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Protein Page:
JARID1A (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
JARID1A 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'. May stimulate transcription mediated by nuclear receptors. May be involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12. Interacts with SUZ12; the interaction is direct. Interacts with the viral protein-binding domain of RB1. Interacts with ESR1, MYC, MYCN and LMO2. Belongs to the JARID1 histone demethylase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 1.14.11.-; Transcription factor; Oxidoreductase
Cellular Component: cytoplasm; nucleolus; nucleus; cyclin-dependent protein kinase activating kinase holoenzyme complex
Molecular Function: DNA binding; zinc ion binding; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; chromatin binding; transcription factor activity
Biological Process: transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; multicellular organismal development; chromatin modification
Reference #:  P29375 (UniProtKB)
Alt. Names/Synonyms: Histone demethylase JARID1A; JARID1A; Jumonji, AT rich interactive domain 1A (RBBP2-like); Jumonji, AT rich interactive domain 1A (RBP2-like); Jumonji/ARID domain-containing protein 1A; KDM5A; lysine (K)-specific demethylase 5A; Lysine-specific demethylase 5A; RBBP-2; RBBP2; RBP2; retinoblastoma binding protein 2; Retinoblastoma-binding protein 2
Gene Symbols: KDM5A
Molecular weight: 192,095 Da
Basal Isoelectric point: 6.12  Predict pI for various phosphorylation states
CST Pathways:  Histone Methylation  |  Notch Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

JARID1A

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


 SS 

SS: 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.


 MS 

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


       human

 
0 1 T46-p IRPLAEKtGICKIRP
0 1 T84 LNELEAMTRVRLDFL
0 1 Y148-p KVGSRLGyLPGKGTG
0 4 S204-p LSTDTQTsPEPGTRM
0 2 T223 KRTRRVKTQSESGDV
0 2 S399-p KEFWRLVsSIEEDVI
0 1 K425-u FGSGFPVkDGRRKIL
0 1 S1085 TDIGVYGSGKNRRKK
0 21 S1111-p DLDLEPLsDLEEGLE
0 1 S1327-p AFNRVVSsVSssPRQ
0 2 S1330-p RVVSsVSssPRQTMD
0 3 S1331-p VVSsVSssPRQTMDY
0 1 Y1338 sPRQTMDYDDEEtDs
0 3 T1343-p MDYDDEEtDsDEDIR
0 3 S1345-p YDDEEtDsDEDIRET
0 1 K1382-s CDEEIPIkSEEVVTH
0 4 T1415-p SCSQGSStPRKQPRK
0 2 S1423-p PRKQPRKsPLVPRSL
0 1 S1438-p EPPVLELsPGAKAQL
0 2 S1488-p LHIMEDDsMEEKPLK
0 2 Y1595 VLDIPSKYDWsGAEE
0 4 S1598-p IPSKYDWsGAEEsDD
0 4 S1603-p DWsGAEEsDDENAVC
0 5 S1666-p AKKQGPVsPGPAPPP
0 1 Y1679-p PPSFIMSyKLPMEDL
  mouse

 
T46 IRPFAEKTGICKIRP
T84-p LNELEAMtRVRLDFL
Y148 KVGSRLGYLPGKGTG
S204-p LSTDIQPsPERGTRM
S223-p KRTRRVKsQSDSGEV
S399 KEFWRLVSSIEEDVI
K425 FGSGFPKKDGQRKML
S1085-p TDIGVYGsGKNRRKK
S1111-p DLDLEPLsDLEEGLE
S1327 AFNRVVSSVSSsPHQ
S1330 RVVSSVSSsPHQTMD
S1331-p VVSSVSSsPHQTMDy
Y1338-p sPHQTMDyDDEEtDs
T1343-p MDyDDEEtDsDEDIR
S1345-p yDDEEtDsDEDIRET
K1382 CDEEIPIKSEEVVTH
T1415 SCSQGSSTPRKQPRK
S1423 PRKQPRKSPLVPRSL
S1438 EPPVLELSPGAKAQL
S1488 LHIMEDDSIEEKPLK
Y1595-p VLDIPSKyDWsGAEE
S1598-p IPSKyDWsGAEEsDD
S1603-p DWsGAEEsDDENAVC
S1666-p AKKQGPDsPGQAPPP
Y1679 PPPFLMSYKLPMEDL
  rat

 
T46 IRPLAEKTGICKIRP
T84 LNELEAMTRVRLDFL
Y148 KVGSRLGYLPGKGTG
S204-p LSTDIQPsPERGTRM
S223 KRTRRVKSQSDSGEV
S399 KEFWRLVSSIEEDVI
K425 FGSGFPIKDGQRKML
S1085 TDIGVYGSGKNRRKK
S1111-p DLDLEPLsDLEEGLE
S1327 AFNRVVSSVSSSPHQ
S1330 RVVSSVSSSPHQAMD
S1331 VVSSVSSSPHQAMDY
Y1338 SPHQAMDYDDEETDS
T1343 MDYDDEETDSDEDIR
S1345 YDDEETDSDEDIRET
K1382 CDEEIPIKSEEVVTH
T1415 SCSQGSSTPRKQPRK
S1423 PRKQPRKSPLVPRSL
S1438 EPPVLELSPGAKAQL
S1488-p LHIMEDDsVEEKPLK
Y1595 VLDIPSKYDWSGAEE
S1598 IPSKYDWSGAEESDD
S1603 DWSGAEESDDENAVC
S1666 AKKQGPDSPGHAPPP
Y1679 PPPFIMSYKLPMEDL
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