dbPTM

KDM5C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KDM5C_HUMAN
UniProt AC	P41229
Protein Name	Lysine-specific demethylase 5C
Gene Name	KDM5C {ECO:0000312\|HGNC:HGNC:11114}
Organism	Homo sapiens (Human).
Sequence Length	1560
Subcellular Localization	Nucleus .
Protein Description	Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. [PubMed: 28262558 Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity]
Protein Sequence	MEPGSDDFLPPPECPVFEPSWAEFRDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRIQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERRILDLYSLSKIVVEEGGYEAICKDRRWARVAQRLNYPPGKNIGSLLRSHYERIVYPYEMYQSGANLVQCNTRPFDNEEKDKEYKPHSIPLRQSVQPSKFNSYGRRAKRLQPDPEPTEEDIEKNPELKKLQIYGAGPKMMGLGLMAKDKTLRKKDKEGPECPPTVVVKEELGGDVKVESTSPKTFLESKEELSHSPEPCTKMTMRLRRNHSNAQFIESYVCRMCSRGDEDDKLLLCDGCDDNYHIFCLLPPLPEIPKGVWRCPKCVMAECKRPPEAFGFEQATREYTLQSFGEMADSFKADYFNMPVHMVPTELVEKEFWRLVNSIEEDVTVEYGADIHSKEFGSGFPVSDSKRHLTPEEEEYATSGWNLNVMPVLEQSVLCHINADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEEVMKKLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYNFAEAVNFCTADWLPAGRQCIEHYRRLRRYCVFSHEELICKMAACPEKLDLNLAAAVHKEMFIMVQEERRLRKALLEKGITEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDGLVCLSHINDLCKCSSSRQYLRYRYTLDELPAMLHKLKVRAESFDTWANKVRVALEVEDGRKRSLEELRALESEARERRFPNSELLQQLKNCLSEAEACVSRALGLVSGQEAGPHRVAGLQMTLTELRAFLDQMNNLPCAMHQIGDVKGVLEQVEAYQAEAREALASLPSSPGLLQSLLERGRQLGVEVPEAQQLQRQVEQARWLDEVKRTLAPSARRGTLAVMRGLLVAGASVAPSPAVDKAQAELQELLTIAERWEEKAHLCLEARQKHPPATLEAIIREAENIPVHLPNIQALKEALAKARAWIADVDEIQNGDHYPCLDDLEGLVAVGRDLPVGLEELRQLELQVLTAHSWREKASKTFLKKNSCYTLLEVLCPCADAGSDSTKRSRWMEKELGLYKSDTELLGLSAQDLRDPGSVIVAFKEGEQKEKEGILQLRRTNSAKPSPLASSSTASSTTSICVCGQVLAGAGALQCDLCQDWFHGRCVSVPRLLSSPRPNPTSSPLLAWWEWDTKFLCPLCMRSRRPRLETILALLVALQRLPVRLPEGEALQCLTERAISWQGRARQALASEDVTALLGRLAELRQRLQAEPRPEEPPNYPAAPASDPLREGSGKDMPKVQGLLENGDSVTSPEKVAPEEGSGKRDLELLSSLLPQLTGPVLELPEATRAPLEELMMEGDLLEVTLDENHSIWQLLQAGQPPDLERIRTLLELEKAERHGSRARGRALERRRRRKVDRGGEGDDPAREELEPKRVRSSGPEAEEVQEEEELEEETGGEGPPAPIPTTGSPSTQENQNGLEPAEGTTSGPSAPFSTLTPRLHLPCPQQPPQQQL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Sumoylation	DPLGYIAKIRPIAEK CCCHHHCEECCCHHH	29.68	-
33	Sumoylation	DPLGYIAKIRPIAEK CCCHHHCEECCCHHH	29.68	-
33	Ubiquitination	DPLGYIAKIRPIAEK CCCHHHCEECCCHHH	29.68	-
40	Ubiquitination	KIRPIAEKSGICKIR EECCCHHHHCCCEEC	44.98	-
40	Ubiquitination	KIRPIAEKSGICKIR EECCCHHHHCCCEEC	44.98	-
45	Ubiquitination	AEKSGICKIRPPADW HHHHCCCEECCCCCC	39.57	-
45	Ubiquitination	AEKSGICKIRPPADW HHHHCCCEECCCCCC	39.57	-
66	Phosphorylation	EVDNFRFTPRIQRLN EECCCEECHHHHHHH	13.85	24719451
82	Ubiquitination	LEAQTRVKLNYLDQI HHHHHHHHHHHHHHH	27.94	-
82	Ubiquitination	LEAQTRVKLNYLDQI HHHHHHHHHHHHHHH	27.94	-
91	Ubiquitination	NYLDQIAKFWEIQGS HHHHHHHHHHEECCC	53.27	-
91	Ubiquitination	NYLDQIAKFWEIQGS HHHHHHHHHHEECCC	53.27	-
101	Ubiquitination	EIQGSSLKIPNVERR EECCCCCCCCCHHHH	59.05	21890473
101	Ubiquitination	EIQGSSLKIPNVERR EECCCCCCCCCHHHH	59.05	21890473
101 (in isoform 1)	Ubiquitination	-	59.05	21890473
101 (in isoform 2)	Ubiquitination	-	59.05	21890473
130	Ubiquitination	GGYEAICKDRRWARV CCHHHHCCCHHHHHH	48.43	-
151	Phosphorylation	PPGKNIGSLLRSHYE CCCCCHHHHHHHHHH	22.04	27067055
188	Ubiquitination	FDNEEKDKEYKPHSI CCCCCCCCCCCCCCC	74.20	-
191	Sumoylation	EEKDKEYKPHSIPLR CCCCCCCCCCCCCCC	37.03	-
191	Sumoylation	EEKDKEYKPHSIPLR CCCCCCCCCCCCCCC	37.03	-
191	Ubiquitination	EEKDKEYKPHSIPLR CCCCCCCCCCCCCCC	37.03	-
194	Phosphorylation	DKEYKPHSIPLRQSV CCCCCCCCCCCCCCC	34.13	24719451
200	Phosphorylation	HSIPLRQSVQPSKFN CCCCCCCCCCHHHCC	19.11	24300666
204	Ubiquitination	LRQSVQPSKFNSYGR CCCCCCHHHCCCCCH	32.56	-
204	Phosphorylation	LRQSVQPSKFNSYGR CCCCCCHHHCCCCCH	32.56	24300666
205	Acetylation	RQSVQPSKFNSYGRR CCCCCHHHCCCCCHH	56.07	25953088
205	Sumoylation	RQSVQPSKFNSYGRR CCCCCHHHCCCCCHH	56.07	28112733
205	Ubiquitination	RQSVQPSKFNSYGRR CCCCCHHHCCCCCHH	56.07	-
229	Sumoylation	PTEEDIEKNPELKKL CCHHHHHHCHHHHHE	77.47	28112733
234	Ubiquitination	IEKNPELKKLQIYGA HHHCHHHHHEEEECC	50.18	-
235	Ubiquitination	EKNPELKKLQIYGAG HHCHHHHHEEEECCC	59.24	-
239	Phosphorylation	ELKKLQIYGAGPKMM HHHHEEEECCCCCHH	6.48	25159151
244	Sumoylation	QIYGAGPKMMGLGLM EEECCCCCHHHHHHH	40.37	28112733
274	Sumoylation	CPPTVVVKEELGGDV CCCEEEEEEECCCCC	33.58	28112733
282	Sumoylation	EELGGDVKVESTSPK EECCCCCEEEECCCC	45.05	-
285	Phosphorylation	GGDVKVESTSPKTFL CCCCEEEECCCCCHH	36.85	25849741
286	Phosphorylation	GDVKVESTSPKTFLE CCCEEEECCCCCHHH	35.23	23403867
287	Phosphorylation	DVKVESTSPKTFLES CCEEEECCCCCHHHC	33.41	27134283
289	Ubiquitination	KVESTSPKTFLESKE EEEECCCCCHHHCHH	52.23	-
290	Phosphorylation	VESTSPKTFLESKEE EEECCCCCHHHCHHH	36.52	23403867
294	Phosphorylation	SPKTFLESKEELSHS CCCCHHHCHHHHCCC	47.73	23403867
295	Sumoylation	PKTFLESKEELSHSP CCCHHHCHHHHCCCC	45.92	28112733
295	Ubiquitination	PKTFLESKEELSHSP CCCHHHCHHHHCCCC	45.92	-
299	Phosphorylation	LESKEELSHSPEPCT HHCHHHHCCCCCCCH	25.79	30266825
301	Phosphorylation	SKEELSHSPEPCTKM CHHHHCCCCCCCHHH	27.81	29255136
306	Ubiquitination	SHSPEPCTKMTMRLR CCCCCCCHHHHHHHH	34.27	-
306	Phosphorylation	SHSPEPCTKMTMRLR CCCCCCCHHHHHHHH	34.27	23927012
307	Ubiquitination	HSPEPCTKMTMRLRR CCCCCCHHHHHHHHH	38.81	-
317	Phosphorylation	MRLRRNHSNAQFIES HHHHHCCCCHHHHHH	37.09	22617229
324	Phosphorylation	SNAQFIESYVCRMCS CCHHHHHHHHHHHHC	20.32	20068231
325	Phosphorylation	NAQFIESYVCRMCSR CHHHHHHHHHHHHCC	7.26	20068231
369	Ubiquitination	PKGVWRCPKCVMAEC CCCCCCCCCCHHHHC	25.22	-
370	Ubiquitination	KGVWRCPKCVMAECK CCCCCCCCCHHHHCC	42.99	-
376	Ubiquitination	PKCVMAECKRPPEAF CCCHHHHCCCCHHHH	3.08	-
377	Ubiquitination	KCVMAECKRPPEAFG CCHHHHCCCCHHHHC	60.49	-
408	Phosphorylation	ADSFKADYFNMPVHM HHHHCCCCCCCCCCC	11.17	27642862
458	Ubiquitination	SGFPVSDSKRHLTPE CCCCCCCCCCCCCHH	24.88	-
459	Ubiquitination	GFPVSDSKRHLTPEE CCCCCCCCCCCCHHH	49.15	-
463	Phosphorylation	SDSKRHLTPEEEEYA CCCCCCCCHHHHHHH	23.64	30576142
469	Phosphorylation	LTPEEEEYATSGWNL CCHHHHHHHCCCCCC	20.61	30576142
472	Phosphorylation	EEEEYATSGWNLNVM HHHHHHCCCCCCCCH	33.37	30576142
550	Ubiquitination	EHLEEVMKKLTPELF HHHHHHHHHHCHHHH	50.21	-
553	Phosphorylation	EEVMKKLTPELFDSQ HHHHHHHCHHHHHCC	24.48	26074081
656	Ubiquitination	CKMAACPEKLDLNLA HHHHCCCHHCCHHHH	67.16	-
657	Ubiquitination	KMAACPEKLDLNLAA HHHCCCHHCCHHHHH	32.23	-
681	Ubiquitination	VQEERRLRKALLEKG HHHHHHHHHHHHHCC	22.01	-
682	Ubiquitination	QEERRLRKALLEKGI HHHHHHHHHHHHCCC	48.23	-
686	Ubiquitination	RLRKALLEKGITEAE HHHHHHHHCCCCHHH	50.52	-
687	Ubiquitination	LRKALLEKGITEAER HHHHHHHCCCCHHHH	56.43	-
751	Phosphorylation	RQYLRYRYTLDELPA CCHHHHEEEHHHHHH	11.61	22817900
775	Ubiquitination	ESFDTWANKVRVALE HHHHHHHHHEEEEEE	34.61	-
776	Ubiquitination	SFDTWANKVRVALEV HHHHHHHHEEEEEEE	24.54	-
799	Phosphorylation	EELRALESEARERRF HHHHHHHHHHHHHCC	37.09	-
809	Phosphorylation	RERRFPNSELLQQLK HHHCCCCHHHHHHHH	29.84	22985185
849	Phosphorylation	RVAGLQMTLTELRAF HCCCHHCCHHHHHHH	19.98	-
893	Phosphorylation	EAREALASLPSSPGL HHHHHHHCCCCCHHH	41.48	28450419
896	Phosphorylation	EALASLPSSPGLLQS HHHHCCCCCHHHHHH	55.23	28176443
897	Phosphorylation	ALASLPSSPGLLQSL HHHCCCCCHHHHHHH	22.50	25159151
903	Phosphorylation	SSPGLLQSLLERGRQ CCHHHHHHHHHHHHH	34.59	28176443
934	Ubiquitination	QARWLDEVKRTLAPS HHHHHHHHHHHHCCC	5.19	-
935	Ubiquitination	ARWLDEVKRTLAPSA HHHHHHHHHHHCCCC	37.30	-
946	Phosphorylation	APSARRGTLAVMRGL CCCCCHHHHHHHHHH	15.10	-
995	Ubiquitination	HLCLEARQKHPPATL HHHHHHHHHCCCCHH	56.30	-
996	Ubiquitination	LCLEARQKHPPATLE HHHHHHHHCCCCHHH	53.15	-
1022	Ubiquitination	HLPNIQALKEALAKA CCCCHHHHHHHHHHH	2.70	-
1023	Ubiquitination	LPNIQALKEALAKAR CCCHHHHHHHHHHHH	43.91	-
1080	Ubiquitination	LQVLTAHSWREKASK HHHHHHCHHHHHHHH	25.93	21890473
1080 (in isoform 3)	Ubiquitination	-	25.93	21890473
1087	Acetylation	SWREKASKTFLKKNS HHHHHHHHHHHHHCC	48.43	7297869
1091	Ubiquitination	KASKTFLKKNSCYTL HHHHHHHHHCCHHHH	45.80	-
1092	Ubiquitination	ASKTFLKKNSCYTLL HHHHHHHHCCHHHHH	57.13	-
1113	Ubiquitination	ADAGSDSTKRSRWME CCCCCCCHHHHHHHH	35.15	-
1114	Ubiquitination	DAGSDSTKRSRWMEK CCCCCCHHHHHHHHH	52.94	-
1120	Ubiquitination	TKRSRWMEKELGLYK HHHHHHHHHHHCCCC	36.10	21890473
1121	Ubiquitination	KRSRWMEKELGLYKS HHHHHHHHHHCCCCC	41.98	21890473
1121 (in isoform 1)	Ubiquitination	-	41.98	21890473
1121 (in isoform 2)	Ubiquitination	-	41.98	21890473
1127	Sumoylation	EKELGLYKSDTELLG HHHHCCCCCHHHHHC	47.07	28112733
1127	Ubiquitination	EKELGLYKSDTELLG HHHHCCCCCHHHHHC	47.07	-
1151	Ubiquitination	GSVIVAFKEGEQKEK CCEEEEEECCCHHHH	55.88	-
1156	Ubiquitination	AFKEGEQKEKEGILQ EEECCCHHHHHCCEE	67.46	-
1221	Phosphorylation	VSVPRLLSSPRPNPT CCHHHHHCCCCCCCC	42.77	17081983
1222	Phosphorylation	SVPRLLSSPRPNPTS CHHHHHCCCCCCCCC	25.54	17081983
1241	Acetylation	AWWEWDTKFLCPLCM EHHCCCCCCHHHHHH	33.59	12439073
1257	Phosphorylation	SRRPRLETILALLVA CCCHHHHHHHHHHHH	26.36	-
1291 (in isoform 4)	Phosphorylation	-	16.11	25849741
1292 (in isoform 4)	Phosphorylation	-	18.11	25849741
1317 (in isoform 3)	Phosphorylation	-	33.09	25849741
1318 (in isoform 3)	Phosphorylation	-	28.96	25849741
1327	Phosphorylation	RPEEPPNYPAAPASD CCCCCCCCCCCCCCC	10.46	-
1333	Phosphorylation	NYPAAPASDPLREGS CCCCCCCCCCCCCCC	38.41	-
1340	Phosphorylation	SDPLREGSGKDMPKV CCCCCCCCCCCCHHH	37.61	-
1342	Acetylation	PLREGSGKDMPKVQG CCCCCCCCCCHHHHH	53.18	26051181
1356	Phosphorylation	GLLENGDSVTSPEKV HHHHCCCCCCCHHHC	28.79	19664994
1358	Phosphorylation	LENGDSVTSPEKVAP HHCCCCCCCHHHCCC	42.38	23401153
1358 (in isoform 2)	Phosphorylation	-	42.38	25849741
1359	Phosphorylation	ENGDSVTSPEKVAPE HCCCCCCCHHHCCCC	28.98	19664994
1359 (in isoform 2)	Phosphorylation	-	28.98	25849741
1369	Phosphorylation	KVAPEEGSGKRDLEL HCCCCCCCCHHHHHH	44.41	30278072
1441	Ubiquitination	IRTLLELEKAERHGS HHHHHHHHHHHHHCH	40.62	-
1442	Ubiquitination	RTLLELEKAERHGSR HHHHHHHHHHHHCHH	69.08	-
1484	Phosphorylation	LEPKRVRSSGPEAEE HCCCCHHCCCCCHHH	36.47	26074081
1485	Phosphorylation	EPKRVRSSGPEAEEV CCCCHHCCCCCHHHH	48.04	26074081
1544	Phosphorylation	SAPFSTLTPRLHLPC CCCCCCCCCCCCCCC	13.37	24719451

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	CNOT4	O95628	PMID:19346402
-	K	Ubiquitination	E3 ubiquitin ligase	E6	P03126	PMID:25231954
-	K	Ubiquitination	E3 ubiquitin ligase	E6	P06463	PMID:25231954

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KDM5C_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 KDM5C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NCOR1_HUMAN	NCOR1	physical	17468742
REST_HUMAN	REST	physical	17468742
HDAC1_HUMAN	HDAC1	physical	17468742
HDAC2_HUMAN	HDAC2	physical	17468742
RING1_HUMAN	RING1	physical	17468742
E2F6_HUMAN	E2F6	physical	17468742
MAX_HUMAN	MAX	physical	17468742
CBX3_HUMAN	CBX3	physical	17468742
RING2_HUMAN	RNF2	physical	17468742
KDM5C_HUMAN	KDM5C	physical	18078810
PCNA_HUMAN	PCNA	physical	21996408
THTPA_HUMAN	THTPA	physical	22939629
SPTN2_HUMAN	SPTBN2	physical	22939629
UBP5_HUMAN	USP5	physical	22939629
LSM2_HUMAN	LSM2	physical	26344197
PITH1_HUMAN	PITHD1	physical	26344197
CSK21_HUMAN	CSNK2A1	physical	26496610
CSK2B_HUMAN	CSNK2B	physical	26496610
E2F6_HUMAN	E2F6	physical	26496610
MAX_HUMAN	MAX	physical	26496610
SET_HUMAN	SET	physical	26496610
XPO1_HUMAN	XPO1	physical	26496610
MBD2_HUMAN	MBD2	physical	26496610
ZN592_HUMAN	ZNF592	physical	26496610
TOX4_HUMAN	TOX4	physical	26496610
MGAP_HUMAN	MGA	physical	26496610
PKCB1_HUMAN	ZMYND8	physical	26496610
VPS41_HUMAN	VPS41	physical	26496610
ZN532_HUMAN	ZNF532	physical	26496610
ZN687_HUMAN	ZNF687	physical	26496610
TSYL2_HUMAN	TSPYL2	physical	26496610
CENPK_HUMAN	CENPK	physical	26496610
GHC1_HUMAN	SLC25A22	physical	26496610
M3K1_HUMAN	MAP3K1	genetic	28319113
TSC1_HUMAN	TSC1	genetic	28319113
MTOR_HUMAN	MTOR	genetic	28319113
WEE1_HUMAN	WEE1	genetic	28319113
VHL_HUMAN	VHL	genetic	28319113

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300534	Mental retardation, X-linked, syndromic, Claes-Jensen type (MRXSCJ)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KDM5C_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-1359, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-317, AND MASSSPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1359, AND MASSSPECTROMETRY.	16964243 [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-317, AND MASSSPECTROMETRY.	17081983 [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-1359, AND MASSSPECTROMETRY.	15302935 [Abstract]