TM201_HUMAN - dbPTM
TM201_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM201_HUMAN
UniProt AC Q5SNT2
Protein Name Transmembrane protein 201
Gene Name TMEM201
Organism Homo sapiens (Human).
Sequence Length 666
Subcellular Localization Isoform 2: Nucleus inner membrane
Multi-pass membrane protein . Cytoplasm, cytoskeleton, spindle pole . The C-terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane in d
Protein Description Involved in nuclear movement during fibroblast polarization and migration. Proposed to be involved in actin-dependent nuclear movement via association with transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow (By similarity). Overexpression can recruit Ran GTPase to the nuclear periphery. [PubMed: 27541860; Isoform 2: May define a distinct membrane domain in the vicinity of the mitotic spindle]
Protein Sequence MEGVSALLARCPTAGLAGGLGVTACAAAGVLLYRIARRMKPTHTMVNCWFCNQDTLVPYGNRNCWDCPHCEQYNGFQENGDYNKPIPAQYLEHLNHVVSSAPSLRDPSQPQQWVSSQVLLCKRCNHHQTTKIKQLAAFAPREEGRYDEEVEVYRHHLEQMYKLCRPCQAAVEYYIKHQNRQLRALLLSHQFKRREADQTHAQNFSSAVKSPVQVILLRALAFLACAFLLTTALYGASGHFAPGTTVPLALPPGGNGSATPDNGTTPGAEGWRQLLGLLPEHMAEKLCEAWAFGQSHQTGVVALGLLTCLLAMLLAGRIRLRRIDAFCTCLWALLLGLHLAEQHLQAASPSWLDTLKFSTTSLCCLVGFTAAVATRKATGPRRFRPRRFFPGDSAGLFPTSPSLAIPHPSVGGSPASLFIPSPPSFLPLANQQLFRSPRRTSPSSLPGRLSRALSLGTIPSLTRADSGYLFSGSRPPSQVSRSGEFPVSDYFSLLSGSCPSSPLPSPAPSVAGSVASSSGSLRHRRPLISPARLNLKGQKLLLFPSPPGEAPTTPSSSDEHSPHNGSLFTMEPPHVPRKPPLQDVKHALDLRSKLERGSACSNRSIKKEDDSSQSSTCVVDTTTRGCSEEAATWRGRFGPSLVRGLLAVSLAANALFTSVFLYQSLR
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
1Acetylation-------MEGVSALL
-------CCCHHHHH		10.2422814378
5Phosphorylation---MEGVSALLARCP
---CCCHHHHHHHCC		24.8520068231
40UbiquitinationYRIARRMKPTHTMVN
HHHHHHCCCCEEEEE		44.98-
82PhosphorylationGFQENGDYNKPIPAQ
CCCCCCCCCCCCCHH		26.8722817900
93UbiquitinationIPAQYLEHLNHVVSS
CCHHHHHHHHCHHHC		29.3622817900
95UbiquitinationAQYLEHLNHVVSSAP
HHHHHHHHCHHHCCC		28.0221890473
131UbiquitinationCNHHQTTKIKQLAAF
CCCCCCHHHHHHHHH		51.8222817900
133 (in isoform 2)Ubiquitination-40.5921890473
133 (in isoform 1)Ubiquitination-40.5921890473
133UbiquitinationHHQTTKIKQLAAFAP
CCCCHHHHHHHHHCC		40.5927667366
146PhosphorylationAPREEGRYDEEVEVY
CCCCCCCCCHHHHHH		38.2719060867
153PhosphorylationYDEEVEVYRHHLEQM
CCHHHHHHHHHHHHH		7.2519060867
154UbiquitinationDEEVEVYRHHLEQMY
CHHHHHHHHHHHHHH		18.8721890473
161PhosphorylationRHHLEQMYKLCRPCQ
HHHHHHHHHHHHHHH		10.6617693683
173PhosphorylationPCQAAVEYYIKHQNR
HHHHHHHHHHHHHHH		12.1428152594
174PhosphorylationCQAAVEYYIKHQNRQ
HHHHHHHHHHHHHHH		7.0328152594
188PhosphorylationQLRALLLSHQFKRRE
HHHHHHHHHHHHHHH		18.4021712546
192 (in isoform 2)Ubiquitination-43.9321890473
192UbiquitinationLLLSHQFKRREADQT
HHHHHHHHHHHHHHH		43.9322817900
192 (in isoform 1)Ubiquitination-43.9321890473
1922-HydroxyisobutyrylationLLLSHQFKRREADQT
HHHHHHHHHHHHHHH		43.93-
416PhosphorylationSVGGSPASLFIPSPP
CCCCCCHHHCCCCCC		27.48-
440PhosphorylationLFRSPRRTSPSSLPG
HHCCCCCCCCCCCCC		46.3930266825
441PhosphorylationFRSPRRTSPSSLPGR
HCCCCCCCCCCCCCH		22.4529255136
443PhosphorylationSPRRTSPSSLPGRLS
CCCCCCCCCCCCHHH		44.2530266825
444PhosphorylationPRRTSPSSLPGRLSR
CCCCCCCCCCCHHHH		41.8030266825
450PhosphorylationSSLPGRLSRALSLGT
CCCCCHHHHHHHHCC		17.7226055452
454PhosphorylationGRLSRALSLGTIPSL
CHHHHHHHHCCCCCC		24.6229255136
457PhosphorylationSRALSLGTIPSLTRA
HHHHHHCCCCCCCCC		34.7030266825
460PhosphorylationLSLGTIPSLTRADSG
HHHCCCCCCCCCCCC		38.2223927012
462PhosphorylationLGTIPSLTRADSGYL
HCCCCCCCCCCCCCC		28.3123927012
466PhosphorylationPSLTRADSGYLFSGS
CCCCCCCCCCCCCCC		28.4923401153
468PhosphorylationLTRADSGYLFSGSRP
CCCCCCCCCCCCCCC		14.4430108239
471PhosphorylationADSGYLFSGSRPPSQ
CCCCCCCCCCCCHHH		33.0121955146
473PhosphorylationSGYLFSGSRPPSQVS
CCCCCCCCCCHHHCC		40.1821955146
477PhosphorylationFSGSRPPSQVSRSGE
CCCCCCHHHCCCCCC		45.9921955146
480PhosphorylationSRPPSQVSRSGEFPV
CCCHHHCCCCCCCCH		17.0621955146
482PhosphorylationPPSQVSRSGEFPVSD
CHHHCCCCCCCCHHH		34.8624144214
488PhosphorylationRSGEFPVSDYFSLLS
CCCCCCHHHHHHHHH		27.1624144214
490PhosphorylationGEFPVSDYFSLLSGS
CCCCHHHHHHHHHCC		6.3830576142
492PhosphorylationFPVSDYFSLLSGSCP
CCHHHHHHHHHCCCC		23.3624144214
495PhosphorylationSDYFSLLSGSCPSSP
HHHHHHHHCCCCCCC		33.6724144214
497PhosphorylationYFSLLSGSCPSSPLP
HHHHHHCCCCCCCCC		21.3424144214
500PhosphorylationLLSGSCPSSPLPSPA
HHHCCCCCCCCCCCC		49.2524144214
501PhosphorylationLSGSCPSSPLPSPAP
HHCCCCCCCCCCCCC		18.6524144214
505PhosphorylationCPSSPLPSPAPSVAG
CCCCCCCCCCCCCCH		41.1824144214
509PhosphorylationPLPSPAPSVAGSVAS
CCCCCCCCCCHHHHC		27.0624144214
513PhosphorylationPAPSVAGSVASSSGS
CCCCCCHHHHCCCCC		12.5524144214
516PhosphorylationSVAGSVASSSGSLRH
CCCHHHHCCCCCCCC		23.9224144214
517PhosphorylationVAGSVASSSGSLRHR
CCHHHHCCCCCCCCC		29.0530576142
518PhosphorylationAGSVASSSGSLRHRR
CHHHHCCCCCCCCCC		29.8824144214
520PhosphorylationSVASSSGSLRHRRPL
HHHCCCCCCCCCCCC		24.9530576142
529PhosphorylationRHRRPLISPARLNLK
CCCCCCCCCEEECCC		21.8628176443
540UbiquitinationLNLKGQKLLLFPSPP
ECCCCCEEEECCCCC		3.7427667366
545PhosphorylationQKLLLFPSPPGEAPT
CEEEECCCCCCCCCC		36.0726074081
552PhosphorylationSPPGEAPTTPSSSDE
CCCCCCCCCCCCCCC		59.3923401153
553PhosphorylationPPGEAPTTPSSSDEH
CCCCCCCCCCCCCCC		21.8026074081
554UbiquitinationPGEAPTTPSSSDEHS
CCCCCCCCCCCCCCC		34.3927667366
555PhosphorylationGEAPTTPSSSDEHSP
CCCCCCCCCCCCCCC		40.1429116813
556PhosphorylationEAPTTPSSSDEHSPH
CCCCCCCCCCCCCCC		42.9129116813
557PhosphorylationAPTTPSSSDEHSPHN
CCCCCCCCCCCCCCC		51.8929116813
561PhosphorylationPSSSDEHSPHNGSLF
CCCCCCCCCCCCCCC		26.3027174698
566PhosphorylationEHSPHNGSLFTMEPP
CCCCCCCCCCCCCCC		26.1527174698
569PhosphorylationPHNGSLFTMEPPHVP
CCCCCCCCCCCCCCC		26.3927174698
578UbiquitinationEPPHVPRKPPLQDVK
CCCCCCCCCCHHHHH		44.9427667366
585UbiquitinationKPPLQDVKHALDLRS
CCCHHHHHHHHHHHH		31.3029967540
604PhosphorylationGSACSNRSIKKEDDS
CCCCCCCCCCCCCCC		42.9025072903
611PhosphorylationSIKKEDDSSQSSTCV
CCCCCCCCCCCCEEE		42.4723663014
612PhosphorylationIKKEDDSSQSSTCVV
CCCCCCCCCCCEEEE		40.8723663014
614PhosphorylationKEDDSSQSSTCVVDT
CCCCCCCCCEEEEEC		29.5723663014
615PhosphorylationEDDSSQSSTCVVDTT
CCCCCCCCEEEEECC		20.4223663014
616PhosphorylationDDSSQSSTCVVDTTT
CCCCCCCEEEEECCC		17.9923663014
621PhosphorylationSSTCVVDTTTRGCSE
CCEEEEECCCCCCCH		20.6120639409
622PhosphorylationSTCVVDTTTRGCSEE
CEEEEECCCCCCCHH		15.2720639409
623PhosphorylationTCVVDTTTRGCSEEA
EEEEECCCCCCCHHH		27.4420639409
627PhosphorylationDTTTRGCSEEAATWR
ECCCCCCCHHHHHHC		41.10-
649PhosphorylationVRGLLAVSLAANALF
HHHHHHHHHHHHHHH		13.4920860994
657PhosphorylationLAANALFTSVFLYQS
HHHHHHHHHHHHHHH		25.4920860994
658PhosphorylationAANALFTSVFLYQSL
HHHHHHHHHHHHHHH		11.9720860994
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 TM201_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM201_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 TM201_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TM201_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 TM201_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-454, 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-441; SER-454 ANDSER-529, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441 AND SER-454, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-146; TYR-153 ANDTYR-161, AND MASS SPECTROMETRY.

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