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Protein Page:
JARID1C (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
JARID1C Histone demethylase that specifically demethylates 'Lys- 4' of histone H3, thereby playing a central role in histone code. 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. Part of two distinct complexes, one containing E2F6, and the other containing REST. Expressed in all tissues examined. Highest levels found in brain and skeletal muscle. Belongs to the JARID1 histone demethylase family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Demethylase; Oxidoreductase; EC 1.14.11.-
Chromosomal Location of Human Ortholog: Xp11.22-p11.21
Cellular Component: nucleoplasm; nucleus
Molecular Function: histone demethylase activity; histone demethylase activity (H3-K4 specific)
Biological Process: negative regulation of transcription, DNA-dependent
Disease: Mental Retardation, X-linked, Syndromic, Claes-jensen Type
Reference #:  P41229 (UniProtKB)
Alt. Names/Synonyms: DXS1272E; Histone demethylase JARID1C; JARID1C; JmjC domain-containing protein SMCX; Jumonji, AT rich interactive domain 1C (RBP2-like); Jumonji/ARID domain-containing protein 1C; KDM5C; lysine (K)-specific demethylase 5C; Lysine-specific demethylase 5C; MRXJ; MRXSJ; Protein SmcX; Protein Xe169; selected cDNA on X; SMCX; Smcx homolog, X chromosome; Smcy homolog, X-linked; XE169
Gene Symbols: KDM5C
Molecular weight: 175,720 Da
Basal Isoelectric point: 5.44  Predict pI for various phosphorylation states
CST Pathways:  Histone Methylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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JARID1C

Protein Structure Not Found.
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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K91‑ub NYLDQIAkFWEIQGS
0 1 K205‑ac RQSVQPSkFNSYGRR
0 5 Y239‑p ELKKLQIyGAGPKMM
0 1 S287‑p DVKVESTsPkTFLES
0 1 K289‑ub KVESTsPkTFLESKE
0 1 S299‑p LESKEELsHsPEPCt
0 22 S301‑p SKEELsHsPEPCtKM
0 1 T306‑p sHsPEPCtKMTMRLR
0 60 S317‑p MRLRRNHsNAQFIES
0 1 Y408 ADSFKADYFNMPVHM
0 1 K459‑ub GFPVSDSkRHLTPEE
0 1 S799‑p EELRALEsEARERRF
0 1 T849‑p RVAGLQMtLTELRAF
0 4 S893 EAREALASLPSsPGL
0 12 S897‑p ALASLPSsPGLLQSL
0 1 T946‑p APSARRGtLAVMRGL
0 1 K1087‑ac SWREKASkTFLKKNS
0 1 K1114 DAGSDSTKRSRWMEk
0 1 K1121‑ub KRSRWMEkELGLYKS
0 1 K1151‑ub GSVIVAFkEGEQkEK
0 1 K1156‑ub AFkEGEQkEKEGILQ
0 2 K1241‑ac AWWEWDTkFLCPLCM
0 1 Y1327‑p RPEEPPNyPAAPAsD
0 1 S1333‑p NyPAAPAsDPLREGs
0 1 S1340‑p sDPLREGsGKDMPKV
0 3 S1356‑p GLLENGDsVtsPEKV
0 2 T1358‑p LENGDsVtsPEKVAP
0 16 S1359‑p ENGDsVtsPEKVAPE
  mouse

 
K91 NYLDQIAKFWEIQGS
K205 RQSVQPSKFNSYGRR
Y239‑p ELKKLQIyGAGPKMM
S287 DVKMESTSPKTFLEG
K289 KMESTSPKTFLEGKE
S299 LEGKEELSHsPEPCT
S301‑p GKEELSHsPEPCTKM
T306 SHsPEPCTKMTMRLR
S317‑p MRLRRNHsNAQFIES
Y408‑p ADSFKADyFNMPVHM
K459 GFPVSDSKRHLTPEE
S799 EELRALESEARERRF
T849 RVAGLQMTLAELRDF
S893‑p EAREALVsQPSsPGL
S897‑p ALVsQPSsPGLLQSL
T946 APSARRGTLAIMRGL
K1087 SWREKASKTFLKKNS
K1114‑ub DAGSDSTkRSRWMEK
K1121 kRSRWMEKELGLYKS
K1151 GSVIVAFKEGEQKEK
K1156 AFKEGEQKEKEGILQ
K1241 AWWEWDTKFLCPLCM
Y1327 KPEESLAYPSDGGEG
- gap
- gap
S1350‑p GLLENGDsVTsPEKV
T1352 LENGDsVTsPEKVAT
S1353‑p ENGDsVTsPEKVATE
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