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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341Alpha-ketoglutarateBy similarity
Metal bindingi190 – 1901Iron; catalytic
Metal bindingi192 – 1921Iron; catalytic
Binding sitei200 – 2001Alpha-ketoglutarateBy similarity
Binding sitei208 – 2081Alpha-ketoglutarateBy similarity
Metal bindingi236 – 2361Zinc1 Publication
Metal bindingi242 – 2421Zinc1 Publication
Metal bindingi278 – 2781Iron; catalytic
Metal bindingi308 – 3081Zinc1 Publication
Metal bindingi310 – 3101Zinc1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri689 – 74759PHD-type 1Add
BLAST
Zinc fingeri809 – 86557PHD-type 2Add
BLAST

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

  • chromatin organization Source: Reactome
  • 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
  • small GTPase mediated signal transduction Source: Reactome
  • 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

BRENDAi1.14.11.27. 2681.
1.14.11.B1. 2681.
ReactomeiREACT_263961. HDMs demethylate histones.
REACT_355391. 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
ProteomesiUP000005640 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

PharmGKBiPA164721503.

Polymorphism and mutation databases

BioMutaiKDM4C.
DMDMi97536525.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10561056Lysine-specific demethylase 4CPRO_0000183177Add
BLAST

Proteomic databases

MaxQBiQ9H3R0.
PaxDbiQ9H3R0.
PRIDEiQ9H3R0.

PTM databases

PhosphoSiteiQ9H3R0.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9H3R0.
CleanExiHS_JMJD2C.
ExpressionAtlasiQ9H3R0. baseline and differential.
GenevisibleiQ9H3R0. HS.

Interactioni

Protein-protein interaction databases

BioGridi116712. 11 interactions.
DIPiDIP-60098N.
IntActiQ9H3R0. 1 interaction.
MINTiMINT-4658283.
STRINGi9606.ENSP00000370710.

Structurei

Secondary structure

1
1056
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Helixi23 – 264Combined sources
Helixi29 – 3810Combined sources
Helixi41 – 444Combined sources
Beta strandi45 – 495Combined sources
Helixi62 – 665Combined sources
Beta strandi68 – 714Combined sources
Beta strandi73 – 808Combined sources
Beta strandi83 – 908Combined sources
Helixi96 – 1049Combined sources
Turni106 – 1083Combined sources
Helixi116 – 12611Combined sources
Beta strandi133 – 1397Combined sources
Helixi158 – 1669Combined sources
Turni171 – 1744Combined sources
Beta strandi177 – 1815Combined sources
Beta strandi186 – 1905Combined sources
Helixi193 – 1953Combined sources
Beta strandi197 – 20610Combined sources
Beta strandi208 – 2136Combined sources
Helixi215 – 2173Combined sources
Helixi218 – 22811Combined sources
Helixi230 – 2356Combined sources
Helixi239 – 2424Combined sources
Beta strandi245 – 2473Combined sources
Helixi249 – 2546Combined sources
Beta strandi260 – 2645Combined sources
Beta strandi269 – 2724Combined sources
Beta strandi277 – 2826Combined sources
Beta strandi284 – 29310Combined sources
Helixi298 – 3047Combined sources
Beta strandi312 – 3143Combined sources
Helixi320 – 3267Combined sources
Turni328 – 3303Combined sources
Helixi331 – 3355Combined sources
Beta strandi898 – 91215Combined sources
Beta strandi917 – 9215Combined sources
Helixi923 – 9253Combined sources
Helixi931 – 9344Combined sources
Beta strandi942 – 9465Combined sources
Beta strandi952 – 96918Combined sources
Beta strandi975 – 9795Combined sources
Helixi980 – 9823Combined sources
Beta strandi986 – 9883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XDPX-ray1.56A875-995[»]
2XMLX-ray2.55A/B1-347[»]
4XDOX-ray1.97A/B10-347[»]
4XDPX-ray2.07A/B10-347[»]
ProteinModelPortaliQ9H3R0.
SMRiQ9H3R0. Positions 10-347, 876-994.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H3R0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 5843JmjNPROSITE-ProRule annotationAdd
BLAST
Domaini144 – 310167JmjCPROSITE-ProRule annotationAdd
BLAST
Domaini877 – 93458Tudor 1Add
BLAST
Domaini935 – 99157Tudor 2Add
BLAST

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 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.Curated
Contains 2 Tudor domains.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri689 – 74759PHD-type 1Add
BLAST
Zinc fingeri809 – 86557PHD-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5141.
GeneTreeiENSGT00530000063342.
HOGENOMiHOG000231125.
InParanoidiQ9H3R0.
OMAiDIIQGER.
OrthoDBiEOG7TQV03.
PhylomeDBiQ9H3R0.
TreeFamiTF106449.

Family and domain databases

InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_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.
PROSITEiPS51184. 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 BAA34500.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI39608.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551L → I in BAB16102 (PubMed:10987278).Curated
Sequence conflicti514 – 5141C → S in BAG64946 (PubMed:14702039).Curated
Sequence conflicti807 – 8071K → R in BAG64946 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti206 – 2061E → D.
Corresponds to variant rs7864351 [ dbSNP | Ensembl ].
VAR_049660
Natural varianti396 – 3961D → N.
Corresponds to variant rs2296067 [ dbSNP | Ensembl ].
VAR_020340
Natural varianti492 – 4921S → T.3 Publications
Corresponds to variant rs35826653 [ dbSNP | Ensembl ].
VAR_049661
Natural varianti697 – 6971N → S.
Corresponds to variant rs35389625 [ dbSNP | Ensembl ].
VAR_049662
Natural varianti767 – 7671Q → E.
Corresponds to variant rs1407856 [ dbSNP | Ensembl ].
VAR_024681
Natural varianti772 – 7721K → R.1 Publication
Corresponds to variant rs1417290 [ dbSNP | Ensembl ].
VAR_049663
Natural varianti1039 – 10391V → I.1 Publication
Corresponds to variant rs913588 [ dbSNP | Ensembl ].
VAR_024682

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MKHYGLPWKRTEEAAADTAL TIM in isoform 4. 1 PublicationVSP_046113
Alternative sequencei809 – 8135KCIFC → GRLGI in isoform 3 and isoform 4. 1 PublicationVSP_045462
Alternative sequencei814 – 1056243Missing in isoform 3 and isoform 4. 1 PublicationVSP_045463Add
BLAST
Alternative sequencei999 – 105658STASD…CQKRQ → VSAGRCHLGTCQVNSLSSPH VSQAQQETYLGFWINSKKSQ CNIFLSGTY in isoform 2. 1 PublicationVSP_018311Add
BLAST

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.
ENST00000543771; ENSP00000445427; ENSG00000107077. [Q9H3R0-3]
GeneIDi23081.
UCSCiuc003zkg.3. human. [Q9H3R0-2]
uc003zkh.3. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
2XDPX-ray1.56A875-995[»]
2XMLX-ray2.55A/B1-347[»]
4XDOX-ray1.97A/B10-347[»]
4XDPX-ray2.07A/B10-347[»]
ProteinModelPortaliQ9H3R0.
SMRiQ9H3R0. Positions 10-347, 876-994.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116712. 11 interactions.
DIPiDIP-60098N.
IntActiQ9H3R0. 1 interaction.
MINTiMINT-4658283.
STRINGi9606.ENSP00000370710.

Chemistry

BindingDBiQ9H3R0.
ChEMBLiCHEMBL6175.
GuidetoPHARMACOLOGYi2677.

PTM databases

PhosphoSiteiQ9H3R0.

Polymorphism and mutation databases

BioMutaiKDM4C.
DMDMi97536525.

Proteomic databases

MaxQBiQ9H3R0.
PaxDbiQ9H3R0.
PRIDEiQ9H3R0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381306; ENSP00000370707; ENSG00000107077. [Q9H3R0-2]
ENST00000381309; ENSP00000370710; ENSG00000107077.
ENST00000543771; ENSP00000445427; ENSG00000107077. [Q9H3R0-3]
GeneIDi23081.
UCSCiuc003zkg.3. human. [Q9H3R0-2]
uc003zkh.3. human. [Q9H3R0-1]

Organism-specific databases

CTDi23081.
GeneCardsiGC09P006720.
H-InvDBHIX0017555.
HGNCiHGNC:17071. KDM4C.
MIMi605469. gene.
neXtProtiNX_Q9H3R0.
PharmGKBiPA164721503.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5141.
GeneTreeiENSGT00530000063342.
HOGENOMiHOG000231125.
InParanoidiQ9H3R0.
OMAiDIIQGER.
OrthoDBiEOG7TQV03.
PhylomeDBiQ9H3R0.
TreeFamiTF106449.

Enzyme and pathway databases

BRENDAi1.14.11.27. 2681.
1.14.11.B1. 2681.
ReactomeiREACT_263961. HDMs demethylate histones.
REACT_355391. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

Miscellaneous databases

ChiTaRSiKDM4C. human.
EvolutionaryTraceiQ9H3R0.
GeneWikiiJMJD2C.
GenomeRNAii23081.
NextBioi44205.
PROiQ9H3R0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H3R0.
CleanExiHS_JMJD2C.
ExpressionAtlasiQ9H3R0. baseline and differential.
GenevisibleiQ9H3R0. HS.

Family and domain databases

InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_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.
PROSITEiPS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines."
    Yang Z.Q., Imoto I., Fukuda Y., Pimkhaokham A., Shimada Y., Imamura M., Sugano S., Nakamura Y., Inazawa J.
    Cancer Res. 60:4735-4739(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS THR-492 AND ARG-772.
  2. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-492.
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), VARIANT THR-492.
    Tissue: Testis and Trachea.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-1039.
    Tissue: Liver.
  6. "Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases."
    Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z., Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.
    Cell 125:467-481(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY.
  7. "Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family."
    Hillringhaus L., Yue W.W., Rose N.R., Ng S.S., Gileadi C., Loenarz C., Bello S.H., Bray J.E., Schofield C.J., Oppermann U.
    J. Biol. Chem. 286:41616-41625(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-347 IN COMPLEX WITH ZINC AND NICKEL ION, COFACTOR, SUBSTRATE SPECIFICITY.

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: July 22, 2015
This is version 133 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

External Data

Dasty 3

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 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.