ZYX_MOUSE - dbPTM
ZYX_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZYX_MOUSE
UniProt AC Q62523
Protein Name Zyxin
Gene Name Zyx
Organism Mus musculus (Mouse).
Sequence Length 564
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Nucleus. Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of HESX1 (By similarity)..
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 MAAPRPPPAISVSVSAPAFYAPQKKFAPVVAPKPKVNPFRPGDSEPPVAAGAQRAQMGRVGEIPPPPPEDFPLPPPPLIGEGDDSEGALGGAFPPPPPPMIEEPFPPAPLEEDIFPSPPPPLEEEGGPEAPTQLPPQPREKVCSIDLEIDSLSSLLDDMTKNDPFKARVSSGYVPPPVATPFVPKPSTKPAPGGTAPLPPWKTPSSSQPPPQPQAKPQVQLHVQPQAKPHVQPQPVSSANTQPRGPLSQAPTPAPKFAPVAPKFTPVVSKFSPGAPSGPGPQPNQKMVPPDAPSSVSTGSPQPPSFTYAQQKEKPLVQEKQHPQPPPAQNQNQVRSPGGPGPLTLKEVEELEQLTQQLMQDMEHPQRQSVAVNESCGKCNQPLARAQPAVRALGQLFHITCFTCHQCQQQLQGQQFYSLEGAPYCEGCYTDTLEKCNTCGQPITDRMLRATGKAYHPQCFTCVVCACPLEGTSFIVDQANQPHCVPDYHKQYAPRCSVCSEPIMPEPGRDETVRVVALDKNFHMKCYKCEDCGKPLSIEADDNGCFPLDGHVLCRKCHSARAQT
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------MAAPRPPPA
------CCCCCCCCC		26.60-
11PhosphorylationPRPPPAISVSVSAPA
CCCCCCEEEEEECCC		15.5023984901
13PhosphorylationPPPAISVSVSAPAFY
CCCCEEEEEECCCEE		11.9923984901
15PhosphorylationPAISVSVSAPAFYAP
CCEEEEEECCCEECC		22.4926824392
20PhosphorylationSVSAPAFYAPQKKFA
EEECCCEECCCCCCC		21.3425777480
24AcetylationPAFYAPQKKFAPVVA
CCEECCCCCCCCEEC		49.1223806337
25AcetylationAFYAPQKKFAPVVAP
CEECCCCCCCCEECC		41.3222826441
35AcetylationPVVAPKPKVNPFRPG
CEECCCCCCCCCCCC		61.8523806337
44PhosphorylationNPFRPGDSEPPVAAG
CCCCCCCCCCCCCCC		58.9029514104
117PhosphorylationLEEDIFPSPPPPLEE
CCCCCCCCCCCCCCC		39.01-
144PhosphorylationQPREKVCSIDLEIDS
CCCHHCCEEEEEHHH		23.3326824392
151PhosphorylationSIDLEIDSLSSLLDD
EEEEEHHHHHHHHHH		35.4926239621
153PhosphorylationDLEIDSLSSLLDDMT
EEEHHHHHHHHHHHH		23.9226239621
154PhosphorylationLEIDSLSSLLDDMTK
EEHHHHHHHHHHHHC		37.9429119230
160PhosphorylationSSLLDDMTKNDPFKA
HHHHHHHHCCCCCHH		33.4217203969
170PhosphorylationDPFKARVSSGYVPPP
CCCHHCCCCCCCCCC		16.7026824392
171PhosphorylationPFKARVSSGYVPPPV
CCHHCCCCCCCCCCC		31.1421454597
173PhosphorylationKARVSSGYVPPPVAT
HHCCCCCCCCCCCCC		16.2529233185
180PhosphorylationYVPPPVATPFVPKPS
CCCCCCCCCCCCCCC		19.93-
237O-linked_GlycosylationHVQPQPVSSANTQPR
CCCCCCCCCCCCCCC		30.3430059200
237PhosphorylationHVQPQPVSSANTQPR
CCCCCCCCCCCCCCC		30.3425338131
238O-linked_GlycosylationVQPQPVSSANTQPRG
CCCCCCCCCCCCCCC		26.2730059200
238PhosphorylationVQPQPVSSANTQPRG
CCCCCCCCCCCCCCC		26.2726824392
244Asymmetric dimethylarginineSSANTQPRGPLSQAP
CCCCCCCCCCCHHCC		49.93-
244MethylationSSANTQPRGPLSQAP
CCCCCCCCCCCHHCC		49.9324129315
248PhosphorylationTQPRGPLSQAPTPAP
CCCCCCCHHCCCCCC		27.6828066266
252PhosphorylationGPLSQAPTPAPKFAP
CCCHHCCCCCCCCCC		34.7926824392
256AcetylationQAPTPAPKFAPVAPK
HCCCCCCCCCCCCCC		57.1523806337
263AcetylationKFAPVAPKFTPVVSK
CCCCCCCCCCCCCCC		52.7323806337
265PhosphorylationAPVAPKFTPVVSKFS
CCCCCCCCCCCCCCC		22.6925619855
269PhosphorylationPKFTPVVSKFSPGAP
CCCCCCCCCCCCCCC		28.3723684622
270AcetylationKFTPVVSKFSPGAPS
CCCCCCCCCCCCCCC		37.9523236377
272PhosphorylationTPVVSKFSPGAPSGP
CCCCCCCCCCCCCCC		26.5926824392
277PhosphorylationKFSPGAPSGPGPQPN
CCCCCCCCCCCCCCC		58.0225619855
294PhosphorylationMVPPDAPSSVSTGSP
CCCCCCCCCCCCCCC		45.1325619855
295PhosphorylationVPPDAPSSVSTGSPQ
CCCCCCCCCCCCCCC		21.0125619855
295O-linked_GlycosylationVPPDAPSSVSTGSPQ
CCCCCCCCCCCCCCC		21.0130059200
297O-linked_GlycosylationPDAPSSVSTGSPQPP
CCCCCCCCCCCCCCC		29.0630059200
297PhosphorylationPDAPSSVSTGSPQPP
CCCCCCCCCCCCCCC		29.0625619855
298PhosphorylationDAPSSVSTGSPQPPS
CCCCCCCCCCCCCCC		39.2525619855
300PhosphorylationPSSVSTGSPQPPSFT
CCCCCCCCCCCCCCC		22.0526824392
305PhosphorylationTGSPQPPSFTYAQQK
CCCCCCCCCCCCCCC		36.5825619855
307PhosphorylationSPQPPSFTYAQQKEK
CCCCCCCCCCCCCCC		23.4525619855
308PhosphorylationPQPPSFTYAQQKEKP
CCCCCCCCCCCCCCC		10.6225619855
336PhosphorylationQNQNQVRSPGGPGPL
CCCCCCCCCCCCCCC		29.1027087446
344PhosphorylationPGGPGPLTLKEVEEL
CCCCCCCCHHHHHHH		38.6325619855
369PhosphorylationMEHPQRQSVAVNESC
CCCHHHHHHHHHCCC		17.7726824392
376S-nitrosocysteineSVAVNESCGKCNQPL
HHHHHCCCCCCCCHH		5.01-
497PhosphorylationKQYAPRCSVCSEPIM
HHCCCCCCCCCCCCC		27.69-
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 ZYX_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of ZYX_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZYX_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-336, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, AND MASSSPECTROMETRY.

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