TM209_HUMAN - dbPTM
TM209_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM209_HUMAN
UniProt AC Q96SK2
Protein Name Transmembrane protein 209
Gene Name TMEM209
Organism Homo sapiens (Human).
Sequence Length 561
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MMQGEAHPSASLIDRTIKMRKETEARKVVLAWGLLNVSMAGMIYTEMTGKLISSYYNVTYWPLWYIELALASLFSLNALFDFWRYFKYTVAPTSLVVSPGQQTLLGLKTAVVQTTPPHDLAATQIPPAPPSPSIQGQSVLSYSPSRSPSTSPKFTTSCMTGYSPQLQGLSSGGSGSYSPGVTYSPVSGYNKLASFSPSPPSPYPTTVGPVESSGLRSRYRSSPTVYNSPTDKEDYMTDLRTLDTFLRSEEEKQHRVKLGSPDSTSPSSSPTFWNYSRSMGDYAQTLKKFQYQLACRSQAPCANKDEADLSSKQAAEEVWARVAMNRQLLDHMDSWTAKFRNWINETILVPLVQEIESVSTQMRRMGCPELQIGEASITSLKQAALVKAPLIPTLNTIVQYLDLTPNQEYLFERIKELSQGGCMSSFRWNRGGDFKGRKWDTDLPTDSAIIMHVFCTYLDSRLPPHPKYPDGKTFTSQHFVQTPNKPDVTNENVFCIYQSAINPPHYELIYQRHVYNLPKGRNNMFHTLLMFLYIIKTKESGMLGRVNLGLSGVNILWIFGE
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
9PhosphorylationMQGEAHPSASLIDRT
CCCCCCCCHHHHHHH		22.1830108239
11PhosphorylationGEAHPSASLIDRTIK
CCCCCCHHHHHHHHH		30.1430108239
18UbiquitinationSLIDRTIKMRKETEA
HHHHHHHHHHCHHHH		31.85-
18 (in isoform 1)Ubiquitination-31.8521890473
18 (in isoform 3)Ubiquitination-31.8521890473
18 (in isoform 4)Ubiquitination-31.8521906983
38PhosphorylationAWGLLNVSMAGMIYT
HHHHHHHHHHHHHHH		11.2225072903
44PhosphorylationVSMAGMIYTEMTGKL
HHHHHHHHHHHHCHH		6.4325072903
45PhosphorylationSMAGMIYTEMTGKLI
HHHHHHHHHHHCHHH		14.3525072903
48PhosphorylationGMIYTEMTGKLISSY
HHHHHHHHCHHHHCH		25.5725072903
57N-linked_GlycosylationKLISSYYNVTYWPLW
HHHHCHHCCCHHHHH		16.06UniProtKB CARBOHYD
88PhosphorylationDFWRYFKYTVAPTSL
HHHHHHCCCCCCCEE		9.1326074081
89PhosphorylationFWRYFKYTVAPTSLV
HHHHHCCCCCCCEEE		15.6926074081
93PhosphorylationFKYTVAPTSLVVSPG
HCCCCCCCEEEECCC		25.5926074081
94PhosphorylationKYTVAPTSLVVSPGQ
CCCCCCCEEEECCCC		20.3630108239
98PhosphorylationAPTSLVVSPGQQTLL
CCCEEEECCCCCHHH		18.8130278072
103PhosphorylationVVSPGQQTLLGLKTA
EECCCCCHHHCCEEE		18.9629978859
109PhosphorylationQTLLGLKTAVVQTTP
CHHHCCEEEEEECCC		29.7224043423
114PhosphorylationLKTAVVQTTPPHDLA
CEEEEEECCCCCCCC		29.6625002506
115PhosphorylationKTAVVQTTPPHDLAA
EEEEEECCCCCCCCC		20.1024043423
123PhosphorylationPPHDLAATQIPPAPP
CCCCCCCCCCCCCCC		22.7930108239
131PhosphorylationQIPPAPPSPSIQGQS
CCCCCCCCCCCCCCE		30.1626657352
133PhosphorylationPPAPPSPSIQGQSVL
CCCCCCCCCCCCEEE		31.7030108239
138PhosphorylationSPSIQGQSVLSYSPS
CCCCCCCEEEEECCC		31.6730108239
141PhosphorylationIQGQSVLSYSPSRSP
CCCCEEEEECCCCCC		22.7830108239
142PhosphorylationQGQSVLSYSPSRSPS
CCCEEEEECCCCCCC		22.0525002506
143PhosphorylationGQSVLSYSPSRSPST
CCEEEEECCCCCCCC		17.0225002506
145PhosphorylationSVLSYSPSRSPSTSP
EEEEECCCCCCCCCC		39.1825002506
153UbiquitinationRSPSTSPKFTTSCMT
CCCCCCCCCCCCCCC		55.92-
176PhosphorylationLSSGGSGSYSPGVTY
CCCCCCCCCCCCCEE		24.9225627689
178PhosphorylationSGGSGSYSPGVTYSP
CCCCCCCCCCCEECC		19.5125627689
189PhosphorylationTYSPVSGYNKLASFS
EECCCCCCCCCCCCC		11.13-
194PhosphorylationSGYNKLASFSPSPPS
CCCCCCCCCCCCCCC		36.3725159151
196PhosphorylationYNKLASFSPSPPSPY
CCCCCCCCCCCCCCC		23.2125159151
198PhosphorylationKLASFSPSPPSPYPT
CCCCCCCCCCCCCCC		48.5225159151
201PhosphorylationSFSPSPPSPYPTTVG
CCCCCCCCCCCCCCC		40.2125159151
203PhosphorylationSPSPPSPYPTTVGPV
CCCCCCCCCCCCCCC		19.9721712546
205PhosphorylationSPPSPYPTTVGPVES
CCCCCCCCCCCCCCC		28.4228152594
206PhosphorylationPPSPYPTTVGPVESS
CCCCCCCCCCCCCCC		20.9728152594
212PhosphorylationTTVGPVESSGLRSRY
CCCCCCCCCCHHHHC		29.9125693802
213PhosphorylationTVGPVESSGLRSRYR
CCCCCCCCCHHHHCC		28.4825693802
219PhosphorylationSSGLRSRYRSSPTVY
CCCHHHHCCCCCCCC		18.9823927012
221PhosphorylationGLRSRYRSSPTVYNS
CHHHHCCCCCCCCCC		31.5623401153
222PhosphorylationLRSRYRSSPTVYNSP
HHHHCCCCCCCCCCC		18.6523927012
224PhosphorylationSRYRSSPTVYNSPTD
HHCCCCCCCCCCCCC		37.2523927012
226PhosphorylationYRSSPTVYNSPTDKE
CCCCCCCCCCCCCHH		16.6423927012
228PhosphorylationSSPTVYNSPTDKEDY
CCCCCCCCCCCHHHH		16.1023927012
230PhosphorylationPTVYNSPTDKEDYMT
CCCCCCCCCHHHHHH		60.5723927012
231 (in isoform 2)Ubiquitination-56.5921890473
232AcetylationVYNSPTDKEDYMTDL
CCCCCCCHHHHHHHH		55.7726051181
232UbiquitinationVYNSPTDKEDYMTDL
CCCCCCCHHHHHHHH		55.77-
232 (in isoform 1)Ubiquitination-55.7721890473
232 (in isoform 3)Ubiquitination-55.7721890473
235PhosphorylationSPTDKEDYMTDLRTL
CCCCHHHHHHHHHHH		11.7328796482
237PhosphorylationTDKEDYMTDLRTLDT
CCHHHHHHHHHHHHH		26.1728796482
241PhosphorylationDYMTDLRTLDTFLRS
HHHHHHHHHHHHHCC		35.9630266825
244PhosphorylationTDLRTLDTFLRSEEE
HHHHHHHHHHCCHHH		27.9030266825
248PhosphorylationTLDTFLRSEEEKQHR
HHHHHHCCHHHHHHC		52.0530266825
256 (in isoform 2)Ubiquitination-5.8721890473
257UbiquitinationEEKQHRVKLGSPDST
HHHHHCCCCCCCCCC		47.2721890473
257 (in isoform 1)Ubiquitination-47.2721890473
257 (in isoform 3)Ubiquitination-47.2721890473
260PhosphorylationQHRVKLGSPDSTSPS
HHCCCCCCCCCCCCC		35.6525159151
263PhosphorylationVKLGSPDSTSPSSSP
CCCCCCCCCCCCCCC		33.8825159151
264PhosphorylationKLGSPDSTSPSSSPT
CCCCCCCCCCCCCCC		52.6225159151
265PhosphorylationLGSPDSTSPSSSPTF
CCCCCCCCCCCCCCH		27.0825159151
267PhosphorylationSPDSTSPSSSPTFWN
CCCCCCCCCCCCHHH		43.1225159151
268PhosphorylationPDSTSPSSSPTFWNY
CCCCCCCCCCCHHHH		43.6625159151
269PhosphorylationDSTSPSSSPTFWNYS
CCCCCCCCCCHHHHC		32.0925159151
271PhosphorylationTSPSSSPTFWNYSRS
CCCCCCCCHHHHCCC		43.1422617229
274N-linked_GlycosylationSSSPTFWNYSRSMGD
CCCCCHHHHCCCCHH		22.25UniProtKB CARBOHYD
275PhosphorylationSSPTFWNYSRSMGDY
CCCCHHHHCCCCHHH		8.9620068231
276PhosphorylationSPTFWNYSRSMGDYA
CCCHHHHCCCCHHHH		18.0530108239
278PhosphorylationTFWNYSRSMGDYAQT
CHHHHCCCCHHHHHH		22.6025159151
282PhosphorylationYSRSMGDYAQTLKKF
HCCCCHHHHHHHHHH		8.5527642862
285PhosphorylationSMGDYAQTLKKFQYQ
CCHHHHHHHHHHHHH		32.1628555341
286 (in isoform 2)Ubiquitination-3.6421890473
2872-HydroxyisobutyrylationGDYAQTLKKFQYQLA
HHHHHHHHHHHHHHH		55.73-
287AcetylationGDYAQTLKKFQYQLA
HHHHHHHHHHHHHHH		55.737409415
287UbiquitinationGDYAQTLKKFQYQLA
HHHHHHHHHHHHHHH		55.73-
287 (in isoform 1)Ubiquitination-55.7321890473
287 (in isoform 3)Ubiquitination-55.7321890473
288UbiquitinationDYAQTLKKFQYQLAC
HHHHHHHHHHHHHHH		40.59-
291PhosphorylationQTLKKFQYQLACRSQ
HHHHHHHHHHHHCCC		14.5026552605
304AcetylationSQAPCANKDEADLSS
CCCCCCCCCHHCCCH		38.1223749302
304UbiquitinationSQAPCANKDEADLSS
CCCCCCCCCHHCCCH		38.12-
311 (in isoform 2)Ubiquitination-35.7621890473
312AcetylationDEADLSSKQAAEEVW
CHHCCCHHHHHHHHH		40.3526051181
312UbiquitinationDEADLSSKQAAEEVW
CHHCCCHHHHHHHHH		40.35-
312 (in isoform 1)Ubiquitination-40.3521890473
312 (in isoform 3)Ubiquitination-40.3521890473
337 (in isoform 2)Ubiquitination-11.6121890473
338UbiquitinationHMDSWTAKFRNWINE
HHHHHHHHHHHHHCH		37.1721890473
338 (in isoform 1)Ubiquitination-37.1721890473
338 (in isoform 3)Ubiquitination-37.1721890473
376PhosphorylationELQIGEASITSLKQA
CCCCCCEECCHHHHH		23.3022210691
378PhosphorylationQIGEASITSLKQAAL
CCCCEECCHHHHHHH		26.0530622161
379PhosphorylationIGEASITSLKQAALV
CCCEECCHHHHHHHH		31.7230622161
381UbiquitinationEASITSLKQAALVKA
CEECCHHHHHHHHHC		37.34-
404PhosphorylationIVQYLDLTPNQEYLF
HHHHHCCCCCHHHHH		21.6226074081
415UbiquitinationEYLFERIKELSQGGC
HHHHHHHHHHHCCCC		59.84-
467UbiquitinationSRLPPHPKYPDGKTF
HCCCCCCCCCCCCCC		67.40-
519AcetylationRHVYNLPKGRNNMFH
HHCCCCCCCCCHHHH		73.9226051181
519UbiquitinationRHVYNLPKGRNNMFH
HHCCCCCCCCCHHHH		73.92-
533PhosphorylationHTLLMFLYIIKTKES
HHHHHHHHHHHHCCC		6.8520068231
537PhosphorylationMFLYIIKTKESGMLG
HHHHHHHHCCCCCCC		29.63-
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 TM209_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM209_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 TM209_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TM209_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 TM209_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-98 AND SER-248, AND MASSSPECTROMETRY.

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