PTN7_HUMAN - dbPTM
PTN7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTN7_HUMAN
UniProt AC P35236
Protein Name Tyrosine-protein phosphatase non-receptor type 7
Gene Name PTPN7
Organism Homo sapiens (Human).
Sequence Length 360
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton.
Protein Description Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction..
Protein Sequence MVQAHGGRSRAQPLTLSLGAAMTQPPPEKTPAKKHVRLQERRGSNVALMLDVRSLGAVEPICSVNTPREVTLHFLRTAGHPLTRWALQRQPPSPKQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYAGQLPEEPSP
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
4 (in isoform 2)Phosphorylation-7.5930108239
9PhosphorylationVQAHGGRSRAQPLTL
CCCCCCCCCCCCEEE		34.93-
20 (in isoform 2)Phosphorylation-10.1924719451
23PhosphorylationLSLGAAMTQPPPEKT
EEECCCCCCCCCCCC		32.9529083192
30PhosphorylationTQPPPEKTPAKKHVR
CCCCCCCCCCHHHHH		27.1529083192
39 (in isoform 2)Phosphorylation-31.42-
42MethylationHVRLQERRGSNVALM
HHHHHHHCCCCEEEE		52.73115385305
44PhosphorylationRLQERRGSNVALMLD
HHHHHCCCCEEEEEE		26.7323401153
54PhosphorylationALMLDVRSLGAVEPI
EEEEEECCCCCEECE		30.8826552605
63PhosphorylationGAVEPICSVNTPREV
CCEECEEECCCCCEE		21.0823401153
66PhosphorylationEPICSVNTPREVTLH
ECEEECCCCCEEEHH		22.9023401153
71PhosphorylationVNTPREVTLHFLRTA
CCCCCEEEHHHHHHC		15.1228634298
73 (in isoform 2)Ubiquitination-15.44-
83 (in isoform 2)Phosphorylation-28.7224719451
93PhosphorylationALQRQPPSPKQLEEE
HHHHCCCCHHHHHHH		51.9528464451
103UbiquitinationQLEEEFLKIPSNFVS
HHHHHHHCCCCCCCC		58.87-
105 (in isoform 3)Phosphorylation-22.95-
106PhosphorylationEEFLKIPSNFVSPED
HHHHCCCCCCCCHHH		46.5028464451
110PhosphorylationKIPSNFVSPEDLDIP
CCCCCCCCHHHCCCC		20.5928348404
114 (in isoform 3)Phosphorylation-6.49-
122UbiquitinationDIPGHASKDRYKTIL
CCCCCCCCCCCCCCC		47.19-
126UbiquitinationHASKDRYKTILPNPQ
CCCCCCCCCCCCCCC		29.95-
134PhosphorylationTILPNPQSRVCLGRA
CCCCCCCCCEECCCC		28.1216479000
142 (in isoform 2)Ubiquitination-44.26-
143PhosphorylationVCLGRAQSQEDGDYI
EECCCCCCCCCCCCC		34.2523401153
149 (in isoform 3)Phosphorylation-11.1227251275
149PhosphorylationQSQEDGDYINANYIR
CCCCCCCCCCCEEEE		11.1228796482
154PhosphorylationGDYINANYIRGYDGK
CCCCCCEEEECCCCC		6.9228796482
159 (in isoform 3)Phosphorylation-65.5927251275
161 (in isoform 2)Ubiquitination-52.01-
165 (in isoform 2)Ubiquitination-8.91-
171PhosphorylationVYIATQGPMPNTVSD
EEEEECCCCCCCHHH		25.8210206983
171 (in isoform 3)Phosphorylation-25.8227251275
177PhosphorylationGPMPNTVSDFWEMVW
CCCCCCHHHHHHHHH		25.67-
182 (in isoform 2)Phosphorylation-2.4324719451
198PhosphorylationIVMLTQLREGKEKCV
HHHHHHHHCCCCCCE		40.5810206983
203UbiquitinationQLREGKEKCVHYWPT
HHHCCCCCCEEECCC		45.07-
210PhosphorylationKCVHYWPTEEETYGP
CCEEECCCCCCCCCC		41.71-
214PhosphorylationYWPTEEETYGPFQIR
ECCCCCCCCCCEEEE		36.74-
215PhosphorylationWPTEEETYGPFQIRI
CCCCCCCCCCEEEEE		26.53-
215 (in isoform 3)Phosphorylation-26.5327251275
226UbiquitinationQIRIQDMKECPEYTV
EEEEECHHHCCCCEE		65.54-
242 (in isoform 2)Ubiquitination-48.84-
246PhosphorylationQYQEERRSVKHILFS
HHHHHHHCCCEEEEE		41.5616479000
248 (in isoform 3)Phosphorylation-26.6127642862
254 (in isoform 3)Phosphorylation-17.9427642862
259 (in isoform 3)Phosphorylation-67.1627642862
265 (in isoform 2)Ubiquitination-23.75-
277O-linked_GlycosylationLVAEVEESPETAAHP
HHEEHHCCCCCCCCC		17.9629351928
287 (in isoform 2)Ubiquitination-6.65-
291OxidationPGPIVVHCSAGIGRT
CCCEEEECCCCCCHH		1.69-
291Cysteine sulfenic acid (-SOH)PGPIVVHCSAGIGRT
CCCEEEECCCCCCHH		1.69-
298O-linked_GlycosylationCSAGIGRTGCFIATR
CCCCCCHHCCEEEEH		32.8429351928
312UbiquitinationRIGCQQLKARGEVDI
HHCCHHHHHCCCCCE		31.53-
312AcetylationRIGCQQLKARGEVDI
HHCCHHHHHCCCCCE		31.5325953088
351 (in isoform 2)Ubiquitination-10.50-
359PhosphorylationGQLPEEPSP------
CCCCCCCCC------		46.6628450419
464 (in isoform 3)Phosphorylation-27251275
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
44SPhosphorylationKinasePRKACAP17612
GPS
44SPhosphorylationKinasePRKCQQ04759
GPS
44SPhosphorylationKinasePKA-FAMILY-GPS
44SPhosphorylationKinasePKA_GROUP-PhosphoELM
66TPhosphorylationKinaseMAPK1P28482
GPS
66TPhosphorylationKinaseMAPK14Q16539
GPS
93SPhosphorylationKinaseMAPK1P28482
GPS
93SPhosphorylationKinaseMAPK14Q16539
GPS
246SPhosphorylationKinasePRKCQQ04759
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTN7_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 PTN7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK01_HUMANMAPK1physical
10702794
MK03_HUMANMAPK3physical
10702794
MK03_HUMANMAPK3physical
10559944
MK03_HUMANMAPK3physical
10206983
MK01_HUMANMAPK1physical
10206983
A4_HUMANAPPphysical
21832049
GMCL1_HUMANGMCL1physical
25416956
CCD57_HUMANCCDC57physical
25416956
MK01_HUMANMAPK1physical
25241761
MK14_HUMANMAPK14physical
25241761
DHYS_HUMANDHPSphysical
27880917
MK01_HUMANMAPK1physical
27880917
MK14_HUMANMAPK14physical
27880917
MK03_HUMANMAPK3physical
27880917
MAOX_HUMANME1physical
27880917
OPA1_HUMANOPA1physical
27880917
PAK4_HUMANPAK4physical
27880917
RFA3_HUMANRPA3physical
27880917
PTN7_HUMANPTPN7physical
27432908
MAPK3_HUMANMAPKAPK3physical
27432908
MPPA_HUMANPMPCAphysical
27432908
MISSL_HUMANMAPK1IP1Lphysical
27432908
MK14_HUMANMAPK14physical
27432908
DCA10_HUMANDCAF10physical
27432908
MK11_HUMANMAPK11physical
27432908
MPPB_HUMANPMPCBphysical
27432908
PNMA2_HUMANPNMA2physical
27432908
SSBP_HUMANSSBP1physical
27432908
RS12_HUMANRPS12physical
27432908
BGAL_HUMANGLB1physical
27432908
ACD11_HUMANACAD11physical
27432908
AROS_HUMANRPS19BP1physical
27432908
MACD1_HUMANMACROD1physical
27432908
SAV1_HUMANSAV1physical
27432908
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTN7_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-143, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND THR-66, AND MASSSPECTROMETRY.
"Haematopoietic protein tyrosine phosphatase (HePTP) phosphorylationby cAMP-dependent protein kinase in T-cells: dynamics and subcellularlocation.";
Nika K., Hyunh H., Williams S., Paul S., Bottini N., Tasken K.,Lombroso P.J., Mustelin T.;
Biochem. J. 378:335-342(2004).
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-44, AND MUTAGENESIS OFSER-44.
"Crosstalk between cAMP-dependent kinase and MAP kinase through aprotein tyrosine phosphatase.";
Saxena M., Williams S., Tasken K., Mustelin T.;
Nat. Cell Biol. 1:305-311(1999).
Cited for: FUNCTION, INTERACTION WITH MAPK1, AND PHOSPHORYLATION AT SER-44.
"Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP).";
Saxena M., Williams S., Brockdorff J., Gilman J., Mustelin T.;
J. Biol. Chem. 274:11693-11700(1999).
Cited for: FUNCTION, INTERACTION WITH MAPK1 AND MAPK3, PHOSPHORYLATION AT THR-66AND SER-93, AND MUTAGENESIS OF THR-66 AND SER-93.

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