PTPRE_HUMAN - dbPTM
PTPRE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRE_HUMAN
UniProt AC P23469
Protein Name Receptor-type tyrosine-protein phosphatase epsilon
Gene Name PTPRE
Organism Homo sapiens (Human).
Sequence Length 700
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Cytoplasm. Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin induces translocation to the membrane (By similarity)..
Isoform 3
Protein Description Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity).; Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake (By similarity).; Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+)..
Protein Sequence MEPLCPLLLVGFSLPLARALRGNETTADSNETTTTSGPPDPGASQPLLAWLLLPLLLLLLVLLLAAYFFRFRKQRKAVVSTSDKKMPNGILEEQEQQRVMLLSRSPSGPKKYFPIPVEHLEEEIRIRSADDCKQFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCHQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIQPQLPDGCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPVHAGPIVVHCSAGVGRTGTFIVIDAMMAMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYTFIYQALLEYYLYGDTELDVSSLEKHLQTMHGTTTHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEYTDYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMIWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGEITIEIKNDTLSEAISIRDFLVTLNQPQARQEEQVRVVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIFSDYANFK
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
23N-linked_GlycosylationLARALRGNETTADSN
HHHHHCCCCCCCCCC		36.69UniProtKB CARBOHYD
30N-linked_GlycosylationNETTADSNETTTTSG
CCCCCCCCCCCCCCC		51.70UniProtKB CARBOHYD
80PhosphorylationKQRKAVVSTSDKKMP
HHHCCEEECCCCCCC		18.6528102081
81PhosphorylationQRKAVVSTSDKKMPN
HHCCEEECCCCCCCC		29.3628102081
82PhosphorylationRKAVVSTSDKKMPNG
HCCEEECCCCCCCCC		39.6728102081
84AcetylationAVVSTSDKKMPNGIL
CEEECCCCCCCCCCC		51.2223749302
103PhosphorylationQQRVMLLSRSPSGPK
HHHHHEEECCCCCCC		27.1023403867
105PhosphorylationRVMLLSRSPSGPKKY
HHHEEECCCCCCCCC		21.7523403867
107PhosphorylationMLLSRSPSGPKKYFP
HEEECCCCCCCCCCC		69.8128464451
111UbiquitinationRSPSGPKKYFPIPVE
CCCCCCCCCCCCCHH		56.08-
112PhosphorylationSPSGPKKYFPIPVEH
CCCCCCCCCCCCHHH		22.2528634298
165PhosphorylationENREKNRYPNILPND
HHHHHCCCCCCCCCC		15.27-
174PhosphorylationNILPNDHSRVILSQL
CCCCCCCCHHHHHHC		30.98-
199UbiquitinationASYIDGYKEKNKFIA
HHHCCCHHHHCCEEE		68.68-
226MethylationWRMVWEQKSATIVML
HHHHHHHHCCEEEEE		30.4623644510
237MethylationIVMLTNLKERKEEKC
EEEECCHHHHHHHHH		58.5023644510
273PhosphorylationCVVLVDYTIRKFCIQ
CEEEEEHHHHHHCCC		15.1624719451
395 (in isoform 2)Ubiquitination-5.5321906983
423UbiquitinationGTTTHFDKIGLEEEF
CCCCHHHHCCCHHHH		37.42-
423AcetylationGTTTHFDKIGLEEEF
CCCCHHHHCCCHHHH		37.427965419
434PhosphorylationEEEFRKLTNVRIMKE
HHHHHHHHCCHHHHH		34.4023532336
440UbiquitinationLTNVRIMKENMRTGN
HHCCHHHHHHCCCCC		43.49-
440AcetylationLTNVRIMKENMRTGN
HHCCHHHHHHCCCCC		43.497668321
445PhosphorylationIMKENMRTGNLPANM
HHHHHCCCCCCCCCC		21.4729116813
453UbiquitinationGNLPANMKKARVIQI
CCCCCCCCEEEEEEE		42.99-
454UbiquitinationNLPANMKKARVIQII
CCCCCCCEEEEEEEC		30.56-
454AcetylationNLPANMKKARVIQII
CCCCCCCEEEEEEEC		30.567668335
464 (in isoform 1)Ubiquitination-29.0521906983
478PhosphorylationSMKRGQEYTDYINAS
HCCCCCCHHCCCCHH		9.3127642862
479PhosphorylationMKRGQEYTDYINASF
CCCCCCHHCCCCHHH		22.9027642862
481PhosphorylationRGQEYTDYINASFID
CCCCHHCCCCHHHCC		6.5627642862
485PhosphorylationYTDYINASFIDGYRQ
HHCCCCHHHCCCCCC		20.4624043423
490PhosphorylationNASFIDGYRQKDYFI
CHHHCCCCCCCCEEE		13.2124043423
605 (in isoform 2)Ubiquitination-36.4921906983
631PhosphorylationHPITVHCSAGAGRTG
CCEEEEEECCCCCCH		18.1728122231
651UbiquitinationSNILERVKAEGLLDV
HHHHHHHHHCCHHHH		47.11-
663UbiquitinationLDVFQAVKSLRLQRP
HHHHHHHHHHCCCCC		46.952190698
664PhosphorylationDVFQAVKSLRLQRPH
HHHHHHHHHCCCCCC		16.4827251275
674 (in isoform 1)Ubiquitination-32.5621906983
679PhosphorylationMVQTLEQYEFCYKVV
HHHHHHHHHHHHHHH		11.12-
694PhosphorylationQDFIDIFSDYANFK-
HHHHHHHHHHHCCC-		30.0028796482
696PhosphorylationFIDIFSDYANFK---
HHHHHHHHHCCC---		11.4012121439
700AcetylationFSDYANFK-------
HHHHHCCC-------		60.2768685
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 PTPRE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRE_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 PTPRE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCNB1_HUMANKCNB1physical
10921884
BZW2_HUMANBZW2physical
27880917
CPVL_HUMANCPVLphysical
27880917
XPO2_HUMANCSE1Lphysical
27880917
GRB2_HUMANGRB2physical
27880917
SAAL1_HUMANSAAL1physical
27880917
XPO1_HUMANXPO1physical
27880917
XPO4_HUMANXPO4physical
27880917
XPOT_HUMANXPOTphysical
27880917
WASF1_HUMANWASF1physical
27880917
CYFP2_HUMANCYFIP2physical
27880917
ABI2_HUMANABI2physical
27880917
EFR3A_HUMANEFR3Aphysical
27880917
BAIP2_HUMANBAIAP2physical
27880917
DLG1_HUMANDLG1physical
27880917
VATL_HUMANATP6V0Cphysical
28514442
PTPRE_HUMANPTPREphysical
27432908
XPO4_HUMANXPO4physical
27432908
SAAL1_HUMANSAAL1physical
27432908
TNPO2_HUMANTNPO2physical
27432908
YIF1B_HUMANYIF1Bphysical
27432908
CERS2_HUMANCERS2physical
27432908
CERS3_HUMANCERS3physical
27432908
TP4A1_HUMANPTP4A1physical
27432908
TNPO3_HUMANTNPO3physical
27432908
SE1L1_HUMANSEL1Lphysical
27432908
S61A2_HUMANSEC61A2physical
27432908
XPO2_HUMANCSE1Lphysical
27432908
TNPO1_HUMANTNPO1physical
27432908
CALX_HUMANCANXphysical
27432908
GLU2B_HUMANPRKCSHphysical
27432908
IPO5_HUMANIPO5physical
27432908
IPO9_HUMANIPO9physical
27432908
PGRC1_HUMANPGRMC1physical
27432908
GANAB_HUMANGANABphysical
27432908
ATPO_HUMANATP5Ophysical
27432908
XPO1_HUMANXPO1physical
27432908
IPO7_HUMANIPO7physical
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
DB00630Alendronate
Regulatory Network of PTPRE_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 TYR-696, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-696, AND MASSSPECTROMETRY.

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