dbPTM

KDM4A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KDM4A_HUMAN
UniProt AC	O75164
Protein Name	Lysine-specific demethylase 4A
Gene Name	KDM4A
Organism	Homo sapiens (Human).
Sequence Length	1064
Subcellular Localization	Nucleus .
Protein Description	Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. [PubMed: 26741168 Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.; Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.]
Protein Sequence	MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESELPPRAGNEEECPEEDMEGVEDGEEGDLKTSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEDLSSEQYEMTECPAALAPVRPTHSSVRQVEDGLTFPDYSDSTEVKFEELKNVKLEEEDEEEEQAAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSGSSRDSISSDSETSEPLSCRAQGQTGVLTVHSYAKGDGRVTVGEPCTRKKGSAARSFSERELAEVADEYMFSLEENKKSKGRRQPLSKLPRHHPLVLQECVSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNETMAQQAPHCAVCMIFQTYHQVEFGGFNQNCGNASDLAPQKQRTKPLIPEMCFTSTGCSTDINLSTPYLEEDGTSILVSCKKCSVRVHASCYGVPPAKASEDWMCSRCSANALEEDCCLCSLRGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCIFCKKRRKRTAGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALQSITAGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQFGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSVASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASESETLN ------CCCHHHCCC	33.05	19413330
3	Phosphorylation	-----MASESETLNP -----CCCHHHCCCC	54.22	24043423
5	Phosphorylation	---MASESETLNPSA ---CCCHHHCCCCCH	33.13	24043423
7	Phosphorylation	-MASESETLNPSARI -CCCHHHCCCCCHHH	40.91	24043423
11	Phosphorylation	ESETLNPSARIMTFY HHHCCCCCHHHHHCC	29.16	24043423
16	Phosphorylation	NPSARIMTFYPTMEE CCCHHHHHCCCCHHH	20.04	-
51	Ubiquitination	LAKVVPPKEWKPRAS CCEECCCCCCCCCCC	70.86	29967540
58	Phosphorylation	KEWKPRASYDDIDDL CCCCCCCCCCCCHHC	30.30	22210691
59	Phosphorylation	EWKPRASYDDIDDLV CCCCCCCCCCCHHCE	19.36	22210691
105	Ubiquitination	RKIANSDKYCTPRYS HHHHCCCCCCCCCCH	41.88	29967540
111	Phosphorylation	DKYCTPRYSEFEELE CCCCCCCCHHHHHHH	17.47	21406692
112	Phosphorylation	KYCTPRYSEFEELER CCCCCCCHHHHHHHH	36.77	21406692
133	Ubiquitination	TFNPPIYGADVNGTL CCCCCCCCCCCCCCE	18.93	22505724
143	Ubiquitination	VNGTLYEKHVDEWNI CCCCEEEECCCCCCH	35.06	29967540
155	Phosphorylation	WNIGRLRTILDLVEK CCHHHHHHHHHHHHH	30.40	23025827
160	Ubiquitination	LRTILDLVEKESGIT HHHHHHHHHHHCCCE	11.16	22817900
161	Ubiquitination	RTILDLVEKESGITI HHHHHHHHHHCCCEE	59.40	21890473
195	Phosphorylation	HTEDMDLYSINYLHF ECCCCCEEEEEEEEC	11.84	-
196	Phosphorylation	TEDMDLYSINYLHFG CCCCCEEEEEEEECC	16.20	-
199	Phosphorylation	MDLYSINYLHFGEPK CCEEEEEEEECCCCC	10.41	-
224	Ubiquitination	KRLERLAKGFFPGSA HHHHHHHCCCCCCCH	61.92	22505724
241	Acetylation	CEAFLRHKMTLISPL HHHHHHHCHHHHHHH	27.44	7670817
251	Ubiquitination	LISPLMLKKYGIPFD HHHHHHHHHHCCCHH	29.95	22817900
251	Acetylation	LISPLMLKKYGIPFD HHHHHHHHHHCCCHH	29.95	7670827
252	Ubiquitination	ISPLMLKKYGIPFDK HHHHHHHHHCCCHHH	44.76	21890473
295	Ubiquitination	STNFATRRWIEYGKQ CCCCCHHHHHHHHHH	34.08	21963094
300	Ubiquitination	TRRWIEYGKQAVLCS HHHHHHHHHHEEEEE	11.65	22817900
301	Ubiquitination	RRWIEYGKQAVLCSC HHHHHHHHHEEEEEC	33.89	-
336	Ubiquitination	YKLWKAGKDNTVIDH HHHHHCCCCCCEEEC	53.30	29967540
355	Ubiquitination	PEAAEFLKESELPPR HHHHHHHHHCCCCCC	65.60	29967540
386	Ubiquitination	DGEEGDLKTSLAKHR CCCCCCHHHHHHHHC	40.59	21963094
391	Ubiquitination	DLKTSLAKHRIGTKR CHHHHHHHHCCCCCC	38.41	22817900
410	Phosphorylation	LEIPQEVSQSELFPK EECCCCCCHHHCCCC	27.51	26657352
412	Phosphorylation	IPQEVSQSELFPKED CCCCCCHHHCCCCHH	28.85	25850435
421	Phosphorylation	LFPKEDLSSEQYEMT CCCCHHCCCCCEECC	44.12	23879269
425	Phosphorylation	EDLSSEQYEMTECPA HHCCCCCEECCCCCH	12.01	27642862
428	Phosphorylation	SSEQYEMTECPAALA CCCCEECCCCCHHHC	23.61	23879269
442	Phosphorylation	APVRPTHSSVRQVED CCCCCCCCCCEECCC	32.76	23879269
452	Phosphorylation	RQVEDGLTFPDYSDS EECCCCCCCCCCCCC	38.36	-
468	Ubiquitination	EVKFEELKNVKLEEE EEEHHHHCCCCCCCC	64.07	29967540
471	Sumoylation	FEELKNVKLEEEDEE HHHHCCCCCCCCCHH	60.62	-
502	Phosphorylation	VGGRLVFSGSKKKSS HCCEEEEECCCCCCC	34.38	21815630
504	Phosphorylation	GRLVFSGSKKKSSSS CEEEEECCCCCCCCC	39.85	29396449
505	Acetylation	RLVFSGSKKKSSSSL EEEEECCCCCCCCCC	68.68	25953088
508	Phosphorylation	FSGSKKKSSSSLGSG EECCCCCCCCCCCCC	44.31	28450419
509	Phosphorylation	SGSKKKSSSSLGSGS ECCCCCCCCCCCCCC	32.59	30576142
510	Phosphorylation	GSKKKSSSSLGSGSS CCCCCCCCCCCCCCC	36.35	28450419
511	Phosphorylation	SKKKSSSSLGSGSSR CCCCCCCCCCCCCCC	38.40	28450419
514	Phosphorylation	KSSSSLGSGSSRDSI CCCCCCCCCCCCCCC	40.57	30576142
516	Phosphorylation	SSSLGSGSSRDSISS CCCCCCCCCCCCCCC	24.73	30576142
517	Phosphorylation	SSLGSGSSRDSISSD CCCCCCCCCCCCCCC	43.56	28450419
520	Phosphorylation	GSGSSRDSISSDSET CCCCCCCCCCCCCCC	24.22	25159151
522	Phosphorylation	GSSRDSISSDSETSE CCCCCCCCCCCCCCC	31.85	30266825
523	Phosphorylation	SSRDSISSDSETSEP CCCCCCCCCCCCCCC	43.41	16603238
525	Phosphorylation	RDSISSDSETSEPLS CCCCCCCCCCCCCCC	44.73	30266825
527	Phosphorylation	SISSDSETSEPLSCR CCCCCCCCCCCCCCE	42.20	28102081
528	Phosphorylation	ISSDSETSEPLSCRA CCCCCCCCCCCCCEE	32.92	23403867
532	Phosphorylation	SETSEPLSCRAQGQT CCCCCCCCCEECCCC	16.57	23403867
546	Phosphorylation	TGVLTVHSYAKGDGR CCEEEEEEEECCCCC	23.58	28555341
547	Phosphorylation	GVLTVHSYAKGDGRV CEEEEEEEECCCCCE	9.46	16094384
570	Phosphorylation	KKGSAARSFSERELA CCCCCCCCCCHHHHH	28.53	28348404
572	Phosphorylation	GSAARSFSERELAEV CCCCCCCCHHHHHHH	36.67	24719451
586	Phosphorylation	VADEYMFSLEENKKS HHHHHHHCHHHCCCC	20.52	27794612
616	Phosphorylation	LVLQECVSDDETSEQ EEEEECCCCCCCCCC	51.51	30576142
620	Phosphorylation	ECVSDDETSEQLTPE ECCCCCCCCCCCCHH	44.55	30576142
621	Phosphorylation	CVSDDETSEQLTPEE CCCCCCCCCCCCHHH	22.69	30576142
625	Phosphorylation	DETSEQLTPEEEAEE CCCCCCCCHHHHHHH	28.48	26657352
814	Phosphorylation	FVNIAERSPVDVSKI HCCHHHHCCCCHHHC	22.30	28555341
820	Ubiquitination	RSPVDVSKIPLPRFK HCCCCHHHCCCCCCE	48.46	-
885	Ubiquitination	FITCFRHKIPNLERA EEEEEHHCCCCHHHH	56.45	-
893	Ubiquitination	IPNLERAKGALQSIT CCCHHHHHHHHHHCC	51.44	29967540
893	Sumoylation	IPNLERAKGALQSIT CCCHHHHHHHHHHCC	51.44	-
893	Sumoylation	IPNLERAKGALQSIT CCCHHHHHHHHHHCC	51.44	-
898	Phosphorylation	RAKGALQSITAGQKV HHHHHHHHCCCCCCE	23.82	29449344
900	Phosphorylation	KGALQSITAGQKVIS HHHHHHCCCCCCEEE	29.95	29449344
904	Ubiquitination	QSITAGQKVISKHKN HHCCCCCCEEEECCC	40.39	29967540
1012	Ubiquitination	TLDEELPKRVKSRLS ECCCCCCHHHHHHHH	80.56	29967540
1016	Phosphorylation	ELPKRVKSRLSVASD CCCHHHHHHHHHHCC	35.28	24719451
1019	Phosphorylation	KRVKSRLSVASDMRF HHHHHHHHHHCCCHH	17.96	25159151
1033	Ubiquitination	FNEIFTEKEVKQEKK HHHCCCHHHHHHHHH	65.82	29967540
1049	Phosphorylation	QRVINSRYREDYIEP HHHHHHHHHHHCHHH	20.41	30576142
1053	Phosphorylation	NSRYREDYIEPALYR HHHHHHHCHHHHHHH	11.48	27642862
1059	Phosphorylation	DYIEPALYRAIME-- HCHHHHHHHHHHC--	10.49	27642862

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
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO22	Q8NEZ5	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL4	Q9UKA2	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	RNF168	Q8IYW5	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	RNF8	O76064	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KDM4A_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 KDM4A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KDM4A_HUMAN	KDM4A	physical	17207460
KDM4C_HUMAN	KDM4C	physical	17207460
H31_HUMAN	HIST1H3A	physical	16732292
H33_BOVIN	H3F3A	physical	16603238
H31_HUMAN	HIST1H3A	physical	16601153
NCOR1_HUMAN	NCOR1	physical	16024779
HDAC1_HUMAN	HDAC1	physical	15927959
HDAC3_HUMAN	HDAC3	physical	15927959
RB_HUMAN	RB1	physical	15927959
ANDR_HUMAN	AR	physical	17555712
H33_HUMAN	H3F3A	physical	21931800
CUL1_HUMAN	CUL1	physical	21757720
FBXL4_HUMAN	FBXL4	physical	21757720
CAZA1_HUMAN	CAPZA1	physical	26344197

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 KDM4A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-547, AND MASSSPECTROMETRY.	16094384 [Abstract]