JUND_HUMAN - dbPTM
JUND_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JUND_HUMAN
UniProt AC P17535
Protein Name Transcription factor jun-D
Gene Name JUND
Organism Homo sapiens (Human).
Sequence Length 347
Subcellular Localization Nucleus.
Protein Description Transcription factor binding AP-1 sites..
Protein Sequence METPFYGDEALSGLGGGASGSGGSFASPGRLFPGAPPTAAAGSMMKKDALTLSLSEQVAAALKPAAAPPPTPLRADGAPSAAPPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSSQFLYPKVAASEEQEFAEGFVKALEDLHKQNQLGAGAAAAAAAAAAGGPSGTATGSAPPGELAPAAAAPEAPVYANLSSYAGGAGGAGGAATVAFAAEPVPFPPPPPPGALGPPRLAALKDEPQTVPDVPSFGESPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQKVLSHVNSGCQLLPQHQVPAY
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
3Phosphorylation-----METPFYGDEA
-----CCCCCCCHHH		19.8722210691
6Phosphorylation--METPFYGDEALSG
--CCCCCCCHHHCCC		25.5222210691
19PhosphorylationSGLGGGASGSGGSFA
CCCCCCCCCCCCCCC		36.4424300666
21PhosphorylationLGGGASGSGGSFASP
CCCCCCCCCCCCCCC		37.1729523821
24PhosphorylationGASGSGGSFASPGRL
CCCCCCCCCCCCCCC		22.5929523821
27PhosphorylationGSGGSFASPGRLFPG
CCCCCCCCCCCCCCC		26.3625159151
38PhosphorylationLFPGAPPTAAAGSMM
CCCCCCCCHHCCHHC		28.0621406692
43PhosphorylationPPTAAAGSMMKKDAL
CCCHHCCHHCHHHCC		15.8125159151
47PhosphorylationAAGSMMKKDALTLSL
HCCHHCHHHCCCCCH		30.2732142685
53PhosphorylationKKDALTLSLSEQVAA
HHHCCCCCHHHHHHH		25.3128348404
54UbiquitinationKDALTLSLSEQVAAA
HHCCCCCHHHHHHHH		8.0022817900
55PhosphorylationDALTLSLSEQVAAAL
HCCCCCHHHHHHHHH		23.7028348404
57PhosphorylationLTLSLSEQVAAALKP
CCCCHHHHHHHHHCC		27.1232142685
63AcetylationEQVAAALKPAAAPPP
HHHHHHHCCCCCCCC		28.0826051181
71PhosphorylationPAAAPPPTPLRADGA
CCCCCCCCCCCCCCC		40.5027050516
74PhosphorylationAPPPTPLRADGAPSA
CCCCCCCCCCCCCCC		31.6632142685
80PhosphorylationLRADGAPSAAPPDGL
CCCCCCCCCCCCCCC		36.2126074081
84UbiquitinationGAPSAAPPDGLLASP
CCCCCCCCCCCCCCC		43.5029967540
90PhosphorylationPPDGLLASPDLGLLK
CCCCCCCCCCCCHHH		20.9330266825
97UbiquitinationSPDLGLLKLASPELE
CCCCCHHHHCCHHHH		47.2321906983
99UbiquitinationDLGLLKLASPELERL
CCCHHHHCCHHHHHH		22.8132015554
100PhosphorylationLGLLKLASPELERLI
CCHHHHCCHHHHHHH		29.3719664994
110PhosphorylationLERLIIQSNGLVTTT
HHHHHHHCCCCEEEC		23.5822199227
115PhosphorylationIQSNGLVTTTPTSSQ
HHCCCCEEECCCHHH		29.9622199227
116PhosphorylationQSNGLVTTTPTSSQF
HCCCCEEECCCHHHH		24.2522199227
117PhosphorylationSNGLVTTTPTSSQFL
CCCCEEECCCHHHHC		18.4025159151
117O-linked_GlycosylationSNGLVTTTPTSSQFL
CCCCEEECCCHHHHC		18.4031492838
119PhosphorylationGLVTTTPTSSQFLYP
CCEEECCCHHHHCCC		38.6322199227
119O-linked_GlycosylationGLVTTTPTSSQFLYP
CCEEECCCHHHHCCC		38.6331492838
120O-linked_GlycosylationLVTTTPTSSQFLYPK
CEEECCCHHHHCCCE		24.2831492838
120PhosphorylationLVTTTPTSSQFLYPK
CEEECCCHHHHCCCE		24.2828122231
121PhosphorylationVTTTPTSSQFLYPKV
EEECCCHHHHCCCEE		27.6822199227
121O-linked_GlycosylationVTTTPTSSQFLYPKV
EEECCCHHHHCCCEE		27.6831492838
127UbiquitinationSSQFLYPKVAASEEQ
HHHHCCCEECCCHHH		30.8329967540
131PhosphorylationLYPKVAASEEQEFAE
CCCEECCCHHHHHHH		31.7425159151
142UbiquitinationEFAEGFVKALEDLHK
HHHHHHHHHHHHHHH		45.0232015554
212PhosphorylationGGAGGAATVAFAAEP
CCCCCCCEEEEECCC		16.3132142685
216PhosphorylationGAATVAFAAEPVPFP
CCCEEEEECCCCCCC		10.9433259812
240SumoylationPPRLAALKDEPQTVP
CCCHHHCCCCCCCCC		56.15-
241UbiquitinationPRLAALKDEPQTVPD
CCHHHCCCCCCCCCC		73.9132015554
245PhosphorylationALKDEPQTVPDVPSF
HCCCCCCCCCCCCCC		44.7323927012
251PhosphorylationQTVPDVPSFGESPPL
CCCCCCCCCCCCCCC		45.8126846344
255PhosphorylationDVPSFGESPPLSPID
CCCCCCCCCCCCCCC		32.0026846344
259PhosphorylationFGESPPLSPIDMDTQ
CCCCCCCCCCCCCHH		26.1126846344
265PhosphorylationLSPIDMDTQERIKAE
CCCCCCCHHHHHHHH		26.2030266825
282UbiquitinationRLRNRIAASKCRKRK
HHHHHHHHHHHHHHH		13.7223000965
284UbiquitinationRNRIAASKCRKRKLE
HHHHHHHHHHHHHHH		33.0723000965
294PhosphorylationKRKLERISRLEEKVK
HHHHHHHHHHHHHHH		36.71-
305PhosphorylationEKVKTLKSQNTELAS
HHHHHHHHHCHHHHH		31.6021406692
308PhosphorylationKTLKSQNTELASTAS
HHHHHHCHHHHHHHH		25.4120068231
312PhosphorylationSQNTELASTASLLRE
HHCHHHHHHHHHHHH		36.8121406692
313PhosphorylationQNTELASTASLLREQ
HCHHHHHHHHHHHHH		18.0421406692
315PhosphorylationTELASTASLLREQVA
HHHHHHHHHHHHHHH		28.2021406692
325UbiquitinationREQVAQLKQKVLSHV
HHHHHHHHHHHHHHH		35.6723000965
327UbiquitinationQVAQLKQKVLSHVNS
HHHHHHHHHHHHHHC		43.4823000965
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
100SPhosphorylationKinaseJNK1P45983
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JUND_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 JUND_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRCA1_HUMANBRCA1physical
12080089
RFWD2_HUMANRFWD2physical
12615916
CSN5_HUMANCOPS5physical
8837781
MEN1_HUMANMEN1physical
9989505
MK08_HUMANMAPK8physical
12052834
MEN1_HUMANMEN1physical
16651450
EP300_HUMANEP300physical
16264271
MEN1_HUMANMEN1physical
10500243
EP300_HUMANEP300physical
17510411
TYY1_HUMANYY1physical
17510411
ARP3_HUMANACTR3physical
20195357
CMC1_HUMANSLC25A12physical
20195357
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 JUND_HUMAN

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Related Literatures of Post-Translational Modification
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-100; SER-255 ANDSER-259, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-251; SER-255AND SER-259, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, 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-251; SER-255 ANDSER-259, 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-255 AND SER-259, ANDMASS SPECTROMETRY.
"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-255, AND MASSSPECTROMETRY.

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