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Protein

Lysine-specific demethylase 4C

Gene

KDM4C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. 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.1 Publication

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei134Alpha-ketoglutarateBy similarity1
Metal bindingi190Iron; catalytic1
Metal bindingi192Iron; catalytic1
Binding sitei200Alpha-ketoglutarateBy similarity1
Binding sitei208Alpha-ketoglutarateBy similarity1
Metal bindingi236Zinc1 Publication1
Metal bindingi242Zinc1 Publication1
Metal bindingi278Iron; catalytic1
Metal bindingi308Zinc1 Publication1
Metal bindingi310Zinc1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri689 – 747PHD-type 1Add BLAST59
Zinc fingeri752 – 785C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST34
Zinc fingeri808 – 865PHD-type 2PROSITE-ProRule annotationAdd BLAST58

GO - Molecular functioni

  • androgen receptor binding Source: BHF-UCL
  • dioxygenase activity Source: UniProtKB-KW
  • enzyme binding Source: BHF-UCL
  • histone demethylase activity Source: Reactome
  • histone demethylase activity (H3-K9 specific) Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • histone H3-K9 demethylation Source: UniProtKB
  • positive regulation of cell proliferation Source: BHF-UCL
  • regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107077-MONOMER.
BRENDAi1.14.11.27. 2681.
1.14.11.B1. 2681.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 4C (EC:1.14.11.-)
Alternative name(s):
Gene amplified in squamous cell carcinoma 1 protein
Short name:
GASC-1 protein
JmjC domain-containing histone demethylation protein 3C
Jumonji domain-containing protein 2C
Gene namesi
Name:KDM4C
Synonyms:GASC1, JHDM3C, JMJD2C, KIAA0780
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:17071. KDM4C.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi23081.
OpenTargetsiENSG00000107077.
ENSG00000274527.
ENSG00000282960.
PharmGKBiPA164721503.

Chemistry databases

ChEMBLiCHEMBL6175.
GuidetoPHARMACOLOGYi2677.

Polymorphism and mutation databases

BioMutaiKDM4C.
DMDMi97536525.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001831771 – 1056Lysine-specific demethylase 4CAdd BLAST1056

Proteomic databases

EPDiQ9H3R0.
MaxQBiQ9H3R0.
PaxDbiQ9H3R0.
PeptideAtlasiQ9H3R0.
PRIDEiQ9H3R0.

PTM databases

iPTMnetiQ9H3R0.
PhosphoSitePlusiQ9H3R0.

Expressioni

Tissue specificityi

Overexpressed in several esophageal squamous cell carcinomas (ESCs).1 Publication

Gene expression databases

BgeeiENSG00000107077.
CleanExiHS_JMJD2C.
ExpressionAtlasiQ9H3R0. baseline and differential.
GenevisibleiQ9H3R0. HS.

Organism-specific databases

HPAiCAB009338.

Interactioni

GO - Molecular functioni

  • androgen receptor binding Source: BHF-UCL
  • enzyme binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi116712. 11 interactors.
DIPiDIP-60098N.
IntActiQ9H3R0. 1 interactor.
MINTiMINT-4658283.
STRINGi9606.ENSP00000370710.

Chemistry databases

BindingDBiQ9H3R0.

Structurei

Secondary structure

11056
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 19Combined sources3
Helixi23 – 26Combined sources4
Helixi29 – 38Combined sources10
Helixi41 – 44Combined sources4
Beta strandi45 – 49Combined sources5
Helixi62 – 66Combined sources5
Beta strandi68 – 71Combined sources4
Beta strandi73 – 80Combined sources8
Beta strandi83 – 90Combined sources8
Helixi96 – 103Combined sources8
Turni106 – 108Combined sources3
Helixi116 – 126Combined sources11
Beta strandi133 – 139Combined sources7
Helixi158 – 166Combined sources9
Turni171 – 174Combined sources4
Beta strandi177 – 181Combined sources5
Beta strandi186 – 190Combined sources5
Helixi193 – 195Combined sources3
Beta strandi197 – 206Combined sources10
Beta strandi208 – 213Combined sources6
Helixi215 – 217Combined sources3
Helixi218 – 228Combined sources11
Helixi230 – 235Combined sources6
Helixi239 – 242Combined sources4
Beta strandi245 – 247Combined sources3
Helixi249 – 255Combined sources7
Beta strandi260 – 264Combined sources5
Beta strandi269 – 272Combined sources4
Beta strandi277 – 282Combined sources6
Beta strandi284 – 293Combined sources10
Helixi296 – 298Combined sources3
Helixi299 – 304Combined sources6
Beta strandi309 – 311Combined sources3
Beta strandi312 – 314Combined sources3
Helixi320 – 326Combined sources7
Turni328 – 330Combined sources3
Helixi331 – 335Combined sources5
Beta strandi345 – 347Combined sources3
Beta strandi898 – 912Combined sources15
Beta strandi917 – 921Combined sources5
Helixi923 – 925Combined sources3
Helixi931 – 934Combined sources4
Beta strandi942 – 946Combined sources5
Beta strandi952 – 969Combined sources18
Beta strandi975 – 979Combined sources5
Helixi980 – 982Combined sources3
Beta strandi986 – 988Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XDPX-ray1.56A875-995[»]
2XMLX-ray2.55A/B1-347[»]
4XDOX-ray1.97A/B10-347[»]
4XDPX-ray2.07A/B10-347[»]
5FJHX-ray2.10A/B3-347[»]
5FJKX-ray1.66A3-347[»]
5KR7X-ray1.90A/B1-350[»]
ProteinModelPortaliQ9H3R0.
SMRiQ9H3R0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H3R0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 58JmjNPROSITE-ProRule annotationAdd BLAST43
Domaini144 – 310JmjCPROSITE-ProRule annotationAdd BLAST167
Domaini877 – 934Tudor 1Add BLAST58
Domaini935 – 991Tudor 2Add BLAST57

Domaini

The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails (By similarity).By similarity

Sequence similaritiesi

Belongs to the JHDM3 histone demethylase family.Curated
Contains 1 C2HC pre-PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 2 Tudor domains.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri689 – 747PHD-type 1Add BLAST59
Zinc fingeri752 – 785C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST34
Zinc fingeri808 – 865PHD-type 2PROSITE-ProRule annotationAdd BLAST58

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IT40. Eukaryota.
COG5141. LUCA.
GeneTreeiENSGT00530000063342.
HOGENOMiHOG000231125.
InParanoidiQ9H3R0.
KOiK06709.
OMAiCIFCRHR.
OrthoDBiEOG091G01FR.
PhylomeDBiQ9H3R0.
TreeFamiTF106449.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51805. EPHD. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H3R0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEVAEVESPL NPSCKIMTFR PSMEEFREFN KYLAYMESKG AHRAGLAKVI
60 70 80 90 100
PPKEWKPRQC YDDIDNLLIP APIQQMVTGQ SGLFTQYNIQ KKAMTVKEFR
110 120 130 140 150
QLANSGKYCT PRYLDYEDLE RKYWKNLTFV APIYGADING SIYDEGVDEW
160 170 180 190 200
NIARLNTVLD VVEEECGISI EGVNTPYLYF GMWKTTFAWH TEDMDLYSIN
210 220 230 240 250
YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL RHKMTLISPS
260 270 280 290 300
VLKKYGIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID
310 320 330 340 350
YGKVAKLCTC RKDMVKISMD IFVRKFQPDR YQLWKQGKDI YTIDHTKPTP
360 370 380 390 400
ASTPEVKAWL QRRRKVRKAS RSFQCARSTS KRPKADEEEE VSDEVDGAEV
410 420 430 440 450
PNPDSVTDDL KVSEKSEAAV KLRNTEASSE EESSASRMQV EQNLSDHIKL
460 470 480 490 500
SGNSCLSTSV TEDIKTEDDK AYAYRSVPSI SSEADDSIPL SSGYEKPEKS
510 520 530 540 550
DPSELSWPKS PESCSSVAES NGVLTEGEES DVESHGNGLE PGEIPAVPSG
560 570 580 590 600
ERNSFKVPSI AEGENKTSKS WRHPLSRPPA RSPMTLVKQQ APSDEELPEV
610 620 630 640 650
LSIEEEVEET ESWAKPLIHL WQTKSPNFAA EQEYNATVAR MKPHCAICTL
660 670 680 690 700
LMPYHKPDSS NEENDARWET KLDEVVTSEG KTKPLIPEMC FIYSEENIEY
710 720 730 740 750
SPPNAFLEED GTSLLISCAK CCVRVHASCY GIPSHEICDG WLCARCKRNA
760 770 780 790 800
WTAECCLCNL RGGALKQTKN NKWAHVMCAV AVPEVRFTNV PERTQIDVGR
810 820 830 840 850
IPLQRLKLKC IFCRHRVKRV SGACIQCSYG RCPASFHVTC AHAAGVLMEP
860 870 880 890 900
DDWPYVVNIT CFRHKVNPNV KSKACEKVIS VGQTVITKHR NTRYYSCRVM
910 920 930 940 950
AVTSQTFYEV MFDDGSFSRD TFPEDIVSRD CLKLGPPAEG EVVQVKWPDG
960 970 980 990 1000
KLYGAKYFGS NIAHMYQVEF EDGSQIAMKR EDIYTLDEEL PKRVKARFST
1010 1020 1030 1040 1050
ASDMRFEDTF YGADIIQGER KRQRVLSSRF KNEYVADPVY RTFLKSSFQK

KCQKRQ
Length:1,056
Mass (Da):119,982
Last modified:May 16, 2006 - v2
Checksum:iCBE871D4FAADD06D
GO
Isoform 2 (identifier: Q9H3R0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     999-1056: STASDMRFED...SFQKKCQKRQ → VSAGRCHLGT...QCNIFLSGTY

Note: No experimental confirmation available.
Show »
Length:1,047
Mass (Da):118,416
Checksum:i5A6E06262786B259
GO
Isoform 3 (identifier: Q9H3R0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     809-813: KCIFC → GRLGI
     814-1056: Missing.

Note: No experimental confirmation available.
Show »
Length:813
Mass (Da):91,891
Checksum:i672012048DEE27AC
GO
Isoform 4 (identifier: Q9H3R0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKHYGLPWKRTEEAAADTALTIM
     809-813: KCIFC → GRLGI
     814-1056: Missing.

Note: No experimental confirmation available.
Show »
Length:835
Mass (Da):94,376
Checksum:iB08576383C57FE4B
GO

Sequence cautioni

The sequence BAA34500 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI39608 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti155L → I in BAB16102 (PubMed:10987278).Curated1
Sequence conflicti514C → S in BAG64946 (PubMed:14702039).Curated1
Sequence conflicti807K → R in BAG64946 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049660206E → D.Corresponds to variant rs7864351dbSNPEnsembl.1
Natural variantiVAR_020340396D → N.Corresponds to variant rs2296067dbSNPEnsembl.1
Natural variantiVAR_049661492S → T.3 PublicationsCorresponds to variant rs35826653dbSNPEnsembl.1
Natural variantiVAR_049662697N → S.Corresponds to variant rs35389625dbSNPEnsembl.1
Natural variantiVAR_024681767Q → E.Corresponds to variant rs1407856dbSNPEnsembl.1
Natural variantiVAR_049663772K → R.1 PublicationCorresponds to variant rs1417290dbSNPEnsembl.1
Natural variantiVAR_0246821039V → I.1 PublicationCorresponds to variant rs913588dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0461131M → MKHYGLPWKRTEEAAADTAL TIM in isoform 4. 1 Publication1
Alternative sequenceiVSP_045462809 – 813KCIFC → GRLGI in isoform 3 and isoform 4. 1 Publication5
Alternative sequenceiVSP_045463814 – 1056Missing in isoform 3 and isoform 4. 1 PublicationAdd BLAST243
Alternative sequenceiVSP_018311999 – 1056STASD…CQKRQ → VSAGRCHLGTCQVNSLSSPH VSQAQQETYLGFWINSKKSQ CNIFLSGTY in isoform 2. 1 PublicationAdd BLAST58

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037901 mRNA. Translation: BAB16102.1.
AB018323 mRNA. Translation: BAA34500.1. Different initiation.
AK304032 mRNA. Translation: BAG64946.1.
AK310439 mRNA. No translation available.
AL354707
, AL137020, AL161443, AL445592, AL513412 Genomic DNA. Translation: CAH73283.1.
AL354707
, AL137020, AL161443, AL513412, AL445592 Genomic DNA. Translation: CAH73284.1.
AL445592
, AL161443, AL513412, AL354707, AL137020 Genomic DNA. Translation: CAI16322.1.
AL445592
, AL137020, AL354707, AL513412, AL161443 Genomic DNA. Translation: CAI16323.1.
AL161443
, AL137020, AL354707, AL513412, AL445592 Genomic DNA. Translation: CAI39606.1.
AL161443
, AL513412, AL445592, AL354707, AL137020 Genomic DNA. Translation: CAI39607.1.
AL161443, AL137020, AL513412 Genomic DNA. Translation: CAI39608.1. Sequence problems.
BC104859 mRNA. Translation: AAI04860.1.
BC104861 mRNA. Translation: AAI04862.1.
BC143571 mRNA. Translation: AAI43572.1.
CCDSiCCDS55285.1. [Q9H3R0-4]
CCDS55286.1. [Q9H3R0-3]
CCDS6471.1. [Q9H3R0-1]
RefSeqiNP_001140167.1. NM_001146695.1. [Q9H3R0-3]
NP_001140168.1. NM_001146696.1. [Q9H3R0-4]
NP_055876.2. NM_015061.3. [Q9H3R0-1]
UniGeneiHs.709425.

Genome annotation databases

EnsembliENST00000381306; ENSP00000370707; ENSG00000107077. [Q9H3R0-2]
ENST00000381309; ENSP00000370710; ENSG00000107077. [Q9H3R0-1]
ENST00000543771; ENSP00000445427; ENSG00000107077. [Q9H3R0-3]
GeneIDi23081.
KEGGihsa:23081.
UCSCiuc003zkg.4. human. [Q9H3R0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037901 mRNA. Translation: BAB16102.1.
AB018323 mRNA. Translation: BAA34500.1. Different initiation.
AK304032 mRNA. Translation: BAG64946.1.
AK310439 mRNA. No translation available.
AL354707
, AL137020, AL161443, AL445592, AL513412 Genomic DNA. Translation: CAH73283.1.
AL354707
, AL137020, AL161443, AL513412, AL445592 Genomic DNA. Translation: CAH73284.1.
AL445592
, AL161443, AL513412, AL354707, AL137020 Genomic DNA. Translation: CAI16322.1.
AL445592
, AL137020, AL354707, AL513412, AL161443 Genomic DNA. Translation: CAI16323.1.
AL161443
, AL137020, AL354707, AL513412, AL445592 Genomic DNA. Translation: CAI39606.1.
AL161443
, AL513412, AL445592, AL354707, AL137020 Genomic DNA. Translation: CAI39607.1.
AL161443, AL137020, AL513412 Genomic DNA. Translation: CAI39608.1. Sequence problems.
BC104859 mRNA. Translation: AAI04860.1.
BC104861 mRNA. Translation: AAI04862.1.
BC143571 mRNA. Translation: AAI43572.1.
CCDSiCCDS55285.1. [Q9H3R0-4]
CCDS55286.1. [Q9H3R0-3]
CCDS6471.1. [Q9H3R0-1]
RefSeqiNP_001140167.1. NM_001146695.1. [Q9H3R0-3]
NP_001140168.1. NM_001146696.1. [Q9H3R0-4]
NP_055876.2. NM_015061.3. [Q9H3R0-1]
UniGeneiHs.709425.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XDPX-ray1.56A875-995[»]
2XMLX-ray2.55A/B1-347[»]
4XDOX-ray1.97A/B10-347[»]
4XDPX-ray2.07A/B10-347[»]
5FJHX-ray2.10A/B3-347[»]
5FJKX-ray1.66A3-347[»]
5KR7X-ray1.90A/B1-350[»]
ProteinModelPortaliQ9H3R0.
SMRiQ9H3R0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116712. 11 interactors.
DIPiDIP-60098N.
IntActiQ9H3R0. 1 interactor.
MINTiMINT-4658283.
STRINGi9606.ENSP00000370710.

Chemistry databases

BindingDBiQ9H3R0.
ChEMBLiCHEMBL6175.
GuidetoPHARMACOLOGYi2677.

PTM databases

iPTMnetiQ9H3R0.
PhosphoSitePlusiQ9H3R0.

Polymorphism and mutation databases

BioMutaiKDM4C.
DMDMi97536525.

Proteomic databases

EPDiQ9H3R0.
MaxQBiQ9H3R0.
PaxDbiQ9H3R0.
PeptideAtlasiQ9H3R0.
PRIDEiQ9H3R0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381306; ENSP00000370707; ENSG00000107077. [Q9H3R0-2]
ENST00000381309; ENSP00000370710; ENSG00000107077. [Q9H3R0-1]
ENST00000543771; ENSP00000445427; ENSG00000107077. [Q9H3R0-3]
GeneIDi23081.
KEGGihsa:23081.
UCSCiuc003zkg.4. human. [Q9H3R0-1]

Organism-specific databases

CTDi23081.
DisGeNETi23081.
GeneCardsiKDM4C.
H-InvDBHIX0017555.
HGNCiHGNC:17071. KDM4C.
HPAiCAB009338.
MIMi605469. gene.
neXtProtiNX_Q9H3R0.
OpenTargetsiENSG00000107077.
ENSG00000274527.
ENSG00000282960.
PharmGKBiPA164721503.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IT40. Eukaryota.
COG5141. LUCA.
GeneTreeiENSGT00530000063342.
HOGENOMiHOG000231125.
InParanoidiQ9H3R0.
KOiK06709.
OMAiCIFCRHR.
OrthoDBiEOG091G01FR.
PhylomeDBiQ9H3R0.
TreeFamiTF106449.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107077-MONOMER.
BRENDAi1.14.11.27. 2681.
1.14.11.B1. 2681.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

Miscellaneous databases

ChiTaRSiKDM4C. human.
EvolutionaryTraceiQ9H3R0.
GeneWikiiJMJD2C.
GenomeRNAii23081.
PROiQ9H3R0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107077.
CleanExiHS_JMJD2C.
ExpressionAtlasiQ9H3R0. baseline and differential.
GenevisibleiQ9H3R0. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51805. EPHD. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKDM4C_HUMAN
AccessioniPrimary (citable) accession number: Q9H3R0
Secondary accession number(s): B4E1Y4
, B7ZL46, F5H347, F5H7P0, O94877, Q2M3M0, Q5JUC9, Q5VYJ2, Q5VYJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 16, 2006
Last modified: November 30, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.