Reviewed, UniProtKB/Swiss-Prot Q9Y2K7 (KDM2A_HUMAN)

Names and origin

Protein names

Recommended name:
    Lysine-specific demethylase 2A
    EC=1.14.11.27
Alternative name(s):
    JmjC domain-containing histone demethylation protein 1A
    [Histone-H3]-lysine-36 demethylase 1A
    F-box/LRR-repeat protein 11
    F-box and leucine-rich repeat protein 11
    F-box protein FBL7
    F-box protein Lilina
    CXXC-type zinc finger protein 8

Gene names

Name:	KDM2A
Synonyms:	CXXC8, FBL7, FBXL11, JHDM1A, KIAA1004

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1162 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.9
Catalytic activity	Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2. Ref.9 Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2. Ref.9
Cofactor	Binds 1 Fe2+ ion per subunit. Ref.9
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.
Subcellular location	Nucleus › nucleoplasm. Note: Punctate expression throughout the nucleoplasm and enriched in the perinucleolar region.
Tissue specificity	Widely expressed, with highest levels in brain, testis and ovary, followed by lung. Ref.2
Domain	The JmjC domain mediates demethylation activity and is required for satellite silencing.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8 Ref.10 Ref.11 Ref.13 Ref.14
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 3 LRR (leucine-rich) repeats. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence BAB15795.1 differs from that shown. Reason: Frameshift at position 410.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Leucine-rich repeat Repeat Zinc-finger
Ligand	DNA-binding Iron Metal-binding Zinc
Molecular function	Chromatin regulator Dioxygenase Oxidoreductase Repressor
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro histone demethylase activity (H3-K36 specific) Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SKP1	P63208	1	EBI-765758,EBI-307486

Alternative products

This entry describes 3 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 3 (identifier: Q9Y2K7-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1162	1162	Lysine-specific demethylase 2A		PRO_0000119855
Regions
	Domain	148 – 316	169	JmjC
	Domain	889 – 936	48	F-box
	Repeat	1000 – 1025	26	LRR 1
	Repeat	1063 – 1091	29	LRR 2
	Repeat	1095 – 1118	24	LRR 3
	Zinc finger	564 – 610	47	CXXC-type
	Zinc finger	617 – 678	62	PHD-type
Sites
	Metal binding	212	1	Iron; catalytic Probable
	Metal binding	214	1	Iron; catalytic By similarity
	Metal binding	284	1	Iron; catalytic By similarity
	Binding site	209	1	Substrate By similarity
	Binding site	229	1	Substrate By similarity
Amino acid modifications
	Modified residue	28	1	Phosphoserine Ref.8
	Modified residue	390	1	Phosphoserine Ref.14
	Modified residue	394	1	Phosphoserine Ref.14
	Modified residue	534	1	Phosphothreonine Ref.10
	Modified residue	550	1	Phosphothreonine Ref.13 Ref.14
	Modified residue	558	1	Phosphoserine Ref.13 Ref.14
	Modified residue	632	1	Phosphothreonine Ref.11
	Modified residue	692	1	Phosphoserine Ref.14
	Modified residue	713	1	Phosphothreonine Ref.13 Ref.14
	Modified residue	718	1	Phosphoserine Ref.13 Ref.14
	Modified residue	720	1	Phosphothreonine Ref.13
	Modified residue	721	1	Phosphoserine Ref.14
	Modified residue	731	1	Phosphoserine Ref.13 Ref.14
	Modified residue	739	1	Phosphoserine Ref.13
	Modified residue	740	1	Phosphoserine Ref.13
	Modified residue	832	1	Phosphoserine Ref.14
	Modified residue	844	1	Phosphothreonine Ref.14
	Modified residue	869	1	Phosphoserine Ref.14
Natural variations
	Alternative sequence	1 – 306	306	Missing in isoform 2.		VSP_017468
	Alternative sequence	774 – 782	9	REKENNPSG → LRQETLDKN in isoform 3.		VSP_017469
	Alternative sequence	783 – 1162	380	Missing in isoform 3.		VSP_017470
Experimental info
	Mutagenesis	212	1	H → A: Abolishes histone demethylase activity. Ref.9
	Mutagenesis	571	1	C → A: Abolishes association with centromeric heterochromatin; when associated with A-574 and A-577.
	Mutagenesis	574	1	C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-577.
	Mutagenesis	577	1	C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-574.
	Sequence conflict	518	1	K → I in AAH47371. Ref.5
	Sequence conflict	657	1	D → G in AAH47371. Ref.5
	Sequence conflict	1128	1	Missing in AAH01203. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 7, 2003. Version 3. Checksum: 88620A363A5C5842	FASTA	1,162	132,793
	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
	Isoform 2. Checksum: C1351A450B4482E0	FASTA	856	96,859
	10 20 30 40 50 60 MQLKIYNIED RTRVPNKFRY PFYYEMCWYV LERYVYCITN RSHLTKEFQK ESLSMDLELN 70 80 90 100 110 120 GLESGNGDEE AVDREPRRLS SRRSVLTSPV ANGVNLDYDG LGKTCRSLPS LKKTLAGDSS 130 140 150 160 170 180 SDCSRGSHNG QVWDPQCAPR KDRQVHLTHF ELEGLRCLVD KLESLPLHKK CVPTGIEDED 190 200 210 220 230 240 ALIADVKILL EELANSDPKL ALTGVPIVQW PKRDKLKFPT RPKVRVPTIP ITKPHTMKPA 250 260 270 280 290 300 PRLTPVRPAA ASPIVSGARR RRVRCRKCKA CVQGECGVCH YCRDMKKFGG PGRMKQSCVL 310 320 330 340 350 360 RQCLAPRLPH SVTCSLCGEV DQNEETQDFE KKLMECCICN EIVHPGCLQM DGEGLLNEEL 370 380 390 400 410 420 PNCWECPKCY QEDSSEKAQK RKMEESDEEA VQAKVLRPLR SCDEPLTPPP HSPTSMLQLI 430 440 450 460 470 480 HDPVSPRGMV TRSSPGAGPS DHHSASRDER FKRRQLLRLQ ATERTMVREK ENNPSGKKEL 490 500 510 520 530 540 SEVEKAKIRG SYLTVTLQRP TKELHGTSIV PKLQAITASS ANLRHSPRVL VQHCPARTPQ 550 560 570 580 590 600 RGDEEGLGGE EEEEEEEEEE DDSAEEGGAA RLNGRGSWAQ DGDESWMQRE VWMSVFRYLS 610 620 630 640 650 660 RRELCECMRV CKTWYKWCCD KRLWTKIDLS RCKAIVPQAL SGIIKRQPVS LDLSWTNISK 670 680 690 700 710 720 KQLTWLVNRL PGLKDLLLAG CSWSAVSALS TSSCPLLRTL DLRWAVGIKD PQIRDLLTPP 730 740 750 760 770 780 ADKPGQDNRS KLRNMTDFRL AGLDITDATL RLIIRHMPLL SRLDLSHCSH LTDQSSNLLT 790 800 810 820 830 840 AVGSSTRYSL TELNMAGCNK LTDQTLIYLR RIANVTLIDL RGCKQITRKA CEHFISDLSI 850 NSLYCLSDEK LIQKIS
	Isoform 3. Checksum: 667E9A3E503C6550	FASTA	782	89,948
	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 TMVLRQETLD KN

References

	« Hide 'large scale' referencesShow '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: 10945468] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"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: 10231032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Brain.
[3]	"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: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"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: 11214971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Spleen.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Eye, Testis and Uterus.
[6]	Pagano M. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 667-1162.
[7]	"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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1134-1162. Tissue: Testis.
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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: 16362057] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF HIS-212.
[10]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-534, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, MASS SPECTROMETRY.
[12]	"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: 19001877] [Abstract] Cited for: FUNCTION, INTERACTION WITH CBX5, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-571; CYS-574 AND CYS-577.
[13]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550; SER-558; THR-713; SER-718; THR-720; SER-731; SER-739 AND SER-740, MASS SPECTROMETRY.
[14]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-394; THR-550; SER-558; SER-692; THR-713; SER-718; SER-721; SER-731; SER-832; THR-844 AND SER-869, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB023221 mRNA. Translation: BAA76848.2. Different initiation.
AK024505 mRNA. Translation: BAB15795.1. Frameshift.
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.

IPI

IPI00166009.
IPI00737083.
IPI00739880.

RefSeq

NP_036440.1.

UniGene

Hs.124147

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YU1	X-ray	2.70	A	1-517	[»]
2YU2	X-ray	2.70	A	1-517	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y2K7. 4 interactions.

PTM databases

PhosphoSite

Q9Y2K7.

Proteomic databases

PRIDE

Q9Y2K7.

Genome annotation databases

Ensembl

ENSG00000173120. Homo sapiens. [Contig view]

GeneID

22992.

KEGG

hsa:22992.

Organism-specific databases

GeneCards

GC11P066644.

H-InvDB

HIX0023005.

HGNC

HGNC:13606. KDM2A.

HPA

CAB012272.

MIM

605657. gene.

PharmGKB

PA28020.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9Y2K7.

Enzyme and pathway databases

BRENDA

1.14.11.27. 247.

Gene expression databases

ArrayExpress

Q9Y2K7.

Bgee

Q9Y2K7.

CleanEx

HS_FBXL11.

Family and domain databases

InterPro

IPR001810. F-box.
IPR013129. TF_JmjC.
IPR003347. TF_JmjC_AAH.
IPR019786. Zinc_finger_PHD-type_CS.
IPR002857. Znf_CXXC.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
[Graphical view]

Pfam

PF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]

SMART

SM00256. FBOX. 1 hit.
SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]

PROSITE

PS50181. FBOX. False negative.
PS51184. JMJC. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

43847.

SOURCE

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Entry information

Entry name

KDM2A_HUMAN

Accession

Primary (citable) accession number: Q9Y2K7
Secondary accession number(s): Q49A21 , Q4G0M3, Q69YY8, Q9BVH5, Q9H7H5, Q9UK66

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	November 7, 2003
Last modified:	June 16, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)