PTPRM_HUMAN - dbPTM
PTPRM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRM_HUMAN
UniProt AC P28827
Protein Name Receptor-type tyrosine-protein phosphatase mu
Gene Name PTPRM
Organism Homo sapiens (Human).
Sequence Length 1452
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control..
Protein Sequence MRGLGTCLATLAGLLLTAAGETFSGGCLFDEPYSTCGYSQSEGDDFNWEQVNTLTKPTSDPWMPSGSFMLVNASGRPEGQRAHLLLPQLKENDTHCIDFHYFVSSKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFWPNFYQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKEIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYLWIQLNANSINGDGPIVAREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTRPGEGGTGSPGPALRTRTKCADPMRGPRKLEVVEVKSRQITIRWEPFGYNVTRCHSYNLTVHYCYQVGGQEQVREEVSWDTENSHPQHTITNLSPYTNVSVKLILMNPEGRKESQELIVQTDEDLPGAVPTESIQGSTFEEKIFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNQSGRVSKLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPPATNQFTTKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERPRRTKKTTEILKCYPVPIHFQNASLLNSQYYFAAEFPADSLQAAQPFTIGDNKTYNGYWNTPLLPYKSYRIYFQAASRANGETKIDCVQVATKGAATPKPVPEPEKQTDHTVKIAGVIAGILLFVIIFLGVVLVMKKRKLAKKRKETMSSTRQEMTVMVNSMDKSYAEQGTNCDEAFSFMDTHNLNGRSVSSPSSFTMKTNTLSTSVPNSYYPDETHTMASDTSSLVQSHTYKKREPADVPYQTGQLHPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLCGDTSVPASQVRSLYYDMNKLDPQTNSSQIKEEFRTLNMVTPTLRVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNSG
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
53PhosphorylationFNWEQVNTLTKPTSD
CCHHHHCCCCCCCCC		36.6326437602
72N-linked_GlycosylationSGSFMLVNASGRPEG
CCCEEEECCCCCCCC		25.16UniProtKB CARBOHYD
92N-linked_GlycosylationLLPQLKENDTHCIDF
ECHHHCCCCCEEEEE		58.87UniProtKB CARBOHYD
131N-linked_GlycosylationPLGNPIWNISGDPTR
CCCCCCEECCCCCCC		21.1916335952
249N-linked_GlycosylationIASFNVVNTTKRDAG
EEEEEEEECCCCCCC		37.43UniProtKB CARBOHYD
264PhosphorylationKYRCMIRTEGGVGIS
CEEEEEEECCCCCCC		28.2318767875
271PhosphorylationTEGGVGISNYAELVV
ECCCCCCCCCEEEEE		20.1923532336
273PhosphorylationGGVGISNYAELVVKE
CCCCCCCCEEEEECC		8.4823532336
406N-linked_GlycosylationRWEPFGYNVTRCHSY
EEEECCCEEEEEEEC		29.12UniProtKB CARBOHYD
414N-linked_GlycosylationVTRCHSYNLTVHYCY
EEEEEECEEEEEEEE		32.05UniProtKB CARBOHYD
454N-linked_GlycosylationTNLSPYTNVSVKLIL
CCCCCCCCEEEEEEE		20.44UniProtKB CARBOHYD
524PhosphorylationEITYKAVSSFDPEID
EEHHHHHHCCCCCCC		30.10-
525PhosphorylationITYKAVSSFDPEIDL
EHHHHHHCCCCCCCC		27.37-
533PhosphorylationFDPEIDLSNQSGRVS
CCCCCCCCCCCCCEE		29.13-
534N-linked_GlycosylationDPEIDLSNQSGRVSK
CCCCCCCCCCCCEEE		47.54UniProtKB CARBOHYD
536PhosphorylationEIDLSNQSGRVSKLG
CCCCCCCCCCEEECC		32.58-
540PhosphorylationSNQSGRVSKLGNETH
CCCCCCEEECCCCCE		22.32-
544N-linked_GlycosylationGRVSKLGNETHFLFF
CCEEECCCCCEEEEE		62.52UniProtKB CARBOHYD
562PhosphorylationPGTTYSFTIRASTAK
CCCEEEEEEECCCCC		12.0124719451
598N-linked_GlycosylationYELETPLNQTDNTVT
EEECCCCCCCCCEEE		43.86UniProtKB CARBOHYD
637PhosphorylationPRRTKKTTEILKCYP
CCCCCCCCHHHHEEE		29.88-
651N-linked_GlycosylationPVPIHFQNASLLNSQ
ECCEEEECHHHCCCE		30.47UniProtKB CARBOHYD
681N-linked_GlycosylationQPFTIGDNKTYNGYW
CCEECCCCCCCCCCC		33.10UniProtKB CARBOHYD
726PhosphorylationVATKGAATPKPVPEP
EECCCCCCCCCCCCC		31.1724719451
778PhosphorylationKKRKETMSSTRQEMT
HHHHHHHHCHHHHHH		35.6628857561
779PhosphorylationKRKETMSSTRQEMTV
HHHHHHHCHHHHHHH		19.4528857561
785PhosphorylationSSTRQEMTVMVNSMD
HCHHHHHHHEEHHCC		12.5129255136
790PhosphorylationEMTVMVNSMDKSYAE
HHHHEEHHCCHHHHH		19.5629255136
818PhosphorylationTHNLNGRSVSSPSSF
CCCCCCCCCCCCCCE		27.9626437602
820PhosphorylationNLNGRSVSSPSSFTM
CCCCCCCCCCCCEEE		37.4730576142
820O-linked_GlycosylationNLNGRSVSSPSSFTM
CCCCCCCCCCCCEEE		37.4728657654
821PhosphorylationLNGRSVSSPSSFTMK
CCCCCCCCCCCEEEE		27.0125159151
823PhosphorylationGRSVSSPSSFTMKTN
CCCCCCCCCEEEEEC		39.7822199227
824PhosphorylationRSVSSPSSFTMKTNT
CCCCCCCCEEEEECC		28.2825159151
826PhosphorylationVSSPSSFTMKTNTLS
CCCCCCEEEEECCCC		21.5030576142
829PhosphorylationPSSFTMKTNTLSTSV
CCCEEEEECCCCCCC		23.7128857561
831PhosphorylationSFTMKTNTLSTSVPN
CEEEEECCCCCCCCC		27.5828857561
833PhosphorylationTMKTNTLSTSVPNSY
EEEECCCCCCCCCCC		19.3228857561
834PhosphorylationMKTNTLSTSVPNSYY
EEECCCCCCCCCCCC		36.5328857561
835PhosphorylationKTNTLSTSVPNSYYP
EECCCCCCCCCCCCC		32.0028857561
839PhosphorylationLSTSVPNSYYPDETH
CCCCCCCCCCCCCCC		21.7028348404
840PhosphorylationSTSVPNSYYPDETHT
CCCCCCCCCCCCCCC		26.1728348404
841PhosphorylationTSVPNSYYPDETHTM
CCCCCCCCCCCCCCC		12.2028348404
845PhosphorylationNSYYPDETHTMASDT
CCCCCCCCCCCCCCH		29.9928348404
847PhosphorylationYYPDETHTMASDTSS
CCCCCCCCCCCCHHH		23.1128348404
850PhosphorylationDETHTMASDTSSLVQ
CCCCCCCCCHHHHHH		30.5128348404
852PhosphorylationTHTMASDTSSLVQSH
CCCCCCCHHHHHHHC		20.0928348404
853PhosphorylationHTMASDTSSLVQSHT
CCCCCCHHHHHHHCC		27.0228348404
854PhosphorylationTMASDTSSLVQSHTY
CCCCCHHHHHHHCCC		34.3528348404
862UbiquitinationLVQSHTYKKREPADV
HHHHCCCCCCCCCCC		46.6529967540
871PhosphorylationREPADVPYQTGQLHP
CCCCCCCCCCCCCCH		20.6829255136
873PhosphorylationPADVPYQTGQLHPAI
CCCCCCCCCCCCHHH		22.5029255136
875UbiquitinationDVPYQTGQLHPAIRV
CCCCCCCCCCHHHHH		39.7329967540
929PhosphorylationENRMKNRYGNIIAYD
HHHHHHHCCCEEEEC		24.7421945579
935PhosphorylationRYGNIIAYDHSRVRL
HCCCEEEECCCEEEE		12.0928796482
938PhosphorylationNIIAYDHSRVRLQTI
CEEEECCCEEEEEEE		29.5828796482
1019PhosphorylationWPDDTEIYKDIKVTL
CCCCCHHHHHCEEEE		9.0730631047
1124PhosphorylationREGVVDIYNCVRELR
HCCCCHHHHHHHHHH		9.6927642862
1169PhosphorylationVPASQVRSLYYDMNK
CCHHHHHHHHHCHHC		23.1327642862
1171PhosphorylationASQVRSLYYDMNKLD
HHHHHHHHHCHHCCC		9.9227642862
1172PhosphorylationSQVRSLYYDMNKLDP
HHHHHHHHCHHCCCC		17.6327642862
1363PhosphorylationDTPVSKRSFLKLIRQ
CCCCCHHHHHHHHHH		38.3724719451
1373UbiquitinationKLIRQVDKWQEEYNG
HHHHHHHHHHHHHCC		52.5033845483
1376PhosphorylationRQVDKWQEEYNGGEG
HHHHHHHHHHCCCCC		62.4224719451
1385PhosphorylationYNGGEGRTVVHCLNG
HCCCCCEEEEEECCC		37.4222468782
1386UbiquitinationNGGEGRTVVHCLNGG
CCCCCEEEEEECCCC		2.3933845483
1398PhosphorylationNGGGRSGTFCAISIV
CCCCCCHHHHHHHHH		19.4522468782
1403PhosphorylationSGTFCAISIVCEMLR
CHHHHHHHHHHHHHC		7.1622468782
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 PTPRM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRM_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 PTPRM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTND1_HUMANCTNND1physical
10753936
DTBP1_HUMANDTNBP1physical
27880917
LMTK2_HUMANLMTK2physical
27880917
EHD4_HUMANEHD4physical
27880917
MRCKA_HUMANCDC42BPAphysical
27880917
NHSL1_HUMANNHSL1physical
27880917
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 PTPRM_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-131, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821 AND SER-824, ANDMASS SPECTROMETRY.

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