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P29375 (KDM5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysine-specific demethylase 5A

EC=1.14.11.-
Alternative name(s):
Histone demethylase JARID1A
Jumonji/ARID domain-containing protein 1A
Retinoblastoma-binding protein 2
Short name=RBBP-2
Gene names
Name:KDM5A
Synonyms:JARID1A, RBBP2, RBP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1690 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May stimulate transcription mediated by nuclear receptors. May be involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Subunit structure

Interacts with SUZ12; the interaction is direct By similarity. Interacts with the viral protein-binding domain of RB1. Interacts with ESR1, MYC, MYCN and LMO2. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.14

Subcellular location

Nucleusnucleolus. Note: Occupies promoters of genes involved in RNA metabolism and mitochondrial function By similarity. Ref.6 Ref.9

Domain

The GSGFP motif is required for the interaction with SUZ12 By similarity.

Sequence similarities

Belongs to the JARID1 histone demethylase family.

Contains 1 ARID domain.

Contains 1 JmjC domain.

Contains 1 JmjN domain.

Contains 3 PHD-type zinc fingers.

Sequence caution

The sequence AAB28544.1 differs from that shown. Reason: Frameshift at several positions.

The sequence BAE06081.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandIron
Metal-binding
Zinc
   Molecular functionChromatin regulator
Developmental protein
Dioxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.8. Source: UniProtKB

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15640446. Source: GDB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29375-1)

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: P29375-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1623-1690: VDWVQCDGGC...LPMEDLKETS → GVVFVTEEERDKKY

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16901690Lysine-specific demethylase 5A
PRO_0000200584

Regions

Domain19 – 6042JmjN
Domain84 – 17491ARID
Domain437 – 603167JmjC
Zinc finger293 – 34351PHD-type 1
Zinc finger1161 – 121858PHD-type 2
Zinc finger1607 – 166155PHD-type 3
Region1623 – 169068Interaction with LMO2
Motif419 – 4235GSGFP motif
Compositional bias1492 – 158796Lys-rich

Sites

Metal binding4831Iron; catalytic By similarity
Metal binding4861Iron; catalytic By similarity
Metal binding5711Iron; catalytic By similarity

Amino acid modifications

Modified residue11111Phosphoserine Ref.15 Ref.16 Ref.17
Modified residue13311Phosphoserine Ref.15
Modified residue15981Phosphoserine Ref.10
Modified residue16031Phosphoserine Ref.10
Modified residue16661Phosphoserine Ref.18

Natural variations

Alternative sequence1623 – 169068VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2.
VSP_035746
Natural variant8651M → T.
Corresponds to variant rs11062385 [ dbSNP | Ensembl ].
VAR_032984
Natural variant11901P → A.
Corresponds to variant rs2229353 [ dbSNP | Ensembl ].
VAR_032985

Experimental info

Sequence conflict14111Q → QVFFGK in AAB28544. Ref.1
Sequence conflict15471E → K in AAB28544. Ref.1
Sequence conflict1612 – 16143AQN → EPD in AAB28544. Ref.1

Secondary structure

......................... 1690
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: FCF6DC22DEF001DF

FASTA1,690192,095
        10         20         30         40         50         60 
MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK IRPPKDWQPP 

        70         80         90        100        110        120 
FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL QGSTLKIPVV ERKILDLYAL 

       130        140        150        160        170        180 
SKIVASKGGF EMVTKEKKWS KVGSRLGYLP GKGTGSLLKS HYERILYPYE LFQSGVSLMG 

       190        200        210        220        230        240 
VQMPNLDLKE KVEPEVLSTD TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ 

       250        260        270        280        290        300 
IFGAGPKVVG LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG 

       310        320        330        340        350        360 
RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE AFGFEQAVRE 

       370        380        390        400        410        420 
YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS IEEDVIVEYG ADISSKDFGS 

       430        440        450        460        470        480 
GFPVKDGRRK ILPEEEEYAL SGWNLNNMPV LEQSVLAHIN VDISGMKVPW LYVGMCFSSF 

       490        500        510        520        530        540 
CWHIEDHWSY SINYLHWGEP KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM 

       550        560        570        580        590        600 
NPNVLMEHGV PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN 

       610        620        630        640        650        660 
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR ESVVQMGVLM 

       670        680        690        700        710        720 
SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL YHPTDLCPCP MQKKCLRYRY 

       730        740        750        760        770        780 
PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL SANFNHKKDL IELRVMLEDA EDRKYPENDL 

       790        800        810        820        830        840 
FRKLRDAVKE AETCASVAQL LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI 

       850        860        870        880        890        900 
SQARQVKNLL DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ 

       910        920        930        940        950        960 
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT VSERWEEKAK 

       970        980        990       1000       1010       1020 
VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK AREWTAKVEA IQSGSNYAYL 

      1030       1040       1050       1060       1070       1080 
EQLESLSAKG RPIPVRLEAL PQVESQVAAA RAWRERTGRT FLKKNSSHTL LQVLSPRTDI 

      1090       1100       1110       1120       1130       1140 
GVYGSGKNRR KKVKELIEKE KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA 

      1150       1160       1170       1180       1190       1200 
MHSLRAANLA KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG 

      1210       1220       1230       1240       1250       1260 
SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT ERAMSWQDRA 

      1270       1280       1290       1300       1310       1320 
RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL QKAAANPDLQ GHLPSFQQSA 

      1330       1340       1350       1360       1370       1380 
FNRVVSSVSS SPRQTMDYDD EETDSDEDIR ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP 

      1390       1400       1410       1420       1430       1440 
IKSEEVVTHM WTAPSFCAEH AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG 

      1450       1460       1470       1480       1490       1500 
AKAQLEELMM VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD 

      1510       1520       1530       1540       1550       1560 
SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK LAKKLAKEEE 

      1570       1580       1590       1600       1610       1620 
RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA EESDDENAVC AAQNCQRPCK 

      1630       1640       1650       1660       1670       1680 
DKVDWVQCDG GCDEWFHQVC VGVSPEMAEN EDYICINCAK KQGPVSPGPA PPPSFIMSYK 

      1690 
LPMEDLKETS 

« Hide

Isoform 2 [UniParc].

Checksum: F308F907C2F899E0
Show »

FASTA1,636186,289

References

« Hide 'large scale' references
[1]"Characterization of the retinoblastoma binding proteins RBP1 and RBP2."
Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E., Vuocolo G.A., Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D., Jones R.E.
Oncogene 8:3149-3156(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH RB1.
[2]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] OF 1-1099 (ISOFORMS 1/2).
Tissue: Eye and Testis.
[5]"Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product."
Defeo-Jones D., Huang P.S., Jones R.E., Haskell K.M., Vuocolo G.A., Hanobik M.G., Huber H.E., Oliff A.
Nature 352:251-254(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1102-1564.
[6]"Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein."
Kim Y.W., Otterson G.A., Kratzke R.A., Coxon A.B., Kaye F.J.
Mol. Cell. Biol. 14:7256-7264(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RB1, SUBCELLULAR LOCATION.
[7]"T-cell oncogene rhombotin-2 interacts with retinoblastoma-binding protein 2."
Mao S., Neale G.A.M., Goorha R.M.
Oncogene 14:1531-1539(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LMO2.
[8]"Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription."
Chan S.W., Hong W.
J. Biol. Chem. 276:28402-28412(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ESR1.
[9]"Binding of pRB to the PHD protein RBP2 promotes cellular differentiation."
Benevolenskaya E.V., Murray H.L., Branton P., Young R.A., Kaelin W.G. Jr.
Mol. Cell 18:623-635(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RB1, FUNCTION.
[10]"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-1598 AND SER-1603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"The retinoblastoma binding protein RBP2 is an H3K4 demethylase."
Klose R.J., Yan Q., Tothova Z., Yamane K., Erdjument-Bromage H., Tempst P., Gilliland D.G., Zhang Y., Kaelin W.G. Jr.
Cell 128:889-900(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3."
Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S., Sennels L., Rappsilber J., Hansen K.H., Salcini A.E., Helin K.
Cell 128:1063-1076(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases."
Iwase S., Lan F., Bayliss P., de la Torre-Ubieta L., Huarte M., Qi H.H., Whetstine J.R., Bonni A., Roberts T.M., Shi Y.
Cell 128:1077-1088(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth."
Secombe J., Li L., Carlos L., Eisenman R.N.
Genes Dev. 21:537-551(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYC AND MYCN.
[15]"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-1111 AND SER-1331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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-1111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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-1111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S66431 mRNA. Translation: AAB28544.1. Frameshift.
AB209999 mRNA. Translation: BAE06081.1. Different initiation.
AC005844 Genomic DNA. No translation available.
AC007406 Genomic DNA. No translation available.
BC048307 mRNA. Translation: AAH48307.1. Different termination.
BC053893 mRNA. Translation: AAH53893.1. Different termination.
BC110916 mRNA. Translation: AAI10917.1. Different termination.
PIRI78879.
RefSeqNP_001036068.1. NM_001042603.2.
UniGeneHs.76272.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXJNMR-A85-175[»]
2KGGNMR-A1609-1659[»]
2KGINMR-A1609-1659[»]
3GL6X-ray1.90A1609-1659[»]
DisProtDP00713.
ProteinModelPortalP29375.
SMRP29375. Positions 18-176, 260-621, 1162-1217, 1608-1659.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111862. 21 interactions.
DIPDIP-472N.
IntActP29375. 2 interactions.
STRING9606.ENSP00000382688.

PTM databases

PhosphoSiteP29375.

Polymorphism databases

DMDM215274124.

Proteomic databases

PaxDbP29375.
PRIDEP29375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399788; ENSP00000382688; ENSG00000073614. [P29375-1]
GeneID5927.
KEGGhsa:5927.
UCSCuc001qif.1. human. [P29375-1]

Organism-specific databases

CTD5927.
GeneCardsGC12M000389.
H-InvDBHIX0010308.
HGNCHGNC:9886. KDM5A.
HPAHPA006201.
MIM180202. gene.
neXtProtNX_P29375.
PharmGKBPA34250.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327026.
HOGENOMHOG000290719.
KOK11446.
OMACVAHYRR.
OrthoDBEOG7D85VK.
PhylomeDBP29375.
TreeFamTF106476.

Gene expression databases

ArrayExpressP29375.
BgeeP29375.
CleanExHS_JARID1A.
HS_RBP2.
GenevestigatorP29375.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
3.30.40.10. 3 hits.
InterProIPR001606. ARID/BRIGHT_DNA-bd.
IPR003347. JmjC_dom.
IPR013637. Lys_sp_deMease_like_dom.
IPR003349. TF_JmjN.
IPR019786. Zinc_finger_PHD-type_CS.
IPR004198. Znf_C5HC2.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF01388. ARID. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF00628. PHD. 2 hits.
PF08429. PLU-1. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 3 hits.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
SSF57903. SSF57903. 3 hits.
PROSITEPS51011. ARID. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKDM5A. human.
EvolutionaryTraceP29375.
GeneWikiJARID1A.
GenomeRNAi5927.
NextBio23088.
PROP29375.
SOURCESearch...

Entry information

Entry nameKDM5A_HUMAN
AccessionPrimary (citable) accession number: P29375
Secondary accession number(s): A8MV76, Q4LE72, Q86XZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM