PTPRU_HUMAN - dbPTM
PTPRU_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRU_HUMAN
UniProt AC Q92729
Protein Name Receptor-type tyrosine-protein phosphatase U
Gene Name PTPRU
Organism Homo sapiens (Human).
Sequence Length 1446
Subcellular Localization Cell junction . Cell membrane
Single-pass type I membrane protein .
Protein Description Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis..
Protein Sequence MARAQALVLALTFQLCAPETETPAAGCTFEEASDPAVPCEYSQAQYDDFQWEQVRIHPGTRAPADLPHGSYLMVNTSQHAPGQRAHVIFQSLSENDTHCVQFSYFLYSRDGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWPNEYQVLFEALISPDRRGYMGLDDILLLSYPCAKAPHFSRLGDVEVNAGQNASFQCMAAGRAAEAERFLLQRQSGALVPAAGVRHISHRRFLATFPLAAVSRAEQDLYRCVSQAPRGAGVSNFAELIVKEPPTPIAPPQLLRAGPTYLIIQLNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVSLQTYKLWHLDPDTEYEISVLLTRPGDGGTGRPGPPLISRTKCAEPMRAPKGLAFAEIQARQLTLQWEPLGYNVTRCHTYTVSLCYHYTLGSSHNQTIRECVKTEQGVSRYTIKNLLPYRNVHVRLVLTNPEGRKEGKEVTFQTDEDVPSGIAAESLTFTPLEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTGKGFGQAALTEITTNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISVYQVIVEEERARRLRREPGGQDCFPVPLTFEAALARGLVHYFGAELAASSLPEAMPFTVGDNQTYRGFWNPPLEPRKAYLIYFQAASHLKGETRLNCIRIARKAACKESKRPLEVSQRSEEMGLILGICAGGLAVLILLLGAIIVIIRKGRDHYAYSYYPKPVNMTKATVNYRQEKTHMMSAVDRSFTDQSTLQEDERLGLSFMDTHGYSTRGDQRSGGVTEASSLLGGSPRRPCGRKGSPYHTGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESFFEGWDATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTIPVSEFKATYKEMIRIDPQSNSSQLREEFQTLNSVTPPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISTDGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEGLESR
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
75N-linked_GlycosylationHGSYLMVNTSQHAPG
CCCEEEEECCCCCCC		21.76UniProtKB CARBOHYD
108PhosphorylationQFSYFLYSRDGHSPG
EEEEEEEECCCCCCC		26.4924719451
167PhosphorylationVLFEALISPDRRGYM
HHHHHHCCCCCCCCC		22.9224260401
207PhosphorylationVNAGQNASFQCMAAG
ECCCCCCCHHHHHCC		24.33-
283 (in isoform 4)Ubiquitination-58.4721906983
283 (in isoform 3)Ubiquitination-58.4721906983
283 (in isoform 2)Ubiquitination-58.4721906983
283 (in isoform 1)Ubiquitination-58.4721906983
283UbiquitinationNFAELIVKEPPTPIA
CCHHHHCCCCCCCCC		58.4722817900
410N-linked_GlycosylationQWEPLGYNVTRCHTY
EEEECCCEEEECEEE		27.21UniProtKB CARBOHYD
440UbiquitinationQTIRECVKTEQGVSR
HHHHHHHHHCCCCCC		58.99-
551PhosphorylationSKLRNETYHVFSNLH
HHHHHCEEEEECCCC		6.98-
563PhosphorylationNLHPGTTYLFSVRAR
CCCCCCEEEEEEECC		12.94-
623PhosphorylationQGRGAPISVYQVIVE
CCCCCCCEEEEEHHH		17.4523403867
625PhosphorylationRGAPISVYQVIVEEE
CCCCCEEEEEHHHHH		7.1123403867
685N-linked_GlycosylationMPFTVGDNQTYRGFW
CCEEECCCCEECCCC		30.11UniProtKB CARBOHYD
710PhosphorylationLIYFQAASHLKGETR
EEEHHHHHCCCCCHH		32.16-
804PhosphorylationQEKTHMMSAVDRSFT
HHHHHHHHHHCCHHC		19.9829449344
809PhosphorylationMMSAVDRSFTDQSTL
HHHHHCCHHCCHHHC		28.2126471730
811PhosphorylationSAVDRSFTDQSTLQE
HHHCCHHCCHHHCCC		34.0826471730
814PhosphorylationDRSFTDQSTLQEDER
CCHHCCHHHCCCHHH		33.6229449344
815PhosphorylationRSFTDQSTLQEDERL
CHHCCHHHCCCHHHH		27.1629449344
832PhosphorylationSFMDTHGYSTRGDQR
EEEECCCCCCCCCCC		10.1627642862
840PhosphorylationSTRGDQRSGGVTEAS
CCCCCCCCCCCCCHH		33.9823186163
843PhosphorylationGDQRSGGVTEASSLL
CCCCCCCCCCHHHHC		5.0932142685
844PhosphorylationDQRSGGVTEASSLLG
CCCCCCCCCHHHHCC		29.1628857561
847PhosphorylationSGGVTEASSLLGGSP
CCCCCCHHHHCCCCC		18.4530576142
848PhosphorylationGGVTEASSLLGGSPR
CCCCCHHHHCCCCCC		34.3629255136
853PhosphorylationASSLLGGSPRRPCGR
HHHHCCCCCCCCCCC		17.2719664994
857PhosphorylationLGGSPRRPCGRKGSP
CCCCCCCCCCCCCCC		26.6233259812
863PhosphorylationRPCGRKGSPYHTGQL
CCCCCCCCCCCCCCC		25.8930266825
865PhosphorylationCGRKGSPYHTGQLHP
CCCCCCCCCCCCCCH		17.4530266825
867PhosphorylationRKGSPYHTGQLHPAV
CCCCCCCCCCCCHHH		22.3030266825
925PhosphorylationRQEPMPAYDRHRVKL
CCCCCCCCHHCCCEE		13.98-
943PhosphorylationLGDPNADYINANYID
CCCCCCCCCCCEECC		8.1527642862
1114PhosphorylationCEGVVDIYNCVKTLC
CCCCHHHHHHHHHHH		9.6928796482
1209PhosphorylationRNRDKNRSMDVLPPD
CCCCCCCCCCCCCCC		28.82-
1345PhosphorylationHFQFLRWSAYRDTPD
EHHHHHHHHCCCCCC		14.6924719451
1418PhosphorylationAAKTLRNYKPNMVET
HHHHHHHCCCCHHEE		22.7629978859
1425PhosphorylationYKPNMVETMDQYHFC
CCCCHHEEHHHHCHH		18.0329978859
1429PhosphorylationMVETMDQYHFCYDVA
HHEEHHHHCHHHHHH		7.8129978859
1433PhosphorylationMDQYHFCYDVALEYL
HHHHCHHHHHHHHHH		16.7129978859
1439PhosphorylationCYDVALEYLEGLESR
HHHHHHHHHHHHHCC		15.7629978859
1445PhosphorylationEYLEGLESR------
HHHHHHHCC------		48.6229978859
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 PTPRU_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRU_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 PTPRU_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IRS1_HUMANIRS1physical
11781100
CTNB1_HUMANCTNNB1physical
16574648
EGFR_HUMANEGFRphysical
8870675
ARL2_HUMANARL2physical
27880917
RHG05_HUMANARHGAP5physical
27880917
NHS_HUMANNHSphysical
27880917
NHSL1_HUMANNHSL1physical
27880917
ST7_HUMANST7physical
27880917
MACOI_HUMANTMEM57physical
27880917
ABI2_HUMANABI2physical
27880917
PTPRK_HUMANPTPRKphysical
28514442
GOLI4_HUMANGOLIM4physical
28514442
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 PTPRU_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-848 AND SER-853, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-853, AND MASSSPECTROMETRY.

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