNGTLTSNVADSPRNKKEKSS
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
7Phosphorylation-MAIRKKSTKSPPVL
-CCCCCCCCCCCCCC		44.0726670566
8PhosphorylationMAIRKKSTKSPPVLS
CCCCCCCCCCCCCCC		44.4122210691
10PhosphorylationIRKKSTKSPPVLSHE
CCCCCCCCCCCCCCH		34.2322210691
28PhosphorylationQNHADIVSCVAMVFL
HCHHHHHHHHHHHHH		11.8322210691
56N-linked_GlycosylationIFVTLQYNVTLPATE
EEEEEEEEEECCCCH		13.82UniProtKB CARBOHYD
112PhosphorylationINRRMHFSKTKHSKF
HHHHHCCCCCCCCCC		25.4130622161
1132-HydroxyisobutyrylationNRRMHFSKTKHSKFN
HHHHCCCCCCCCCCC		61.73-
113UbiquitinationNRRMHFSKTKHSKFN
HHHHCCCCCCCCCCC		61.73-
114PhosphorylationRRMHFSKTKHSKFNE
HHHCCCCCCCCCCCC		32.5630622161
162PhosphorylationAYPHNLMTFQMKFFY
CCCCCCCHHHHHHHH		17.55-
246PhosphorylationFYFSNEKYQKGFSLW
HHCCCHHHHHCCHHH		14.8520860994
251PhosphorylationEKYQKGFSLWAVLFV
HHHHHCCHHHHHHHH		31.5020860994
252UbiquitinationKYQKGFSLWAVLFVL
HHHHCCHHHHHHHHH		2.9621890473
264PhosphorylationFVLGRLLTLILSVLT
HHHHHHHHHHHHHHH		19.1529888752
268PhosphorylationRLLTLILSVLTVGFG
HHHHHHHHHHHHHHH		14.2129888752
283UbiquitinationLARAENQKLDFSTGN
HHHHHHCCCCCCCCC		62.7021890473
283UbiquitinationLARAENQKLDFSTGN
HHHHHHCCCCCCCCC		62.7021890473
2832-HydroxyisobutyrylationLARAENQKLDFSTGN
HHHHHHCCCCCCCCC		62.70-
327PhosphorylationLRRWREHSAFQAPAV
HHHHHHCCCCCCCCC		26.4823911959
335MalonylationAFQAPAVKKKPTVTK
CCCCCCCCCCCCCCC		58.1326320211
3352-HydroxyisobutyrylationAFQAPAVKKKPTVTK
CCCCCCCCCCCCCCC		58.13-
339PhosphorylationPAVKKKPTVTKGRSS
CCCCCCCCCCCCCCC		50.0826657352
341PhosphorylationVKKKPTVTKGRSSKK
CCCCCCCCCCCCCCC		30.20-
345PhosphorylationPTVTKGRSSKKGTEN
CCCCCCCCCCCCCCC		56.0029214152
346PhosphorylationTVTKGRSSKKGTENG
CCCCCCCCCCCCCCC		36.7124719451
348UbiquitinationTKGRSSKKGTENGVN
CCCCCCCCCCCCCCC		73.37-
350PhosphorylationGRSSKKGTENGVNGT
CCCCCCCCCCCCCCE		34.8523927012
357PhosphorylationTENGVNGTLTSNVAD
CCCCCCCEEECCCCC		22.9723927012
359PhosphorylationNGVNGTLTSNVADSP
CCCCCEEECCCCCCC		20.3523401153
360PhosphorylationGVNGTLTSNVADSPR
CCCCEEECCCCCCCC		32.2123927012
365PhosphorylationLTSNVADSPRNKKEK
EECCCCCCCCCCCCC		18.9329255136
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 TRAM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRAM1_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 TRAM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
US02_HCMVMUS2physical
19121997
US11_HCMVMUS11physical
19121997
DERL1_HUMANDERL1physical
19121997
HM13_HUMANHM13physical
19121997
1A02_HUMANHLA-Aphysical
19121997
1A03_HUMANHLA-Aphysical
19121997
1A01_HUMANHLA-Aphysical
19121997
1A26_HUMANHLA-Aphysical
19121997
BAP31_HUMANBCAP31physical
18555783
A4_HUMANAPPphysical
21832049
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 TRAM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-365, 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-365, AND MASSSPECTROMETRY.
"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-365, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND MASSSPECTROMETRY.
"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-365, AND MASSSPECTROMETRY.

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