JADE3_HUMAN - dbPTM
JADE3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JADE3_HUMAN
UniProt AC Q92613
Protein Name Protein Jade-3
Gene Name JADE3
Organism Homo sapiens (Human).
Sequence Length 823
Subcellular Localization
Protein Description Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo..
Protein Sequence MKRHRPVSSSDSSDESPSTSFTSGSMYRIKSKIPNEHKKPAEVFRKDLISAMKLPDSHHINPDSYYLFADTWKEEWEKGVQVPASPDTVPQPSLRIIAEKVKDVLFIRPRKYIHCSSPDTTEPGYINIMELAASVCRYDLDDMDIFWLQELNEDLAEMGCGPVDENLMEKTVEVLERHCHENMNHAIETEEGLGIEYDEDVICDVCRSPDSEEGNDMVFCDKCNVCVHQACYGILKVPEGSWLCRSCVLGIYPQCVLCPKKGGALKTTKTGTKWAHVSCALWIPEVSIACPERMEPITKISHIPPSRWALVCNLCKLKTGACIQCSIKSCITAFHVTCAFEHGLEMKTILDEGDEVKFKSYCLKHSQNRQKLGEAEYPHHRAKEQSQAKSEKTSLRAQKLRELEEEFYSLVRVEDVAAELGMPTLAVDFIYNYWKLKRKSNFNKPLFPPKEDEENGLVQPKEESIHTRMRMFMHLRQDLERVRNLCYMISRREKLKLSHNKIQEQIFGLQVQLLNQEIDAGLPLTNALENSLFYPPPRITLKLKMPKSTPEDHRNSSTETDQQPHSPDSSSSVHSIRNMQVPQESLEMRTKSYPRYPLESKNNRLLASLSHSRSEAKESSPAWRTPSSECYHGQSLGKPLVLQAALHGQSSIGNGKSQPNSKFAKSNGLEGSWSGNVTQKDSSSEMFCDQEPVFSPHLVSQGSFRKSTVEHFSRSFKETTNRWVKNTEDLQCYVKPTKNMSPKEQFWGRQVLRRSAGRAPYQENDGYCPDLELSDSEAESDGNKEKVRVRKDSSDRENPPHDSRRDCHGKSKTHPLSHSSMQR
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
8PhosphorylationMKRHRPVSSSDSSDE
CCCCCCCCCCCCCCC
27.1420873877
9PhosphorylationKRHRPVSSSDSSDES
CCCCCCCCCCCCCCC
38.1020873877
10PhosphorylationRHRPVSSSDSSDESP
CCCCCCCCCCCCCCC
33.7220873877
12PhosphorylationRPVSSSDSSDESPST
CCCCCCCCCCCCCCC
41.4520873877
13PhosphorylationPVSSSDSSDESPSTS
CCCCCCCCCCCCCCC
50.8430576142
16PhosphorylationSSDSSDESPSTSFTS
CCCCCCCCCCCCCCC
29.1920873877
18PhosphorylationDSSDESPSTSFTSGS
CCCCCCCCCCCCCCC
46.0620873877
19PhosphorylationSSDESPSTSFTSGSM
CCCCCCCCCCCCCCC
31.1120873877
20PhosphorylationSDESPSTSFTSGSMY
CCCCCCCCCCCCCCE
30.7520873877
22PhosphorylationESPSTSFTSGSMYRI
CCCCCCCCCCCCEEE
31.7623312004
23PhosphorylationSPSTSFTSGSMYRIK
CCCCCCCCCCCEEEC
27.1927251275
25PhosphorylationSTSFTSGSMYRIKSK
CCCCCCCCCEEECCC
16.6527251275
27PhosphorylationSFTSGSMYRIKSKIP
CCCCCCCEEECCCCC
15.7522817900
30AcetylationSGSMYRIKSKIPNEH
CCCCEEECCCCCCCC
36.3819608861
32AcetylationSMYRIKSKIPNEHKK
CCEEECCCCCCCCCC
58.1219608861
38AcetylationSKIPNEHKKPAEVFR
CCCCCCCCCCHHHHH
55.0323749302
39AcetylationKIPNEHKKPAEVFRK
CCCCCCCCCHHHHHH
51.9026051181
46UbiquitinationKPAEVFRKDLISAMK
CCHHHHHHHHHHHCC
45.48-
78UbiquitinationTWKEEWEKGVQVPAS
CHHHHHHHCCCCCCC
66.51-
85PhosphorylationKGVQVPASPDTVPQP
HCCCCCCCCCCCCCC
19.7623401153
88PhosphorylationQVPASPDTVPQPSLR
CCCCCCCCCCCCCHH
37.1530266825
93PhosphorylationPDTVPQPSLRIIAEK
CCCCCCCCHHHHHHH
25.6524732914
112PhosphorylationLFIRPRKYIHCSSPD
EEECCCCEEECCCCC
9.3627080861
116PhosphorylationPRKYIHCSSPDTTEP
CCCEEECCCCCCCCC
30.6426074081
117PhosphorylationRKYIHCSSPDTTEPG
CCEEECCCCCCCCCC
31.9926074081
120PhosphorylationIHCSSPDTTEPGYIN
EECCCCCCCCCCCCC
36.1226074081
121PhosphorylationHCSSPDTTEPGYINI
ECCCCCCCCCCCCCH
47.7826074081
125PhosphorylationPDTTEPGYINIMELA
CCCCCCCCCCHHHHH
11.0827080861
208PhosphorylationVICDVCRSPDSEEGN
CEEEECCCCCCCCCC
28.1220873877
211PhosphorylationDVCRSPDSEEGNDMV
EECCCCCCCCCCCCE
40.7120873877
273AcetylationKTTKTGTKWAHVSCA
EECCCCCCEEEEEEE
43.6725953088
299AcetylationERMEPITKISHIPPS
CCCCCCCEECCCCHH
42.8223236377
316AcetylationALVCNLCKLKTGACI
HHHHHHHCCCCCCEE
57.0725953088
318UbiquitinationVCNLCKLKTGACIQC
HHHHHCCCCCCEEEC
30.33-
348PhosphorylationEHGLEMKTILDEGDE
HCCCEEEEECCCCCC
26.01-
357UbiquitinationLDEGDEVKFKSYCLK
CCCCCCEEHHHHHHH
45.05-
364AcetylationKFKSYCLKHSQNRQK
EHHHHHHHHCHHHHH
37.3325953088
364UbiquitinationKFKSYCLKHSQNRQK
EHHHHHHHHCHHHHH
37.33-
371AcetylationKHSQNRQKLGEAEYP
HHCHHHHHHCCCCCH
56.0423749302
371UbiquitinationKHSQNRQKLGEAEYP
HHCHHHHHHCCCCCH
56.04-
377PhosphorylationQKLGEAEYPHHRAKE
HHHCCCCCHHHHHHH
18.2125404012
383AcetylationEYPHHRAKEQSQAKS
CCHHHHHHHHHHHHH
57.1323236377
386PhosphorylationHHRAKEQSQAKSEKT
HHHHHHHHHHHHHHH
32.9525404012
389AcetylationAKEQSQAKSEKTSLR
HHHHHHHHHHHHHHH
52.0623236377
408PhosphorylationRELEEEFYSLVRVED
HHHHHHHHHHCCHHH
12.3627642862
433PhosphorylationAVDFIYNYWKLKRKS
HHHHHHHHHHHHCCC
6.2220058876
440PhosphorylationYWKLKRKSNFNKPLF
HHHHHCCCCCCCCCC
51.16-
461AcetylationENGLVQPKEESIHTR
CCCCCCCCHHHHHHH
57.9523954790
464PhosphorylationLVQPKEESIHTRMRM
CCCCCHHHHHHHHHH
22.2927251275
467PhosphorylationPKEESIHTRMRMFMH
CCHHHHHHHHHHHHH
25.2127251275
496UbiquitinationISRREKLKLSHNKIQ
HHHHHHHCCCCHHHH
60.04-
548PhosphorylationLKLKMPKSTPEDHRN
EEEECCCCCCCCCCC
43.2421955146
549PhosphorylationKLKMPKSTPEDHRNS
EEECCCCCCCCCCCC
36.5021955146
556PhosphorylationTPEDHRNSSTETDQQ
CCCCCCCCCCCCCCC
38.3029255136
557PhosphorylationPEDHRNSSTETDQQP
CCCCCCCCCCCCCCC
33.5429255136
558PhosphorylationEDHRNSSTETDQQPH
CCCCCCCCCCCCCCC
42.6029255136
560PhosphorylationHRNSSTETDQQPHSP
CCCCCCCCCCCCCCC
38.9129255136
566PhosphorylationETDQQPHSPDSSSSV
CCCCCCCCCCCCCCH
36.7729255136
569PhosphorylationQQPHSPDSSSSVHSI
CCCCCCCCCCCHHHH
35.1929255136
570PhosphorylationQPHSPDSSSSVHSIR
CCCCCCCCCCHHHHH
33.7329255136
571PhosphorylationPHSPDSSSSVHSIRN
CCCCCCCCCHHHHHC
40.0929255136
572PhosphorylationHSPDSSSSVHSIRNM
CCCCCCCCHHHHHCC
26.2929255136
575PhosphorylationDSSSSVHSIRNMQVP
CCCCCHHHHHCCCCC
22.5322167270
585PhosphorylationNMQVPQESLEMRTKS
CCCCCHHHHHHHCCC
25.1221815630
592PhosphorylationSLEMRTKSYPRYPLE
HHHHHCCCCCCCCCC
39.4925159151
601AcetylationPRYPLESKNNRLLAS
CCCCCCCCCCHHHHH
49.1925953088
608PhosphorylationKNNRLLASLSHSRSE
CCCHHHHHHHCCHHH
30.3020068231
610PhosphorylationNRLLASLSHSRSEAK
CHHHHHHHCCHHHHH
19.5420068231
612PhosphorylationLLASLSHSRSEAKES
HHHHHHCCHHHHHCC
33.8429116813
613MethylationLASLSHSRSEAKESS
HHHHHCCHHHHHCCC
32.85115480711
614PhosphorylationASLSHSRSEAKESSP
HHHHCCHHHHHCCCC
44.9429759185
617AcetylationSHSRSEAKESSPAWR
HCCHHHHHCCCCCCC
54.8226051181
620PhosphorylationRSEAKESSPAWRTPS
HHHHHCCCCCCCCCC
21.5221815630
625PhosphorylationESSPAWRTPSSECYH
CCCCCCCCCCCCCCC
19.4725159151
627PhosphorylationSPAWRTPSSECYHGQ
CCCCCCCCCCCCCCC
37.8526074081
628PhosphorylationPAWRTPSSECYHGQS
CCCCCCCCCCCCCCC
32.6526074081
631PhosphorylationRTPSSECYHGQSLGK
CCCCCCCCCCCCCCC
12.6326074081
635PhosphorylationSECYHGQSLGKPLVL
CCCCCCCCCCCCHHH
43.6225159151
638AcetylationYHGQSLGKPLVLQAA
CCCCCCCCCHHHHHH
40.2319608861
650PhosphorylationQAALHGQSSIGNGKS
HHHHCCCCCCCCCCC
28.6326074081
651PhosphorylationAALHGQSSIGNGKSQ
HHHCCCCCCCCCCCC
26.9926074081
656AcetylationQSSIGNGKSQPNSKF
CCCCCCCCCCCCCCC
50.3323749302
662AcetylationGKSQPNSKFAKSNGL
CCCCCCCCCCHHCCC
56.8525953088
665AcetylationQPNSKFAKSNGLEGS
CCCCCCCHHCCCCCC
47.8125953088
672PhosphorylationKSNGLEGSWSGNVTQ
HHCCCCCCCCCCCCC
14.5325159151
674PhosphorylationNGLEGSWSGNVTQKD
CCCCCCCCCCCCCCC
23.3725627689
695PhosphorylationCDQEPVFSPHLVSQG
ECCCCCCCHHHHCCC
16.1924732914
700PhosphorylationVFSPHLVSQGSFRKS
CCCHHHHCCCCCCHH
34.8724732914
703PhosphorylationPHLVSQGSFRKSTVE
HHHHCCCCCCHHHHH
17.7824732914
706UbiquitinationVSQGSFRKSTVEHFS
HCCCCCCHHHHHHHH
48.76-
707PhosphorylationSQGSFRKSTVEHFSR
CCCCCCHHHHHHHHH
33.1725159151
708PhosphorylationQGSFRKSTVEHFSRS
CCCCCHHHHHHHHHH
32.7126074081
715PhosphorylationTVEHFSRSFKETTNR
HHHHHHHHHHHHHHH
39.20-
725UbiquitinationETTNRWVKNTEDLQC
HHHHHHHCCCCCCEE
51.71-
733PhosphorylationNTEDLQCYVKPTKNM
CCCCCEEEECCCCCC
9.8827642862
735AcetylationEDLQCYVKPTKNMSP
CCCEEEECCCCCCCH
22.0923749302
735UbiquitinationEDLQCYVKPTKNMSP
CCCEEEECCCCCCCH
22.0919608861
738AcetylationQCYVKPTKNMSPKEQ
EEEECCCCCCCHHHH
60.2125953088
741PhosphorylationVKPTKNMSPKEQFWG
ECCCCCCCHHHHHHH
42.0626074081
743AcetylationPTKNMSPKEQFWGRQ
CCCCCCHHHHHHHHH
57.7626051181
755PhosphorylationGRQVLRRSAGRAPYQ
HHHHHHHHCCCCCCC
28.7423312004
761PhosphorylationRSAGRAPYQENDGYC
HHCCCCCCCCCCCCC
27.7228450419
767PhosphorylationPYQENDGYCPDLELS
CCCCCCCCCCCCCCC
12.0423663014
774PhosphorylationYCPDLELSDSEAESD
CCCCCCCCHHHHCCC
29.7023401153
776PhosphorylationPDLELSDSEAESDGN
CCCCCCHHHHCCCCC
35.0230278072
780PhosphorylationLSDSEAESDGNKEKV
CCHHHHCCCCCCCCE
58.8422617229
793PhosphorylationKVRVRKDSSDRENPP
CEEECCCCCCCCCCC
36.8527273156
794PhosphorylationVRVRKDSSDRENPPH
EEECCCCCCCCCCCC
51.3123663014
803PhosphorylationRENPPHDSRRDCHGK
CCCCCCCCCCCCCCC
26.6123663014
812UbiquitinationRDCHGKSKTHPLSHS
CCCCCCCCCCCCCHH
55.10-

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 JADE3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JADE3_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 JADE3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of JADE3_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 JADE3_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-30; LYS-32; LYS-461 ANDLYS-638, 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-85, AND MASSSPECTROMETRY.
"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-85; THR-560; SER-566;SER-774 AND SER-776, AND MASS SPECTROMETRY.
"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-774; SER-776 ANDSER-780, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-566, 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-566, AND MASSSPECTROMETRY.
"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-85, AND MASSSPECTROMETRY.

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