PTN9_HUMAN - dbPTM
PTN9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTN9_HUMAN
UniProt AC P43378
Protein Name Tyrosine-protein phosphatase non-receptor type 9
Gene Name PTPN9
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Cytoplasm .
Protein Description Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus..
Protein Sequence MEPATAPRPDMAPELTPEEEQATKQFLEEINKWTVQYNVSPLSWNVAVKFLMARKFDVLRAIELFHSYRETRRKEGIVKLKPHEEPLRSEILSGKFTILNVRDPTGASIALFTARLHHPHKSVQHVVLQALFYLLDRAVDSFETQRNGLVFIYDMCGSNYANFELDLGKKVLNLLKGAFPARLKKVLIVGAPIWFRVPYSIISLLLKDKVRERIQILKTSEVTQHLPRECLPENLGGYVKIDLATWNFQFLPQVNGHPDPFDEIILFSLPPALDWDSVHVPGPHAMTIQELVDYVNARQKQGIYEEYEDIRRENPVGTFHCSMSPGNLEKNRYGDVPCLDQTRVKLTKRSGHTQTDYINASFMDGYKQKNAYIGTQGPLENTYRDFWLMVWEQKVLVIVMTTRFEEGGRRKCGQYWPLEKDSRIRFGFLTVTNLGVENMNHYKKTTLEIHNTEERQKRQVTHFQFLSWPDYGVPSSAASLIDFLRVVRNQQSLAVSNMGARSKGQCPEPPIVVHCSAGIGRTGTFCSLDICLAQLEELGTLNVFQTVSRMRTQRAFSIQTPEQYYFCYKAILEFAEKEGMVSSGQNLLAVESQ
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-------MEPATAPR
-------CCCCCCCC		14.5419413330
67PhosphorylationRAIELFHSYRETRRK
HHHHHHHHHHHHHCC		20.6730206219
68PhosphorylationAIELFHSYRETRRKE
HHHHHHHHHHHHCCC		12.1430206219
71PhosphorylationLFHSYRETRRKEGIV
HHHHHHHHHCCCCCE		27.1230206219
79UbiquitinationRRKEGIVKLKPHEEP
HCCCCCEECCCCCCC		49.20-
89PhosphorylationPHEEPLRSEILSGKF
CCCCCCHHHHHCCCE		36.3520068231
93PhosphorylationPLRSEILSGKFTILN
CCHHHHHCCCEEEEE		45.6720068231
97PhosphorylationEILSGKFTILNVRDP
HHHCCCEEEEEECCC		28.2120068231
133PhosphorylationVVLQALFYLLDRAVD
HHHHHHHHHHHHHHH		13.75-
141PhosphorylationLLDRAVDSFETQRNG
HHHHHHHCHHHHHCC		20.5527251275
144PhosphorylationRAVDSFETQRNGLVF
HHHHCHHHHHCCEEE		30.7127251275
153PhosphorylationRNGLVFIYDMCGSNY
HCCEEEEEECCCCCC		6.0227251275
158PhosphorylationFIYDMCGSNYANFEL
EEEECCCCCCCEEEE		23.0327251275
160PhosphorylationYDMCGSNYANFELDL
EECCCCCCCEEEEHH		12.4827251275
170UbiquitinationFELDLGKKVLNLLKG
EEEHHHHHHHHHHCC		50.59-
176UbiquitinationKKVLNLLKGAFPARL
HHHHHHHCCCCCHHH		51.89-
185UbiquitinationAFPARLKKVLIVGAP
CCCHHHCEEEEECCC		47.0321890473
218UbiquitinationRERIQILKTSEVTQH
HHHHHHHCCCHHHHC		52.19-
300UbiquitinationDYVNARQKQGIYEEY
HHHHHHHHCCCCHHH		44.96-
304PhosphorylationARQKQGIYEEYEDIR
HHHHCCCCHHHHHHH		14.9928796482
307PhosphorylationKQGIYEEYEDIRREN
HCCCCHHHHHHHHHC		13.6328796482
318PhosphorylationRRENPVGTFHCSMSP
HHHCCCEEEECCCCC		15.5022199227
322PhosphorylationPVGTFHCSMSPGNLE
CCEEEECCCCCCCCC		17.4525159151
324PhosphorylationGTFHCSMSPGNLEKN
EEEECCCCCCCCCCC		17.2325159151
330UbiquitinationMSPGNLEKNRYGDVP
CCCCCCCCCCCCCCC		50.30-
333PhosphorylationGNLEKNRYGDVPCLD
CCCCCCCCCCCCCCC		27.3729052541
342PhosphorylationDVPCLDQTRVKLTKR
CCCCCCCCEEEEEEC		36.7829052541
357PhosphorylationSGHTQTDYINASFMD
CCCCCCCCEEHHHCC		10.2428796482
367UbiquitinationASFMDGYKQKNAYIG
HHHCCCCCCCCCCCC		61.39-
372PhosphorylationGYKQKNAYIGTQGPL
CCCCCCCCCCCCCCC		14.8521406692
375PhosphorylationQKNAYIGTQGPLENT
CCCCCCCCCCCCCCC		22.3120068231
382PhosphorylationTQGPLENTYRDFWLM
CCCCCCCCCHHHHHH		15.5721406692
383PhosphorylationQGPLENTYRDFWLMV
CCCCCCCCHHHHHHH		21.5521406692
442PhosphorylationGVENMNHYKKTTLEI
CCCCCCCCCCCEEEE		14.80-
444UbiquitinationENMNHYKKTTLEIHN
CCCCCCCCCEEEECC		39.31-
498SulfoxidationQSLAVSNMGARSKGQ
CCHHHCCCCCCCCCC		3.2821406390
503UbiquitinationSNMGARSKGQCPEPP
CCCCCCCCCCCCCCC		47.66-
557PhosphorylationMRTQRAFSIQTPEQY
HHCCCCCCCCCHHHH		16.8926552605
560PhosphorylationQRAFSIQTPEQYYFC
CCCCCCCCHHHHHHH		27.4227251275
564PhosphorylationSIQTPEQYYFCYKAI
CCCCHHHHHHHHHHH		9.2427251275
565PhosphorylationIQTPEQYYFCYKAIL
CCCHHHHHHHHHHHH		6.2026552605
568PhosphorylationPEQYYFCYKAILEFA
HHHHHHHHHHHHHHH		8.1127251275
592PhosphorylationQNLLAVESQ------
CCEEEEECC------		34.2925159151
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 PTN9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTN9_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 PTN9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RTN3_HUMANRTN3physical
16189514
RTN3_HUMANRTN3physical
25416956
ATRAP_HUMANAGTRAPphysical
25416956
REEP6_HUMANREEP6physical
25416956
MAL2_HUMANMAL2physical
25416956
CKLF5_HUMANCMTM5physical
25416956
LZTR1_HUMANLZTR1physical
27880917
PYC_HUMANPCphysical
27880917
FA26D_HUMANFAM26Dphysical
28514442
LZTR1_HUMANLZTR1physical
27432908
PTN9_HUMANPTPN9physical
27432908
GEMI8_HUMANGEMIN8physical
27432908
FSIP1_HUMANFSIP1physical
27432908
SMN_HUMANSMN1physical
27432908
DDX20_HUMANDDX20physical
27432908
GEMI4_HUMANGEMIN4physical
27432908
MPPA_HUMANPMPCAphysical
27432908
S39A7_HUMANSLC39A7physical
27432908
STRAP_HUMANSTRAPphysical
27432908
TBA3C_HUMANTUBA3Cphysical
27432908
AAR2_HUMANAAR2physical
27432908
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 PTN9_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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