dbPTM

JADE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	JADE1_HUMAN
UniProt AC	Q6IE81
Protein Name	Protein Jade-1
Gene Name	JADE1
Organism	Homo sapiens (Human).
Sequence Length	842
Subcellular Localization	Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, cilium basal body . Localizes to the ciliary transition zone.
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. Transcriptional coactivator, it may also promote acetylation of nucleosomal histone H4 by KAT5. Promotes apoptosis. May act as a renal tumor suppressor. Negatively regulates canonical Wnt signaling; at least in part, cooperates with NPHP4 in this function..
Protein Sequence	MKRGRLPSSSEDSDDNGSLSTTWSQNSRSQHRRSSCSRHEDRKPSEVFRTDLITAMKLHDSYQLNPDEYYVLADPWRQEWEKGVQVPVSPGTIPQPVARVVSEEKSLMFIRPKKYIVSSGSEPPELGYVDIRTLADSVCRYDLNDMDAAWLELTNEEFKEMGMPELDEYTMERVLEEFEQRCYDNMNHAIETEEGLGIEYDEDVVCDVCQSPDGEDGNEMVFCDKCNICVHQACYGILKVPEGSWLCRTCALGVQPKCLLCPKKGGAMKPTRSGTKWVHVSCALWIPEVSIGSPEKMEPITKVSHIPSSRWALVCSLCNEKFGASIQCSVKNCRTAFHVTCAFDRGLEMKTILAENDEVKFKSYCPKHSSHRKPEESLGKGAAQENGAPECSPRNPLEPFASLEQNREEAHRVSVRKQKLQQLEDEFYTFVNLLDVARALRLPEEVVDFLYQYWKLKRKVNFNKPLITPKKDEEDNLAKREQDVLFRRLQLFTHLRQDLERVRNLTYMVTRREKIKRSVCKVQEQIFNLYTKLLEQERVSGVPSSCSSSSLENMLLFNSPSVGPDAPKIEDLKWHSAFFRKQMGTSLVHSLKKPHKRDPLQNSPGSEGKTLLKQPDLCGRREGMVVPESFLGLEKTFAEARLISAQQKNGVVMPDHGKRRDNRFHCDLIKGDLKDKSFKQSHKPLRSTDVSQRHLDNTRAATSPGVGQSAPGTRKEIVPKCNGSLIKVNYNQTAVKVPTTPASPVKNWGGFRIPKKGERQQQGEAHDGACHQHSDYPYLGLGRVPAKERAKSKLKSDNENDGYVPDVEMSDSESEASEKKCIHTSSTISRRTDIIRRSILAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MKRGRLPSSSEDSDD CCCCCCCCCCCCCCC	51.60	21406692
9	Phosphorylation	KRGRLPSSSEDSDDN CCCCCCCCCCCCCCC	35.49	21406692
10	Phosphorylation	RGRLPSSSEDSDDNG CCCCCCCCCCCCCCC	50.16	21406692
13	Phosphorylation	LPSSSEDSDDNGSLS CCCCCCCCCCCCCCC	42.69	21406692
18	Phosphorylation	EDSDDNGSLSTTWSQ CCCCCCCCCCCCCCC	25.96	21406692
20	Phosphorylation	SDDNGSLSTTWSQNS CCCCCCCCCCCCCCC	26.03	-
43	Acetylation	CSRHEDRKPSEVFRT CCCCCCCCHHHHCHH	66.28	26051181
45	Phosphorylation	RHEDRKPSEVFRTDL CCCCCCHHHHCHHHH	49.80	28555341
82	Ubiquitination	PWRQEWEKGVQVPVS HHHHHHHCCCCCCCC	66.51	-
89	Phosphorylation	KGVQVPVSPGTIPQP CCCCCCCCCCCCCCC	16.13	30266825
89 (in isoform 3)	Phosphorylation	-	16.13	-
92	Phosphorylation	QVPVSPGTIPQPVAR CCCCCCCCCCCCCEE	32.63	30266825
92 (in isoform 3)	Phosphorylation	-	32.63	-
102	Phosphorylation	QPVARVVSEEKSLMF CCCEEECCCCCEEEE	36.86	-
105	Ubiquitination	ARVVSEEKSLMFIRP EEECCCCCEEEEECC	44.85	-
114	Sumoylation	LMFIRPKKYIVSSGS EEEECCCEEEEECCC	42.78	-
114	Sumoylation	LMFIRPKKYIVSSGS EEEECCCEEEEECCC	42.78	28112733
114	Ubiquitination	LMFIRPKKYIVSSGS EEEECCCEEEEECCC	42.78	-
121	Phosphorylation	KYIVSSGSEPPELGY EEEEECCCCCCCCCC	49.21	-
257	Acetylation	CALGVQPKCLLCPKK CCCCCCCCEEECCCC	22.03	26051181
257	Ubiquitination	CALGVQPKCLLCPKK CCCCCCCCEEECCCC	22.03	-
263	Acetylation	PKCLLCPKKGGAMKP CCEEECCCCCCCCCC	64.15	25953088
293	Phosphorylation	IPEVSIGSPEKMEPI CCCCCCCCHHHCCCC	28.37	27422710
302	Ubiquitination	EKMEPITKVSHIPSS HHCCCCCEECCCCHH	42.32	-
302	Acetylation	EKMEPITKVSHIPSS HHCCCCCEECCCCHH	42.32	23749302
331	Acetylation	ASIQCSVKNCRTAFH CEEEEEECCCCHHEE	33.75	25953088
360	Acetylation	LAENDEVKFKSYCPK EECCCCEEEHHHCCC	45.05	26051181
360	Ubiquitination	LAENDEVKFKSYCPK EECCCCEEEHHHCCC	45.05	-
363	Phosphorylation	NDEVKFKSYCPKHSS CCCEEEHHHCCCCCC	34.79	29116813
364	Phosphorylation	DEVKFKSYCPKHSSH CCEEEHHHCCCCCCC	17.23	21964256
373	Acetylation	PKHSSHRKPEESLGK CCCCCCCCCHHHCCC	51.89	23236377
377	Phosphorylation	SHRKPEESLGKGAAQ CCCCCHHHCCCCHHH	40.54	29116813
380	Ubiquitination	KPEESLGKGAAQENG CCHHHCCCCHHHHCC	51.15	-
380	Acetylation	KPEESLGKGAAQENG CCHHHCCCCHHHHCC	51.15	23749302
392 (in isoform 3)	Phosphorylation	-	25.82	-
392	Phosphorylation	ENGAPECSPRNPLEP HCCCCCCCCCCCCCC	25.82	29255136
402	Phosphorylation	NPLEPFASLEQNREE CCCCCCCCHHHHHHH	32.58	26074081
468	Phosphorylation	NFNKPLITPKKDEED CCCCCCCCCCCCHHC	36.42	23312004
470	Acetylation	NKPLITPKKDEEDNL CCCCCCCCCCHHCCH	65.29	19811757
493	Phosphorylation	FRRLQLFTHLRQDLE HHHHHHHHHHHHHHH	28.70	20068231
501	Methylation	HLRQDLERVRNLTYM HHHHHHHHHHCCHHH	39.74	24376903
501	Dimethylation	HLRQDLERVRNLTYM HHHHHHHHHHCCHHH	39.74	-
503	Methylation	RQDLERVRNLTYMVT HHHHHHHHCCHHHHH	38.37	24376911
503	Dimethylation	RQDLERVRNLTYMVT HHHHHHHHCCHHHHH	38.37	-
507	Phosphorylation	ERVRNLTYMVTRREK HHHHCCHHHHHCHHH	7.86	22817900
532	Ubiquitination	QIFNLYTKLLEQERV HHHHHHHHHHHHHHH	37.20	-
547	Phosphorylation	SGVPSSCSSSSLENM CCCCCCCCCHHHHHH	34.89	27251275
548	Phosphorylation	GVPSSCSSSSLENML CCCCCCCCHHHHHHH	28.42	27251275
549	Phosphorylation	VPSSCSSSSLENMLL CCCCCCCHHHHHHHC	23.73	27251275
550	Phosphorylation	PSSCSSSSLENMLLF CCCCCCHHHHHHHCC	41.47	27251275
559	Phosphorylation	ENMLLFNSPSVGPDA HHHHCCCCCCCCCCC	15.95	27251275
561	Phosphorylation	MLLFNSPSVGPDAPK HHCCCCCCCCCCCCC	39.26	27251275
573	Sumoylation	APKIEDLKWHSAFFR CCCHHHCCHHHHHHH	56.00	28112733
585	Phosphorylation	FFRKQMGTSLVHSLK HHHHHHCCHHHHHCC	17.34	21406692
586	Phosphorylation	FRKQMGTSLVHSLKK HHHHHCCHHHHHCCC	23.75	21406692
590	Phosphorylation	MGTSLVHSLKKPHKR HCCHHHHHCCCCCCC	34.11	25159151
603	Phosphorylation	KRDPLQNSPGSEGKT CCCCCCCCCCCCCCC	20.06	23401153
606	Phosphorylation	PLQNSPGSEGKTLLK CCCCCCCCCCCCHHC	46.70	30266825
609	Acetylation	NSPGSEGKTLLKQPD CCCCCCCCCHHCCCC	31.76	25953088
610	Phosphorylation	SPGSEGKTLLKQPDL CCCCCCCCHHCCCCC	48.45	28111955
702	Phosphorylation	LDNTRAATSPGVGQS HHCCCCCCCCCCCCC	34.17	30266825
703	Phosphorylation	DNTRAATSPGVGQSA HCCCCCCCCCCCCCC	18.22	30266825
709	Phosphorylation	TSPGVGQSAPGTRKE CCCCCCCCCCCCCCC	30.42	30266825
713	Phosphorylation	VGQSAPGTRKEIVPK CCCCCCCCCCCCCCC	37.19	29396449
724	Phosphorylation	IVPKCNGSLIKVNYN CCCCCCCCEEEEECC	16.96	24719451
739	Phosphorylation	QTAVKVPTTPASPVK CCEEECCCCCCCCCC	48.69	21712546
740	Phosphorylation	TAVKVPTTPASPVKN CEEECCCCCCCCCCC	15.70	30266825
743	Phosphorylation	KVPTTPASPVKNWGG ECCCCCCCCCCCCCC	31.28	30266825
796	Phosphorylation	RAKSKLKSDNENDGY HHHHHCCCCCCCCCC	56.98	25278378
803	Phosphorylation	SDNENDGYVPDVEMS CCCCCCCCCCCCCCC	16.21	25278378
810	Phosphorylation	YVPDVEMSDSESEAS CCCCCCCCCCCCHHH	25.20	30576142
812	Phosphorylation	PDVEMSDSESEASEK CCCCCCCCCCHHHHH	35.40	30576142
814	Phosphorylation	VEMSDSESEASEKKC CCCCCCCCHHHHHHH	42.27	30576142
817	Phosphorylation	SDSESEASEKKCIHT CCCCCHHHHHHHCCC	45.99	30576142
824	Phosphorylation	SEKKCIHTSSTISRR HHHHHCCCCCHHHHH	12.40	20068231
825	Phosphorylation	EKKCIHTSSTISRRT HHHHCCCCCHHHHHH	16.01	20068231
826	Phosphorylation	KKCIHTSSTISRRTD HHHCCCCCHHHHHHH	30.80	20068231
827	Phosphorylation	KCIHTSSTISRRTDI HHCCCCCHHHHHHHH	23.80	20068231
829	Phosphorylation	IHTSSTISRRTDIIR CCCCCHHHHHHHHHH	18.79	20068231
832	Phosphorylation	SSTISRRTDIIRRSI CCHHHHHHHHHHHHH	30.36	24702127

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
18	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
20	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:23001567

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of JADE1_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 JADE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VHL_HUMAN	VHL	physical	12169691
CTNB1_HUMAN	CTNNB1	physical	18806787
KAT5_HUMAN	KAT5	physical	15502158
KAT7_HUMAN	KAT7	physical	18684714
KAT7_HUMAN	KAT7	physical	19187766
ING5_HUMAN	ING5	physical	19187766
EAF6_HUMAN	MEAF6	physical	19187766
H32_HUMAN	HIST2H3C	physical	19187766
KAT7_HUMAN	KAT7	physical	22144582
EAF6_HUMAN	MEAF6	physical	22144582
ING4_HUMAN	ING4	physical	22144582
PKD1_HUMAN	PKD1	physical	23001567
AKT1_HUMAN	AKT1	physical	23824745
UB2E1_HUMAN	UBE2E1	physical	18806787
UBE2H_HUMAN	UBE2H	physical	18806787
NPHP4_HUMAN	NPHP4	physical	22654112
KAT7_HUMAN	KAT7	physical	26186194
KAT7_HUMAN	KAT7	physical	24739512
KAT7_HUMAN	KAT7	physical	28514442
KAT7_MOUSE	Kat7	physical	26919559
PLK1_HUMAN	PLK1	physical	26919559
HDGR2_MOUSE	Hdgfrp2	physical	26919559
BYST_MOUSE	Bysl	physical	26919559
CCD86_MOUSE	Ccdc86	physical	26919559
DDX18_MOUSE	Ddx18	physical	26919559
ABCF1_MOUSE	Abcf1	physical	26919559
CA131_MOUSE	2810004N23Rik	physical	26919559
AROS_MOUSE	Rps19bp1	physical	26919559
RPB2_MOUSE	Polr2b	physical	26919559
RRP12_MOUSE	Rrp12	physical	26919559
IF2P_MOUSE	Eif5b	physical	26919559
L10K_MOUSE	D8Ertd738e	physical	26919559
AATF_MOUSE	Aatf	physical	26919559
TTF1_MOUSE	Ttf1	physical	26919559
RPA34_MOUSE	Cd3eap	physical	26919559
HMGN1_MOUSE	Hmgn1	physical	26919559
TDIF2_MOUSE	Dnttip2	physical	26919559
TOPRS_MOUSE	Topors	physical	26919559
P20L1_MOUSE	Phf20l1	physical	26919559
MAP1A_MOUSE	Map1a	physical	26919559
PHF2_MOUSE	Phf2	physical	26919559
P66B_MOUSE	Gatad2b	physical	26919559
NOL10_MOUSE	Nol10	physical	26919559
SPB1_MOUSE	Ftsj3	physical	26919559
SFSWA_MOUSE	Sfswap	physical	26919559
RT12_MOUSE	Mrps12	physical	26919559
ATPK_MOUSE	Atp5j2	physical	26919559
GPTC8_MOUSE	Gpatch8	physical	26919559
SMCA2_MOUSE	Smarca2	physical	26919559
BUD13_MOUSE	Bud13	physical	26919559
UBN1_MOUSE	Ubn1	physical	26919559
KDM5A_MOUSE	Kdm5a	physical	26919559
MTA2_MOUSE	Mta2	physical	26919559
TOP1_MOUSE	Top1	physical	26919559
CHD4_MOUSE	Chd4	physical	26919559
NOP58_MOUSE	Nop58	physical	26919559
RL1D1_MOUSE	Rsl1d1	physical	26919559
SFR19_MOUSE	Scaf1	physical	26919559
RL23A_MOUSE	Rpl23a	physical	26919559
DDX27_MOUSE	Ddx27	physical	26919559
BBX_MOUSE	Bbx	physical	26919559
H15_MOUSE	Hist1h1b	physical	26919559
UBP16_MOUSE	Usp16	physical	26919559
CWC25_MOUSE	Cwc25	physical	26919559
PUF60_MOUSE	Puf60	physical	26919559
NOP56_MOUSE	Nop56	physical	26919559
POGZ_MOUSE	Pogz	physical	26919559
NOG1_MOUSE	Gtpbp4	physical	26919559
FBRL_MOUSE	Fbl	physical	26919559

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 JADE1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-89; THR-92 AND SER-603,AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-89 AND SER-743, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-89 AND THR-92, AND MASSSPECTROMETRY.	18220336 [Abstract]
"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-8; SER-9; SER-10 ANDSER-13, AND MASS SPECTROMETRY.	17081983 [Abstract]