Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lysine-specific demethylase 2A

Gene

KDM2A

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-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.2 Publications

Catalytic activityi

Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2.1 Publication
Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.1 Publication

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei209SubstrateBy similarity1
Metal bindingi212Iron; catalyticCurated1
Metal bindingi214Iron; catalyticPROSITE-ProRule annotation1
Binding sitei229SubstrateBy similarity1
Metal bindingi284Iron; catalyticPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri564 – 610CXXC-typePROSITE-ProRule annotationAdd BLAST47
Zinc fingeri617 – 678PHD-typePROSITE-ProRule annotationAdd BLAST62

GO - Molecular functioni

GO - Biological processi

  • double-strand break repair via nonhomologous end joining Source: UniProtKB
  • histone H3-K36 demethylation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS10620-MONOMER.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
SIGNORiQ9Y2K7.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:KDM2A
Synonyms:CXXC8, FBL7, FBXL11, JHDM1A, KIAA1004
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:13606. KDM2A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi212H → A: Abolishes histone demethylase activity. 1 Publication1
Mutagenesisi571C → A: Abolishes association with centromeric heterochromatin; when associated with A-574 and A-577. 1 Publication1
Mutagenesisi574C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-577. 1 Publication1
Mutagenesisi577C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-574. 1 Publication1

Organism-specific databases

DisGeNETi22992.
OpenTargetsiENSG00000173120.
PharmGKBiPA164721195.

Chemistry databases

ChEMBLiCHEMBL1938210.
GuidetoPHARMACOLOGYi2671.

Polymorphism and mutation databases

BioMutaiKDM2A.
DMDMi38257795.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001198551 – 1162Lysine-specific demethylase 2AAdd BLAST1162

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28PhosphoserineCombined sources1
Modified residuei390PhosphoserineCombined sources1
Modified residuei394PhosphoserineCombined sources1
Modified residuei550PhosphothreonineCombined sources1
Modified residuei558PhosphoserineCombined sources1
Modified residuei632PhosphothreonineCombined sources1
Modified residuei692PhosphoserineCombined sources1
Modified residuei713PhosphothreonineCombined sources1
Modified residuei718PhosphoserineBy similarity1
Modified residuei731PhosphoserineCombined sources1
Modified residuei825PhosphoserineCombined sources1
Modified residuei832PhosphoserineCombined sources1
Modified residuei869PhosphoserineCombined sources1
Modified residuei883PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y2K7.
PaxDbiQ9Y2K7.
PeptideAtlasiQ9Y2K7.
PRIDEiQ9Y2K7.

PTM databases

iPTMnetiQ9Y2K7.
PhosphoSitePlusiQ9Y2K7.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in brain, testis and ovary, followed by lung.1 Publication

Gene expression databases

BgeeiENSG00000173120.
CleanExiHS_FBXL11.
ExpressionAtlasiQ9Y2K7. baseline and differential.
GenevisibleiQ9Y2K7. HS.

Organism-specific databases

HPAiCAB012272.
HPA042975.
HPA044251.

Interactioni

Subunit structurei

Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By similarity). Interacts with CBX5/HP1A; the interaction promotes CBX5 localization to chromatin.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SKP1P632082EBI-765758,EBI-307486

Protein-protein interaction databases

BioGridi116639. 33 interactors.
DIPiDIP-34596N.
IntActiQ9Y2K7. 18 interactors.
MINTiMINT-1185543.
STRINGi9606.ENSP00000432786.

Chemistry databases

BindingDBiQ9Y2K7.

Structurei

Secondary structure

11162
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Helixi40 – 45Combined sources6
Helixi59 – 61Combined sources3
Helixi64 – 70Combined sources7
Beta strandi76 – 80Combined sources5
Turni82 – 85Combined sources4
Helixi95 – 101Combined sources7
Helixi123 – 130Combined sources8
Turni134 – 136Combined sources3
Beta strandi141 – 146Combined sources6
Helixi154 – 156Combined sources3
Helixi161 – 166Combined sources6
Helixi168 – 172Combined sources5
Helixi175 – 177Combined sources3
Beta strandi199 – 203Combined sources5
Beta strandi208 – 212Combined sources5
Helixi215 – 217Combined sources3
Beta strandi219 – 227Combined sources9
Beta strandi229 – 234Combined sources6
Helixi238 – 249Combined sources12
Beta strandi254 – 256Combined sources3
Helixi258 – 261Combined sources4
Beta strandi266 – 270Combined sources5
Beta strandi275 – 278Combined sources4
Beta strandi283 – 287Combined sources5
Beta strandi292 – 299Combined sources8
Beta strandi302 – 304Combined sources3
Helixi305 – 317Combined sources13
Helixi329 – 345Combined sources17
Helixi352 – 362Combined sources11
Helixi455 – 469Combined sources15
Helixi473 – 475Combined sources3
Beta strandi480 – 483Combined sources4
Helixi485 – 498Combined sources14
Beta strandi499 – 501Combined sources3
Helixi504 – 507Combined sources4
Helixi575 – 578Combined sources4
Helixi586 – 590Combined sources5
Helixi592 – 594Combined sources3
Helixi605 – 607Combined sources3
Turni621 – 623Combined sources3
Helixi629 – 632Combined sources4
Helixi635 – 637Combined sources3
Beta strandi640 – 642Combined sources3
Turni643 – 645Combined sources3
Helixi651 – 653Combined sources3
Beta strandi664 – 671Combined sources8
Turni673 – 675Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YU1X-ray2.70A1-517[»]
2YU2X-ray2.70A1-517[»]
4BBQX-ray2.24A/B567-681[»]
ProteinModelPortaliQ9Y2K7.
SMRiQ9Y2K7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y2K7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini148 – 316JmjCPROSITE-ProRule annotationAdd BLAST169
Domaini889 – 936F-boxAdd BLAST48
Repeati961 – 982LRR 1Add BLAST22
Repeati984 – 1010LRR 2Add BLAST27
Repeati1048 – 1073LRR 3Add BLAST26
Repeati1074 – 1103LRR 4Add BLAST30
Repeati1104 – 1128LRR 5Add BLAST25
Repeati1129 – 1156LRR 6Add BLAST28

Domaini

The JmjC domain mediates demethylation activity and is required for satellite silencing.
The CXXC zinc finger preferentially recognizes nonmethylated CpG DNA, and binding is blocked when the CpG DNA is methylated.

Sequence similaritiesi

Belongs to the JHDM1 histone demethylase family.Curated
Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
Contains 1 F-box domain.Curated
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 6 LRR (leucine-rich) repeats.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri564 – 610CXXC-typePROSITE-ProRule annotationAdd BLAST47
Zinc fingeri617 – 678PHD-typePROSITE-ProRule annotationAdd BLAST62

Keywords - Domaini

Leucine-rich repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1633. Eukaryota.
KOG1947. Eukaryota.
ENOG410XQXU. LUCA.
GeneTreeiENSGT00550000074396.
HOGENOMiHOG000007396.
InParanoidiQ9Y2K7.
KOiK10276.
OMAiMECSECA.
OrthoDBiEOG091G00M1.
PhylomeDBiQ9Y2K7.
TreeFamiTF106480.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR003347. JmjC_dom.
IPR032675. L_dom-like.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
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]
PfamiPF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF16866. PHD_4. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00367. LRR_CC. 3 hits.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51184. JMJC. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2K7-1) [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
MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLHTNKYN
60 70 80 90 100
ANFVTFMEGK DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM
110 120 130 140 150
CVGSRRMVDV MDVNTQKGIE MTMAQWTRYY ETPEEEREKL YNVISLEFSH
160 170 180 190 200
TRLENMVQRP STVDFIDWVD NMWPRHLKES QTESTNAILE MQYPKVQKYC
210 220 230 240 250
LMSVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN LELYENWLLS
260 270 280 290 300
GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL
310 320 330 340 350
HSFNIPMQLK IYNIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL
360 370 380 390 400
TKEFQKESLS MDLELNGLES GNGDEEAVDR EPRRLSSRRS VLTSPVANGV
410 420 430 440 450
NLDYDGLGKT CRSLPSLKKT LAGDSSSDCS RGSHNGQVWD PQCAPRKDRQ
460 470 480 490 500
VHLTHFELEG LRCLVDKLES LPLHKKCVPT GIEDEDALIA DVKILLEELA
510 520 530 540 550
NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP HTMKPAPRLT
560 570 580 590 600
PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM
610 620 630 640 650
KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH
660 670 680 690 700
PGCLQMDGEG LLNEELPNCW ECPKCYQEDS SEKAQKRKME ESDEEAVQAK
710 720 730 740 750
VLRPLRSCDE PLTPPPHSPT SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS
760 770 780 790 800
ASRDERFKRR QLLRLQATER TMVREKENNP SGKKELSEVE KAKIRGSYLT
810 820 830 840 850
VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC PARTPQRGDE
860 870 880 890 900
EGLGGEEEEE EEEEEEDDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS
910 920 930 940 950
VFRYLSRREL CECMRVCKTW YKWCCDKRLW TKIDLSRCKA IVPQALSGII
960 970 980 990 1000
KRQPVSLDLS WTNISKKQLT WLVNRLPGLK DLLLAGCSWS AVSALSTSSC
1010 1020 1030 1040 1050
PLLRTLDLRW AVGIKDPQIR DLLTPPADKP GQDNRSKLRN MTDFRLAGLD
1060 1070 1080 1090 1100
ITDATLRLII RHMPLLSRLD LSHCSHLTDQ SSNLLTAVGS STRYSLTELN
1110 1120 1130 1140 1150
MAGCNKLTDQ TLIYLRRIAN VTLIDLRGCK QITRKACEHF ISDLSINSLY
1160
CLSDEKLIQK IS
Length:1,162
Mass (Da):132,793
Last modified:November 7, 2003 - v3
Checksum:i88620A363A5C5842
GO
Isoform 2 (identifier: Q9Y2K7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-306: Missing.

Note: No experimental confirmation available.
Show »
Length:856
Mass (Da):96,859
Checksum:iC1351A450B4482E0
GO
Isoform 4 (identifier: Q9Y2K7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-542: Missing.

Show »
Length:620
Mass (Da):69,898
Checksum:i48020F8357601D46
GO
Isoform 5 (identifier: Q9Y2K7-5) [UniParc]FASTAAdd to basket

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

Show »
Length:723
Mass (Da):81,678
Checksum:iBC40E0405B687BB9
GO
Isoform 3 (identifier: Q9Y2K7-3) [UniParc]FASTAAdd to basket

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

Show »
Length:782
Mass (Da):89,948
Checksum:i667E9A3E503C6550
GO

Sequence cautioni

The sequence AAD56012 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA76848 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB15795 differs from that shown. Reason: Frameshift at position 410.Curated
The sequence BAJ05817 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti518K → I in AAH47371 (PubMed:15489334).Curated1
Sequence conflicti657D → G in AAH47371 (PubMed:15489334).Curated1
Sequence conflicti1128Missing in AAH01203 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0469381 – 542Missing in isoform 4. 1 PublicationAdd BLAST542
Alternative sequenceiVSP_0469391 – 439Missing in isoform 5. 1 PublicationAdd BLAST439
Alternative sequenceiVSP_0174681 – 306Missing in isoform 2. 1 PublicationAdd BLAST306
Alternative sequenceiVSP_046940440 – 492DPQCA…LIADV → MCSGRFQNIQVNPDFPRGRI SNSFRRTSSTENKTKTLGKL HQEPRQLQSDGKR in isoform 5. 1 PublicationAdd BLAST53
Alternative sequenceiVSP_017469774 – 782REKENNPSG → LRQETLDKN in isoform 3. 2 Publications9
Alternative sequenceiVSP_017470783 – 1162Missing in isoform 3. 2 PublicationsAdd BLAST380

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44657.1. [Q9Y2K7-1]
CCDS58148.1. [Q9Y2K7-5]
RefSeqiNP_001243334.1. NM_001256405.1. [Q9Y2K7-5]
NP_036440.1. NM_012308.2. [Q9Y2K7-1]
XP_011543163.1. XM_011544861.1. [Q9Y2K7-2]
UniGeneiHs.124147.

Genome annotation databases

EnsembliENST00000398645; ENSP00000381640; ENSG00000173120. [Q9Y2K7-3]
ENST00000529006; ENSP00000432786; ENSG00000173120. [Q9Y2K7-1]
ENST00000530342; ENSP00000435776; ENSG00000173120. [Q9Y2K7-5]
GeneIDi22992.
KEGGihsa:22992.
UCSCiuc001ojw.4. human. [Q9Y2K7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44657.1. [Q9Y2K7-1]
CCDS58148.1. [Q9Y2K7-5]
RefSeqiNP_001243334.1. NM_001256405.1. [Q9Y2K7-5]
NP_036440.1. NM_012308.2. [Q9Y2K7-1]
XP_011543163.1. XM_011544861.1. [Q9Y2K7-2]
UniGeneiHs.124147.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YU1X-ray2.70A1-517[»]
2YU2X-ray2.70A1-517[»]
4BBQX-ray2.24A/B567-681[»]
ProteinModelPortaliQ9Y2K7.
SMRiQ9Y2K7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116639. 33 interactors.
DIPiDIP-34596N.
IntActiQ9Y2K7. 18 interactors.
MINTiMINT-1185543.
STRINGi9606.ENSP00000432786.

Chemistry databases

BindingDBiQ9Y2K7.
ChEMBLiCHEMBL1938210.
GuidetoPHARMACOLOGYi2671.

PTM databases

iPTMnetiQ9Y2K7.
PhosphoSitePlusiQ9Y2K7.

Polymorphism and mutation databases

BioMutaiKDM2A.
DMDMi38257795.

Proteomic databases

EPDiQ9Y2K7.
PaxDbiQ9Y2K7.
PeptideAtlasiQ9Y2K7.
PRIDEiQ9Y2K7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398645; ENSP00000381640; ENSG00000173120. [Q9Y2K7-3]
ENST00000529006; ENSP00000432786; ENSG00000173120. [Q9Y2K7-1]
ENST00000530342; ENSP00000435776; ENSG00000173120. [Q9Y2K7-5]
GeneIDi22992.
KEGGihsa:22992.
UCSCiuc001ojw.4. human. [Q9Y2K7-1]

Organism-specific databases

CTDi22992.
DisGeNETi22992.
GeneCardsiKDM2A.
HGNCiHGNC:13606. KDM2A.
HPAiCAB012272.
HPA042975.
HPA044251.
MIMi605657. gene.
neXtProtiNX_Q9Y2K7.
OpenTargetsiENSG00000173120.
PharmGKBiPA164721195.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1633. Eukaryota.
KOG1947. Eukaryota.
ENOG410XQXU. LUCA.
GeneTreeiENSGT00550000074396.
HOGENOMiHOG000007396.
InParanoidiQ9Y2K7.
KOiK10276.
OMAiMECSECA.
OrthoDBiEOG091G00M1.
PhylomeDBiQ9Y2K7.
TreeFamiTF106480.

Enzyme and pathway databases

BioCyciZFISH:HS10620-MONOMER.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
SIGNORiQ9Y2K7.

Miscellaneous databases

ChiTaRSiKDM2A. human.
EvolutionaryTraceiQ9Y2K7.
GeneWikiiKDM2A.
GenomeRNAii22992.
PROiQ9Y2K7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173120.
CleanExiHS_FBXL11.
ExpressionAtlasiQ9Y2K7. baseline and differential.
GenevisibleiQ9Y2K7. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR003347. JmjC_dom.
IPR032675. L_dom-like.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
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]
PfamiPF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF16866. PHD_4. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00367. LRR_CC. 3 hits.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51184. JMJC. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKDM2A_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2K7
Secondary accession number(s): D4QA03
, E9PIL6, I3VM55, Q49A21, Q4G0M3, Q69YY8, Q9BVH5, Q9H7H5, Q9UK66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: November 30, 2016
This is version 156 of the entry and version 3 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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