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Q9H3R0

- KDM4C_HUMAN

UniProt

Q9H3R0 - KDM4C_HUMAN

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Protein

Lysine-specific demethylase 4C

Gene

KDM4C

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

  1. androgen receptor binding Source: BHF-UCL
  2. dioxygenase activity Source: UniProtKB-KW
  3. enzyme binding Source: BHF-UCL
  4. histone demethylase activity (H3-K9 specific) Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. histone H3-K9 demethylation Source: UniProtKB
  2. positive regulation of cell proliferation Source: BHF-UCL
  3. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  4. 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

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: Chromosome 9

Organism-specific databases

HGNCiHGNC:17071. KDM4C.

Subcellular locationi

Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  1. nuclear chromatin Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164721503.

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.
GenevestigatoriQ9H3R0.

Interactioni

Protein-protein interaction databases

BioGridi116712. 9 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 – 193
Helixi23 – 264
Helixi29 – 3810
Helixi41 – 444
Beta strandi45 – 495
Helixi62 – 665
Beta strandi68 – 714
Beta strandi73 – 808
Beta strandi83 – 908
Helixi96 – 1049
Turni106 – 1083
Helixi116 – 12611
Beta strandi133 – 1397
Helixi158 – 1669
Beta strandi172 – 1754
Beta strandi177 – 1815
Beta strandi186 – 1905
Helixi193 – 1953
Beta strandi197 – 20610
Beta strandi208 – 2136
Helixi215 – 2173
Helixi218 – 22811
Helixi230 – 2356
Helixi239 – 2424
Beta strandi245 – 2473
Helixi249 – 2546
Beta strandi260 – 2645
Beta strandi269 – 2724
Beta strandi277 – 2826
Beta strandi284 – 29310
Helixi296 – 2983
Helixi299 – 3024
Helixi320 – 3267
Turni328 – 3303
Helixi331 – 3355
Beta strandi898 – 91215
Beta strandi917 – 9215
Helixi923 – 9253
Helixi931 – 9344
Beta strandi942 – 9465
Beta strandi952 – 96918
Beta strandi975 – 9795
Helixi980 – 9823
Beta strandi986 – 9883

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XDPX-ray1.56A875-995[»]
2XMLX-ray2.55A/B1-347[»]
ProteinModelPortaliQ9H3R0.
SMRiQ9H3R0. Positions 10-347, 711-750, 876-1023.
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.
KOiK06709.
OMAiDIIQGER.
OrthoDBiEOG7TQV03.
PhylomeDBiQ9H3R0.
TreeFamiTF106449.

Family and domain databases

InterProiIPR003347. JmjC_dom.
IPR003349. TF_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. Align

Isoform 1 (identifier: Q9H3R0) [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.
The sequence CAI39608.1 differs from that shown. Reason: Erroneous gene model prediction.

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:
EMBL
GenBank
DDBJ
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]
CCDS55287.1. [Q9H3R0-2]
CCDS6471.1. [Q9H3R0-1]
RefSeqiNP_001140166.1. NM_001146694.1. [Q9H3R0-2]
NP_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.3. human. [Q9H3R0-2]
uc003zkh.3. human. [Q9H3R0-1]

Polymorphism databases

DMDMi97536525.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS55285.1. [Q9H3R0-4 ]
CCDS55286.1. [Q9H3R0-3 ]
CCDS55287.1. [Q9H3R0-2 ]
CCDS6471.1. [Q9H3R0-1 ]
RefSeqi NP_001140166.1. NM_001146694.1. [Q9H3R0-2 ]
NP_001140167.1. NM_001146695.1. [Q9H3R0-3 ]
NP_001140168.1. NM_001146696.1. [Q9H3R0-4 ]
NP_055876.2. NM_015061.3. [Q9H3R0-1 ]
UniGenei Hs.709425.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XDP X-ray 1.56 A 875-995 [» ]
2XML X-ray 2.55 A/B 1-347 [» ]
ProteinModelPortali Q9H3R0.
SMRi Q9H3R0. Positions 10-347, 711-750, 876-1023.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116712. 9 interactions.
DIPi DIP-60098N.
IntActi Q9H3R0. 1 interaction.
MINTi MINT-4658283.
STRINGi 9606.ENSP00000370710.

Chemistry

BindingDBi Q9H3R0.
ChEMBLi CHEMBL6175.

PTM databases

PhosphoSitei Q9H3R0.

Polymorphism databases

DMDMi 97536525.

Proteomic databases

MaxQBi Q9H3R0.
PaxDbi Q9H3R0.
PRIDEi Q9H3R0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381306 ; ENSP00000370707 ; ENSG00000107077 . [Q9H3R0-2 ]
ENST00000381309 ; ENSP00000370710 ; ENSG00000107077 . [Q9H3R0-1 ]
ENST00000543771 ; ENSP00000445427 ; ENSG00000107077 . [Q9H3R0-3 ]
GeneIDi 23081.
KEGGi hsa:23081.
UCSCi uc003zkg.3. human. [Q9H3R0-2 ]
uc003zkh.3. human. [Q9H3R0-1 ]

Organism-specific databases

CTDi 23081.
GeneCardsi GC09P006720.
H-InvDB HIX0017555.
HGNCi HGNC:17071. KDM4C.
MIMi 605469. gene.
neXtProti NX_Q9H3R0.
PharmGKBi PA164721503.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5141.
GeneTreei ENSGT00530000063342.
HOGENOMi HOG000231125.
InParanoidi Q9H3R0.
KOi K06709.
OMAi DIIQGER.
OrthoDBi EOG7TQV03.
PhylomeDBi Q9H3R0.
TreeFami TF106449.

Miscellaneous databases

ChiTaRSi KDM4C. human.
EvolutionaryTracei Q9H3R0.
GeneWikii JMJD2C.
GenomeRNAii 23081.
NextBioi 44205.
PROi Q9H3R0.
SOURCEi Search...

Gene expression databases

Bgeei Q9H3R0.
CleanExi HS_JMJD2C.
ExpressionAtlasi Q9H3R0. baseline and differential.
Genevestigatori Q9H3R0.

Family and domain databases

InterProi IPR003347. JmjC_dom.
IPR003349. TF_JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
[Graphical view ]
Pfami PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view ]
SMARTi SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
SM00333. TUDOR. 2 hits.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 124 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