TMX2_HUMAN - dbPTM
TMX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMX2_HUMAN
UniProt AC Q9Y320
Protein Name Thioredoxin-related transmembrane protein 2
Gene Name TMX2
Organism Homo sapiens (Human).
Sequence Length 296
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description
Protein Sequence MAVLAPLIALVYSVPRLSRWLAQPYYLLSALLSAAFLLVRKLPPLCHGLPTQREDGNPCDFDWREVEILMFLSAIVMMKNRRSITVEQHIGNIFMFSKVANTILFFRLDIRMGLLYITLCIVFLMTCKPPLYMGPEYIKYFNDKTIDEELERDKRVTWIVEFFANWSNDCQSFAPIYADLSLKYNCTGLNFGKVDVGRYTDVSTRYKVSTSPLTKQLPTLILFQGGKEAMRRPQIDKKGRAVSWTFSEENVIREFNLNELYQRAKKLSKAGDNIPEEQPVASTPTTVSDGENKKDK
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
12PhosphorylationAPLIALVYSVPRLSR
HHHHHHHHCHHHHHH		12.5624043423
13PhosphorylationPLIALVYSVPRLSRW
HHHHHHHCHHHHHHH		20.4024043423
18PhosphorylationVYSVPRLSRWLAQPY
HHCHHHHHHHHHHHH		23.7724043423
41UbiquitinationAAFLLVRKLPPLCHG
HHHHHHHHCCHHHCC		58.8427667366
50UbiquitinationPPLCHGLPTQREDGN
CHHHCCCCCCCCCCC		30.9533845483
73PhosphorylationVEILMFLSAIVMMKN
HHHHHHHHHHHHHCC		12.5120068231
75UbiquitinationILMFLSAIVMMKNRR
HHHHHHHHHHHCCCC		1.5133845483
79AcetylationLSAIVMMKNRRSITV
HHHHHHHCCCCCEEE		29.257710617
83 (in isoform 2)Phosphorylation-21.26-
83PhosphorylationVMMKNRRSITVEQHI
HHHCCCCCEEEEEHH		21.2621406692
85PhosphorylationMKNRRSITVEQHIGN
HCCCCCEEEEEHHHC		21.1621406692
97PhosphorylationIGNIFMFSKVANTIL
HHCHHHHHHHCCCHH		17.9021406692
99UbiquitinationNIFMFSKVANTILFF
CHHHHHHHCCCHHHH		4.8733845483
101UbiquitinationFMFSKVANTILFFRL
HHHHHHCCCHHHHHH		30.5522817900
106 (in isoform 2)Ubiquitination-7.3121890473
106UbiquitinationVANTILFFRLDIRMG
HCCCHHHHHHHHHHH		7.3127667366
113UbiquitinationFRLDIRMGLLYITLC
HHHHHHHHHHHHHHH		11.5933845483
116UbiquitinationDIRMGLLYITLCIVF
HHHHHHHHHHHHHHH		9.2633845483
121UbiquitinationLLYITLCIVFLMTCK
HHHHHHHHHHHHHCC		2.4933845483
124UbiquitinationITLCIVFLMTCKPPL
HHHHHHHHHHCCCCC		1.6033845483
132PhosphorylationMTCKPPLYMGPEYIK
HHCCCCCCCCHHHHH		13.05-
138UbiquitinationLYMGPEYIKYFNDKT
CCCCHHHHHHCCCCC		2.5133845483
139UbiquitinationYMGPEYIKYFNDKTI
CCCHHHHHHCCCCCC		42.7722817900
144UbiquitinationYIKYFNDKTIDEELE
HHHHCCCCCCCHHHH		48.7821906983
144 (in isoform 1)Ubiquitination-48.7821890473
146UbiquitinationKYFNDKTIDEELERD
HHCCCCCCCHHHHHH		8.4833845483
155UbiquitinationEELERDKRVTWIVEF
HHHHHHHCEEEEEHH		35.0721963094
155 (in isoform 2)Ubiquitination-35.0721890473
165UbiquitinationWIVEFFANWSNDCQS
EEEHHHHCCCCCCCH		37.2433845483
169UbiquitinationFFANWSNDCQSFAPI
HHHCCCCCCCHHHHE		26.7333845483
175UbiquitinationNDCQSFAPIYADLSL
CCCCHHHHEECEEEE		20.3633845483
177UbiquitinationCQSFAPIYADLSLKY
CCHHHHEECEEEEEE		7.9423000965
177 (in isoform 2)Ubiquitination-7.9421890473
179UbiquitinationSFAPIYADLSLKYNC
HHHHEECEEEEEEEC		21.5933845483
182UbiquitinationPIYADLSLKYNCTGL
HEECEEEEEEECCCC		9.9233845483
187UbiquitinationLSLKYNCTGLNFGKV
EEEEEECCCCCCCEE		40.8633845483
187PhosphorylationLSLKYNCTGLNFGKV
EEEEEECCCCCCCEE		40.8621712546
189 (in isoform 2)Ubiquitination-2.30-
189UbiquitinationLKYNCTGLNFGKVDV
EEEECCCCCCCEEEE		2.3021963094
193AcetylationCTGLNFGKVDVGRYT
CCCCCCCEEEECEEC		30.9925953088
193 (in isoform 1)Ubiquitination-30.9921890473
193UbiquitinationCTGLNFGKVDVGRYT
CCCCCCCEEEECEEC		30.9921906983
199UbiquitinationGKVDVGRYTDVSTRY
CEEEECEECCCCCEE		11.0233845483
200UbiquitinationKVDVGRYTDVSTRYK
EEEECEECCCCCEEE		28.6733845483
206PhosphorylationYTDVSTRYKVSTSPL
ECCCCCEEEEECCCC		18.8123312004
206UbiquitinationYTDVSTRYKVSTSPL
ECCCCCEEEEECCCC		18.8133845483
207UbiquitinationTDVSTRYKVSTSPLT
CCCCCEEEEECCCCH		26.8133845483
207MalonylationTDVSTRYKVSTSPLT
CCCCCEEEEECCCCH		26.8126320211
209PhosphorylationVSTRYKVSTSPLTKQ
CCCEEEEECCCCHHC		21.0030108239
210PhosphorylationSTRYKVSTSPLTKQL
CCEEEEECCCCHHCC		37.0330266825
211PhosphorylationTRYKVSTSPLTKQLP
CEEEEECCCCHHCCC		15.4829255136
214PhosphorylationKVSTSPLTKQLPTLI
EEECCCCHHCCCEEE		21.8229255136
215 (in isoform 1)Ubiquitination-58.4821890473
215UbiquitinationVSTSPLTKQLPTLIL
EECCCCHHCCCEEEE		58.4823000965
224UbiquitinationLPTLILFQGGKEAMR
CCEEEEECCCHHHHH		57.1733845483
227UbiquitinationLILFQGGKEAMRRPQ
EEEECCCHHHHHCCC		49.4721963094
228UbiquitinationILFQGGKEAMRRPQI
EEECCCHHHHHCCCC		51.4723503661
231UbiquitinationQGGKEAMRRPQIDKK
CCCHHHHHCCCCCCC		54.9327667366
231 (in isoform 2)Ubiquitination-54.9321890473
2372-HydroxyisobutyrylationMRRPQIDKKGRAVSW
HHCCCCCCCCCCCEE		59.77-
241UbiquitinationQIDKKGRAVSWTFSE
CCCCCCCCCEEECCC		14.3633845483
243PhosphorylationDKKGRAVSWTFSEEN
CCCCCCCEEECCCHH		21.2930266825
245PhosphorylationKGRAVSWTFSEENVI
CCCCCEEECCCHHHH		15.1330266825
247PhosphorylationRAVSWTFSEENVIRE
CCCEEECCCHHHHHH		36.3030266825
255 (in isoform 2)Ubiquitination-10.1521890473
255UbiquitinationEENVIREFNLNELYQ
CHHHHHHCCHHHHHH		10.1533845483
261PhosphorylationEFNLNELYQRAKKLS
HCCHHHHHHHHHHHH		6.9728152594
265UbiquitinationNELYQRAKKLSKAGD
HHHHHHHHHHHHCCC		57.3333845483
266UbiquitinationELYQRAKKLSKAGDN
HHHHHHHHHHHCCCC		57.9423503661
269 (in isoform 1)Ubiquitination-67.8221890473
269UbiquitinationQRAKKLSKAGDNIPE
HHHHHHHHCCCCCCC		67.8227667366
276UbiquitinationKAGDNIPEEQPVAST
HCCCCCCCCCCCCCC		66.5233845483
282PhosphorylationPEEQPVASTPTTVSD
CCCCCCCCCCCCCCC		34.8423401153
283PhosphorylationEEQPVASTPTTVSDG
CCCCCCCCCCCCCCC		18.2130266825
285PhosphorylationQPVASTPTTVSDGEN
CCCCCCCCCCCCCCC		39.6622167270
286PhosphorylationPVASTPTTVSDGENK
CCCCCCCCCCCCCCC		21.1523401153
288PhosphorylationASTPTTVSDGENKKD
CCCCCCCCCCCCCCC		37.4929255136
293UbiquitinationTVSDGENKKDK----
CCCCCCCCCCC----		59.0333845483
293 (in isoform 1)Ubiquitination-59.0321890473
300UbiquitinationKKDK-----------
CCCC-----------		33845483
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 TMX2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMX2_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 TMX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDUV3_HUMANNDUFV3physical
26186194
NDUA7_HUMANNDUFA7physical
26186194
NDUV3_HUMANNDUFV3physical
28514442
NDUA7_HUMANNDUFA7physical
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 TMX2_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-243, 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-288, AND MASSSPECTROMETRY.

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