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Q9Y2K7

- KDM2A_HUMAN

UniProt

Q9Y2K7 - KDM2A_HUMAN

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Protein
Lysine-specific demethylase 2A
Gene
KDM2A, CXXC8, FBL7, FBXL11, JHDM1A, KIAA1004
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

Binds 1 Fe2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei209 – 2091Substrate By similarity
Metal bindingi212 – 2121Iron; catalytic Inferred
Metal bindingi214 – 2141Iron; catalytic By similarity
Binding sitei229 – 2291Substrate By similarity
Metal bindingi284 – 2841Iron; catalytic By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri564 – 61047CXXC-type
Add
BLAST
Zinc fingeri617 – 67862PHD-type
Add
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

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
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 H3K36me2.2 Publications

GO - Cellular componenti

  1. nuclear chromatin Source: Ensembl
  2. nucleolus Source: HPA
  3. nucleoplasm Source: UniProtKB-SubCell
  4. 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 2A
PRO_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

ArrayExpressiQ9Y2K7.
BgeeiQ9Y2K7.
CleanExiHS_FBXL11.
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.1 Publication

Protein-protein interaction databases

BioGridi116639. 15 interactions.
DIPiDIP-34596N.
IntActiQ9Y2K7. 10 interactions.
MINTiMINT-1185543.
STRINGi9606.ENSP00000384903.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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, 891-1145.

Miscellaneous databases

EvolutionaryTraceiQ9Y2K7.

Family & Domainsi

Domains and Repeats

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

Domaini

The JmjC domain mediates demethylation activity and is required for satellite silencing.2 Publications
The CXXC zinc finger preferentially recognizes nonmethylated CpG DNA, and binding is blocked when the CpG DNA is methylated.2 Publications

Sequence similaritiesi

Contains 1 F-box domain.
Contains 1 JmjC domain.

Keywords - Domaini

Leucine-rich repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG290496.
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

MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLHTNKYN     50
ANFVTFMEGK DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM 100
CVGSRRMVDV MDVNTQKGIE MTMAQWTRYY ETPEEEREKL YNVISLEFSH 150
TRLENMVQRP STVDFIDWVD NMWPRHLKES QTESTNAILE MQYPKVQKYC 200
LMSVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN LELYENWLLS 250
GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL 300
HSFNIPMQLK IYNIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL 350
TKEFQKESLS MDLELNGLES GNGDEEAVDR EPRRLSSRRS VLTSPVANGV 400
NLDYDGLGKT CRSLPSLKKT LAGDSSSDCS RGSHNGQVWD PQCAPRKDRQ 450
VHLTHFELEG LRCLVDKLES LPLHKKCVPT GIEDEDALIA DVKILLEELA 500
NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP HTMKPAPRLT 550
PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM 600
KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH 650
PGCLQMDGEG LLNEELPNCW ECPKCYQEDS SEKAQKRKME ESDEEAVQAK 700
VLRPLRSCDE PLTPPPHSPT SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS 750
ASRDERFKRR QLLRLQATER TMVREKENNP SGKKELSEVE KAKIRGSYLT 800
VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC PARTPQRGDE 850
EGLGGEEEEE EEEEEEDDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS 900
VFRYLSRREL CECMRVCKTW YKWCCDKRLW TKIDLSRCKA IVPQALSGII 950
KRQPVSLDLS WTNISKKQLT WLVNRLPGLK DLLLAGCSWS AVSALSTSSC 1000
PLLRTLDLRW AVGIKDPQIR DLLTPPADKP GQDNRSKLRN MTDFRLAGLD 1050
ITDATLRLII RHMPLLSRLD LSHCSHLTDQ SSNLLTAVGS STRYSLTELN 1100
MAGCNKLTDQ TLIYLRRIAN VTLIDLRGCK QITRKACEHF ISDLSINSLY 1150
CLSDEKLIQK IS 1162
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 BAB15795.1 differs from that shown. Reason: Frameshift at position 410.
The sequence AAD56012.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA76848.2 differs from that shown. Reason: Erroneous initiation.
The sequence BAJ05817.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 542542Missing in isoform 4.
VSP_046938Add
BLAST
Alternative sequencei1 – 439439Missing in isoform 5.
VSP_046939Add
BLAST
Alternative sequencei1 – 306306Missing in isoform 2.
VSP_017468Add
BLAST
Alternative sequencei440 – 49253DPQCA…LIADV → MCSGRFQNIQVNPDFPRGRI SNSFRRTSSTENKTKTLGKL HQEPRQLQSDGKR in isoform 5.
VSP_046940Add
BLAST
Alternative sequencei774 – 7829REKENNPSG → LRQETLDKN in isoform 3.
VSP_017469
Alternative sequencei783 – 1162380Missing in isoform 3.
VSP_017470Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti518 – 5181K → I in AAH47371. 1 Publication
Sequence conflicti657 – 6571D → G in AAH47371. 1 Publication
Sequence conflicti1128 – 11281Missing in AAH01203. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000308783; ENSP00000309302; ENSG00000173120. [Q9Y2K7-4]
ENST00000398645; 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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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, 891-1145.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116639. 15 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 ENST00000308783 ; ENSP00000309302 ; ENSG00000173120 . [Q9Y2K7-4 ]
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.
InParanoidi Q9Y2K7.
KOi K10276.
OMAi CEAFISE.
OrthoDBi EOG78SQH0.
PhylomeDBi Q9Y2K7.
TreeFami TF106480.

Miscellaneous databases

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

Gene expression databases

ArrayExpressi Q9Y2K7.
Bgeei Q9Y2K7.
CleanExi HS_FBXL11.
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: July 9, 2014
This is version 131 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

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