EM55_HUMAN - dbPTM
EM55_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EM55_HUMAN
UniProt AC Q00013
Protein Name 55 kDa erythrocyte membrane protein
Gene Name MPP1
Organism Homo sapiens (Human).
Sequence Length 466
Subcellular Localization Membrane
Lipid-anchor. Cell projection, stereocilium. Colocalizes with WHRN at stereocilium tip during hair cell development (By similarity). Colocalizes with MPP5 in the retina, at the outer limiting membrane (OLM). Colocalizes with WHRN in the ret
Protein Description Essential regulator of neutrophil polarity. Regulates neutrophil polarization by regulating AKT1 phosphorylation through a mechanism that is independent of PIK3CG activity (By similarity)..
Protein Sequence MTLKASEGESGGSMHTALSDLYLEHLLQKRSRPEAVSHPLNTVTEDMYTNGSPAPGSPAQVKGQEVRKVRLIQFEKVTEEPMGITLKLNEKQSCTVARILHGGMIHRQGSLHVGDEILEINGTNVTNHSVDQLQKAMKETKGMISLKVIPNQQSRLPALQMFMRAQFDYDPKKDNLIPCKEAGLKFATGDIIQIINKDDSNWWQGRVEGSSKESAGLIPSPELQEWRVASMAQSAPSEAPSCSPFGKKKKYKDKYLAKHSSIFDQLDVVSYEEVVRLPAFKRKTLVLIGASGVGRSHIKNALLSQNPEKFVYPVPYTTRPPRKSEEDGKEYHFISTEEMTRNISANEFLEFGSYQGNMFGTKFETVHQIHKQNKIAILDIEPQTLKIVRTAELSPFIVFIAPTDQGTQTEALQQLQKDSEAIRSQYAHYFDLSLVNNGVDETLKKLQEAFDQACSSPQWVPVSWVY
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
2Acetylation------MTLKASEGE
------CCEECCCCC		36.6525944712
6Phosphorylation--MTLKASEGESGGS
--CCEECCCCCCCCC		44.5423186163
10PhosphorylationLKASEGESGGSMHTA
EECCCCCCCCCHHHH		60.3528796482
13PhosphorylationSEGESGGSMHTALSD
CCCCCCCCHHHHHHH		15.7728796482
16PhosphorylationESGGSMHTALSDLYL
CCCCCHHHHHHHHHH		22.2028796482
19PhosphorylationGSMHTALSDLYLEHL
CCHHHHHHHHHHHHH		24.0928796482
22PhosphorylationHTALSDLYLEHLLQK
HHHHHHHHHHHHHHH		18.2928796482
27 (in isoform 2)Phosphorylation-6.43-
29UbiquitinationYLEHLLQKRSRPEAV
HHHHHHHHCCCHHHH		52.92-
31PhosphorylationEHLLQKRSRPEAVSH
HHHHHHCCCHHHHCC		60.2627080861
37PhosphorylationRSRPEAVSHPLNTVT
CCCHHHHCCCCCCCC		26.8329978859
42PhosphorylationAVSHPLNTVTEDMYT
HHCCCCCCCCCCCCC		36.1729978859
44PhosphorylationSHPLNTVTEDMYTNG
CCCCCCCCCCCCCCC		24.9929978859
48PhosphorylationNTVTEDMYTNGSPAP
CCCCCCCCCCCCCCC		14.9128796482
49PhosphorylationTVTEDMYTNGSPAPG
CCCCCCCCCCCCCCC		26.8521712546
52PhosphorylationEDMYTNGSPAPGSPA
CCCCCCCCCCCCCCC		21.6926055452
57PhosphorylationNGSPAPGSPAQVKGQ
CCCCCCCCCCCCCCE		18.9223401153
76UbiquitinationVRLIQFEKVTEEPMG
EEEEEEEECCCCCCC		56.60-
91UbiquitinationITLKLNEKQSCTVAR
EEEEECCCCCCEEEE		46.57-
91AcetylationITLKLNEKQSCTVAR
EEEEECCCCCCEEEE		46.5725953088
110PhosphorylationGMIHRQGSLHVGDEI
CCCCCCCCEECCCEE		13.6323401153
147UbiquitinationTKGMISLKVIPNQQS
CCCCEEEEECCCCCC		31.18-
147AcetylationTKGMISLKVIPNQQS
CCCCEEEEECCCCCC		31.1825953088
154 (in isoform 3)Phosphorylation-26.48-
154PhosphorylationKVIPNQQSRLPALQM
EECCCCCCCCHHHHH		26.4823186163
180UbiquitinationKDNLIPCKEAGLKFA
CCCEEEHHHHCCEEC		45.29-
197UbiquitinationDIIQIINKDDSNWWQ
CEEEEEECCCCCCCC		53.13-
212AcetylationGRVEGSSKESAGLIP
CEECCCCHHCCCCCC		58.3423749302
212UbiquitinationGRVEGSSKESAGLIP
CEECCCCHHCCCCCC		58.34-
220PhosphorylationESAGLIPSPELQEWR
HCCCCCCCHHHHHHH		24.8223917254
230PhosphorylationLQEWRVASMAQSAPS
HHHHHHHHHHHCCCC		16.2820068231
231SulfoxidationQEWRVASMAQSAPSE
HHHHHHHHHHCCCCC		2.5821406390
234PhosphorylationRVASMAQSAPSEAPS
HHHHHHHCCCCCCCC		32.3920068231
237PhosphorylationSMAQSAPSEAPSCSP
HHHHCCCCCCCCCCC		46.2228450419
241PhosphorylationSAPSEAPSCSPFGKK
CCCCCCCCCCCCCCC		33.9823401153
243PhosphorylationPSEAPSCSPFGKKKK
CCCCCCCCCCCCCHH		27.8323401153
247UbiquitinationPSCSPFGKKKKYKDK
CCCCCCCCCHHHCHH		62.89-
247AcetylationPSCSPFGKKKKYKDK
CCCCCCCCCHHHCHH		62.8925953088
248UbiquitinationSCSPFGKKKKYKDKY
CCCCCCCCHHHCHHH		55.68-
251PhosphorylationPFGKKKKYKDKYLAK
CCCCCHHHCHHHHHH		33.04-
255PhosphorylationKKKYKDKYLAKHSSI
CHHHCHHHHHHCCCH		23.25-
258UbiquitinationYKDKYLAKHSSIFDQ
HCHHHHHHCCCHHHH		41.23-
260PhosphorylationDKYLAKHSSIFDQLD
HHHHHHCCCHHHHCC		25.1527080861
261PhosphorylationKYLAKHSSIFDQLDV
HHHHHCCCHHHHCCC		27.3028857561
281MethylationVVRLPAFKRKTLVLI
HCCCCCCCCCEEEEE		55.90-
291PhosphorylationTLVLIGASGVGRSHI
EEEEECCCCCCHHHH		28.8828270605
296PhosphorylationGASGVGRSHIKNALL
CCCCCCHHHHHHHHH		24.5228270605
299UbiquitinationGVGRSHIKNALLSQN
CCCHHHHHHHHHCCC		30.64-
309UbiquitinationLLSQNPEKFVYPVPY
HHCCCCCCCEECCCC		41.19-
316PhosphorylationKFVYPVPYTTRPPRK
CCEECCCCCCCCCCC		22.4522817900
317PhosphorylationFVYPVPYTTRPPRKS
CEECCCCCCCCCCCC		15.4023186163
318PhosphorylationVYPVPYTTRPPRKSE
EECCCCCCCCCCCCC		35.0223186163
323UbiquitinationYTTRPPRKSEEDGKE
CCCCCCCCCCCCCCE		68.91-
324PhosphorylationTTRPPRKSEEDGKEY
CCCCCCCCCCCCCEE		47.7123186163
329UbiquitinationRKSEEDGKEYHFIST
CCCCCCCCEEEEECH		68.38-
331PhosphorylationSEEDGKEYHFISTEE
CCCCCCEEEEECHHH		12.9117360941
335PhosphorylationGKEYHFISTEEMTRN
CCEEEEECHHHHCCC		28.9022210691
336PhosphorylationKEYHFISTEEMTRNI
CEEEEECHHHHCCCC		31.0224043423
340PhosphorylationFISTEEMTRNISANE
EECHHHHCCCCCHHH		24.6824043423
344PhosphorylationEEMTRNISANEFLEF
HHHCCCCCHHHHHHH		28.7027251275
371UbiquitinationETVHQIHKQNKIAIL
HHHHHHHHCCCEEEE		58.14-
374UbiquitinationHQIHKQNKIAILDIE
HHHHHCCCEEEEECC		30.90-
384PhosphorylationILDIEPQTLKIVRTA
EEECCCCCEEEEEEE		40.5127067055
386UbiquitinationDIEPQTLKIVRTAEL
ECCCCCEEEEEEEEC		42.41-
403PhosphorylationFIVFIAPTDQGTQTE
EEEEEECCCCCHHHH		31.7528857561
407PhosphorylationIAPTDQGTQTEALQQ
EECCCCCHHHHHHHH		27.0426657352
409PhosphorylationPTDQGTQTEALQQLQ
CCCCCHHHHHHHHHH		24.0628857561
417UbiquitinationEALQQLQKDSEAIRS
HHHHHHHHHHHHHHH		72.34-
424PhosphorylationKDSEAIRSQYAHYFD
HHHHHHHHHHHHHHH		22.7928450419
426PhosphorylationSEAIRSQYAHYFDLS
HHHHHHHHHHHHHHH		9.1528450419
429PhosphorylationIRSQYAHYFDLSLVN
HHHHHHHHHHHHHHC		7.2128450419
433PhosphorylationYAHYFDLSLVNNGVD
HHHHHHHHHHCCCHH		31.9228450419
442PhosphorylationVNNGVDETLKKLQEA
HCCCHHHHHHHHHHH		39.1428450419
466PhosphorylationWVPVSWVY-------
CEECCCCC-------		13.43-
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 EM55_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EM55_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 EM55_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AMOL2_HUMANAMOTL2physical
16189514
DNPEP_HUMANDNPEPphysical
25416956
KLH12_HUMANKLHL12physical
25416956
DKC1_HUMANDKC1physical
26496610
HDAC2_HUMANHDAC2physical
26496610
AGFG1_HUMANAGFG1physical
26496610
NCBP1_HUMANNCBP1physical
26496610
PRDX1_HUMANPRDX1physical
26496610
PRDX2_HUMANPRDX2physical
26496610
TAF1B_HUMANTAF1Bphysical
26496610
FA13A_HUMANFAM13Aphysical
26496610
PRDX5_HUMANPRDX5physical
26496610
TAF9B_HUMANTAF9Bphysical
26496610
MGN2_HUMANMAGOHBphysical
26496610
MTA70_HUMANMETTL3physical
26496610
CLSPN_HUMANCLSPNphysical
26496610
RT26_HUMANMRPS26physical
26496610
RT15_HUMANMRPS15physical
26496610
SARNP_HUMANSARNPphysical
26496610
NAF1_HUMANNAF1physical
26496610
F102B_HUMANFAM102Bphysical
26496610
MYH11_HUMANMYH11physical
28514442
HD_HUMANHTTphysical
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 EM55_HUMAN

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Related Literatures of Post-Translational Modification
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 THR-49; SER-57 AND SER-243,AND MASS SPECTROMETRY.

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