TMX1_HUMAN - dbPTM
TMX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMX1_HUMAN
UniProt AC Q9H3N1
Protein Name Thioredoxin-related transmembrane protein 1
Gene Name TMX1
Organism Homo sapiens (Human).
Sequence Length 280
Subcellular Localization Membrane
Single-pass type I membrane protein . Endoplasmic reticulum membrane
Single-pass type I membrane protein . Predominantly found in the endoplasmic reticulum.
Protein Description May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions..
Protein Sequence MAPSGSLAVPLAVLVLLLWGAPWTHGRRSNVRVITDENWRELLEGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNIAKVDVTEQPGLSGRFIITALPTIYHCKDGEFRRYQGPRTKKDFINFISDKEWKSIEPVSSWFGPGSVLMSSMSALFQLSMWIRTCHNYFIEDLGLPVWGSYTVFALATLFSGLLLGLCMIFVADCLCPSKRRRPQPYPYPSKKLLSESAQPLKKVEEEQEADEEDVSEEEAESKEGTNKDFPQNAIRQRSLGPSLATDKS
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
102PhosphorylationFIITALPTIYHCKDG
EEEEECCEEEECCCC		34.7128152594
104PhosphorylationITALPTIYHCKDGEF
EEECCEEEECCCCCC		12.0228152594
106S-palmitoylationALPTIYHCKDGEFRR
ECCEEEECCCCCCHH		2.1129575903
107UbiquitinationLPTIYHCKDGEFRRY
CCEEEECCCCCCHHC		56.2933845483
1072-HydroxyisobutyrylationLPTIYHCKDGEFRRY
CCEEEECCCCCCHHC		56.29-
120UbiquitinationRYQGPRTKKDFINFI
HCCCCCCHHHHHHHC		52.1823000965
121UbiquitinationYQGPRTKKDFINFIS
CCCCCCHHHHHHHCC		58.2023000965
1212-HydroxyisobutyrylationYQGPRTKKDFINFIS
CCCCCCHHHHHHHCC		58.20-
130UbiquitinationFINFISDKEWKSIEP
HHHHCCCCCCCCCCC		59.7029967540
1302-HydroxyisobutyrylationFINFISDKEWKSIEP
HHHHCCCCCCCCCCC		59.70-
165S-palmitoylationLSMWIRTCHNYFIED
HHHHHHHHHHHHHHH		1.0929575903
205S-palmitoylationCMIFVADCLCPSKRR
HHHHHHHHCCCCCCC		2.8022045338
207S-palmitoylationIFVADCLCPSKRRRP
HHHHHHCCCCCCCCC		4.4922045338
217PhosphorylationKRRRPQPYPYPSKKL
CCCCCCCCCCCCHHH		15.3428152594
219PhosphorylationRRPQPYPYPSKKLLS
CCCCCCCCCCHHHHC		17.8128152594
221PhosphorylationPQPYPYPSKKLLSES
CCCCCCCCHHHHCCC		36.2623401153
222UbiquitinationQPYPYPSKKLLSESA
CCCCCCCHHHHCCCC		42.8323000965
2222-HydroxyisobutyrylationQPYPYPSKKLLSESA
CCCCCCCHHHHCCCC		42.83-
223UbiquitinationPYPYPSKKLLSESAQ
CCCCCCHHHHCCCCC		60.0223000965
226PhosphorylationYPSKKLLSESAQPLK
CCCHHHHCCCCCCCH		39.6829255136
228PhosphorylationSKKLLSESAQPLKKV
CHHHHCCCCCCCHHH		28.9130266825
233AcetylationSESAQPLKKVEEEQE
CCCCCCCHHHHHHHH		62.5525953088
233UbiquitinationSESAQPLKKVEEEQE
CCCCCCCHHHHHHHH		62.5521906983
2332-HydroxyisobutyrylationSESAQPLKKVEEEQE
CCCCCCCHHHHHHHH		62.55-
234UbiquitinationESAQPLKKVEEEQEA
CCCCCCHHHHHHHHC		63.66-
247PhosphorylationEADEEDVSEEEAESK
HCCCCCCCHHHHHHH		52.1729255136
253PhosphorylationVSEEEAESKEGTNKD
CCHHHHHHHCCCCCC		42.9522167270
257PhosphorylationEAESKEGTNKDFPQN
HHHHHCCCCCCCCHH		39.9423927012
259UbiquitinationESKEGTNKDFPQNAI
HHHCCCCCCCCHHHH		61.6633845483
270PhosphorylationQNAIRQRSLGPSLAT
HHHHHHHCCCCCHHC		29.3729255136
274PhosphorylationRQRSLGPSLATDKS-
HHHCCCCCHHCCCC-		28.9230266825
277PhosphorylationSLGPSLATDKS----
CCCCCHHCCCC----		49.6130266825
279AcetylationGPSLATDKS------
CCCHHCCCC------		54.4325953088
279UbiquitinationGPSLATDKS------
CCCHHCCCC------		54.4324816145
280PhosphorylationPSLATDKS-------
CCHHCCCC-------		48.5430266825
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 TMX1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMX1_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 TMX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LMAN1_HUMANLMAN1physical
26344197
SSRA_HUMANSSR1physical
26344197
THIO_HUMANTXNphysical
26344197
VDAC1_HUMANVDAC1physical
26344197
VDAC2_HUMANVDAC2physical
26344197
VDAC3_HUMANVDAC3physical
26344197
FGFR4_HUMANFGFR4physical
28514442
PLXB2_HUMANPLXNB2physical
28514442
EHD1_HUMANEHD1physical
28514442
CD320_HUMANCD320physical
28514442
GMCL1_HUMANGMCL1physical
28514442
EPHA7_HUMANEPHA7physical
28514442
GRM1C_HUMANGRAMD1Cphysical
28514442
GRM1B_HUMANGRAMD1Bphysical
28514442
NRP1_HUMANNRP1physical
28514442
GRM1A_HUMANGRAMD1Aphysical
28514442
LRFN1_HUMANLRFN1physical
28514442
PDXL2_HUMANPODXL2physical
28514442
CSPG5_HUMANCSPG5physical
28514442
SQSTM_HUMANSQSTM1physical
28514442
T179B_HUMANTMEM179Bphysical
28514442
CD276_HUMANCD276physical
28514442
UFSP2_HUMANUFSP2physical
28514442
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 TMX1_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-247; SER-270 ANDSER-280, AND MASS SPECTROMETRY.
"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-247, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, 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-247; SER-270 ANDSER-280, AND MASS 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-280, AND MASSSPECTROMETRY.
"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-247, 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-247, AND MASSSPECTROMETRY.

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