dbPTM

KDM6A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KDM6A_HUMAN
UniProt AC	O15550
Protein Name	Lysine-specific demethylase 6A
Gene Name	KDM6A
Organism	Homo sapiens (Human).
Sequence Length	1401
Subcellular Localization	Nucleus .
Protein Description	Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. [PubMed: 17851529]
Protein Sequence	MKSCGVSLATAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARTKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKSCSNTSALAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGHAVSHPPVQQQAHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRPTGVAQVRSTGIPNGPTADSSLPTNSVSGQQPQLALTRVPSVSQPGVRPACPGQPLANGPFSAGHVPCSTSRTLGSTDTILIGNNHITGSGSNGNVPYLQRNALTLPHNRTNLTSSAEEPWKNQLSNSTQGLHKGQSSHSAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNILTVPETSRHTGETPNSTASVEGLPNHVHQMTADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGTGTCDKVNNIHPAVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPMKTDLLLVNHKPSPQIIPSMSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGRRRKGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMIKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCARKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Acetylation	AAFGDEEKKMAAGKA HHHCCHHHHHHCCCC	45.89	25953088
29	Acetylation	EKKMAAGKASGESEE HHHHHCCCCCCCCCC	34.35	25953088
80	Phosphorylation	LGKAVRCYESLILKA HHHHHHHHHHHHHHC	9.66	30619164
82	Phosphorylation	KAVRCYESLILKAEG HHHHHHHHHHHHCCC	8.34	30619164
225	Ubiquitination	QRKYHSAKEAYEQLL HHHHHCHHHHHHHHH	45.98	21890473
382	Ubiquitination	YLNATRSKSCSNTSA HHHCCCCCCCCCHHH	52.79	-
387	Phosphorylation	RSKSCSNTSALAARI CCCCCCCHHHHHHHH	10.09	-
388	Phosphorylation	SKSCSNTSALAARIK CCCCCCHHHHHHHHH	26.07	-
412	Ubiquitination	PQGSLQNKTKLLPSI CCCCCCCCCCCCCCH	33.79	-
445	Phosphorylation	MNTAQQNTSDNWSGG CCCCHHCCCCCCCCC	32.87	28348404
446	Phosphorylation	NTAQQNTSDNWSGGH CCCHHCCCCCCCCCC	36.17	28348404
450	Phosphorylation	QNTSDNWSGGHAVSH HCCCCCCCCCCCCCC	40.94	28348404
456	Phosphorylation	WSGGHAVSHPPVQQQ CCCCCCCCCCCHHHH	30.93	28348404
466	Phosphorylation	PVQQQAHSWCLTPQK CHHHHCHHHHCCHHH	23.62	28348404
470	Phosphorylation	QAHSWCLTPQKLQHL HCHHHHCCHHHHHHH	22.12	24719451
519	Methylation	PTGVAQVRSTGIPNG CCCEEEECCCCCCCC	19.20	-
535	Phosphorylation	TADSSLPTNSVSGQQ CCCCCCCCCCCCCCC	45.48	-
539	Phosphorylation	SLPTNSVSGQQPQLA CCCCCCCCCCCCEEE	30.61	-
549	Methylation	QPQLALTRVPSVSQP CCEEEEEECCCCCCC	38.92	-
552	Phosphorylation	LALTRVPSVSQPGVR EEEEECCCCCCCCCC	31.38	-
621	Methylation	ALTLPHNRTNLTSSA CCCCCCCCCCCCCCC	23.20	115919725
626	O-linked_Glycosylation	HNRTNLTSSAEEPWK CCCCCCCCCCCCHHH	30.62	23301498
633	Acetylation	SSAEEPWKNQLSNST CCCCCHHHHHCCCCC	45.60	25953088
639	Phosphorylation	WKNQLSNSTQGLHKG HHHHCCCCCCCCCCC	20.80	27251275
640	Phosphorylation	KNQLSNSTQGLHKGQ HHHCCCCCCCCCCCC	30.79	27251275
719	Sumoylation	ITLTKESKPSGNILT EEEECCCCCCCCEEE	44.27	-
719	Sumoylation	ITLTKESKPSGNILT EEEECCCCCCCCEEE	44.27	-
719	Acetylation	ITLTKESKPSGNILT EEEECCCCCCCCEEE	44.27	26051181
731	O-linked_Glycosylation	ILTVPETSRHTGETP EEECCCCCCCCCCCC	22.02	23301498
734	Phosphorylation	VPETSRHTGETPNST CCCCCCCCCCCCCCC	35.29	27080861
737	Phosphorylation	TSRHTGETPNSTASV CCCCCCCCCCCCCCC	29.16	27080861
740	Phosphorylation	HTGETPNSTASVEGL CCCCCCCCCCCCCCC	26.93	27080861
741	Phosphorylation	TGETPNSTASVEGLP CCCCCCCCCCCCCCC	29.59	27080861
743	Phosphorylation	ETPNSTASVEGLPNH CCCCCCCCCCCCCCC	22.31	27080861
755	Phosphorylation	PNHVHQMTADAVCSP CCCCEEECCCEECCC	18.15	27080861
761	Phosphorylation	MTADAVCSPSHGDSK ECCCEECCCCCCCCC	23.88	30108239
763	Phosphorylation	ADAVCSPSHGDSKSP CCEECCCCCCCCCCC	24.65	30108239
767	Phosphorylation	CSPSHGDSKSPGLLS CCCCCCCCCCCCCCC	39.36	30108239
769	Phosphorylation	PSHGDSKSPGLLSSD CCCCCCCCCCCCCCC	28.31	29255136
774	Phosphorylation	SKSPGLLSSDNPQLS CCCCCCCCCCCHHHH	40.46	29255136
775	Phosphorylation	KSPGLLSSDNPQLSA CCCCCCCCCCHHHHH	41.18	29255136
799	Acetylation	VGTGTCDKVNNIHPA CCCCCCCCCCCEECC	49.35	25953088
811	Phosphorylation	HPAVHTKTDNSVASS ECCEECCCCCCCCCC	41.38	30278072
814	Phosphorylation	VHTKTDNSVASSPSS EECCCCCCCCCCCCC	23.13	23403867
817	Phosphorylation	KTDNSVASSPSSAIS CCCCCCCCCCCCCCC	40.40	25159151
818	Phosphorylation	TDNSVASSPSSAIST CCCCCCCCCCCCCCC	21.04	23927012
820	Phosphorylation	NSVASSPSSAISTAT CCCCCCCCCCCCCCC	34.06	23927012
821	Phosphorylation	SVASSPSSAISTATP CCCCCCCCCCCCCCC	32.76	23927012
824	Phosphorylation	SSPSSAISTATPSPK CCCCCCCCCCCCCCC	16.23	30278072
825	Phosphorylation	SPSSAISTATPSPKS CCCCCCCCCCCCCCC	28.56	23927012
827	Phosphorylation	SSAISTATPSPKSTE CCCCCCCCCCCCCCC	25.12	23927012
829	Phosphorylation	AISTATPSPKSTEQT CCCCCCCCCCCCCCC	40.37	25159151
832	Phosphorylation	TATPSPKSTEQTTTN CCCCCCCCCCCCCCC	40.33	27080861
836	Phosphorylation	SPKSTEQTTTNSVTS CCCCCCCCCCCCCCC	29.38	27080861
837	Phosphorylation	PKSTEQTTTNSVTSL CCCCCCCCCCCCCCC	24.55	27080861
842	Phosphorylation	QTTTNSVTSLNSPHS CCCCCCCCCCCCCCC	27.58	27080861
843	Phosphorylation	TTTNSVTSLNSPHSG CCCCCCCCCCCCCCC	24.33	27080861
846	Phosphorylation	NSVTSLNSPHSGLHT CCCCCCCCCCCCCEE	29.32	27080861
849	Phosphorylation	TSLNSPHSGLHTING CCCCCCCCCCEECCC	46.57	27080861
853	Phosphorylation	SPHSGLHTINGEGME CCCCCCEECCCCCCC	22.60	27080861
862	Phosphorylation	NGEGMEESQSPMKTD CCCCCCCCCCCCCCC	23.74	27080861
864	Phosphorylation	EGMEESQSPMKTDLL CCCCCCCCCCCCCEE	35.92	27080861
909	Phosphorylation	NLGKNGLSNSSILLD HHCCCCCCCCCEECC	35.74	22210691
911	Phosphorylation	GKNGLSNSSILLDKC CCCCCCCCCEECCCC	18.51	22210691
912	Phosphorylation	KNGLSNSSILLDKCP CCCCCCCCEECCCCC	22.85	22210691
925	Phosphorylation	CPPPRPPSSPYPPLP CCCCCCCCCCCCCCC	46.78	25278378
926	Phosphorylation	PPPRPPSSPYPPLPK CCCCCCCCCCCCCCC	33.94	25278378
928	Phosphorylation	PRPPSSPYPPLPKDK CCCCCCCCCCCCCCC	21.30	25278378
940	Phosphorylation	KDKLNPPTPSIYLEN CCCCCCCCCCEECCC	30.81	9381176
942	Phosphorylation	KLNPPTPSIYLENKR CCCCCCCCEECCCCC	26.75	22210691
1018	Ubiquitination	NWDPTGTKKIWHCES CCCCCCCCEEEEECC	43.54	-
1053	Ubiquitination	SLREENEKRSHHKDH HHHHHHHHHCCCCCC	71.44	-
1061	Phosphorylation	RSHHKDHSDSESTSS HCCCCCCCCCCCCCC	53.63	25849741
1063	Phosphorylation	HHKDHSDSESTSSDN CCCCCCCCCCCCCCC	36.14	30177828
1065	Phosphorylation	KDHSDSESTSSDNSG CCCCCCCCCCCCCCC	37.23	30177828
1066	Phosphorylation	DHSDSESTSSDNSGR CCCCCCCCCCCCCCC	28.35	30177828
1086	Phosphorylation	FKTIKFGTNIDLSDD CCEEEEECCCCCCCC	31.94	20068231
1091	Phosphorylation	FGTNIDLSDDKKWKL EECCCCCCCCCCCEE	39.76	20068231
1097	Ubiquitination	LSDDKKWKLQLHELT CCCCCCCEEHHHHHH	34.92	-
1131	Phosphorylation	HTILGMNTVQLYMKV CHHCCCCEEEEEEEC	10.75	-
1154	Phosphorylation	QENNNFCSVNINIGP CCCCCEEEEEEEECC	17.67	-
1284	Phosphorylation	MARNIKVSDPKLFEM HHCCCCCCCHHHHHH	43.10	-
1287	Ubiquitination	NIKVSDPKLFEMIKY CCCCCCHHHHHHHHH	71.45	-
1301	Ubiquitination	YCLLRTLKQCQTLRE HHHHHHHHHHHHHHH	48.71	-

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 KDM6A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KDM6A_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 KDM6A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TLE1_HUMAN	TLE1	physical	9854018
KMT2D_HUMAN	KMT2D	physical	17761849
KMT2C_HUMAN	KMT2C	physical	17761849
NCOA6_HUMAN	NCOA6	physical	17761849
N4BP2_HUMAN	N4BP2	physical	17761849
PAXI1_HUMAN	PAXIP1	physical	17761849
PP6R3_HUMAN	PPP6R3	physical	17761849
ZN281_HUMAN	ZNF281	physical	17761849
PRSR1_HUMAN	PROSER1	physical	17761849
ASH2L_HUMAN	ASH2L	physical	17761849
RBBP5_HUMAN	RBBP5	physical	17761849
WDR5_HUMAN	WDR5	physical	17761849
H31T_HUMAN	HIST3H3	physical	17761849
PAXI1_HUMAN	PAXIP1	physical	17500065
RBBP5_HUMAN	RBBP5	physical	17500065
H31_HUMAN	HIST1H3A	physical	17713478
NKX25_HUMAN	NKX2-5	physical	22192413
GATA4_HUMAN	GATA4	physical	22192413
SRF_HUMAN	SRF	physical	22192413
TBX5_HUMAN	TBX5	physical	22192413
H32_HUMAN	HIST2H3C	physical	21575637
WDR5_HUMAN	WDR5	physical	17825402
ASH2L_HUMAN	ASH2L	physical	17825402
RBBP5_HUMAN	RBBP5	physical	17825402
MSH6_HUMAN	MSH6	genetic	28319113
PTEN_HUMAN	PTEN	genetic	28319113

Drug and Disease Associations

Kegg Disease
OMIM Disease
300867	Kabuki syndrome 2 (KABUK2)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KDM6A_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-769 AND SER-829, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-818, AND MASSSPECTROMETRY.	15302935 [Abstract]