TM192_HUMAN - dbPTM
TM192_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM192_HUMAN
UniProt AC Q8IY95
Protein Name Transmembrane protein 192
Gene Name TMEM192
Organism Homo sapiens (Human).
Sequence Length 271
Subcellular Localization Lysosome membrane
Multi-pass membrane protein . Late endosome .
Protein Description
Protein Sequence MAAGGRMEDGSLDITQSIEDDPLLDAQLLPHHSLQAHFRPRFHPLPTVIIVNLLWFIHLVFVVLAFLTGVLCSYPNPNEDKCPGNYTNPLKVQTVIILGKVILWILHLLLECYIQYHHSKIRNRGYNLIYRSTRHLKRLALMIQSSGNTVLLLILCMQHSFPEPGRLYLDLILAILALELICSLICLLIYTVKIRRFNKAKPEPDILEEEKIYAYPSNITSETGFRTISSLEEIVEKQGDTIEYLKRHNALLSKRLLALTSSDLGCQPSRT
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
11PhosphorylationGGRMEDGSLDITQSI
CCCCCCCCCCCCCCC		34.8827422710
15PhosphorylationEDGSLDITQSIEDDP
CCCCCCCCCCCCCCC		18.8717525332
17PhosphorylationGSLDITQSIEDDPLL
CCCCCCCCCCCCCCC		21.2117525332
130PhosphorylationNRGYNLIYRSTRHLK
HCCHHHHHHCHHHHH		11.15-
160PhosphorylationLILCMQHSFPEPGRL
HHHHHHCCCCCCCHH		26.13-
199UbiquitinationVKIRRFNKAKPEPDI
HHHHHHCCCCCCCCC		55.8929901268
201UbiquitinationIRRFNKAKPEPDILE
HHHHCCCCCCCCCCC		52.0722817900
209UbiquitinationPEPDILEEEKIYAYP
CCCCCCCCCCEEECC		62.2321890473
211UbiquitinationPDILEEEKIYAYPSN
CCCCCCCCEEECCCC		44.2730230243
213PhosphorylationILEEEKIYAYPSNIT
CCCCCCEEECCCCCC		15.9121945579
215PhosphorylationEEEKIYAYPSNITSE
CCCCEEECCCCCCCC		7.1021945579
217PhosphorylationEKIYAYPSNITSETG
CCEEECCCCCCCCCC		28.3421945579
220PhosphorylationYAYPSNITSETGFRT
EECCCCCCCCCCCCC		25.4321945579
221PhosphorylationAYPSNITSETGFRTI
ECCCCCCCCCCCCCC		29.3921945579
223PhosphorylationPSNITSETGFRTISS
CCCCCCCCCCCCCHH		41.1927642862
227PhosphorylationTSETGFRTISSLEEI
CCCCCCCCCHHHHHH		23.9728102081
229PhosphorylationETGFRTISSLEEIVE
CCCCCCCHHHHHHHH		28.4030266825
230PhosphorylationTGFRTISSLEEIVEK
CCCCCCHHHHHHHHH		35.6330266825
237UbiquitinationSLEEIVEKQGDTIEY
HHHHHHHHCCCHHHH		49.0032015554
241PhosphorylationIVEKQGDTIEYLKRH
HHHHCCCHHHHHHHH		23.6426434776
242 (in isoform 2)Ubiquitination-3.7921890473
244PhosphorylationKQGDTIEYLKRHNAL
HCCCHHHHHHHHHHH		17.4224247654
246UbiquitinationGDTIEYLKRHNALLS
CCHHHHHHHHHHHHH		51.1921906983
246 (in isoform 1)Ubiquitination-51.1921890473
250 (in isoform 2)Ubiquitination-12.0721890473
254UbiquitinationRHNALLSKRLLALTS
HHHHHHHHHHHHHHH		47.2123000965
254 (in isoform 1)Ubiquitination-47.2121890473
260PhosphorylationSKRLLALTSSDLGCQ
HHHHHHHHHCCCCCC		22.1529396449
261PhosphorylationKRLLALTSSDLGCQP
HHHHHHHHCCCCCCC		23.7825850435
262PhosphorylationRLLALTSSDLGCQPS
HHHHHHHCCCCCCCC		31.4530108239
266GlutathionylationLTSSDLGCQPSRT--
HHHCCCCCCCCCC--		7.5622555962
269PhosphorylationSDLGCQPSRT-----
CCCCCCCCCC-----		23.7525159151
271PhosphorylationLGCQPSRT-------
CCCCCCCC-------		47.5021815630
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 TM192_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM192_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 TM192_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TM192_HUMAN !!
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 TM192_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, 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-11; THR-15 AND SER-17,AND MASS SPECTROMETRY.
"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 TYR-213, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, AND MASSSPECTROMETRY.

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