PTPRR_HUMAN - dbPTM
PTPRR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRR_HUMAN
UniProt AC Q15256
Protein Name Receptor-type tyrosine-protein phosphatase R
Gene Name PTPRR
Organism Homo sapiens (Human).
Sequence Length 657
Subcellular Localization Isoform Alpha: Cell membrane
Single-pass type I membrane protein.
Isoform Delta: Cytoplasm, perinuclear region. Locates to the perinuclear areas within the cytoplasm.
Isoform Gamma: Cytoplasm, perinuclear region. Locates to the perinuclear ar
Protein Description Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus (By similarity)..
Protein Sequence MRRAVCFPALCLLLNLHAAGCFSGNNDHFLAINQKKSGKPVFIYKHSQDIEKSLDIAPQKIYRHSYHSSSEAQVSKRHQIVNSAFPRPAYDPSLNLLAMDGQDLEVENLPIPAANVIVVTLQMDVNKLNITLLRIFRQGVAAALGLLPQQVHINRLIGKKNSIELFVSPINRKTGISDALPSEEVLRSLNINVLHQSLSQFGITEVSPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFVIIVTCLMILYRLKERFQLSLRQDKEKNQEIHLSPITLQPALSEAKTVHSMVQPEQAPKVLNVVVDPQGRGAPEIKATTATSVCPSPFKMKPIGLQERRGSNVSLTLDMSSLGNIEPFVSIPTPREKVAMEYLQSASRILTRSQLRDVVASSHLLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHALCLYESRLSAETVQ
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
44PhosphorylationSGKPVFIYKHSQDIE
CCCCEEEEECCCCHH		7.38-
47PhosphorylationPVFIYKHSQDIEKSL
CEEEEECCCCHHHHH		25.9526074081
53PhosphorylationHSQDIEKSLDIAPQK
CCCCHHHHHCCCCHH		20.6326074081
62PhosphorylationDIAPQKIYRHSYHSS
CCCCHHHHHCCCCCC		14.8726074081
129N-linked_GlycosylationQMDVNKLNITLLRIF
ECCHHHHHHHHHHHH		27.15UniProtKB CARBOHYD
258PhosphorylationLKERFQLSLRQDKEK
HHHHHCHHCCCCHHH		15.6624719451
272PhosphorylationKNQEIHLSPITLQPA
HCCCEEECCCCCHHH		10.4925159151
275PhosphorylationEIHLSPITLQPALSE
CEEECCCCCHHHHCC		23.7923312004
324PhosphorylationTATSVCPSPFKMKPI
EECCCCCCCCCCCCC		37.5325159151
339PhosphorylationGLQERRGSNVSLTLD
CCCCCCCCCEEEEEE		32.0421777200
342PhosphorylationERRGSNVSLTLDMSS
CCCCCCEEEEEEHHH		21.64-
358PhosphorylationGNIEPFVSIPTPREK
CCCCCCCCCCCHHHH		24.19-
361PhosphorylationEPFVSIPTPREKVAM
CCCCCCCCHHHHHHH		33.0511493009
370PhosphorylationREKVAMEYLQSASRI
HHHHHHHHHHHHHHH		9.2825884760
421PhosphorylationRHGTKNRYKTILPNP
CCCCCCCEEECCCCC		23.1326270265
423PhosphorylationGTKNRYKTILPNPLS
CCCCCEEECCCCCHH		20.8626270265
430PhosphorylationTILPNPLSRVCLRPK
ECCCCCHHCCCCCCC		24.7526270265
440PhosphorylationCLRPKNVTDSLSTYI
CCCCCCCCHHHHHHH		29.30-
456PhosphorylationANYIRGYSGKEKAFI
HHHCCCCCCCCCEEE		46.33-
504PhosphorylationKNEKCVLYWPEKRGI
HCCEEEEECCHHHCC		9.8729083192
529PhosphorylationVNECDNYTIRNLVLK
EECCCCEEEEEEEEC		21.5124719451
547PhosphorylationHTQHVKHYWYTSWPD
CCCCCEEEEECCCCC		8.3925884760
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
339SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRR_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 PTPRR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK01_HUMANMAPK1physical
9857190
MK03_HUMANMAPK3physical
9857190
MK07_HUMANMAPK7physical
12042304
MK03_HUMANMAPK3physical
10419510
MK01_HUMANMAPK1physical
10419510
MK01_HUMANMAPK1physical
26186194
MK14_HUMANMAPK14physical
26186194
MK01_HUMANMAPK1physical
25241761
P5CS_HUMANALDH18A1physical
27880917
DHYS_HUMANDHPSphysical
27880917
MK01_HUMANMAPK1physical
27880917
MK14_HUMANMAPK14physical
27880917
MK03_HUMANMAPK3physical
27880917
PNMA2_HUMANPNMA2physical
27880917
TRI11_HUMANTRIM11physical
27880917
WASC5_HUMANKIAA0196physical
27880917
TBCD5_HUMANTBC1D5physical
27880917
DJC13_HUMANDNAJC13physical
27880917
SNX6_HUMANSNX6physical
27880917
MK14_HUMANMAPK14physical
28514442
MK01_HUMANMAPK1physical
28514442
PTPRR_HUMANPTPRRphysical
27432908
MISSL_HUMANMAPK1IP1Lphysical
27432908
MK14_HUMANMAPK14physical
27432908
MAPK3_HUMANMAPKAPK3physical
27432908
MD2BP_HUMANMAD2L1BPphysical
27432908
TRI11_HUMANTRIM11physical
27432908
CBS_HUMANCBSphysical
27432908
MK11_HUMANMAPK11physical
27432908
DHYS_HUMANDHPSphysical
27432908
HS74L_HUMANHSPA4Lphysical
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 PTPRR_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-370, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory