Q9Y2K7 (KDM2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1162 AA.
Sequence status	Complete.
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 Ref.11
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. Ref.11
Subcellular location	Nucleus › nucleoplasm. Note: Punctate expression throughout the nucleoplasm and enriched in the perinucleolar region. Specifically nucleates at CpG islands where it's presence results in chromatin depleted in H3K36me2. Ref.11 Ref.16
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. Ref.9 Ref.16 The CXXC zinc finger preferentially recognizes nonmethylated CpG DNA, and binding is blocked when the CpG DNA is methylated. Ref.9 Ref.16
Sequence similarities	Belongs to the JHDM1 histone demethylase family. Contains 1 CXXC-type zinc finger. Contains 1 F-box domain. Contains 1 JmjC domain. Contains 6 LRR (leucine-rich) repeats. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence AAD56012.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA76848.2 differs from that shown. Reason: Erroneous initiation. The sequence BAB15795.1 differs from that shown. Reason: Frameshift at position 410.

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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3-K36 demethylation Inferred from mutant phenotype Ref.16. Source: MGI regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear chromatin Inferred from electronic annotation. Source: Compara nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	histone demethylase activity (H3-K36 specific) Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW unmethylated CpG binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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

961 – 982

22

LRR 1

Repeat

984 – 1010

27

LRR 2

Repeat

1048 – 1073

26

LRR 3

Repeat

1074 – 1103

30

LRR 4

Repeat

1104 – 1128

25

LRR 5

Repeat

1129 – 1156

28

LRR 6

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 Ref.15 Ref.17 Ref.18

Modified residue

390

1

Phosphoserine Ref.14

Modified residue

394

1

Phosphoserine Ref.17

Modified residue

550

1

Phosphothreonine Ref.12 Ref.14 Ref.15 Ref.17

Modified residue

558

1

Phosphoserine Ref.12 Ref.14 Ref.17

Modified residue

632

1

Phosphothreonine Ref.10

Modified residue

692

1

Phosphoserine Ref.13 Ref.15

Modified residue

713

1

Phosphothreonine Ref.12 Ref.14

Modified residue

731

1

Phosphoserine Ref.12 Ref.14

Modified residue

832

1

Phosphoserine Ref.14

Modified residue

869

1

Phosphoserine Ref.15 Ref.17

Modified residue

883

1

Phosphoserine Ref.17

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. Ref.11

Mutagenesis

574

1

C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-577. Ref.11

Mutagenesis

577

1

C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-574. Ref.11

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1162

Helix Strand Turn

Details...

Beta strand

36 – 38

3

Helix

40 – 45

6

Helix

59 – 61

3

Helix

64 – 70

7

Beta strand

76 – 80

5

Turn

82 – 85

4

Helix

95 – 101

7

Helix

123 – 130

8

Turn

134 – 136

3

Beta strand

141 – 146

6

Helix

154 – 156

3

Helix

161 – 166

6

Helix

168 – 172

5

Helix

175 – 177

3

Beta strand

199 – 203

5

Beta strand

208 – 212

5

Helix

215 – 217

3

Beta strand

219 – 227

9

Beta strand

229 – 234

6

Helix

238 – 249

12

Beta strand

254 – 256

3

Helix

258 – 261

4

Beta strand

266 – 270

5

Beta strand

275 – 278

4

Beta strand

283 – 287

5

Beta strand

292 – 299

8

Beta strand

302 – 304

3

Helix

305 – 317

13

Helix

329 – 345

17

Helix

352 – 362

11

Helix

455 – 469

15

Helix

473 – 475

3

Beta strand

480 – 483

4

Helix

485 – 498

14

Beta strand

499 – 501

3

Helix

504 – 507

4

Helix

575 – 578

4

Helix

586 – 590

5

Helix

592 – 594

3

Helix

605 – 607

3

Turn

621 – 623

3

Helix

629 – 632

4

Helix

635 – 637

3

Beta strand

640 – 642

3

Turn

643 – 645

3

Helix

651 – 653

3

Beta strand

664 – 671

8

Turn

673 – 675

3

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 [UniParc]. 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 [UniParc]. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1134-1162. Tissue: Testis.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF HIS-212.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"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.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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, MASS SPECTROMETRY. Tissue: T-cell.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; THR-550; SER-558; THR-713; SER-731 AND SER-832, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"CpG islands recruit a histone H3 lysine 36 demethylase." Blackledge N.P., Zhou J.C., Tolstorukov M.Y., Farcas A.M., Park P.J., Klose R.J. Mol. Cell 38:179-190(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN CXXC ZINC FINGER.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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_001243334.1. NM_001256405.1.
NP_036440.1. NM_012308.2.

UniGene

Hs.124147.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9Y2K7.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34596N.

IntAct

Q9Y2K7. 7 interactions.

MINT

MINT-1185543.

STRING

9606.ENSP00000384903.

PTM databases

PhosphoSite

Q9Y2K7.

Polymorphism databases

DMDM

38257795.

Proteomic databases

PaxDb

Q9Y2K7.

PRIDE

Q9Y2K7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000398645; ENSP00000381640; ENSG00000173120.
ENST00000529006; ENSP00000432786; ENSG00000173120.

GeneID

22992.

KEGG

hsa:22992.

UCSC

uc001ojw.3. human.

Organism-specific databases

CTD

22992.

GeneCards

GC11P066888.

HGNC

HGNC:13606. KDM2A.

HPA

CAB012272.

MIM

605657. gene.

neXtProt

NX_Q9Y2K7.

PharmGKB

PA164721195.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG290496.

InParanoid

Q9Y2K7.

KO

K10276.

OMA

LERYLYC.

OrthoDB

EOG4TF0JF.

Gene expression databases

ArrayExpress

Q9Y2K7.

Bgee

Q9Y2K7.

CleanEx

HS_FBXL11.

Genevestigator

Q9Y2K7.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR001810. F-box_dom_cyclin-like.
IPR003347. JmjC_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR002857. Znf_CXXC.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[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

BindingDB

Q9Y2K7.

ChEMBL

CHEMBL1938210.

ChiTaRS

KDM2A. human.

EvolutionaryTrace

Q9Y2K7.

GenomeRNAi

22992.

NextBio

43847.

SOURCE

Search...

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:	May 1, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.