MPZL1_HUMAN - dbPTM
MPZL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPZL1_HUMAN
UniProt AC O95297
Protein Name Myelin protein zero-like protein 1
Gene Name MPZL1
Organism Homo sapiens (Human).
Sequence Length 269
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Cell surface receptor, which is involved in signal transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. Is a major receptor for concanavalin-A (ConA) and is involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases. Isoform 3 seems to have a dominant negative role; it blocks tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, may be involved in regulation of integrin-mediated cell motility..
Protein Sequence MAASAGAGAVIAAPDSRRWLWSVLAAALGLLTAGVSALEVYTPKEIFVANGTQGKLTCKFKSTSTTGGLTSVSWSFQPEGADTTVSFFHYSQGQVYLGNYPPFKDRISWAGDLDKKDASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYVVEKENLPVFPVWVVVGIVTAVVLGLTLLISMILAVLYRRKNSKRDYTGCSTSESLSPVKQAPRKSPSDTEGLVKSLPSGSHQGPVIYAQLDHSGGHHSDKINKSESVVYADIRKN
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
4Phosphorylation----MAASAGAGAVI
----CCCCCCCCEEE		20.0728188228
16PhosphorylationAVIAAPDSRRWLWSV
EEEECCCHHHHHHHH		23.7623401153
22PhosphorylationDSRRWLWSVLAAALG
CHHHHHHHHHHHHHH		12.70-
32PhosphorylationAAALGLLTAGVSALE
HHHHHHHHHCCCEEE		26.80-
50N-linked_GlycosylationPKEIFVANGTQGKLT
CCEEEEEECCCCEEE		49.0630392906
50N-linked_GlycosylationPKEIFVANGTQGKLT
CCEEEEEECCCCEEE		49.0630392906
55UbiquitinationVANGTQGKLTCKFKS
EEECCCCEEEEEEEE		30.70-
89 (in isoform 4)Ubiquitination-21.2321890473
107UbiquitinationYPPFKDRISWAGDLD
CCCCCCCEECCCCCC		6.0521890473
114 (in isoform 2)Ubiquitination-61.7821890473
115 (in isoform 3)Ubiquitination-60.9121906983
115 (in isoform 1)Ubiquitination-60.9121890473
115UbiquitinationSWAGDLDKKDASINI
ECCCCCCCCCCCEEE		60.9121906983
116UbiquitinationWAGDLDKKDASINIE
CCCCCCCCCCCEEEE		59.18-
119PhosphorylationDLDKKDASINIENMQ
CCCCCCCCEEEECEE		26.7125332170
130N-linked_GlycosylationENMQFIHNGTYICDV
ECEEEEECCEEEEEC		39.4230392906
133 (in isoform 4)Ubiquitination-10.8421890473
138UbiquitinationGTYICDVKNPPDIVV
CEEEEECCCCCCEEE		50.95-
151MethylationVVQPGHIRLYVVEKE
EECCCEEEEEEEECC		17.81115489747
196PhosphorylationVLYRRKNSKRDYTGC
HHHHHHCCCCCCCCC		31.9127794612
200PhosphorylationRKNSKRDYTGCSTSE
HHCCCCCCCCCCCCC		14.7425159151
200DephosphorylationRKNSKRDYTGCSTSE
HHCCCCCCCCCCCCC		14.749792637
200 (in isoform 3)Phosphorylation-14.7428796482
201 (in isoform 3)Phosphorylation-35.6828796482
201PhosphorylationKNSKRDYTGCSTSES
HCCCCCCCCCCCCCC		35.6823927012
204PhosphorylationKRDYTGCSTSESLSP
CCCCCCCCCCCCCCC		35.9930266825
205PhosphorylationRDYTGCSTSESLSPV
CCCCCCCCCCCCCCC		40.3630266825
205 (in isoform 3)Phosphorylation-40.3628796482
206PhosphorylationDYTGCSTSESLSPVK
CCCCCCCCCCCCCCC		14.6429255136
206 (in isoform 3)Phosphorylation-14.6428796482
208PhosphorylationTGCSTSESLSPVKQA
CCCCCCCCCCCCCCC		33.6429255136
209 (in isoform 3)Phosphorylation-6.1928796482
210PhosphorylationCSTSESLSPVKQAPR
CCCCCCCCCCCCCCC		36.6119664994
212 (in isoform 2)Ubiquitination-6.8821890473
213 (in isoform 1)Ubiquitination-44.0921890473
213UbiquitinationSESLSPVKQAPRKSP
CCCCCCCCCCCCCCC		44.0921906983
218UbiquitinationPVKQAPRKSPSDTEG
CCCCCCCCCCCCCCC		66.70-
219PhosphorylationVKQAPRKSPSDTEGL
CCCCCCCCCCCCCCH		30.8029255136
221PhosphorylationQAPRKSPSDTEGLVK
CCCCCCCCCCCCHHH		65.3429255136
223PhosphorylationPRKSPSDTEGLVKSL
CCCCCCCCCCHHHCC		35.9730266825
227 (in isoform 2)Ubiquitination-6.10-
228UbiquitinationSDTEGLVKSLPSGSH
CCCCCHHHCCCCCCC		51.85-
229PhosphorylationDTEGLVKSLPSGSHQ
CCCCHHHCCCCCCCC		37.7221945579
232PhosphorylationGLVKSLPSGSHQGPV
CHHHCCCCCCCCCCE		59.2121945579
234PhosphorylationVKSLPSGSHQGPVIY
HHCCCCCCCCCCEEE		19.5821945579
241DephosphorylationSHQGPVIYAQLDHSG
CCCCCEEEEEECCCC		6.6310681522
241PhosphorylationSHQGPVIYAQLDHSG
CCCCCEEEEEECCCC		6.6321945579
247PhosphorylationIYAQLDHSGGHHSDK
EEEEECCCCCCCCCC		46.2521945579
252PhosphorylationDHSGGHHSDKINKSE
CCCCCCCCCCCCCCC		34.6221945579
254UbiquitinationSGGHHSDKINKSESV
CCCCCCCCCCCCCCE		51.71-
256 (in isoform 2)Ubiquitination-47.7621890473
257UbiquitinationHHSDKINKSESVVYA
CCCCCCCCCCCEEEE		60.1021890473
257 (in isoform 1)Ubiquitination-60.1021890473
258PhosphorylationHSDKINKSESVVYAD
CCCCCCCCCCEEEEE		30.5321945579
260PhosphorylationDKINKSESVVYADIR
CCCCCCCCEEEEECC		24.7923927012
263DephosphorylationNKSESVVYADIRKN-
CCCCCEEEEECCCC-		9.0810681522
263PhosphorylationNKSESVVYADIRKN-
CCCCCEEEEECCCC-		9.0819664994
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
241YPhosphorylationKinaseSRCP12931
PSP
241YPhosphorylationKinaseSRC64-PhosphoELM
263YPhosphorylationKinaseSRCP12931
PSP
263YPhosphorylationKinaseSRC64-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPZL1_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 MPZL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN11_HUMANPTPN11physical
9792637
SRC_HUMANSRCphysical
11751924
IFIH1_HUMANIFIH1physical
28514442
PTN11_HUMANPTPN11physical
28514442
FTO_HUMANFTOphysical
28514442
ACTBL_HUMANACTBL2physical
28514442
AL1A2_HUMANALDH1A2physical
28514442
CBWD1_HUMANCBWD1physical
28514442
DPOA2_HUMANPOLA2physical
28514442
HSP7C_HUMANHSPA8physical
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 MPZL1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50, AND MASS SPECTROMETRY.
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-241; SER-260 ANDTYR-263, AND MASS 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-221, AND MASSSPECTROMETRY.
"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-204; SER-208; SER-210;SER-219; SER-260 AND TYR-263, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 AND SER-219, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, 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-263, AND MASSSPECTROMETRY.
"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-241 AND TYR-263, ANDMASS SPECTROMETRY.
"Dissecting the interaction of SHP-2 with PZR, an immunoglobulinfamily protein containing immunoreceptor tyrosine-based inhibitorymotifs.";
Zhao R., Zhao Z.J.;
J. Biol. Chem. 275:5453-5459(2000).
Cited for: PHOSPHORYLATION AT TYR-241 AND TYR-263, INTERACTION WITH PTPN11,DEPHOSPHORYLATION BY PTPN11, AND MUTAGENESIS OF TYR-241 AND TYR-263.

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