VEZF1_HUMAN - dbPTM
VEZF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VEZF1_HUMAN
UniProt AC Q14119
Protein Name Vascular endothelial zinc finger 1
Gene Name VEZF1
Organism Homo sapiens (Human).
Sequence Length 521
Subcellular Localization Nucleus .
Protein Description Possible transcription factor. Specifically binds to the CT/GC-rich region of the interleukin-3 promoter and mediates tax transactivation of IL-3..
Protein Sequence MEANWTAFLFQAHEASHHQQQAAQNSLLPLLSSAVEPPDQKPLLPIPITQKPQGAPETLKDAIGIKKEKPKTSFVCTYCSKAFRDSYHLRRHESCHTGIKLVSRPKKTPTTVVPLISTIAGDSSRTSLVSTIAGILSTVTTSSSGTNPSSSASTTAMPVTQSVKKPSKPVKKNHACEMCGKAFRDVYHLNRHKLSHSDEKPFECPICNQRFKRKDRMTYHVRSHEGGITKPYTCSVCGKGFSRPDHLSCHVKHVHSTERPFKCQTCTAAFATKDRLRTHMVRHEGKVSCNICGKLLSAAYITSHLKTHGQSQSINCNTCKQGISKTCMSEETSNQKQQQQQQQQQQQQQQQQQQHVTSWPGKQVETLRLWEEAVKARKKEAANLCQTSTAATTPVTLTTPFSITSSVSSGTMSNPVTVAAAMSMRSPVNVSSAVNITSPMNIGHPVTITSPLSMTSPLTLTTPVNLPTPVTAPVNIAHPVTITSPMNLPTPMTLAAPLNIAMRPVESMPFLPQALPTSPPW
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
41SumoylationAVEPPDQKPLLPIPI
CCCCCCCCCCCCCCC		45.04-
66SumoylationLKDAIGIKKEKPKTS
HHHHHCCCCCCCCCE		50.06-
66AcetylationLKDAIGIKKEKPKTS
HHHHHCCCCCCCCCE		50.0625953088
66SumoylationLKDAIGIKKEKPKTS
HHHHHCCCCCCCCCE		50.06-
86PhosphorylationCSKAFRDSYHLRRHE
CCHHHHHHHHHHCCC		15.3623186163
87PhosphorylationSKAFRDSYHLRRHES
CHHHHHHHHHHCCCC		14.7923186163
103O-linked_GlycosylationHTGIKLVSRPKKTPT
CCCEEEECCCCCCCC		53.9930059200
108O-linked_GlycosylationLVSRPKKTPTTVVPL
EECCCCCCCCCEEEE		31.8130059200
110O-linked_GlycosylationSRPKKTPTTVVPLIS
CCCCCCCCCEEEEEE		37.1430059200
111O-linked_GlycosylationRPKKTPTTVVPLIST
CCCCCCCCEEEEEEC		22.2530059200
117O-linked_GlycosylationTTVVPLISTIAGDSS
CCEEEEEECCCCCCC		22.8030059200
118O-linked_GlycosylationTVVPLISTIAGDSSR
CEEEEEECCCCCCCH		14.0930059200
123O-linked_GlycosylationISTIAGDSSRTSLVS
EECCCCCCCHHHHHH		22.3230059200
124O-linked_GlycosylationSTIAGDSSRTSLVST
ECCCCCCCHHHHHHH		44.3030059200
126O-linked_GlycosylationIAGDSSRTSLVSTIA
CCCCCCHHHHHHHHH		28.4930059200
126PhosphorylationIAGDSSRTSLVSTIA
CCCCCCHHHHHHHHH		28.4928122231
127O-linked_GlycosylationAGDSSRTSLVSTIAG
CCCCCHHHHHHHHHH		26.1830059200
127PhosphorylationAGDSSRTSLVSTIAG
CCCCCHHHHHHHHHH		26.1820068231
130PhosphorylationSSRTSLVSTIAGILS
CCHHHHHHHHHHHHH		21.2720068231
131PhosphorylationSRTSLVSTIAGILST
CHHHHHHHHHHHHHH		13.8420068231
137PhosphorylationSTIAGILSTVTTSSS
HHHHHHHHHEECCCC		20.9320068231
137O-linked_GlycosylationSTIAGILSTVTTSSS
HHHHHHHHHEECCCC		20.9330059200
138O-linked_GlycosylationTIAGILSTVTTSSSG
HHHHHHHHEECCCCC		20.5830059200
138PhosphorylationTIAGILSTVTTSSSG
HHHHHHHHEECCCCC		20.5828122231
140PhosphorylationAGILSTVTTSSSGTN
HHHHHHEECCCCCCC		22.5028122231
141O-linked_GlycosylationGILSTVTTSSSGTNP
HHHHHEECCCCCCCC		23.4430059200
141PhosphorylationGILSTVTTSSSGTNP
HHHHHEECCCCCCCC		23.4428122231
142PhosphorylationILSTVTTSSSGTNPS
HHHHEECCCCCCCCC		17.0920068231
142O-linked_GlycosylationILSTVTTSSSGTNPS
HHHHEECCCCCCCCC		17.0930059200
143PhosphorylationLSTVTTSSSGTNPSS
HHHEECCCCCCCCCC		30.6020068231
143O-linked_GlycosylationLSTVTTSSSGTNPSS
HHHEECCCCCCCCCC		30.6030059200
144PhosphorylationSTVTTSSSGTNPSSS
HHEECCCCCCCCCCC		49.7820068231
146PhosphorylationVTTSSSGTNPSSSAS
EECCCCCCCCCCCCC		46.0028122231
146O-linked_GlycosylationVTTSSSGTNPSSSAS
EECCCCCCCCCCCCC		46.0030059200
149PhosphorylationSSSGTNPSSSASTTA
CCCCCCCCCCCCCCC		38.7120068231
149O-linked_GlycosylationSSSGTNPSSSASTTA
CCCCCCCCCCCCCCC		38.7130059200
150PhosphorylationSSGTNPSSSASTTAM
CCCCCCCCCCCCCCC		31.0520068231
150O-linked_GlycosylationSSGTNPSSSASTTAM
CCCCCCCCCCCCCCC		31.0530059200
151PhosphorylationSGTNPSSSASTTAMP
CCCCCCCCCCCCCCC		30.4920068231
153PhosphorylationTNPSSSASTTAMPVT
CCCCCCCCCCCCCCC		28.3920068231
154O-linked_GlycosylationNPSSSASTTAMPVTQ
CCCCCCCCCCCCCCC		20.4930059200
154PhosphorylationNPSSSASTTAMPVTQ
CCCCCCCCCCCCCCC		20.4920068231
155PhosphorylationPSSSASTTAMPVTQS
CCCCCCCCCCCCCCC		20.6120068231
160O-linked_GlycosylationSTTAMPVTQSVKKPS
CCCCCCCCCCCCCCC		14.8430059200
160PhosphorylationSTTAMPVTQSVKKPS
CCCCCCCCCCCCCCC		14.8428122231
162PhosphorylationTAMPVTQSVKKPSKP
CCCCCCCCCCCCCCC		26.9128122231
181UbiquitinationHACEMCGKAFRDVYH
HHHHHCCHHHHHHHH		39.15-
195PhosphorylationHLNRHKLSHSDEKPF
HHHCCCCCCCCCCCC		26.2523663014
197PhosphorylationNRHKLSHSDEKPFEC
HCCCCCCCCCCCCCC		44.0525159151
200UbiquitinationKLSHSDEKPFECPIC
CCCCCCCCCCCCCCC		61.06-
256PhosphorylationCHVKHVHSTERPFKC
EEEEECCCCCCCCCC		30.7620068231
257PhosphorylationHVKHVHSTERPFKCQ
EEEECCCCCCCCCCC		22.5720068231
273UbiquitinationCTAAFATKDRLRTHM
CCCEEECHHHHHHHH		37.10-
286UbiquitinationHMVRHEGKVSCNICG
HHHCCCCEEEECHHH		28.17-
294AcetylationVSCNICGKLLSAAYI
EEECHHHHHHHHHHH		41.6725953088
297PhosphorylationNICGKLLSAAYITSH
CHHHHHHHHHHHHHH		22.6820068231
300PhosphorylationGKLLSAAYITSHLKT
HHHHHHHHHHHHHHH		12.4020068231
302PhosphorylationLLSAAYITSHLKTHG
HHHHHHHHHHHHHHC		9.4520068231
303PhosphorylationLSAAYITSHLKTHGQ
HHHHHHHHHHHHHCC		19.7720068231
320UbiquitinationSINCNTCKQGISKTC
CCCCCCCCCCHHHHH		49.90-
320AcetylationSINCNTCKQGISKTC
CCCCCCCCCCHHHHH		49.9025953088
325UbiquitinationTCKQGISKTCMSEET
CCCCCHHHHHCCHHH		43.77-
325AcetylationTCKQGISKTCMSEET
CCCCCHHHHHCCHHH		43.7725953088
362UbiquitinationHVTSWPGKQVETLRL
HHHHCCCCHHHHHHH		47.2821890473
362AcetylationHVTSWPGKQVETLRL
HHHHCCCCHHHHHHH		47.2819608861
375UbiquitinationRLWEEAVKARKKEAA
HHHHHHHHHHHHHHH		49.90-
387PhosphorylationEAANLCQTSTAATTP
HHHHHHCCCCCCCCC		27.3522210691
388PhosphorylationAANLCQTSTAATTPV
HHHHHCCCCCCCCCE		7.0922210691
389PhosphorylationANLCQTSTAATTPVT
HHHHCCCCCCCCCEE		24.5722210691
392PhosphorylationCQTSTAATTPVTLTT
HCCCCCCCCCEEEEC		29.2122210691
393PhosphorylationQTSTAATTPVTLTTP
CCCCCCCCCEEEECC		15.8422210691
409PhosphorylationSITSSVSSGTMSNPV
EEEECCCCCCCCCCH		35.8122210691
411PhosphorylationTSSVSSGTMSNPVTV
EECCCCCCCCCCHHH		21.2622210691
413PhosphorylationSVSSGTMSNPVTVAA
CCCCCCCCCCHHHHH		37.5122210691
417PhosphorylationGTMSNPVTVAAAMSM
CCCCCCHHHHHHHHC		12.9925332170
423PhosphorylationVTVAAAMSMRSPVNV
HHHHHHHHCCCCCCC		13.3025332170
447PhosphorylationMNIGHPVTITSPLSM
CCCCCCEEECCCCCC		24.0026074081
449PhosphorylationIGHPVTITSPLSMTS
CCCCEEECCCCCCCC		18.2226074081
450PhosphorylationGHPVTITSPLSMTSP
CCCEEECCCCCCCCC		21.7226074081
453PhosphorylationVTITSPLSMTSPLTL
EEECCCCCCCCCCEE		24.3326074081
517PhosphorylationFLPQALPTSPPW---
CCCCCCCCCCCC---		55.5020068231
518PhosphorylationLPQALPTSPPW----
CCCCCCCCCCC----		27.3320068231
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 VEZF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VEZF1_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 VEZF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VEZF1_HUMAN !!
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 VEZF1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-362, AND MASS SPECTROMETRY.

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