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Q9Y2K7 (KDM2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysine-specific demethylase 2A

EC=1.14.11.27
Alternative name(s):
CXXC-type zinc finger protein 8
F-box and leucine-rich repeat protein 11
F-box protein FBL7
F-box protein Lilina
F-box/LRR-repeat protein 11
JmjC domain-containing histone demethylation protein 1A
[Histone-H3]-lysine-36 demethylase 1A
Gene names
Name:KDM2A
Synonyms:CXXC8, FBL7, FBXL11, JHDM1A, KIAA1004
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1162 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis. Ref.12 Ref.14

Catalytic activity

Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2. Ref.12

Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2. Ref.12

Cofactor

Binds 1 Fe2+ ion per subunit. Ref.12

Subunit structure

Part of a SCF (SKP1-cullin-F-box) protein ligase complex By similarity. Interacts with CBX5/HP1A; the interaction promotes CBX5 localization to chromatin. Ref.14

Subcellular location

Nucleusnucleoplasm. Note: Punctate expression throughout the nucleoplasm and enriched in the perinucleolar region. Specifically nucleates at CpG islands where it's presence results in chromatin depleted in H3K36me2. Ref.14 Ref.19

Tissue specificity

Widely expressed, with highest levels in brain, testis and ovary, followed by lung. Ref.4

Domain

The JmjC domain mediates demethylation activity and is required for satellite silencing. Ref.12 Ref.19

The CXXC zinc finger preferentially recognizes nonmethylated CpG DNA, and binding is blocked when the CpG DNA is methylated. Ref.12 Ref.19

Sequence similarities

Belongs to the JHDM1 histone demethylase family.

Contains 1 CXXC-type zinc finger.

Contains 1 F-box domain.

Contains 1 JmjC domain.

Contains 6 LRR (leucine-rich) repeats.

Contains 1 PHD-type zinc finger.

Sequence caution

The sequence AAD56012.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA76848.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAB15795.1 differs from that shown. Reason: Frameshift at position 410.

The sequence BAJ05817.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2K7-1)

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.
Isoform 2 (identifier: Q9Y2K7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-306: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9Y2K7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-542: Missing.
Isoform 5 (identifier: Q9Y2K7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-439: Missing.
     440-492: DPQCAPRKDR...EDEDALIADV → MCSGRFQNIQ...PRQLQSDGKR
Isoform 3 (identifier: Q9Y2K7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     774-782: REKENNPSG → LRQETLDKN
     783-1162: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11621162Lysine-specific demethylase 2A
PRO_0000119855

Regions

Domain148 – 316169JmjC
Domain889 – 93648F-box
Repeat961 – 98222LRR 1
Repeat984 – 101027LRR 2
Repeat1048 – 107326LRR 3
Repeat1074 – 110330LRR 4
Repeat1104 – 112825LRR 5
Repeat1129 – 115628LRR 6
Zinc finger564 – 61047CXXC-type
Zinc finger617 – 67862PHD-type

Sites

Metal binding2121Iron; catalytic Probable
Metal binding2141Iron; catalytic By similarity
Metal binding2841Iron; catalytic By similarity
Binding site2091Substrate By similarity
Binding site2291Substrate By similarity

Amino acid modifications

Modified residue281Phosphoserine Ref.11 Ref.18 Ref.20 Ref.21
Modified residue3901Phosphoserine Ref.17
Modified residue3941Phosphoserine Ref.20
Modified residue5501Phosphothreonine Ref.15 Ref.17 Ref.18 Ref.20
Modified residue5581Phosphoserine Ref.15 Ref.17 Ref.20
Modified residue6321Phosphothreonine Ref.13
Modified residue6921Phosphoserine Ref.16 Ref.18
Modified residue7131Phosphothreonine Ref.15 Ref.17
Modified residue7311Phosphoserine Ref.15 Ref.17
Modified residue8321Phosphoserine Ref.17
Modified residue8691Phosphoserine Ref.18 Ref.20
Modified residue8831Phosphoserine Ref.20

Natural variations

Alternative sequence1 – 542542Missing in isoform 4.
VSP_046938
Alternative sequence1 – 439439Missing in isoform 5.
VSP_046939
Alternative sequence1 – 306306Missing in isoform 2.
VSP_017468
Alternative sequence440 – 49253DPQCA…LIADV → MCSGRFQNIQVNPDFPRGRI SNSFRRTSSTENKTKTLGKL HQEPRQLQSDGKR in isoform 5.
VSP_046940
Alternative sequence774 – 7829REKENNPSG → LRQETLDKN in isoform 3.
VSP_017469
Alternative sequence783 – 1162380Missing in isoform 3.
VSP_017470

Experimental info

Mutagenesis2121H → A: Abolishes histone demethylase activity. Ref.12
Mutagenesis5711C → A: Abolishes association with centromeric heterochromatin; when associated with A-574 and A-577. Ref.14
Mutagenesis5741C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-577. Ref.14
Mutagenesis5771C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-574. Ref.14
Sequence conflict5181K → I in AAH47371. Ref.8
Sequence conflict6571D → G in AAH47371. Ref.8
Sequence conflict11281Missing in AAH01203. Ref.8

Secondary structure

.............................................................................................. 1162
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 7, 2003. Version 3.
Checksum: 88620A363A5C5842

FASTA1,162132,793
        10         20         30         40         50         60 
MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLHTNKYN ANFVTFMEGK 

        70         80         90        100        110        120 
DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM CVGSRRMVDV MDVNTQKGIE 

       130        140        150        160        170        180 
MTMAQWTRYY ETPEEEREKL YNVISLEFSH TRLENMVQRP STVDFIDWVD NMWPRHLKES 

       190        200        210        220        230        240 
QTESTNAILE MQYPKVQKYC LMSVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN 

       250        260        270        280        290        300 
LELYENWLLS GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL 

       310        320        330        340        350        360 
HSFNIPMQLK IYNIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKEFQKESLS 

       370        380        390        400        410        420 
MDLELNGLES GNGDEEAVDR EPRRLSSRRS VLTSPVANGV NLDYDGLGKT CRSLPSLKKT 

       430        440        450        460        470        480 
LAGDSSSDCS RGSHNGQVWD PQCAPRKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT 

       490        500        510        520        530        540 
GIEDEDALIA DVKILLEELA NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP 

       550        560        570        580        590        600 
HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM 

       610        620        630        640        650        660 
KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG 

       670        680        690        700        710        720 
LLNEELPNCW ECPKCYQEDS SEKAQKRKME ESDEEAVQAK VLRPLRSCDE PLTPPPHSPT 

       730        740        750        760        770        780 
SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP 

       790        800        810        820        830        840 
SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC 

       850        860        870        880        890        900 
PARTPQRGDE EGLGGEEEEE EEEEEEDDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS 

       910        920        930        940        950        960 
VFRYLSRREL CECMRVCKTW YKWCCDKRLW TKIDLSRCKA IVPQALSGII KRQPVSLDLS 

       970        980        990       1000       1010       1020 
WTNISKKQLT WLVNRLPGLK DLLLAGCSWS AVSALSTSSC PLLRTLDLRW AVGIKDPQIR 

      1030       1040       1050       1060       1070       1080 
DLLTPPADKP GQDNRSKLRN MTDFRLAGLD ITDATLRLII RHMPLLSRLD LSHCSHLTDQ 

      1090       1100       1110       1120       1130       1140 
SSNLLTAVGS STRYSLTELN MAGCNKLTDQ TLIYLRRIAN VTLIDLRGCK QITRKACEHF 

      1150       1160 
ISDLSINSLY CLSDEKLIQK IS 

« Hide

Isoform 2 [UniParc].

Checksum: C1351A450B4482E0
Show »

FASTA85696,859
Isoform 4 [UniParc].

Checksum: 48020F8357601D46
Show »

FASTA62069,898
Isoform 5 [UniParc].

Checksum: BC40E0405B687BB9
Show »

FASTA72381,678
Isoform 3 [UniParc].

Checksum: 667E9A3E503C6550
Show »

FASTA78289,948

References

« Hide 'large scale' references
[1]"cDNA cloning and expression analysis of new members of the mammalian F-box protein family."
Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.
Genomics 67:40-47(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Tsuneoka M., Tanaka Y., Okamoto K., Teye K.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[3]Iuchi S., Green H.
Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
[4]"Prediction of the coding sequences of unidentified human genes. XIII. 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., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Brain.
[5]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[6]"Characterization of long cDNA clones from human adult spleen."
Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.
DNA Res. 7:357-366(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Spleen.
[7]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 1; 2 AND 3).
Tissue: Eye, Testis and Uterus.
[9]Pagano M.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 667-1162.
[10]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1134-1162.
Tissue: Testis.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Histone demethylation by a family of JmjC domain-containing proteins."
Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., Tempst P., Zhang Y.
Nature 439:811-816(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF HIS-212.
[13]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[14]"KDM2A represses transcription of centromeric satellite repeats and maintains the heterochromatic state."
Frescas D., Guardavaccaro D., Kuchay S.M., Kato H., Poleshko A., Basrur V., Elenitoba-Johnson K.S., Katz R.A., Pagano M.
Cell Cycle 7:3539-3547(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CBX5, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-571; CYS-574 AND CYS-577.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550; SER-558; THR-713 AND SER-731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; THR-550; SER-558; THR-713; SER-731 AND SER-832, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-550; SER-692 AND SER-869, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"CpG islands recruit a histone H3 lysine 36 demethylase."
Blackledge N.P., Zhou J.C., Tolstorukov M.Y., Farcas A.M., Park P.J., Klose R.J.
Mol. Cell 38:179-190(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DOMAIN CXXC ZINC-FINGER.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-394; THR-550; SER-558; SER-869 AND SER-883, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023221 mRNA. Translation: BAA76848.2. Different initiation.
AB490246 mRNA. Translation: BAJ05817.1. Different initiation.
JQ710743 mRNA. Translation: AFK81542.1.
JQ710744 mRNA. Translation: AFK81543.1.
AK024505 mRNA. Translation: BAB15795.1. Frameshift.
AP000729 Genomic DNA. No translation available.
AP001885 Genomic DNA. No translation available.
BC001203 mRNA. Translation: AAH01203.1.
BC047371 mRNA. Translation: AAH47371.1.
BC047486 mRNA. Translation: AAH47486.1.
BC064360 mRNA. Translation: AAH64360.1.
AF179221 mRNA. Translation: AAD56012.1. Different initiation.
AL117517 mRNA. Translation: CAH10721.1.
CCDSCCDS44657.1. [Q9Y2K7-1]
CCDS58148.1. [Q9Y2K7-5]
RefSeqNP_001243334.1. NM_001256405.1. [Q9Y2K7-5]
NP_036440.1. NM_012308.2. [Q9Y2K7-1]
UniGeneHs.124147.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YU1X-ray2.70A1-517[»]
2YU2X-ray2.70A1-517[»]
4BBQX-ray2.24A/B567-681[»]
ProteinModelPortalQ9Y2K7.
SMRQ9Y2K7. Positions 34-364, 450-517, 567-676, 891-1145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116639. 15 interactions.
DIPDIP-34596N.
IntActQ9Y2K7. 10 interactions.
MINTMINT-1185543.
STRING9606.ENSP00000384903.

Chemistry

BindingDBQ9Y2K7.
ChEMBLCHEMBL1938210.
GuidetoPHARMACOLOGY2671.

PTM databases

PhosphoSiteQ9Y2K7.

Polymorphism databases

DMDM38257795.

Proteomic databases

MaxQBQ9Y2K7.
PaxDbQ9Y2K7.
PRIDEQ9Y2K7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308783; ENSP00000309302; ENSG00000173120. [Q9Y2K7-4]
ENST00000398645; ENSP00000381640; ENSG00000173120. [Q9Y2K7-3]
ENST00000529006; ENSP00000432786; ENSG00000173120. [Q9Y2K7-1]
ENST00000530342; ENSP00000435776; ENSG00000173120. [Q9Y2K7-5]
GeneID22992.
KEGGhsa:22992.
UCSCuc001ojw.3. human. [Q9Y2K7-1]

Organism-specific databases

CTD22992.
GeneCardsGC11P066888.
HGNCHGNC:13606. KDM2A.
HPACAB012272.
HPA042975.
HPA044251.
MIM605657. gene.
neXtProtNX_Q9Y2K7.
PharmGKBPA164721195.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290496.
InParanoidQ9Y2K7.
KOK10276.
OMACEAFISE.
OrthoDBEOG78SQH0.
PhylomeDBQ9Y2K7.
TreeFamTF106480.

Gene expression databases

ArrayExpressQ9Y2K7.
BgeeQ9Y2K7.
CleanExHS_FBXL11.
GenevestigatorQ9Y2K7.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001810. F-box_dom.
IPR003347. JmjC_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS51184. JMJC. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKDM2A. human.
EvolutionaryTraceQ9Y2K7.
GeneWikiKDM2A.
GenomeRNAi22992.
NextBio35533673.
PROQ9Y2K7.
SOURCESearch...

Entry information

Entry nameKDM2A_HUMAN
AccessionPrimary (citable) accession number: Q9Y2K7
Secondary accession number(s): D4QA03 expand/collapse secondary AC list , E9PIL6, I3VM55, Q49A21, Q4G0M3, Q69YY8, Q9BVH5, Q9H7H5, Q9UK66
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: July 9, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM