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Q9Y2K7

- KDM2A_HUMAN

UniProt

Q9Y2K7 - KDM2A_HUMAN

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Protein

Lysine-specific demethylase 2A

Gene

KDM2A

Organism
Homo sapiens (Human)
Status
Reviewed - 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 Fe(2+) ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei209 – 2091SubstrateBy similarity
Metal bindingi212 – 2121Iron; catalyticCurated
Metal bindingi214 – 2141Iron; catalyticPROSITE-ProRule annotation
Binding sitei229 – 2291SubstrateBy similarity
Metal bindingi284 – 2841Iron; catalyticPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri564 – 61047CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri617 – 67862PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. histone demethylase activity (H3-K36 specific) Source: UniProtKB-EC
  2. unmethylated CpG binding Source: Ensembl
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. histone H3-K36 demethylation Source: MGI
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. 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

ReactomeiREACT_228178. HDMs demethylate histones.

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
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:13606. KDM2A.

Subcellular locationi

Nucleusnucleoplasm 2 Publications
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.

GO - Cellular componenti

  1. nuclear chromatin Source: Ensembl
  2. nucleolus Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi212 – 2121H → A: Abolishes histone demethylase activity. 1 Publication
Mutagenesisi571 – 5711C → A: Abolishes association with centromeric heterochromatin; when associated with A-574 and A-577. 1 Publication
Mutagenesisi574 – 5741C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-577. 1 Publication
Mutagenesisi577 – 5771C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-574. 1 Publication

Organism-specific databases

PharmGKBiPA164721195.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11621162Lysine-specific demethylase 2APRO_0000119855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Phosphoserine4 Publications
Modified residuei390 – 3901Phosphoserine1 Publication
Modified residuei394 – 3941Phosphoserine1 Publication
Modified residuei550 – 5501Phosphothreonine4 Publications
Modified residuei558 – 5581Phosphoserine3 Publications
Modified residuei632 – 6321Phosphothreonine1 Publication
Modified residuei692 – 6921Phosphoserine2 Publications
Modified residuei713 – 7131Phosphothreonine2 Publications
Modified residuei731 – 7311Phosphoserine2 Publications
Modified residuei832 – 8321Phosphoserine1 Publication
Modified residuei869 – 8691Phosphoserine2 Publications
Modified residuei883 – 8831Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y2K7.
PaxDbiQ9Y2K7.
PRIDEiQ9Y2K7.

PTM databases

PhosphoSiteiQ9Y2K7.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Y2K7.
CleanExiHS_FBXL11.
ExpressionAtlasiQ9Y2K7. baseline and differential.
GenevestigatoriQ9Y2K7.

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

Protein-protein interaction databases

BioGridi116639. 17 interactions.
DIPiDIP-34596N.
IntActiQ9Y2K7. 10 interactions.
MINTiMINT-1185543.
STRINGi9606.ENSP00000384903.

Structurei

Secondary structure

1
1162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383Combined sources
Helixi40 – 456Combined sources
Helixi59 – 613Combined sources
Helixi64 – 707Combined sources
Beta strandi76 – 805Combined sources
Turni82 – 854Combined sources
Helixi95 – 1017Combined sources
Helixi123 – 1308Combined sources
Turni134 – 1363Combined sources
Beta strandi141 – 1466Combined sources
Helixi154 – 1563Combined sources
Helixi161 – 1666Combined sources
Helixi168 – 1725Combined sources
Helixi175 – 1773Combined sources
Beta strandi199 – 2035Combined sources
Beta strandi208 – 2125Combined sources
Helixi215 – 2173Combined sources
Beta strandi219 – 2279Combined sources
Beta strandi229 – 2346Combined sources
Helixi238 – 24912Combined sources
Beta strandi254 – 2563Combined sources
Helixi258 – 2614Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi275 – 2784Combined sources
Beta strandi283 – 2875Combined sources
Beta strandi292 – 2998Combined sources
Beta strandi302 – 3043Combined sources
Helixi305 – 31713Combined sources
Helixi329 – 34517Combined sources
Helixi352 – 36211Combined sources
Helixi455 – 46915Combined sources
Helixi473 – 4753Combined sources
Beta strandi480 – 4834Combined sources
Helixi485 – 49814Combined sources
Beta strandi499 – 5013Combined sources
Helixi504 – 5074Combined sources
Helixi575 – 5784Combined sources
Helixi586 – 5905Combined sources
Helixi592 – 5943Combined sources
Helixi605 – 6073Combined sources
Turni621 – 6233Combined sources
Helixi629 – 6324Combined sources
Helixi635 – 6373Combined sources
Beta strandi640 – 6423Combined sources
Turni643 – 6453Combined sources
Helixi651 – 6533Combined sources
Beta strandi664 – 6718Combined sources
Turni673 – 6753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YU1X-ray2.70A1-517[»]
2YU2X-ray2.70A1-517[»]
4BBQX-ray2.24A/B567-681[»]
ProteinModelPortaliQ9Y2K7.
SMRiQ9Y2K7. Positions 34-364, 450-517, 567-676, 891-1140.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y2K7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini148 – 316169JmjCPROSITE-ProRule annotationAdd
BLAST
Domaini889 – 93648F-boxAdd
BLAST
Repeati961 – 98222LRR 1Add
BLAST
Repeati984 – 101027LRR 2Add
BLAST
Repeati1048 – 107326LRR 3Add
BLAST
Repeati1074 – 110330LRR 4Add
BLAST
Repeati1104 – 112825LRR 5Add
BLAST
Repeati1129 – 115628LRR 6Add
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri564 – 61047CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri617 – 67862PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Leucine-rich repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG290496.
GeneTreeiENSGT00550000074396.
InParanoidiQ9Y2K7.
KOiK10276.
OMAiCEAFISE.
OrthoDBiEOG78SQH0.
PhylomeDBiQ9Y2K7.
TreeFamiTF106480.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001810. 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]
PfamiPF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
SM00558. JmjC. 1 hit.
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. Align

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 AAD56012.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA76848.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB15795.1 differs from that shown. Reason: Frameshift at position 410. Curated
The sequence BAJ05817.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti518 – 5181K → I in AAH47371. (PubMed:15489334)Curated
Sequence conflicti657 – 6571D → G in AAH47371. (PubMed:15489334)Curated
Sequence conflicti1128 – 11281Missing in AAH01203. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 542542Missing in isoform 4. 1 PublicationVSP_046938Add
BLAST
Alternative sequencei1 – 439439Missing in isoform 5. 1 PublicationVSP_046939Add
BLAST
Alternative sequencei1 – 306306Missing in isoform 2. 1 PublicationVSP_017468Add
BLAST
Alternative sequencei440 – 49253DPQCA…LIADV → MCSGRFQNIQVNPDFPRGRI SNSFRRTSSTENKTKTLGKL HQEPRQLQSDGKR in isoform 5. 1 PublicationVSP_046940Add
BLAST
Alternative sequencei774 – 7829REKENNPSG → LRQETLDKN in isoform 3. 2 PublicationsVSP_017469
Alternative sequencei783 – 1162380Missing in isoform 3. 2 PublicationsVSP_017470Add
BLAST

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]
UniGeneiHs.124147.

Genome annotation databases

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

Polymorphism databases

DMDMi38257795.

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 .
CCDSi CCDS44657.1. [Q9Y2K7-1 ]
CCDS58148.1. [Q9Y2K7-5 ]
RefSeqi NP_001243334.1. NM_001256405.1. [Q9Y2K7-5 ]
NP_036440.1. NM_012308.2. [Q9Y2K7-1 ]
UniGenei Hs.124147.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YU1 X-ray 2.70 A 1-517 [» ]
2YU2 X-ray 2.70 A 1-517 [» ]
4BBQ X-ray 2.24 A/B 567-681 [» ]
ProteinModelPortali Q9Y2K7.
SMRi Q9Y2K7. Positions 34-364, 450-517, 567-676, 891-1140.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116639. 17 interactions.
DIPi DIP-34596N.
IntActi Q9Y2K7. 10 interactions.
MINTi MINT-1185543.
STRINGi 9606.ENSP00000384903.

Chemistry

BindingDBi Q9Y2K7.
ChEMBLi CHEMBL1938210.
GuidetoPHARMACOLOGYi 2671.

PTM databases

PhosphoSitei Q9Y2K7.

Polymorphism databases

DMDMi 38257795.

Proteomic databases

MaxQBi Q9Y2K7.
PaxDbi Q9Y2K7.
PRIDEi Q9Y2K7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398645 ; ENSP00000381640 ; ENSG00000173120 . [Q9Y2K7-3 ]
ENST00000529006 ; ENSP00000432786 ; ENSG00000173120 . [Q9Y2K7-1 ]
ENST00000530342 ; ENSP00000435776 ; ENSG00000173120 . [Q9Y2K7-5 ]
GeneIDi 22992.
KEGGi hsa:22992.
UCSCi uc001ojw.3. human. [Q9Y2K7-1 ]

Organism-specific databases

CTDi 22992.
GeneCardsi GC11P066888.
HGNCi HGNC:13606. KDM2A.
HPAi CAB012272.
HPA042975.
HPA044251.
MIMi 605657. gene.
neXtProti NX_Q9Y2K7.
PharmGKBi PA164721195.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG290496.
GeneTreei ENSGT00550000074396.
InParanoidi Q9Y2K7.
KOi K10276.
OMAi CEAFISE.
OrthoDBi EOG78SQH0.
PhylomeDBi Q9Y2K7.
TreeFami TF106480.

Enzyme and pathway databases

Reactomei REACT_228178. HDMs demethylate histones.

Miscellaneous databases

ChiTaRSi KDM2A. human.
EvolutionaryTracei Q9Y2K7.
GeneWikii KDM2A.
GenomeRNAii 22992.
NextBioi 35533673.
PROi Q9Y2K7.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y2K7.
CleanExi HS_FBXL11.
ExpressionAtlasi Q9Y2K7. baseline and differential.
Genevestigatori Q9Y2K7.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR001810. 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 ]
Pfami PF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view ]
SMARTi SM00256. FBOX. 1 hit.
SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS51184. JMJC. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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].

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 26, 2014
This is version 134 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

External Data

Dasty 3