ZYX_HUMAN - dbPTM
ZYX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZYX_HUMAN
UniProt AC Q15942
Protein Name Zyxin
Gene Name ZYX
Organism Homo sapiens (Human).
Sequence Length 572
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Cell junction, focal adhesion. Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of HESX1.
Protein Description Adhesion plaque protein. Binds alpha-actinin and the CRP protein. Important for targeting TES and ENA/VASP family members to focal adhesions and for the formation of actin-rich structures. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity)..
Protein Sequence MAAPRPSPAISVSVSAPAFYAPQKKFGPVVAPKPKVNPFRPGDSEPPPAPGAQRAQMGRVGEIPPPPPEDFPLPPPPLAGDGDDAEGALGGAFPPPPPPIEESFPPAPLEEEIFPSPPPPPEEEGGPEAPIPPPPQPREKVSSIDLEIDSLSSLLDDMTKNDPFKARVSSGYVPPPVATPFSSKSSTKPAAGGTAPLPPWKSPSSSQPLPQVPAPAQSQTQFHVQPQPQPKPQVQLHVQSQTQPVSLANTQPRGPPASSPAPAPKFSPVTPKFTPVASKFSPGAPGGSGSQPNQKLGHPEALSAGTGSPQPPSFTYAQQREKPRVQEKQHPVPPPAQNQNQVRSPGAPGPLTLKEVEELEQLTQQLMQDMEHPQRQNVAVNELCGRCHQPLARAQPAVRALGQLFHIACFTCHQCAQQLQGQQFYSLEGAPYCEGCYTDTLEKCNTCGEPITDRMLRATGKAYHPHCFTCVVCARPLEGTSFIVDQANRPHCVPDYHKQYAPRCSVCSEPIMPEPGRDETVRVVALDKNFHMKCYKCEDCGKPLSIEADDNGCFPLDGHVLCRKCHTARAQT
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------MAAPRPSPA
------CCCCCCCCC		26.6019413330
5Methylation---MAAPRPSPAISV
---CCCCCCCCCEEE		39.33115386663
7O-linked_Glycosylation-MAAPRPSPAISVSV
-CCCCCCCCCEEEEE		28.3930059200
7Phosphorylation-MAAPRPSPAISVSV
-CCCCCCCCCEEEEE		28.3928450419
11O-linked_GlycosylationPRPSPAISVSVSAPA
CCCCCCEEEEEECCC		15.5030059200
11PhosphorylationPRPSPAISVSVSAPA
CCCCCCEEEEEECCC		15.5030108239
13O-linked_GlycosylationPSPAISVSVSAPAFY
CCCCEEEEEECCCEE		11.9930059200
13PhosphorylationPSPAISVSVSAPAFY
CCCCEEEEEECCCEE		11.9930108239
15O-linked_GlycosylationPAISVSVSAPAFYAP
CCEEEEEECCCEECC		22.4930059200
15PhosphorylationPAISVSVSAPAFYAP
CCEEEEEECCCEECC		22.4923401153
20PhosphorylationSVSAPAFYAPQKKFG
EEECCCEECCCCCCC		21.3428796482
24AcetylationPAFYAPQKKFGPVVA
CCEECCCCCCCCCCC		49.3523954790
25"N6,N6-dimethyllysine"AFYAPQKKFGPVVAP
CEECCCCCCCCCCCC		50.75-
25AcetylationAFYAPQKKFGPVVAP
CEECCCCCCCCCCCC		50.7526051181
25MethylationAFYAPQKKFGPVVAP
CEECCCCCCCCCCCC		50.75-
35MalonylationPVVAPKPKVNPFRPG
CCCCCCCCCCCCCCC		61.8526320211
44PhosphorylationNPFRPGDSEPPPAPG
CCCCCCCCCCCCCCC		58.9028555341
108UbiquitinationEESFPPAPLEEEIFP
HHCCCCCCCCCCCCC		46.1821890473
116PhosphorylationLEEEIFPSPPPPPEE
CCCCCCCCCCCCCHH		39.0126074081
122UbiquitinationPSPPPPPEEEGGPEA
CCCCCCCHHHCCCCC		74.5721890473
142PhosphorylationPQPREKVSSIDLEID
CCCCHHCCCCEEEHH		32.4222167270
143PhosphorylationQPREKVSSIDLEIDS
CCCHHCCCCEEEHHH		24.1022167270
150PhosphorylationSIDLEIDSLSSLLDD
CCEEEHHHHHHHHHH		35.4930278072
152PhosphorylationDLEIDSLSSLLDDMT
EEEHHHHHHHHHHHH		23.9223663014
153PhosphorylationLEIDSLSSLLDDMTK
EEHHHHHHHHHHHHC		37.9423663014
159PhosphorylationSSLLDDMTKNDPFKA
HHHHHHHHCCCCCCC		33.4229978859
165AcetylationMTKNDPFKARVSSGY
HHCCCCCCCEECCCC		40.447960499
165MethylationMTKNDPFKARVSSGY
HHCCCCCCCEECCCC		40.447960499
165UbiquitinationMTKNDPFKARVSSGY
HHCCCCCCCEECCCC		40.44-
169O-linked_GlycosylationDPFKARVSSGYVPPP
CCCCCEECCCCCCCC		16.7030059200
169PhosphorylationDPFKARVSSGYVPPP
CCCCCEECCCCCCCC		16.7021945579
170O-linked_GlycosylationPFKARVSSGYVPPPV
CCCCEECCCCCCCCC		31.1430059200
170PhosphorylationPFKARVSSGYVPPPV
CCCCEECCCCCCCCC		31.1421945579
172PhosphorylationKARVSSGYVPPPVAT
CCEECCCCCCCCCCC		16.2521945579
179O-linked_GlycosylationYVPPPVATPFSSKSS
CCCCCCCCCCCCCCC		25.7130059200
179PhosphorylationYVPPPVATPFSSKSS
CCCCCCCCCCCCCCC		25.7121945579
182O-linked_GlycosylationPPVATPFSSKSSTKP
CCCCCCCCCCCCCCC		37.7530059200
182PhosphorylationPPVATPFSSKSSTKP
CCCCCCCCCCCCCCC		37.7521945579
183O-linked_GlycosylationPVATPFSSKSSTKPA
CCCCCCCCCCCCCCC		36.6230059200
183PhosphorylationPVATPFSSKSSTKPA
CCCCCCCCCCCCCCC		36.6221945579
185PhosphorylationATPFSSKSSTKPAAG
CCCCCCCCCCCCCCC		45.2328857561
186PhosphorylationTPFSSKSSTKPAAGG
CCCCCCCCCCCCCCC		44.1628857561
187PhosphorylationPFSSKSSTKPAAGGT
CCCCCCCCCCCCCCC		48.4128857561
188MalonylationFSSKSSTKPAAGGTA
CCCCCCCCCCCCCCC		34.3132601280
201MethylationTAPLPPWKSPSSSQP
CCCCCCCCCCCCCCC		59.26115978009
202PhosphorylationAPLPPWKSPSSSQPL
CCCCCCCCCCCCCCC		26.5823401153
204PhosphorylationLPPWKSPSSSQPLPQ
CCCCCCCCCCCCCCC		50.1125159151
205PhosphorylationPPWKSPSSSQPLPQV
CCCCCCCCCCCCCCC		36.0525159151
206PhosphorylationPWKSPSSSQPLPQVP
CCCCCCCCCCCCCCC		39.9123663014
218PhosphorylationQVPAPAQSQTQFHVQ
CCCCCCCCCCEEEEC		36.9826074081
220O-linked_GlycosylationPAPAQSQTQFHVQPQ
CCCCCCCCEEEECCC		38.1530059200
220PhosphorylationPAPAQSQTQFHVQPQ
CCCCCCCCEEEECCC		38.1526074081
231AcetylationVQPQPQPKPQVQLHV
ECCCCCCCCCEEEEE		42.7226051181
240O-linked_GlycosylationQVQLHVQSQTQPVSL
CEEEEECCCCCCEEE		33.8230059200
240PhosphorylationQVQLHVQSQTQPVSL
CEEEEECCCCCCEEE		33.8229514088
242O-linked_GlycosylationQLHVQSQTQPVSLAN
EEEECCCCCCEEECC		39.8430059200
242PhosphorylationQLHVQSQTQPVSLAN
EEEECCCCCCEEECC		39.8429514088
246O-linked_GlycosylationQSQTQPVSLANTQPR
CCCCCCEEECCCCCC		28.5730059200
246PhosphorylationQSQTQPVSLANTQPR
CCCCCCEEECCCCCC		28.5729514088
250O-linked_GlycosylationQPVSLANTQPRGPPA
CCEEECCCCCCCCCC		34.0530059200
250PhosphorylationQPVSLANTQPRGPPA
CCEEECCCCCCCCCC		34.0525159151
253Asymmetric dimethylarginineSLANTQPRGPPASSP
EECCCCCCCCCCCCC		61.50-
253MethylationSLANTQPRGPPASSP
EECCCCCCCCCCCCC		61.50-
258O-linked_GlycosylationQPRGPPASSPAPAPK
CCCCCCCCCCCCCCC		42.5030059200
258PhosphorylationQPRGPPASSPAPAPK
CCCCCCCCCCCCCCC		42.5029255136
259O-linked_GlycosylationPRGPPASSPAPAPKF
CCCCCCCCCCCCCCC		27.4730059200
259PhosphorylationPRGPPASSPAPAPKF
CCCCCCCCCCCCCCC		27.4719664994
265AcetylationSSPAPAPKFSPVTPK
CCCCCCCCCCCCCCC		61.6626051181
265MalonylationSSPAPAPKFSPVTPK
CCCCCCCCCCCCCCC		61.6626320211
265UbiquitinationSSPAPAPKFSPVTPK
CCCCCCCCCCCCCCC		61.6621890473
267O-linked_GlycosylationPAPAPKFSPVTPKFT
CCCCCCCCCCCCCCC		25.2930059200
267PhosphorylationPAPAPKFSPVTPKFT
CCCCCCCCCCCCCCC		25.2922167270
270PhosphorylationAPKFSPVTPKFTPVA
CCCCCCCCCCCCCCC		24.9322167270
272AcetylationKFSPVTPKFTPVASK
CCCCCCCCCCCCCCC		53.1387857
272MethylationKFSPVTPKFTPVASK
CCCCCCCCCCCCCCC		53.1387857
272UbiquitinationKFSPVTPKFTPVASK
CCCCCCCCCCCCCCC		53.13-
274PhosphorylationSPVTPKFTPVASKFS
CCCCCCCCCCCCCCC		23.9923927012
278O-linked_GlycosylationPKFTPVASKFSPGAP
CCCCCCCCCCCCCCC		34.1730059200
278PhosphorylationPKFTPVASKFSPGAP
CCCCCCCCCCCCCCC		34.1722167270
279AcetylationKFTPVASKFSPGAPG
CCCCCCCCCCCCCCC		39.8719608861
279MethylationKFTPVASKFSPGAPG
CCCCCCCCCCCCCCC		39.8719608861
279UbiquitinationKFTPVASKFSPGAPG
CCCCCCCCCCCCCCC		39.8719608861
281PhosphorylationTPVASKFSPGAPGGS
CCCCCCCCCCCCCCC		26.5929255136
288PhosphorylationSPGAPGGSGSQPNQK
CCCCCCCCCCCCCCC		40.9823927012
290PhosphorylationGAPGGSGSQPNQKLG
CCCCCCCCCCCCCCC		44.1323927012
295MethylationSGSQPNQKLGHPEAL
CCCCCCCCCCCHHHH		64.1824129315
295UbiquitinationSGSQPNQKLGHPEAL
CCCCCCCCCCCHHHH		64.18-
303PhosphorylationLGHPEALSAGTGSPQ
CCCHHHHHCCCCCCC		31.5329255136
306PhosphorylationPEALSAGTGSPQPPS
HHHHHCCCCCCCCCC		33.9129255136
308PhosphorylationALSAGTGSPQPPSFT
HHHCCCCCCCCCCCC		21.8729255136
313PhosphorylationTGSPQPPSFTYAQQR
CCCCCCCCCCHHCCC		36.5821945579
315PhosphorylationSPQPPSFTYAQQREK
CCCCCCCCHHCCCCC		23.4521945579
316PhosphorylationPQPPSFTYAQQREKP
CCCCCCCHHCCCCCC		10.6221945579
328AcetylationEKPRVQEKQHPVPPP
CCCCCCCCCCCCCCC		36.4926051181
328UbiquitinationEKPRVQEKQHPVPPP
CCCCCCCCCCCCCCC		36.49-
343MethylationAQNQNQVRSPGAPGP
CCCCCCCCCCCCCCC		27.63115386655
344PhosphorylationQNQNQVRSPGAPGPL
CCCCCCCCCCCCCCC		28.9119664994
352PhosphorylationPGAPGPLTLKEVEEL
CCCCCCCCHHHHHHH		38.6323927012
367SulfoxidationEQLTQQLMQDMEHPQ
HHHHHHHHHHCCCHH		2.4930846556
370SulfoxidationTQQLMQDMEHPQRQN
HHHHHHHCCCHHHHH		2.6130846556
463PhosphorylationLRATGKAYHPHCFTC
HHHHCCCCCCCCEEE		21.2628152594
480PhosphorylationCARPLEGTSFIVDQA
ECCCCCCCCEEEECC		15.8728270605
481PhosphorylationARPLEGTSFIVDQAN
CCCCCCCCEEEECCC		24.6725159151
505PhosphorylationKQYAPRCSVCSEPIM
HHCCCCCCCCCCCCC		27.6926657352
508PhosphorylationAPRCSVCSEPIMPEP
CCCCCCCCCCCCCCC		44.2323312004
512SulfoxidationSVCSEPIMPEPGRDE
CCCCCCCCCCCCCCC		4.5030846556
520PhosphorylationPEPGRDETVRVVALD
CCCCCCCCEEEEEEC		20.2223312004
5282-HydroxyisobutyrylationVRVVALDKNFHMKCY
EEEEEECCCCEEEEE		63.46-
528AcetylationVRVVALDKNFHMKCY
EEEEEECCCCEEEEE		63.4687861
533AcetylationLDKNFHMKCYKCEDC
ECCCCEEEEEEECCC		26.3327178108
536AcetylationNFHMKCYKCEDCGKP
CCEEEEEEECCCCCC		40.3926051181
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
142SPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZYX_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 ZYX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEBL_HUMANNEBLphysical
15004028
LASP1_HUMANLASP1physical
15004028
LATS1_HUMANLATS1physical
10831611
ACTN1_HUMANACTN1physical
10224105
BCAR1_HUMANBCAR1physical
11782456
CASL_HUMANNEDD9physical
11782456
ENAH_HUMANENAHphysical
10801818
VASP_HUMANVASPphysical
10801818
VHL_HUMANVHLphysical
22286099
NIBL1_HUMANFAM129Bphysical
22863883
GARS_HUMANGARSphysical
22863883
NUDC_HUMANNUDCphysical
22863883
PAPOA_HUMANPAPOLAphysical
22863883
PAXI_HUMANPXNphysical
22863883
SC23B_HUMANSEC23Bphysical
22863883
SC24C_HUMANSEC24Cphysical
22863883
LIN7A_HUMANLIN7Aphysical
25416956
PDLI5_HUMANPDLIM5physical
25416956
PF21A_HUMANPHF21Aphysical
25416956
IMP3_HUMANIMP3physical
25416956
YPEL3_HUMANYPEL3physical
25416956
RT4I1_HUMANRTN4IP1physical
25416956
CD2AP_HUMANCD2APphysical
26344197
RT4I1_HUMANRTN4IP1physical
21516116
SIR1_HUMANSIRT1physical
19173742
SIAH2_HUMANSIAH2physical
27030211
LATS2_HUMANLATS2physical
27030211
CCAR1_HUMANCCAR1physical
28514442
TANC2_HUMANTANC2physical
28514442
ENAH_HUMANENAHphysical
28514442
FKB15_HUMANFKBP15physical
28514442
SBP2L_HUMANSECISBP2Lphysical
28514442
ZFR_HUMANZFRphysical
28514442
TB10B_HUMANTBC1D10Bphysical
28514442
TES_HUMANTESphysical
28514442
GMPPA_HUMANGMPPAphysical
28514442
EVL_HUMANEVLphysical
28514442
UBE2N_HUMANUBE2Nphysical
27173435
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 ZYX_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-259; SER-267; THR-270; SER-281; SER-288 ANDSER-344, AND MASS SPECTROMETRY.
"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-279, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-259; SER-267; THR-270; SER-281; SER-288 ANDSER-344, AND MASS SPECTROMETRY.
"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-169; SER-259; SER-267;THR-270; THR-274; SER-281; SER-288; SER-308 AND SER-344, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-313, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-267; SER-281AND SER-344, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; THR-179 ANDSER-344, AND MASS 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-143; SER-259; SER-308AND SER-344, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-281; SER-290AND SER-344, AND MASS SPECTROMETRY.
"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-344, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-267 ANDSER-344, AND MASS SPECTROMETRY.

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