PLST_HUMAN - dbPTM
PLST_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLST_HUMAN
UniProt AC P13797
Protein Name Plastin-3
Gene Name PLS3
Organism Homo sapiens (Human).
Sequence Length 630
Subcellular Localization Cytoplasm.
Protein Description Actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. May play a role in the regulation of bone development..
Protein Sequence MDEMATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLMLDGDRNKDGKISFDEFVYIFQEVKSSDIAKTFRKAINRKEGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRNEALAALLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRIDINMSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNKYPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVLEDLGDGQKANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGARVYALPEDLVEVKPKMVMTVFACLMGRGMKRV
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
6Phosphorylation--MDEMATTQISKDE
--CCHHHHCCCCHHH		20.2323186163
7Phosphorylation-MDEMATTQISKDEL
-CCHHHHCCCCHHHH		17.8623186163
10PhosphorylationEMATTQISKDELDEL
HHHHCCCCHHHHHHH		25.0020068231
11UbiquitinationMATTQISKDELDELK
HHHCCCCHHHHHHHH		57.77-
18UbiquitinationKDELDELKEAFAKVD
HHHHHHHHHHHHCCC		44.97-
182-HydroxyisobutyrylationKDELDELKEAFAKVD
HHHHHHHHHHHHCCC		44.97-
30UbiquitinationKVDLNSNGFICDYEL
CCCCCCCCEECCHHH		17.08-
35PhosphorylationSNGFICDYELHELFK
CCCEECCHHHHHHHH		18.91-
37UbiquitinationGFICDYELHELFKEA
CEECCHHHHHHHHHC		2.87-
42UbiquitinationYELHELFKEANMPLP
HHHHHHHHHCCCCCC		69.42-
46SulfoxidationELFKEANMPLPGYKV
HHHHHCCCCCCCHHH		4.6830846556
51PhosphorylationANMPLPGYKVREIIQ
CCCCCCCHHHHHHHH		12.3629691806
52UbiquitinationNMPLPGYKVREIIQK
CCCCCCHHHHHHHHH		40.5121890473
522-HydroxyisobutyrylationNMPLPGYKVREIIQK
CCCCCCHHHHHHHHH		40.51-
52AcetylationNMPLPGYKVREIIQK
CCCCCCHHHHHHHHH		40.5126051181
59UbiquitinationKVREIIQKLMLDGDR
HHHHHHHHHHCCCCC		26.0021890473
592-HydroxyisobutyrylationKVREIIQKLMLDGDR
HHHHHHHHHHCCCCC		26.00-
59AcetylationKVREIIQKLMLDGDR
HHHHHHHHHHCCCCC		26.0027452117
66MethylationKLMLDGDRNKDGKIS
HHHCCCCCCCCCCEE		58.59115487929
69UbiquitinationLDGDRNKDGKISFDE
CCCCCCCCCCEEHHH		68.14-
78UbiquitinationKISFDEFVYIFQEVK
CEEHHHHHHHHHHHC		3.18-
85UbiquitinationVYIFQEVKSSDIAKT
HHHHHHHCCCHHHHH		43.41-
91AcetylationVKSSDIAKTFRKAIN
HCCCHHHHHHHHHHH		48.8326051181
91UbiquitinationVKSSDIAKTFRKAIN
HCCCHHHHHHHHHHH		48.8321890473
912-HydroxyisobutyrylationVKSSDIAKTFRKAIN
HCCCHHHHHHHHHHH		48.83-
100UbiquitinationFRKAINRKEGICALG
HHHHHHHCCCEEECC		56.6621890473
109PhosphorylationGICALGGTSELSSEG
CEEECCCCCCCCCCC		19.7529978859
110PhosphorylationICALGGTSELSSEGT
EEECCCCCCCCCCCC		39.5529978859
113PhosphorylationLGGTSELSSEGTQHS
CCCCCCCCCCCCCCC		23.4528192239
113UbiquitinationLGGTSELSSEGTQHS
CCCCCCCCCCCCCCC		23.4521890473
114PhosphorylationGGTSELSSEGTQHSY
CCCCCCCCCCCCCCC		53.3117525332
117PhosphorylationSELSSEGTQHSYSEE
CCCCCCCCCCCCCHH		21.0317525332
120PhosphorylationSSEGTQHSYSEEEKY
CCCCCCCCCCHHHHH		22.1225159151
121PhosphorylationSEGTQHSYSEEEKYA
CCCCCCCCCHHHHHH		20.2729978859
122PhosphorylationEGTQHSYSEEEKYAF
CCCCCCCCHHHHHHH		41.3629978859
126UbiquitinationHSYSEEEKYAFVNWI
CCCCHHHHHHHHHHH		45.20-
127PhosphorylationSYSEEEKYAFVNWIN
CCCHHHHHHHHHHHH		14.4625159151
135UbiquitinationAFVNWINKALENDPD
HHHHHHHHHHHCCCC		45.2621890473
135UbiquitinationAFVNWINKALENDPD
HHHHHHHHHHHCCCC		45.2621890473
135UbiquitinationAFVNWINKALENDPD
HHHHHHHHHHHCCCC		45.2621890473
136UbiquitinationFVNWINKALENDPDC
HHHHHHHHHHCCCCC		18.67-
143GlutathionylationALENDPDCRHVIPMN
HHHCCCCCCCCCCCC		3.8422555962
144MethylationLENDPDCRHVIPMNP
HHCCCCCCCCCCCCC		34.19115487921
146UbiquitinationNDPDCRHVIPMNPNT
CCCCCCCCCCCCCCH		2.44-
158UbiquitinationPNTDDLFKAVGDGIV
CCHHHHHHHHCCCCE		49.84-
1582-HydroxyisobutyrylationPNTDDLFKAVGDGIV
CCHHHHHHHHCCCCE		49.84-
167GlutathionylationVGDGIVLCKMINLSV
HCCCCEEEEECCCCC		1.6222555962
167S-palmitoylationVGDGIVLCKMINLSV
HCCCCEEEEECCCCC		1.6229575903
168UbiquitinationGDGIVLCKMINLSVP
CCCCEEEEECCCCCC		38.3621906983
169SulfoxidationDGIVLCKMINLSVPD
CCCEEEEECCCCCCC		2.1030846556
173PhosphorylationLCKMINLSVPDTIDE
EEEECCCCCCCCCCH		27.41-
185AcetylationIDERAINKKKLTPFI
CCHHHCCCCCCCCHH		45.217677627
203PhosphorylationNLNLALNSASAIGCH
CHHHHHHHCCCCCCE		25.1718452278
205PhosphorylationNLALNSASAIGCHVV
HHHHHHCCCCCCEEE		21.9018452278
244UbiquitinationIGLFADIELSRNEAL
HHCCCCCCCCHHHHH		41.04-
246PhosphorylationLFADIELSRNEALAA
CCCCCCCCHHHHHHH		21.9220068231
265SulfoxidationGETLEELMKLSPEEL
CCHHHHHHCCCHHHH		4.6730846556
266UbiquitinationETLEELMKLSPEELL
CHHHHHHCCCHHHHH		59.44-
268PhosphorylationLEELMKLSPEELLLR
HHHHHCCCHHHHHHH		25.4228192239
284PhosphorylationANFHLENSGWQKINN
HHHHHHCCCCHHCCC		31.8428857561
287UbiquitinationHLENSGWQKINNFSA
HHHCCCCHHCCCCCC		40.03-
293PhosphorylationWQKINNFSADIKDSK
CHHCCCCCCCCCCCH		27.4429255136
297AcetylationNNFSADIKDSKAYFH
CCCCCCCCCCHHHHH		57.4026051181
297UbiquitinationNNFSADIKDSKAYFH
CCCCCCCCCCHHHHH		57.40-
2972-HydroxyisobutyrylationNNFSADIKDSKAYFH
CCCCCCCCCCHHHHH		57.40-
300AcetylationSADIKDSKAYFHLLN
CCCCCCCHHHHHHHH		58.18-
300UbiquitinationSADIKDSKAYFHLLN
CCCCCCCHHHHHHHH		58.1821890473
3002-HydroxyisobutyrylationSADIKDSKAYFHLLN
CCCCCCCHHHHHHHH		58.18-
302PhosphorylationDIKDSKAYFHLLNQI
CCCCCHHHHHHHHHH		8.6828152594
323PhosphorylationEGEPRIDINMSGFNE
CCCCCCEECCCCCCC		4.3018669648
325SulfoxidationEPRIDINMSGFNETD
CCCCEECCCCCCCHH		4.1830846556
326PhosphorylationPRIDINMSGFNETDD
CCCEECCCCCCCHHH		35.4325159151
331PhosphorylationNMSGFNETDDLKRAE
CCCCCCCHHHHHHHH		35.6023403867
335AcetylationFNETDDLKRAESMLQ
CCCHHHHHHHHHHHH		57.4626051181
335UbiquitinationFNETDDLKRAESMLQ
CCCHHHHHHHHHHHH		57.46-
3352-HydroxyisobutyrylationFNETDDLKRAESMLQ
CCCHHHHHHHHHHHH		57.46-
339PhosphorylationDDLKRAESMLQQADK
HHHHHHHHHHHHHHH		24.6529255136
340SulfoxidationDLKRAESMLQQADKL
HHHHHHHHHHHHHHH		2.7030846556
346UbiquitinationSMLQQADKLGCRQFV
HHHHHHHHHCCCCCC		50.20-
3462-HydroxyisobutyrylationSMLQQADKLGCRQFV
HHHHHHHHHCCCCCC		50.20-
346AcetylationSMLQQADKLGCRQFV
HHHHHHHHHCCCCCC		50.2026051181
354PhosphorylationLGCRQFVTPADVVSG
HCCCCCCCHHHHHCC		17.6621815630
360PhosphorylationVTPADVVSGNPKLNL
CCHHHHHCCCCCCHH		32.4727251275
364AcetylationDVVSGNPKLNLAFVA
HHHCCCCCCHHHHHH		54.74-
364UbiquitinationDVVSGNPKLNLAFVA
HHHCCCCCCHHHHHH		54.74-
369UbiquitinationNPKLNLAFVANLFNK
CCCCHHHHHHHHHHH		6.33-
381PhosphorylationFNKYPALTKPENQDI
HHHCCCCCCCCCCCC		46.8120068231
382UbiquitinationNKYPALTKPENQDID
HHCCCCCCCCCCCCC		51.7021906983
382AcetylationNKYPALTKPENQDID
HHCCCCCCCCCCCCC		51.7026051181
388PhosphorylationTKPENQDIDWTLLEG
CCCCCCCCCCEEECC		3.2418669648
391PhosphorylationENQDIDWTLLEGETR
CCCCCCCEEECCCCH		20.0921082442
397PhosphorylationWTLLEGETREERTFR
CEEECCCCHHHHHHH		54.9920068231
402PhosphorylationGETREERTFRNWMNS
CCCHHHHHHHHHHHH		30.17-
409PhosphorylationTFRNWMNSLGVNPHV
HHHHHHHHCCCCCCH		15.47-
424UbiquitinationNHLYADLQDALVILQ
HHHHHHHHHHHHHHH		34.18-
434UbiquitinationLVILQLYERIKVPVD
HHHHHHHHHCCCCCC		57.43-
437UbiquitinationLQLYERIKVPVDWSK
HHHHHHCCCCCCHHH		46.8621890473
444MethylationKVPVDWSKVNKPPYP
CCCCCHHHCCCCCCC		45.64115975173
4442-HydroxyisobutyrylationKVPVDWSKVNKPPYP
CCCCCHHHCCCCCCC		45.64-
446AcetylationPVDWSKVNKPPYPKL
CCCHHHCCCCCCCCC		55.65-
446UbiquitinationPVDWSKVNKPPYPKL
CCCHHHCCCCCCCCC		55.65-
447UbiquitinationVDWSKVNKPPYPKLG
CCHHHCCCCCCCCCC		50.81-
452UbiquitinationVNKPPYPKLGANMKK
CCCCCCCCCCCCHHH		54.43-
459AcetylationKLGANMKKLENCNYA
CCCCCHHHHHCCCCH		50.7123749302
459UbiquitinationKLGANMKKLENCNYA
CCCCCHHHHHCCCCH		50.71-
471UbiquitinationNYAVELGKHPAKFSL
CCHHHCCCCCCCEEE		60.07-
471MalonylationNYAVELGKHPAKFSL
CCHHHCCCCCCCEEE		60.0726320211
471AcetylationNYAVELGKHPAKFSL
CCHHHCCCCCCCEEE		60.0726051181
475AcetylationELGKHPAKFSLVGIG
HCCCCCCCEEEEEEC		39.68-
477PhosphorylationGKHPAKFSLVGIGGQ
CCCCCCEEEEEECCC		22.8018187866
492PhosphorylationDLNDGNQTLTLALVW
CCCCCCHHHHHHHHH		26.2218187866
518UbiquitinationEDLGDGQKANDDIIV
HHHCCCCCCCCCCHH		55.47-
531PhosphorylationIVNWVNRTLSEAGKS
HHHHHHHHHHHCCCC		29.4525404012
533PhosphorylationNWVNRTLSEAGKSTS
HHHHHHHHHCCCCCC		25.4525404012
537UbiquitinationRTLSEAGKSTSIQSF
HHHHHCCCCCCHHHH		58.57-
5372-HydroxyisobutyrylationRTLSEAGKSTSIQSF
HHHHHCCCCCCHHHH		58.57-
538PhosphorylationTLSEAGKSTSIQSFK
HHHHCCCCCCHHHHC		26.8627794612
539PhosphorylationLSEAGKSTSIQSFKD
HHHCCCCCCHHHHCC		33.0827794612
540PhosphorylationSEAGKSTSIQSFKDK
HHCCCCCCHHHHCCC		26.2226657352
543PhosphorylationGKSTSIQSFKDKTIS
CCCCCHHHHCCCCCC		32.3727794612
545MethylationSTSIQSFKDKTISSS
CCCHHHHCCCCCCHH		64.6615618555
545AcetylationSTSIQSFKDKTISSS
CCCHHHHCCCCCCHH		64.6626051181
545UbiquitinationSTSIQSFKDKTISSS
CCCHHHHCCCCCCHH		64.66-
5452-HydroxyisobutyrylationSTSIQSFKDKTISSS
CCCHHHHCCCCCCHH		64.66-
545MalonylationSTSIQSFKDKTISSS
CCCHHHHCCCCCCHH		64.6626320211
569AcetylationIQPGCINYDLVKSGN
HCCCCCCCCHHHCCC		7.25-
582AcetylationGNLTEDDKHNNAKYA
CCCCCCCCCCCHHHH		61.6321466224
587UbiquitinationDDKHNNAKYAVSMAR
CCCCCCHHHHHHHHH		35.55-
587AcetylationDDKHNNAKYAVSMAR
CCCCCCHHHHHHHHH		35.5526051181
598UbiquitinationSMARRIGARVYALPE
HHHHHHCCEEEECCH		8.73-
601PhosphorylationRRIGARVYALPEDLV
HHHCCEEEECCHHHC		9.25-
611UbiquitinationPEDLVEVKPKMVMTV
CHHHCCCCHHHHHHH		25.9721890473
611AcetylationPEDLVEVKPKMVMTV
CHHHCCCCHHHHHHH		25.9727452117
613UbiquitinationDLVEVKPKMVMTVFA
HHCCCCHHHHHHHHH		38.11-
617PhosphorylationVKPKMVMTVFACLMG
CCHHHHHHHHHHHHC		10.8920068231
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 PLST_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLST_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 PLST_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PSMD6_HUMANPSMD6physical
22939629
SODC_HUMANSOD1physical
22939629
THG1_HUMANTHG1Lphysical
22939629
TRXR1_HUMANTXNRD1physical
22939629
SNX3_HUMANSNX3physical
22939629
ANXA6_HUMANANXA6physical
22863883
TALDO_HUMANTALDO1physical
22863883
TYSY_HUMANTYMSphysical
22863883
GDIR1_HUMANARHGDIAphysical
26344197
ENOG_HUMANENO2physical
26344197
FKB14_HUMANFKBP14physical
26344197
CH10_HUMANHSPE1physical
26344197
PLSI_HUMANPLS1physical
28514442
KLH23_HUMANKLHL23physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
166710Osteoporosis (OSTEOP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLST_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 SER-326 AND THR-391, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND THR-492, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-168, AND MASSSPECTROMETRY.

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