Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Zyxin  

UniProtKB / Swiss-Prot ID :  ZYX_HUMAN

Gene Name (Synonyms) : 
ZYX  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Cell junction, focal adhesion. Note=Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of HESX1. 

Protein Function :  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 MAAPRPSPAISVSVSAPAFYAPQKKFGPVVAPKPKVNPFRPGDSEPPPAPGAQRAQMGRVGEIPPPPPED...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
223H -> L (in dbSNP:rs11978404). VAR_034081
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAPRP
---CCCCCC
26.60UniProtKB
Link-
24N6-acetyllysineYAPQKKFGP
CCCCCCCCC
49.35HPRD
Link-
24N6-acetyllysineYAPQKKFGP
CCCCCCCCC
49.35Phosphositeplus
Link-
142PhosphoserineREKVSSIDL
CCCCCCCCC
32.42HPRD
Link-
142PhosphoserineREKVSSIDL
CCCCCCCCC
32.42PhosphoELM
Link-
142PhosphoserineREKVSSIDL
CCCCCCCCC
32.42Phosphositeplus
Link-
142PhosphoserineREKVSSIDL
CCCCCCCCC
32.42SysPTM
Link-
142Phosphoserine.REKVSSIDL
CCCCCCCCC
32.42UniProtKB
Link-
143PhosphoserineEKVSSIDLE
CCCCCCCCC
24.10HPRD
Link-
143PhosphoserineEKVSSIDLE
CCCCCCCCC
24.10Phosphositeplus
Link-
143Phosphoserine.EKVSSIDLE
CCCCCCCCC
24.10UniProtKB
Link-
149Caspase cleavage aspartic acidDLEIDSLSS
CCCCCCCCC
33.86Phosphositeplus
Link-
150PhosphoserineLEIDSLSSL
CCCCCCCCC
35.49HPRD
Link-
150PhosphoserineLEIDSLSSL
CCCCCCCCC
35.49Phosphositeplus
Link-
169PhosphoserineKARVSSGYV
CCCCCCCCC
16.70HPRD
Link-
169PhosphoserineKARVSSGYV
CCCCCCCCC
16.70PhosphoELM
Link-
169PhosphoserineKARVSSGYV
CCCCCCCCC
16.70Phosphositeplus
Link-
169Phosphoserine.KARVSSGYV
CCCCCCCCC
16.70UniProtKB
Link-
170PhosphoserineARVSSGYVP
CCCCCCCCC
31.14HPRD
Link-
170PhosphoserineARVSSGYVP
CCCCCCCCC
31.14PhosphoELM
Link-
170PhosphoserineARVSSGYVP
CCCCCCCCC
31.14Phosphositeplus
Link-
172PhosphotyrosineVSSGYVPPP
CCCCCCCCC
16.25HPRD
Link-
172PhosphotyrosineVSSGYVPPP
CCCCCCCCC
16.25Phosphositeplus
Link-
179PhosphothreoninePPVATPFSS
CCCCCCCCC
25.71HPRD
Link-
179PhosphothreoninePPVATPFSS
CCCCCCCCC
25.71PhosphoELM
Link-
179PhosphothreoninePPVATPFSS
CCCCCCCCC
25.71Phosphositeplus
Link-
179PhosphothreoninePPVATPFSS
CCCCCCCCC
25.71SysPTM
Link-
179Phosphothreonine.PPVATPFSS
CCCCCCCCC
25.71UniProtKB
Link-
258PhosphoserineGPPASSPAP
CCCCCCCCC
42.50HPRD
Link-
258PhosphoserineGPPASSPAP
CCCCCCCCC
42.50PhosphoELM
Link-
258PhosphoserineGPPASSPAP
CCCCCCCCC
42.50Phosphositeplus
Link-
259PhosphoserinePPASSPAPA
CCCCCCCCC
27.47HPRD
Link-
259PhosphoserinePPASSPAPA
CCCCCCCCC
27.47PhosphoELM
Link-
259PhosphoserinePPASSPAPA
CCCCCCCCC
27.47Phosphositeplus
Link-
259PhosphoserinePPASSPAPA
CCCCCCCCC
27.47SysPTM
Link-
259Phosphoserine.PPASSPAPA
CCCCCCCCC
27.47UniProtKB
Link-
265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)APAPKFSPV
CCCCCCCCC
61.66Phosphositeplus
Link-
267PhosphoserineAPKFSPVTP
CCCCCCCCC
25.29HPRD
Link-
267PhosphoserineAPKFSPVTP
CCCCCCCCC
25.29PhosphoELM
Link-
267PhosphoserineAPKFSPVTP
CCCCCCCCC
25.29Phosphositeplus
Link-
267PhosphoserineAPKFSPVTP
CCCCCCCCC
25.29SysPTM
Link-
267Phosphoserine.APKFSPVTP
CCCCCCCCC
25.29UniProtKB
Link-
270PhosphothreonineFSPVTPKFT
CCCCCCCCC
24.93HPRD
Link-
270PhosphothreonineFSPVTPKFT
CCCCCCCCC
24.93PhosphoELM
Link-
270PhosphothreonineFSPVTPKFT
CCCCCCCCC
24.93Phosphositeplus
Link-
270Phosphothreonine.FSPVTPKFT
CCCCCCCCC
24.93UniProtKB
Link-
274PhosphothreonineTPKFTPVAS
CCCCCCCCC
23.99HPRD
Link-
274PhosphothreonineTPKFTPVAS
CCCCCCCCC
23.99PhosphoELM
Link-
274PhosphothreonineTPKFTPVAS
CCCCCCCCC
23.99Phosphositeplus
Link-
274Phosphothreonine.TPKFTPVAS
CCCCCCCCC
23.99UniProtKB
Link-
278PhosphoserineTPVASKFSP
CCCCCCCCC
34.17HPRD
Link-
278PhosphoserineTPVASKFSP
CCCCCCCCC
34.17PhosphoELM
Link-
279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PVASKFSPG
CCCCCCCCC
39.87Phosphositeplus
Link-
279N6-acetyllysinePVASKFSPG
CCCCCCCCC
39.87HPRD
Link-
279N6-acetyllysinePVASKFSPG
CCCCCCCCC
39.87Phosphositeplus
Link-
279N6-acetyllysine.PVASKFSPG
CCCCCCCCC
39.87UniProtKB
Link-
281PhosphoserineASKFSPGAP
CCCCCCCCC
26.59HPRD
Link-
281PhosphoserineASKFSPGAP
CCCCCCCCC
26.59PhosphoELM
Link-
281PhosphoserineASKFSPGAP
CCCCCCCCC
26.59Phosphositeplus
Link-
281PhosphoserineASKFSPGAP
CCCCCCCCC
26.59SysPTM
Link-
281Phosphoserine.ASKFSPGAP
CCCCCCCCC
26.59UniProtKB
Link-
288PhosphoserineAPGGSGSQP
CCCCCCCCC
40.98HPRD
Link-
288PhosphoserineAPGGSGSQP
CCCCCCCCC
40.98PhosphoELM
Link-
288PhosphoserineAPGGSGSQP
CCCCCCCCC
40.98Phosphositeplus
Link-
288Phosphoserine.APGGSGSQP
CCCCCCCCC
40.98UniProtKB
Link-
290PhosphoserineGGSGSQPNQ
CCCCCCCCC
44.13HPRD
Link-
290PhosphoserineGGSGSQPNQ
CCCCCCCCC
44.13PhosphoELM
Link-
290PhosphoserineGGSGSQPNQ
CCCCCCCCC
44.13Phosphositeplus
Link-
290Phosphoserine.GGSGSQPNQ
CCCCCCCCC
44.13UniProtKB
Link-
303PhosphoserinePEALSAGTG
CCCCCCCCC
31.53HPRD
Link-
303PhosphoserinePEALSAGTG
CCCCCCCCC
31.53PhosphoELM
Link-
303PhosphoserinePEALSAGTG
CCCCCCCCC
31.53Phosphositeplus
Link-
306PhosphothreonineLSAGTGSPQ
CCCCCCCCC
33.91HPRD
Link-
306PhosphothreonineLSAGTGSPQ
CCCCCCCCC
33.91Phosphositeplus
Link-
308PhosphoserineAGTGSPQPP
CCCCCCCCC
21.87HPRD
Link-
308PhosphoserineAGTGSPQPP
CCCCCCCCC
21.87PhosphoELM
Link-
308PhosphoserineAGTGSPQPP
CCCCCCCCC
21.87Phosphositeplus
Link-
308Phosphoserine.AGTGSPQPP
CCCCCCCCC
21.87UniProtKB
Link-
313PhosphoserinePQPPSFTYA
CCCCCCCCC
36.58HPRD
Link-
313PhosphoserinePQPPSFTYA
CCCCCCCCC
36.58PhosphoELM
Link-
313PhosphoserinePQPPSFTYA
CCCCCCCCC
36.58Phosphositeplus
Link-
313Phosphoserine.PQPPSFTYA
CCCCCCCCC
36.58UniProtKB
Link-
315PhosphothreoninePPSFTYAQQ
CCCCCCCCC
23.45HPRD
Link-
315PhosphothreoninePPSFTYAQQ
CCCCCCCCC
23.45PhosphoELM
Link-
316PhosphotyrosinePSFTYAQQR
CCCCCCCCC
10.62Phosphositeplus
Link-
344PhosphoserineNQVRSPGAP
CCCCCCCCC
28.91HPRD
Link-
344PhosphoserineNQVRSPGAP
CCCCCCCCC
28.91PhosphoELM
Link-
344PhosphoserineNQVRSPGAP
CCCCCCCCC
28.91Phosphositeplus
Link-
344PhosphoserineNQVRSPGAP
CCCCCCCCC
28.91SysPTM
Link-
344Phosphoserine.NQVRSPGAP
CCCCCCCCC
28.91UniProtKB
Link-
352PhosphothreoninePGPLTLKEV
CCCCCCCCC
38.63HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
LASP1_HUMANphysical interactionMINT-50541MINT15004028
LATS1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
colocalizati
EBI-444208
EBI-444303
EBI-444
intact10831611
10831611
10831611
10831611
10831611
10831611
10831611
10831611
10831611
10831611
ACTN1_HUMANin vitro
in vivo
HPRD:03592HPRD10224105
11423549
VAV_HUMANin vitro
yeast 2-hybrid
HPRD:03592HPRD8622875
VASP_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03592HPRD10801818
10851246
7644520
10882740
ACTN1_HUMANENSP00000346417STRING
CSK_HUMANENSP00000346417STRING
VASP_HUMANENSP00000346417STRING
LATS1_HUMANENSP00000346417STRING
CAN1_HUMANENSP00000346417STRING
RPH3L_HUMANENSP00000346417STRING
FAK1_HUMANENSP00000346417STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures