ETV3_HUMAN - dbPTM
ETV3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ETV3_HUMAN
UniProt AC P41162
Protein Name ETS translocation variant 3
Gene Name ETV3
Organism Homo sapiens (Human).
Sequence Length 512
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor that contribute to growth arrest during terminal macrophage differentiation by repressing target genes involved in Ras-dependent proliferation. Represses MMP1 promoter activity..
Protein Sequence MKAGCSIVEKPEGGGGYQFPDWAYKTESSPGSRQIQLWHFILELLQKEEFRHVIAWQQGEYGEFVIKDPDEVARLWGRRKCKPQMNYDKLSRALRYYYNKRILHKTKGKRFTYKFNFNKLVMPNYPFINIRSSGVVPQSAPPVPTASSRFHFPPLDTHSPTNDVQPGRFSASSLTASGQESSNGTDRKTELSELEDGSAADWRRGVDPVSSRNAIGGGGIGHQKRKPDIMLPLFARPGMYPDPHSPFAVSPIPGRGGVLNVPISPALSLTPTIFSYSPSPGLSPFTSSSCFSFNPEEMKHYLHSQACSVFNYHLSPRTFPRYPGLMVPPLQCQMHPEESTQFSIKLQPPPVGRKNRERVESSEESAPVTTPTMASIPPRIKVEPASEKDPESLRQSAREKEEHTQEEGTVPSRTIEEEKGTIFARPAAPPIWPSVPISTPSGEPLEVTEDSEDRPGKEPSAPEKKEDALMPPKLRLKRRWNDDPEARELSKSGKFLWNGSGPQGLATAAADA
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
2Ubiquitination------MKAGCSIVE
------CCCCEEEEE		54.1929967540
6Phosphorylation--MKAGCSIVEKPEG
--CCCCEEEEECCCC		28.8423312004
10UbiquitinationAGCSIVEKPEGGGGY
CCEEEEECCCCCCCC		37.1629967540
17PhosphorylationKPEGGGGYQFPDWAY
CCCCCCCCCCCCCEE		15.4023312004
24PhosphorylationYQFPDWAYKTESSPG
CCCCCCEEECCCCCC		17.7523312004
25UbiquitinationQFPDWAYKTESSPGS
CCCCCEEECCCCCCH		37.7621963094
26PhosphorylationFPDWAYKTESSPGSR
CCCCEEECCCCCCHH		28.5529052541
28PhosphorylationDWAYKTESSPGSRQI
CCEEECCCCCCHHHH		47.2523312004
29PhosphorylationWAYKTESSPGSRQIQ
CEEECCCCCCHHHHH		27.3529052541
32PhosphorylationKTESSPGSRQIQLWH
ECCCCCCHHHHHHHH		25.1322817900
80UbiquitinationARLWGRRKCKPQMNY
HHHHCCCCCCCCCCH		45.2929967540
82UbiquitinationLWGRRKCKPQMNYDK
HHCCCCCCCCCCHHH		41.1229967540
89UbiquitinationKPQMNYDKLSRALRY
CCCCCHHHHHHHHHH		37.69-
109UbiquitinationILHKTKGKRFTYKFN
EECCCCCCCEEEEEC		45.9923000965
114UbiquitinationKGKRFTYKFNFNKLV
CCCCEEEEECCCEEE		30.6721890473
114UbiquitinationKGKRFTYKFNFNKLV
CCCCEEEEECCCEEE		30.6721890473
114 (in isoform 2)Ubiquitination-30.6721890473
114 (in isoform 1)Ubiquitination-30.6721890473
119UbiquitinationTYKFNFNKLVMPNYP
EEEECCCEEECCCCC		38.0223000965
132PhosphorylationYPFINIRSSGVVPQS
CCEEEEECCCCCCCC		27.8723403867
133PhosphorylationPFINIRSSGVVPQSA
CEEEEECCCCCCCCC		26.2623403867
139PhosphorylationSSGVVPQSAPPVPTA
CCCCCCCCCCCCCCC		36.3530266825
145PhosphorylationQSAPPVPTASSRFHF
CCCCCCCCCCCCCCC		39.1323663014
147PhosphorylationAPPVPTASSRFHFPP
CCCCCCCCCCCCCCC		25.2323663014
148PhosphorylationPPVPTASSRFHFPPL
CCCCCCCCCCCCCCC		36.1823663014
157PhosphorylationFHFPPLDTHSPTNDV
CCCCCCCCCCCCCCC		31.7530266825
159PhosphorylationFPPLDTHSPTNDVQP
CCCCCCCCCCCCCCC		35.2023401153
161PhosphorylationPLDTHSPTNDVQPGR
CCCCCCCCCCCCCCC		47.2530266825
170PhosphorylationDVQPGRFSASSLTAS
CCCCCCEECCCEEEC		26.3629255136
172PhosphorylationQPGRFSASSLTASGQ
CCCCEECCCEEECCC		25.3629255136
173PhosphorylationPGRFSASSLTASGQE
CCCEECCCEEECCCC		29.4729255136
175PhosphorylationRFSASSLTASGQESS
CEECCCEEECCCCCC		22.2629255136
188UbiquitinationSSNGTDRKTELSELE
CCCCCCCCCCHHHHC		49.5129967540
224UbiquitinationGGGIGHQKRKPDIML
CCCCCCCCCCCCCEE		57.6327667366
240PhosphorylationLFARPGMYPDPHSPF
CCCCCCCCCCCCCCC		15.4829978859
245PhosphorylationGMYPDPHSPFAVSPI
CCCCCCCCCCCCCCC		27.4022167270
250PhosphorylationPHSPFAVSPIPGRGG
CCCCCCCCCCCCCCC		17.4322167270
264PhosphorylationGVLNVPISPALSLTP
CEECCCCCCCCCCCC		9.6921552520
268PhosphorylationVPISPALSLTPTIFS
CCCCCCCCCCCEEEE		32.1028348404
270PhosphorylationISPALSLTPTIFSYS
CCCCCCCCCEEEECC		18.2728348404
272PhosphorylationPALSLTPTIFSYSPS
CCCCCCCEEEECCCC		29.4428348404
275PhosphorylationSLTPTIFSYSPSPGL
CCCCEEEECCCCCCC		22.3528348404
276PhosphorylationLTPTIFSYSPSPGLS
CCCEEEECCCCCCCC		17.5328348404
277PhosphorylationTPTIFSYSPSPGLSP
CCEEEECCCCCCCCC		20.0828348404
301PhosphorylationNPEEMKHYLHSQACS
CHHHHHHHHHHCCCH		10.6923312004
304PhosphorylationEMKHYLHSQACSVFN
HHHHHHHHCCCHHHC		19.5123312004
308PhosphorylationYLHSQACSVFNYHLS
HHHHCCCHHHCCCCC		32.5328348404
312PhosphorylationQACSVFNYHLSPRTF
CCCHHHCCCCCCCCC		7.8328152594
315PhosphorylationSVFNYHLSPRTFPRY
HHHCCCCCCCCCCCC		10.0628152594
318PhosphorylationNYHLSPRTFPRYPGL
CCCCCCCCCCCCCCC		41.18-
361PhosphorylationKNRERVESSEESAPV
CCHHHHHCCCCCCCC		39.9427282143
362PhosphorylationNRERVESSEESAPVT
CHHHHHCCCCCCCCC		31.7025884760
369PhosphorylationSEESAPVTTPTMASI
CCCCCCCCCCCHHCC		26.4624114839
370PhosphorylationEESAPVTTPTMASIP
CCCCCCCCCCHHCCC		19.5930624053
372PhosphorylationSAPVTTPTMASIPPR
CCCCCCCCHHCCCCC		24.2328985074
375PhosphorylationVTTPTMASIPPRIKV
CCCCCHHCCCCCCCC		25.4624719451
381SumoylationASIPPRIKVEPASEK
HCCCCCCCCCCCCCC		41.65-
381AcetylationASIPPRIKVEPASEK
HCCCCCCCCCCCCCC		41.6526051181
381SumoylationASIPPRIKVEPASEK
HCCCCCCCCCCCCCC		41.6528112733
386PhosphorylationRIKVEPASEKDPESL
CCCCCCCCCCCHHHH		56.7630576142
388SumoylationKVEPASEKDPESLRQ
CCCCCCCCCHHHHHH		75.8828112733
388UbiquitinationKVEPASEKDPESLRQ
CCCCCCCCCHHHHHH		75.8824816145
388AcetylationKVEPASEKDPESLRQ
CCCCCCCCCHHHHHH		75.8819608861
404PhosphorylationAREKEEHTQEEGTVP
HHHHHHHHCCCCCCC		40.7428348404
419UbiquitinationSRTIEEEKGTIFARP
CCCCEECCCCEEEEC		65.7129967540
473AcetylationEDALMPPKLRLKRRW
HHCCCCCCCCCHHHC		40.1325953088
494AcetylationRELSKSGKFLWNGSG
HHHHHCCCCCCCCCC		44.3625953088
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 ETV3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ETV3_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 ETV3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NSD3_HUMANWHSC1L1physical
23455924
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 ETV3_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-388, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND MASSSPECTROMETRY.

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