P29375 (KDM5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [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	1690 AA.
Sequence status	Complete.
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.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	Nucleus › nucleolus. 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 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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.8. Source: UniProtKB transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Inferred from direct assay PubMed 15640446. Source: GDB chromatin binding Inferred from electronic annotation. Source: Compara 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 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW 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 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

Motif

419 – 423

5

GSGFP motif

Compositional bias

1492 – 1587

96

Lys-rich

Sites

Metal binding

483

1

Iron; catalytic By similarity

Metal binding

486

1

Iron; catalytic By similarity

Metal binding

571

1

Iron; catalytic By similarity

Amino acid modifications

Modified residue

1111

1

Phosphoserine Ref.15 Ref.16 Ref.17

Modified residue

1331

1

Phosphoserine Ref.15

Modified residue

1598

1

Phosphoserine Ref.10

Modified residue

1603

1

Phosphoserine Ref.10

Modified residue

1666

1

Phosphoserine Ref.18

Natural variations

Alternative sequence

1623 – 1690

68

VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2.

VSP_035746

Natural variant

865

1

M → T.
Corresponds to variant rs11062385 [ dbSNP | Ensembl ].

VAR_032984

Natural variant

1190

1

P → A.
Corresponds to variant rs2229353 [ dbSNP | Ensembl ].

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

Secondary structure

1

.

.

.

.

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.

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.

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.

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.

.

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.

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.

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.

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1690

Helix Strand Turn

Details...

Helix

85 – 101

17

Helix

118 – 128

11

Helix

131 – 136

6

Helix

139 – 146

8

Helix

154 – 162

9

Turn

163 – 166

4

Helix

167 – 173

7

Beta strand

1620 – 1627

8

Beta strand

1629 – 1632

4

Beta strand

1635 – 1637

3

Helix

1639 – 1641

3

Helix

1645 – 1650

6

Turn

1656 – 1658

3

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 [UniParc]. 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] [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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, 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-1666, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00021363.
IPI01014284.

PIR

I78879.

RefSeq

NP_001036068.1. NM_001042603.1.

UniGene

Hs.76272.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P29375.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-472N.

IntAct

P29375. 1 interaction.

STRING

9606.ENSP00000382688.

PTM databases

PhosphoSite

P29375.

Polymorphism databases

DMDM

215274124.

Proteomic databases

PaxDb

P29375.

PRIDE

P29375.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000399788; ENSP00000382688; ENSG00000073614.

GeneID

5927.

KEGG

hsa:5927.

UCSC

uc001qif.1. human.

Organism-specific databases

CTD

5927.

GeneCards

GC12M000389.

H-InvDB

HIX0010308.

HGNC

HGNC:9886. KDM5A.

HPA

HPA006201.

MIM

180202. gene.

neXtProt

NX_P29375.

PharmGKB

PA34250.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG327026.

HOGENOM

HOG000290719.

KO

K11446.

OMA

ECSKPRE.

OrthoDB

EOG4GB758.

Gene expression databases

ArrayExpress

P29375.

Bgee

P29375.

CleanEx

HS_JARID1A.
HS_RBP2.

Genevestigator

P29375.

GermOnline

ENSG00000073614. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.60. 1 hit.
3.30.40.10. 3 hits.

InterPro

IPR001606. 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]

Pfam

PF01388. 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]

SMART

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

SUPFAM

SSF46774. ARID. 1 hit.
SSF57903. FYVE_PHD_ZnF. 3 hits.

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

ChiTaRS

KDM5A. human.

EvolutionaryTrace

P29375.

GenomeRNAi

5927.

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:	May 1, 2013
This is version 134 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.