NEXN_HUMAN - dbPTM
NEXN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEXN_HUMAN
UniProt AC Q0ZGT2
Protein Name Nexilin
Gene Name NEXN {ECO:0000312|HGNC:HGNC:29557}
Organism Homo sapiens (Human).
Sequence Length 675
Subcellular Localization Cytoplasm, cytoskeleton . Cell junction, adherens junction . Cytoplasm, myofibril, sarcomere, Z line . Localizes to the cell-matrix AJ. Not found at the cell-cell AJ.
Protein Description Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity..
Protein Sequence MNDISQKAEILLSSSKPVPKTYVPKLGKGDVKDKFEAMQRAREERNQRRSRDEKQRRKEQYIREREWNRRKQEIKEMLASDDEEDVSSKVEKAYVPKLTGTVKGRFAEMEKQRQEEQRKRTEEERKRRIEQDMLEKRKIQRELAKRAEQIEDINNTGTESASEEGDDSLLITVVPVKSYKTSGKMKKNFEDLEKEREEKERIKYEEDKRIRYEEQRPSLKEAKCLSLVMDDEIESEAKKESLSPGKLKLTFEELERQRQENRKKQAEEEARKRLEEEKRAFEEARRQMVNEDEENQDTAKIFKGYRPGKLKLSFEEMERQRREDEKRKAEEEARRRIEEEKKAFAEARRNMVVDDDSPEMYKTISQEFLTPGKLEINFEELLKQKMEEEKRRTEEERKHKLEMEKQEFEQLRQEMGEEEEENETFGLSREYEELIKLKRSGSIQAKNLKSKFEKIGQLSEKEIQKKIEEERARRRAIDLEIKEREAENFHEEDDVDVRPARKSEAPFTHKVNMKARFEQMAKAREEEEQRRIEEQKLLRMQFEQREIDAALQKKREEEEEEEGSIMNGSTAEDEEQTRSGAPWFKKPLKNTSVVDSEPVRFTVKVTGEPKPEITWWFEGEILQDGEDYQYIERGETYCLYLPETFPEDGGEYMCKAVNNKGSAASTCILTIESKN
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
13PhosphorylationQKAEILLSSSKPVPK
HHHHHHHCCCCCCCC		29.1728555341
16MalonylationEILLSSSKPVPKTYV
HHHHCCCCCCCCCCC		52.5626320211
16 (in isoform 4)Phosphorylation-52.5623927012
80PhosphorylationEIKEMLASDDEEDVS
HHHHHHCCCCHHHHH		41.4522167270
87PhosphorylationSDDEEDVSSKVEKAY
CCCHHHHHHHHHHHH		36.4423403867
88PhosphorylationDDEEDVSSKVEKAYV
CCHHHHHHHHHHHHH		40.3423403867
94 (in isoform 4)Phosphorylation-28.4924719451
96 (in isoform 4)Phosphorylation-17.1724719451
98 (in isoform 4)Phosphorylation-4.3424719451
101PhosphorylationYVPKLTGTVKGRFAE
HHCCCHHCHHHHHHH		17.5128060719
133SulfoxidationKRRIEQDMLEKRKIQ
HHHHHHHHHHHHHHH		5.3530846556
1362-HydroxyisobutyrylationIEQDMLEKRKIQREL
HHHHHHHHHHHHHHH		55.84-
136UbiquitinationIEQDMLEKRKIQREL
HHHHHHHHHHHHHHH		55.84-
154 (in isoform 4)Phosphorylation-52.9424719451
156PhosphorylationQIEDINNTGTESASE
HHHHHHCCCCCCCCC		40.7830266825
158PhosphorylationEDINNTGTESASEEG
HHHHCCCCCCCCCCC		25.4030266825
160PhosphorylationINNTGTESASEEGDD
HHCCCCCCCCCCCCC		36.6130266825
162PhosphorylationNTGTESASEEGDDSL
CCCCCCCCCCCCCCE		45.5230266825
168PhosphorylationASEEGDDSLLITVVP
CCCCCCCCEEEEEEE		29.8021712546
172PhosphorylationGDDSLLITVVPVKSY
CCCCEEEEEEECCCC		18.5420068231
179 (in isoform 4)Phosphorylation-16.7424719451
181PhosphorylationVPVKSYKTSGKMKKN
EECCCCCCCCCHHHC		34.18-
182PhosphorylationPVKSYKTSGKMKKNF
ECCCCCCCCCHHHCH		32.06-
203AcetylationREEKERIKYEEDKRI
HHHHHHHCHHHHHCC		53.4820167786
212PhosphorylationEEDKRIRYEEQRPSL
HHHHCCCHHHHCCCH		22.8028060719
218PhosphorylationRYEEQRPSLKEAKCL
CHHHHCCCHHHHHHH		55.0228555341
226PhosphorylationLKEAKCLSLVMDDEI
HHHHHHHHHHCCHHH		28.5226657352
235PhosphorylationVMDDEIESEAKKESL
HCCHHHHHHHHHHCC		48.8224732914
241PhosphorylationESEAKKESLSPGKLK
HHHHHHHCCCCCCCC		42.9223927012
243PhosphorylationEAKKESLSPGKLKLT
HHHHHCCCCCCCCCC		40.6730266825
288SulfoxidationFEEARRQMVNEDEEN
HHHHHHHHCCCCCCC		3.1130846556
293 (in isoform 4)Phosphorylation-53.3124719451
298PhosphorylationEDEENQDTAKIFKGY
CCCCCHHHHHHHCCC		21.7820068231
301 (in isoform 4)Phosphorylation-3.9124719451
306 (in isoform 4)Phosphorylation-42.0124719451
311UbiquitinationGYRPGKLKLSFEEME
CCCCCCEEECHHHHH		45.64-
313PhosphorylationRPGKLKLSFEEMERQ
CCCCEEECHHHHHHH		29.0828348404
357PhosphorylationNMVVDDDSPEMYKTI
CCCCCCCCHHHHHHH		29.7422617229
361PhosphorylationDDDSPEMYKTISQEF
CCCCHHHHHHHCHHH		11.8724732914
363PhosphorylationDSPEMYKTISQEFLT
CCHHHHHHHCHHHCC		14.3630266825
365PhosphorylationPEMYKTISQEFLTPG
HHHHHHHCHHHCCCC		28.9619664994
370PhosphorylationTISQEFLTPGKLEIN
HHCHHHCCCCCEEEC		35.0022617229
405AcetylationKHKLEMEKQEFEQLR
HHHHHHHHHHHHHHH		54.5420167786
424PhosphorylationEEEEENETFGLSREY
CHHHHHHCCCCCHHH		34.2928270605
428PhosphorylationENETFGLSREYEELI
HHHCCCCCHHHHHHH		24.3628270605
431PhosphorylationTFGLSREYEELIKLK
CCCCCHHHHHHHHHH		17.3728270605
436UbiquitinationREYEELIKLKRSGSI
HHHHHHHHHHHCCCC		61.66-
440PhosphorylationELIKLKRSGSIQAKN
HHHHHHHCCCCCCCC		34.9929514088
442PhosphorylationIKLKRSGSIQAKNLK
HHHHHCCCCCCCCHH		16.8729514088
446AcetylationRSGSIQAKNLKSKFE
HCCCCCCCCHHHHHH		46.5720167786
454MalonylationNLKSKFEKIGQLSEK
CHHHHHHHHHCCCHH		56.0926320211
461MalonylationKIGQLSEKEIQKKIE
HHHCCCHHHHHHHHH		57.6626320211
482UbiquitinationRAIDLEIKEREAENF
HHHHHHHHHHHHHHC		41.15-
500 (in isoform 4)Phosphorylation-22.4424719451
503PhosphorylationDVRPARKSEAPFTHK
CCCCCCCCCCCCCCC		33.1824702127
564PhosphorylationEEEEEEGSIMNGSTA
HHHHHHCCCCCCCCC		23.1921712546
569PhosphorylationEGSIMNGSTAEDEEQ
HCCCCCCCCCCCHHH		21.3126055452
570PhosphorylationGSIMNGSTAEDEEQT
CCCCCCCCCCCHHHH		35.1521712546
577PhosphorylationTAEDEEQTRSGAPWF
CCCCHHHHCCCCCCC		30.0424732914
579PhosphorylationEDEEQTRSGAPWFKK
CCHHHHCCCCCCCCC		42.5717929957
586MalonylationSGAPWFKKPLKNTSV
CCCCCCCCCCCCCCC		46.2226320211
589MalonylationPWFKKPLKNTSVVDS
CCCCCCCCCCCCCCC		67.7026320211
592PhosphorylationKKPLKNTSVVDSEPV
CCCCCCCCCCCCCCE		29.5417929957
602PhosphorylationDSEPVRFTVKVTGEP
CCCCEEEEEEECCCC		14.6218491316
636PhosphorylationQYIERGETYCLYLPE
EEEECCCEEEEECCC		23.5124043423
637PhosphorylationYIERGETYCLYLPET
EEECCCEEEEECCCC		3.9924043423
640PhosphorylationRGETYCLYLPETFPE
CCCEEEEECCCCCCC		19.3624043423
644PhosphorylationYCLYLPETFPEDGGE
EEEECCCCCCCCCCE		42.4224043423
652PhosphorylationFPEDGGEYMCKAVNN
CCCCCCEEEEEECCC		15.8724043423
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 NEXN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NEXN_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 NEXN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GELS_HUMANGSNphysical
28514442
MYO1B_HUMANMYO1Bphysical
28514442
ACTB_HUMANACTBphysical
28514442
NEB1_HUMANPPP1R9Aphysical
28514442
ACTA_HUMANACTA2physical
28514442
ACTBL_HUMANACTBL2physical
28514442
ANK3_HUMANANK3physical
28514442
ARP10_HUMANACTR10physical
28514442
CPVL_HUMANCPVLphysical
28514442
LIMA1_HUMANLIMA1physical
28514442
MYO1D_HUMANMYO1Dphysical
28514442
FBX34_HUMANFBXO34physical
28514442
FBX46_HUMANFBXO46physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613122Cardiomyopathy, dilated 1CC (CMD1CC)
613876Cardiomyopathy, familial hypertrophic 20 (CMH20)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NEXN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, 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-80 AND SER-357, AND MASSSPECTROMETRY.
"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-80, 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-80; SER-365 AND SER-569,AND MASS SPECTROMETRY.
"Molecular cloning of NELIN, a putative human cytoskeleton regulationgene.";
Zhao Y., Wei Y.-J., Cao H.-Q., Ding J.-F.;
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 33:19-24(2001).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-675 (ISOFORM 1), FUNCTION, TISSUESPECIFICITY, AND VARIANT ARG-245.
"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 THR-370, AND MASSSPECTROMETRY.

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