PIEZ1_HUMAN - dbPTM
PIEZ1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIEZ1_HUMAN
UniProt AC Q92508
Protein Name Piezo-type mechanosensitive ion channel component 1
Gene Name PIEZO1
Organism Homo sapiens (Human).
Sequence Length 2521
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane . Cell membrane
Multi-pass membrane protein . Cell projection, lamellipodium membrane . In erythrocytes, located in the plas
Protein Description Pore-forming subunit of a mechanosensitive non-specific cation channel. [PubMed: 23479567]
Protein Sequence MEPHVLGAVLYWLLLPCALLAACLLRFSGLSLVYLLFLLLLPWFPGPTRCGLQGHTGRLLRALLGLSLLFLVAHLALQICLHIVPRLDQLLGPSCSRWETLSRHIGVTRLDLKDIPNAIRLVAPDLGILVVSSVCLGICGRLARNTRQSPHPRELDDDERDVDASPTAGLQEAATLAPTRRSRLAARFRVTAHWLLVAAGRVLAVTLLALAGIAHPSALSSVYLLLFLALCTWWACHFPISTRGFSRLCVAVGCFGAGHLICLYCYQMPLAQALLPPAGIWARVLGLKDFVGPTNCSSPHALVLNTGLDWPVYASPGVLLLLCYATASLRKLRAYRPSGQRKEAAKGYEARELELAELDQWPQERESDQHVVPTAPDTEADNCIVHELTGQSSVLRRPVRPKRAEPREASPLHSLGHLIMDQSYVCALIAMMVWSITYHSWLTFVLLLWACLIWTVRSRHQLAMLCSPCILLYGMTLCCLRYVWAMDLRPELPTTLGPVSLRQLGLEHTRYPCLDLGAMLLYTLTFWLLLRQFVKEKLLKWAESPAALTEVTVADTEPTRTQTLLQSLGELVKGVYAKYWIYVCAGMFIVVSFAGRLVVYKIVYMFLFLLCLTLFQVYYSLWRKLLKAFWWLVVAYTMLVLIAVYTFQFQDFPAYWRNLTGFTDEQLGDLGLEQFSVSELFSSILVPGFFLLACILQLHYFHRPFMQLTDMEHVSLPGTRLPRWAHRQDAVSGTPLLREEQQEHQQQQQEEEEEEEDSRDEGLGVATPHQATQVPEGAAKWGLVAERLLELAAGFSDVLSRVQVFLRRLLELHVFKLVALYTVWVALKEVSVMNLLLVVLWAFALPYPRFRPMASCLSTVWTCVIIVCKMLYQLKVVNPQEYSSNCTEPFPNSTNLLPTEISQSLLYRGPVDPANWFGVRKGFPNLGYIQNHLQVLLLLVFEAIVYRRQEHYRRQHQLAPLPAQAVFASGTRQQLDQDLLGCLKYFINFFFYKFGLEICFLMAVNVIGQRMNFLVTLHGCWLVAILTRRHRQAIARLWPNYCLFLALFLLYQYLLCLGMPPALCIDYPWRWSRAVPMNSALIKWLYLPDFFRAPNSTNLISDFLLLLCASQQWQVFSAERTEEWQRMAGVNTDRLEPLRGEPNPVPNFIHCRSYLDMLKVAVFRYLFWLVLVVVFVTGATRISIFGLGYLLACFYLLLFGTALLQRDTRARLVLWDCLILYNVTVIISKNMLSLLACVFVEQMQTGFCWVIQLFSLVCTVKGYYDPKEMMDRDQDCLLPVEEAGIIWDSVCFFFLLLQRRVFLSHYYLHVRADLQATALLASRGFALYNAANLKSIDFHRRIEEKSLAQLKRQMERIRAKQEKHRQGRVDRSRPQDTLGPKDPGLEPGPDSPGGSSPPRRQWWRPWLDHATVIHSGDYFLFESDSEEEEEAVPEDPRPSAQSAFQLAYQAWVTNAQAVLRRRQQEQEQARQEQAGQLPTGGGPSQEVEPAEGPEEAAAGRSHVVQRVLSTAQFLWMLGQALVDELTRWLQEFTRHHGTMSDVLRAERYLLTQELLQGGEVHRGVLDQLYTSQAEATLPGPTEAPNAPSTVSSGLGAEEPLSSMTDDMGSPLSTGYHTRSGSEEAVTDPGEREAGASLYQGLMRTASELLLDRRLRIPELEEAELFAEGQGRALRLLRAVYQCVAAHSELLCYFIIILNHMVTASAGSLVLPVLVFLWAMLSIPRPSKRFWMTAIVFTEIAVVVKYLFQFGFFPWNSHVVLRRYENKPYFPPRILGLEKTDGYIKYDLVQLMALFFHRSQLLCYGLWDHEEDSPSKEHDKSGEEEQGAEEGPGVPAATTEDHIQVEARVGPTDGTPEPQVELRPRDTRRISLRFRRRKKEGPARKGAAAIEAEDREEEEGEEEKEAPTGREKRPSRSGGRVRAAGRRLQGFCLSLAQGTYRPLRRFFHDILHTKYRAATDVYALMFLADVVDFIIIIFGFWAFGKHSAATDITSSLSDDQVPEAFLVMLLIQFSTMVVDRALYLRKTVLGKLAFQVALVLAIHLWMFFILPAVTERMFNQNVVAQLWYFVKCIYFALSAYQIRCGYPTRILGNFLTKKYNHLNLFLFQGFRLVPFLVELRAVMDWVWTDTTLSLSSWMCVEDIYANIFIIKCSRETEKKYPQPKGQKKKKIVKYGMGGLIILFLIAIIWFPLLFMSLVRSVVGVVNQPIDVTVTLKLGGYEPLFTMSAQQPSIIPFTAQAYEELSRQFDPQPLAMQFISQYSPEDIVTAQIEGSSGALWRISPPSRAQMKRELYNGTADITLRFTWNFQRDLAKGGTVEYANEKHMLALAPNSTARRQLASLLEGTSDQSVVIPNLFPKYIRAPNGPEANPVKQLQPNEEADYLGVRIQLRREQGAGATGFLEWWVIELQECRTDCNLLPMVIFSDKVSPPSLGFLAGYGIMGLYVSIVLVIGKFVRGFFSEISHSIMFEELPCVDRILKLCQDIFLVRETRELELEEELYAKLIFLYRSPETMIKWTREKE
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
11PhosphorylationHVLGAVLYWLLLPCA
HHHHHHHHHHHHHHH		6.3424043423
100PhosphorylationPSCSRWETLSRHIGV
CCCHHHHHHHHHCCC		24.0729083192
102PhosphorylationCSRWETLSRHIGVTR
CHHHHHHHHHCCCCC		29.2729083192
108PhosphorylationLSRHIGVTRLDLKDI
HHHHCCCCCCCCCHH		21.9429083192
113UbiquitinationGVTRLDLKDIPNAIR
CCCCCCCCHHCCHHH		53.9623000965
146PhosphorylationCGRLARNTRQSPHPR
HHHHHHCCCCCCCCC		25.2426699800
149PhosphorylationLARNTRQSPHPRELD
HHHCCCCCCCCCCCC		23.1426699800
165PhosphorylationDERDVDASPTAGLQE
CCCCCCCCCCCCHHH		20.5130266825
167PhosphorylationRDVDASPTAGLQEAA
CCCCCCCCCCHHHHH		30.7530266825
175PhosphorylationAGLQEAATLAPTRRS
CCHHHHHHHCCCHHH		30.4229255136
179PhosphorylationEAATLAPTRRSRLAA
HHHHHCCCHHHHHHH		32.8629255136
295N-linked_GlycosylationKDFVGPTNCSSPHAL
CCCCCCCCCCCCCEE		27.14UniProtKB CARBOHYD
346UbiquitinationGQRKEAAKGYEAREL
CCCHHHHCCCCHHHH		69.9029967540
367PhosphorylationQWPQERESDQHVVPT
CCCCHHCCCCCCCCC		49.1125002506
374PhosphorylationSDQHVVPTAPDTEAD
CCCCCCCCCCCCCCC		38.9325002506
378PhosphorylationVVPTAPDTEADNCIV
CCCCCCCCCCCCEEE		31.8225002506
389PhosphorylationNCIVHELTGQSSVLR
CEEEEHHHCCCCCCC		30.1430266825
392PhosphorylationVHELTGQSSVLRRPV
EEHHHCCCCCCCCCC		24.6126657352
393PhosphorylationHELTGQSSVLRRPVR
EHHHCCCCCCCCCCC		19.7930266825
535UbiquitinationLLLRQFVKEKLLKWA
HHHHHHHHHHHHHHH		50.8822817900
537UbiquitinationLRQFVKEKLLKWAES
HHHHHHHHHHHHHCC		54.0922817900
540UbiquitinationFVKEKLLKWAESPAA
HHHHHHHHHHCCCCC		55.5921963094
544PhosphorylationKLLKWAESPAALTEV
HHHHHHCCCCCCCEE		16.4626471730
561PhosphorylationADTEPTRTQTLLQSL
CCCCCCHHHHHHHHH		28.5224043423
563PhosphorylationTEPTRTQTLLQSLGE
CCCCHHHHHHHHHHH		28.9024043423
567PhosphorylationRTQTLLQSLGELVKG
HHHHHHHHHHHHHHH		38.0124043423
620PhosphorylationTLFQVYYSLWRKLLK
HHHHHHHHHHHHHHH		12.0824719451
732PhosphorylationAHRQDAVSGTPLLRE
HHCCCCCCCCCHHHH		38.3730266825
734PhosphorylationRQDAVSGTPLLREEQ
CCCCCCCCCHHHHHH		11.8523401153
758PhosphorylationEEEEEEDSRDEGLGV
HHHHHHHHHHCCCCC		44.9326471730
767PhosphorylationDEGLGVATPHQATQV
HCCCCCCCHHCCCCC		20.9223186163
772PhosphorylationVATPHQATQVPEGAA
CCCHHCCCCCCCHHH		24.4323186163
796PhosphorylationLELAAGFSDVLSRVQ
HHHHHCCHHHHHHHH		26.3723403867
800PhosphorylationAGFSDVLSRVQVFLR
HCCHHHHHHHHHHHH		30.1923403867
821PhosphorylationVFKLVALYTVWVALK
HHHHHHHHHHHHHHH		6.90-
822PhosphorylationFKLVALYTVWVALKE
HHHHHHHHHHHHHHH		14.56-
899O-linked_GlycosylationNSTNLLPTEISQSLL
CCCCCCCCCHHHHHH		46.01OGP
960PhosphorylationRRQHQLAPLPAQAVF
HHHHCCCCCCHHHHH		47.6818669648
965PhosphorylationLAPLPAQAVFASGTR
CCCCCHHHHHCCCCH		10.6618669648
1016PhosphorylationQRMNFLVTLHGCWLV
HHHCHHHHHHHHHHH		18.3824719451
1027PhosphorylationCWLVAILTRRHRQAI
HHHHHHHHHHHHHHH		21.3924719451
1165PhosphorylationLKVAVFRYLFWLVLV
HHHHHHHHHHHHHHH		8.52-
1190PhosphorylationSIFGLGYLLACFYLL
HHHHHHHHHHHHHHH		2.0118669648
1195PhosphorylationGYLLACFYLLLFGTA
HHHHHHHHHHHHHHH		9.05-
1213PhosphorylationRDTRARLVLWDCLIL
CCHHHHHHHHHHHHH		4.1817081983
1215PhosphorylationTRARLVLWDCLILYN
HHHHHHHHHHHHHHC		6.1818669648
1224PhosphorylationCLILYNVTVIISKNM
HHHHHCCCEEECCCH		11.4427174698
1228PhosphorylationYNVTVIISKNMLSLL
HCCCEEECCCHHHHH		13.5727174698
1267AcetylationVKGYYDPKEMMDRDQ
HCCCCCHHHHCCCCC		56.1719608861
1334UbiquitinationLYNAANLKSIDFHRR
HHHHHCCCCCCHHHH		45.2121963094
1345UbiquitinationFHRRIEEKSLAQLKR
HHHHHCHHHHHHHHH		37.6721963094
1351UbiquitinationEKSLAQLKRQMERIR
HHHHHHHHHHHHHHH		28.6223503661
1360UbiquitinationQMERIRAKQEKHRQG
HHHHHHHHHHHHHCC		49.49-
1372PhosphorylationRQGRVDRSRPQDTLG
HCCCCCCCCCCCCCC		43.8023403867
1377PhosphorylationDRSRPQDTLGPKDPG
CCCCCCCCCCCCCCC		28.5023403867
1381UbiquitinationPQDTLGPKDPGLEPG
CCCCCCCCCCCCCCC		74.81-
1391PhosphorylationGLEPGPDSPGGSSPP
CCCCCCCCCCCCCCC		28.6929255136
1395PhosphorylationGPDSPGGSSPPRRQW
CCCCCCCCCCCCHHC		45.6629255136
1396PhosphorylationPDSPGGSSPPRRQWW
CCCCCCCCCCCHHCC		42.0529255136
1423PhosphorylationGDYFLFESDSEEEEE
CCEEEEECCCHHHHH		38.8218669648
1439PhosphorylationVPEDPRPSAQSAFQL
CCCCCCCCHHHHHHH		39.9724043423
1442PhosphorylationDPRPSAQSAFQLAYQ
CCCCCHHHHHHHHHH		30.6624043423
1448PhosphorylationQSAFQLAYQAWVTNA
HHHHHHHHHHHHHHH		13.8324043423
1453PhosphorylationLAYQAWVTNAQAVLR
HHHHHHHHHHHHHHH		17.7124043423
1479PhosphorylationEQAGQLPTGGGPSQE
HHCCCCCCCCCCCCC		57.98-
1509PhosphorylationHVVQRVLSTAQFLWM
HHHHHHHHHHHHHHH		20.88-
1510PhosphorylationVVQRVLSTAQFLWML
HHHHHHHHHHHHHHH		21.95-
1619PhosphorylationSTGYHTRSGSEEAVT
CCCCCCCCCCCCCCC		48.0729255136
1621PhosphorylationGYHTRSGSEEAVTDP
CCCCCCCCCCCCCCC		33.2529255136
1626PhosphorylationSGSEEAVTDPGEREA
CCCCCCCCCCCCCHH		43.4521945579
1636PhosphorylationGEREAGASLYQGLMR
CCCHHHHHHHHHHHH		27.0521945579
1638PhosphorylationREAGASLYQGLMRTA
CHHHHHHHHHHHHHH		9.6821945579
1644PhosphorylationLYQGLMRTASELLLD
HHHHHHHHHHHHHHC		22.1423927012
1646PhosphorylationQGLMRTASELLLDRR
HHHHHHHHHHHHCCC		28.3219664994
1721PhosphorylationVFLWAMLSIPRPSKR
HHHHHHHCCCCCCCC		19.9124719451
1766UbiquitinationVLRRYENKPYFPPRI
EEEEECCCCCCCCCC		29.2022817900
1820PhosphorylationPSKEHDKSGEEEQGA
CCCCCCCCCCHHCCC		58.4525849741
1837PhosphorylationGPGVPAATTEDHIQV
CCCCCCCCCCCCEEE		32.5921955146
1838PhosphorylationPGVPAATTEDHIQVE
CCCCCCCCCCCEEEE		34.3921955146
1851PhosphorylationVEARVGPTDGTPEPQ
EEEECCCCCCCCCCC		40.9229255136
1854PhosphorylationRVGPTDGTPEPQVEL
ECCCCCCCCCCCEEC		27.5623401153
1878UbiquitinationLRFRRRKKEGPARKG
HHHHHCCCCCCCCCC		67.1223503661
1884UbiquitinationKKEGPARKGAAAIEA
CCCCCCCCCCCEEEC		55.8221963094
1903UbiquitinationEEEGEEEKEAPTGRE
HHCCCCCCCCCCCCC		63.5621963094
1952PhosphorylationFFHDILHTKYRAATD
HHHHHHHHHHHHHHH		26.7326074081
1953UbiquitinationFHDILHTKYRAATDV
HHHHHHHHHHHHHHH		23.2221890473
1954PhosphorylationHDILHTKYRAATDVY
HHHHHHHHHHHHHHH		13.4626074081
2096UbiquitinationILGNFLTKKYNHLNL
HHHHHHHHHCCCCCC		56.2421890473
2294N-linked_GlycosylationQMKRELYNGTADITL
HHHHHHHHCCCCEEE		54.7019349973
2296PhosphorylationKRELYNGTADITLRF
HHHHHHCCCCEEEEE		19.9520068231
2313UbiquitinationNFQRDLAKGGTVEYA
ECCCHHHCCCEEEEC		66.2321890473
2316PhosphorylationRDLAKGGTVEYANEK
CHHHCCCEEEECCCC		20.8722210691
2319PhosphorylationAKGGTVEYANEKHML
HCCCEEEECCCCCEE		15.4722210691
2340PhosphorylationTARRQLASLLEGTSD
HHHHHHHHHHCCCCC		41.9226074081
2345PhosphorylationLASLLEGTSDQSVVI
HHHHHCCCCCCEEEC		21.5426074081
2346PhosphorylationASLLEGTSDQSVVIP
HHHHCCCCCCEEECC		44.5026074081
2349PhosphorylationLEGTSDQSVVIPNLF
HCCCCCCEEECCCCC		24.2826074081
2359PhosphorylationIPNLFPKYIRAPNGP
CCCCCHHHCCCCCCC		8.9026074081
2372UbiquitinationGPEANPVKQLQPNEE
CCCCCCCCCCCCCCC		46.6921906983
2479UbiquitinationPCVDRILKLCQDIFL
CHHHHHHHHHHHHHH		44.8621963094
2507PhosphorylationYAKLIFLYRSPETMI
HHHHHHHHCCHHHHH		9.7825954137
2509PhosphorylationKLIFLYRSPETMIKW
HHHHHHCCHHHHHHH		17.3325954137
2512PhosphorylationFLYRSPETMIKWTRE
HHHCCHHHHHHHHHC		27.8125954137
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 PIEZ1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIEZ1_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 PIEZ1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PIEZ1_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
194380Dehydrated hereditary stomatocytosis with or without pseudohyperkalemia and/or perinatal edema (DHS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIEZ1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1267, AND MASS SPECTROMETRY.
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-2294, AND MASSSPECTROMETRY.
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-1646, 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-1391; SER-1396; SER-1646AND THR-1854, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1646, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1646, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1646, AND MASSSPECTROMETRY.

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