Reviewed, UniProtKB/Swiss-Prot P29375 (KDM5A_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1690 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.10 Ref.12 Ref.13 Ref.14
Cofactor	Fe2+ By similarity.
Subunit structure	Interacts with the viral protein-binding domain of RB1. Interacts with ESR1, MYC, MYCN and LMO2. Ref.8 Ref.10 Ref.1 Ref.6 Ref.7 Ref.15
Subcellular location	Nucleus › nucleolus. Ref.10 Ref.6
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Iron Metal-binding Zinc
Molecular function	Chromatin regulator Developmental protein Dioxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription Ref.8 Inferred from direct assay. Source: GDB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.5 Traceable author statement. Source: ProtInc transcription activator activity Ref.8 Inferred from direct assay. Source: GDB transcription factor activity Ref.1 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1690	1690	Lysine-specific demethylase 5A		PRO_0000200584
Regions
	Domain	19 – 60	42	JmjN
	Domain	84 – 174	91	ARID
	Domain	437 – 603	167	JmjC
	Zinc finger	293 – 343	51	PHD-type 1
	Zinc finger	1161 – 1218	58	PHD-type 2
	Zinc finger	1607 – 1661	55	PHD-type 3
	Region	1623 – 1690	68	Interaction with LMO2
	Compositional bias	1492 – 1587	96	Lys-rich
Amino acid modifications
	Modified residue	1111	1	Phosphoserine Ref.11 Ref.16
	Modified residue	1331	1	Phosphoserine Ref.16 Ref.9
	Modified residue	1598	1	Phosphoserine Ref.11
	Modified residue	1603	1	Phosphoserine Ref.11
	Modified residue	1666	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	1623 – 1690	68	VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2.		VSP_035746
	Natural variant	865	1	M → T: dbSNP rs11062385.		VAR_032984
	Natural variant	1190	1	P → A: dbSNP rs2229353.		VAR_032985
Experimental info
	Sequence conflict	1411	1	Q → QVFFGK in AAB28544. Ref.1
	Sequence conflict	1547	1	E → K in AAB28544. Ref.1
	Sequence conflict	1612 – 1614	3	AQN → EPD in AAB28544. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: FCF6DC22DEF001DF	FASTA	1,690	192,095
	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
	Isoform 2. Checksum: F308F907C2F899E0	FASTA	1,636	186,289
	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 DKGVVFVTEE ERDKKY

References

	« Hide 'large scale' referencesShow '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: 8414517] [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. , 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: 16541075] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1099 (ISOFORM 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: 1857421] [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: 7935440] [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: 9129143] [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: 11358960] [Abstract] Cited for: FUNCTION, INTERACTION WITH ESR1.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1331 AND SER-1666, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"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: 15949438] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RB1, FUNCTION.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111; SER-1598 AND SER-1603, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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: 17320163] [Abstract] Cited for: FUNCTION.
[13]	"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: 17320161] [Abstract] Cited for: FUNCTION.
[14]	"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: 17320160] [Abstract] Cited for: FUNCTION.
[15]	"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: 17311883] [Abstract] Cited for: INTERACTION WITH MYC AND MYCN.
[16]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111 AND SER-1331, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00619935.
IPI00872073.

PIR

I78879.

RefSeq

NP_001036068.1.
NP_005047.2.

UniGene

Hs.76272

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JXJ	NMR	-	A	85-175	[»]
2KGG	NMR	-	A	1609-1659	[»]
2KGI	NMR	-	A	1609-1659	[»]
3GL6	X-ray	1.90	A	1609-1659	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:472N.

PTM databases

PhosphoSite

P29375.

Proteomic databases

PRIDE

P29375.

Genome annotation databases

Ensembl

ENSG00000073614. Homo sapiens. [Contig view]

GeneID

5927.

KEGG

hsa:5927.

Organism-specific databases

GeneCards

GC12M000263.

H-InvDB

HIX0010308.

HGNC

HGNC:9886. KDM5A.

HPA

HPA006201.

MIM

180202. gene.

PharmGKB

PA34250.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P29375.

Gene expression databases

ArrayExpress

P29375.

Bgee

P29375.

CleanEx

HS_JARID1A.
HS_RBP2.

GermOnline

ENSG00000073614. Homo sapiens.

Family and domain databases

InterPro

IPR001606. ARID.
IPR013637. PLU-1.
IPR013129. TF_JmjC.
IPR003347. TF_JmjC_AAH.
IPR003349. TF_JmjN.
IPR019786. Zinc_finger_PHD-type_CS.
IPR004198. Znf_C5HC2.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
[Graphical view]

Gene3D

G3DSA:1.10.150.60. ARID. 1 hit.

Pfam

PF01388. ARID. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF00628. PHD. 3 hits.
PF08429. PLU-1. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]

SMART

SM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 3 hits.
[Graphical view]

PROSITE

PS51011. 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]

ProtoNet

Search...

Other Resources

NextBio

23088.

SOURCE

Search...

Entry information

Entry name

KDM5A_HUMAN

Accession

Primary (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:	June 16, 2009
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)