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Protein

Lysine-specific demethylase 5A

Gene

KDM5A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity).By similarity5 Publications

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi483Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi486Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi571Iron; catalyticPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri293 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1161 – 1218PHD-type 2PROSITE-ProRule annotationAdd BLAST58
Zinc fingeri1607 – 1661PHD-type 3PROSITE-ProRule annotationAdd BLAST55

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Developmental protein, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000073614-MONOMER.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
SIGNORiP29375.

Names & Taxonomyi

Protein namesi
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 namesi
Name:KDM5A
Synonyms:JARID1A, RBBP2, RBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9886. KDM5A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5927.
OpenTargetsiENSG00000073614.
PharmGKBiPA34250.

Chemistry databases

ChEMBLiCHEMBL2424504.
GuidetoPHARMACOLOGYi2680.

Polymorphism and mutation databases

BioMutaiKDM5A.
DMDMi215274124.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002005841 – 1690Lysine-specific demethylase 5AAdd BLAST1690

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei204PhosphoserineCombined sources1
Modified residuei1111PhosphoserineCombined sources1
Modified residuei1330PhosphoserineCombined sources1
Modified residuei1331PhosphoserineCombined sources1
Modified residuei1343PhosphothreonineBy similarity1
Modified residuei1345PhosphoserineBy similarity1
Modified residuei1438PhosphoserineCombined sources1
Modified residuei1488PhosphoserineCombined sources1
Modified residuei1595PhosphotyrosineBy similarity1
Modified residuei1598PhosphoserineCombined sources1
Modified residuei1603PhosphoserineCombined sources1
Modified residuei1666PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP29375.
MaxQBiP29375.
PaxDbiP29375.
PeptideAtlasiP29375.
PRIDEiP29375.

PTM databases

iPTMnetiP29375.
PhosphoSitePlusiP29375.
SwissPalmiP29375.

Expressioni

Gene expression databases

BgeeiENSG00000073614.
CleanExiHS_JARID1A.
HS_RBP2.
ExpressionAtlasiP29375. baseline and differential.
GenevisibleiP29375. HS.

Organism-specific databases

HPAiHPA006201.

Interactioni

Subunit structurei

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. Interacts with HDAC1 (By similarity). Interacts with ARNTL/BMAL1 and CLOCK.By similarity7 Publications

Protein-protein interaction databases

BioGridi111862. 27 interactors.
DIPiDIP-472N.
IntActiP29375. 10 interactors.
STRINGi9606.ENSP00000382688.

Chemistry databases

BindingDBiP29375.

Structurei

Secondary structure

11690
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 30Combined sources3
Helixi32 – 43Combined sources12
Turni44 – 46Combined sources3
Beta strandi47 – 51Combined sources5
Turni65 – 67Combined sources3
Beta strandi73 – 76Combined sources4
Turni77 – 80Combined sources4
Helixi81 – 83Combined sources3
Helixi85 – 100Combined sources16
Helixi117 – 126Combined sources10
Helixi130 – 135Combined sources6
Helixi139 – 145Combined sources7
Helixi154 – 173Combined sources20
Beta strandi174 – 176Combined sources3
Turni350 – 353Combined sources4
Helixi363 – 378Combined sources16
Helixi382 – 384Combined sources3
Helixi387 – 399Combined sources13
Beta strandi401 – 403Combined sources3
Beta strandi406 – 414Combined sources9
Helixi415 – 418Combined sources4
Beta strandi427 – 429Combined sources3
Helixi433 – 435Combined sources3
Helixi436 – 439Combined sources4
Helixi445 – 447Combined sources3
Helixi448 – 450Combined sources3
Helixi455 – 459Combined sources5
Beta strandi470 – 474Combined sources5
Beta strandi479 – 483Combined sources5
Helixi486 – 488Combined sources3
Beta strandi490 – 499Combined sources10
Beta strandi501 – 506Combined sources6
Helixi508 – 510Combined sources3
Helixi511 – 521Combined sources11
Helixi524 – 526Combined sources3
Helixi531 – 534Combined sources4
Helixi542 – 547Combined sources6
Beta strandi553 – 557Combined sources5
Beta strandi562 – 565Combined sources4
Beta strandi570 – 586Combined sources17
Helixi589 – 591Combined sources3
Helixi592 – 604Combined sources13
Helixi613 – 621Combined sources9
Helixi629 – 655Combined sources27
Beta strandi661 – 663Combined sources3
Helixi666 – 668Combined sources3
Helixi671 – 673Combined sources3
Beta strandi685 – 688Combined sources4
Beta strandi693 – 695Combined sources3
Helixi703 – 705Combined sources3
Beta strandi711 – 713Combined sources3
Beta strandi716 – 720Combined sources5
Helixi724 – 743Combined sources20
Helixi766 – 772Combined sources7
Helixi779 – 784Combined sources6
Beta strandi1620 – 1627Combined sources8
Beta strandi1629 – 1632Combined sources4
Beta strandi1635 – 1637Combined sources3
Helixi1639 – 1641Combined sources3
Helixi1645 – 1650Combined sources6
Turni1656 – 1658Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JXJNMR-A85-175[»]
2KGGNMR-A1609-1659[»]
2KGINMR-A1609-1659[»]
3GL6X-ray1.90A1609-1659[»]
5C11X-ray2.80A1609-1659[»]
5CEHX-ray3.14A12-797[»]
5E6HX-ray2.24A1-588[»]
5ISLX-ray1.69A1-588[»]
5IVBX-ray1.39A1-588[»]
5IVCX-ray1.57A1-588[»]
5IVEX-ray1.78A1-588[»]
5IVFX-ray1.68A1-588[»]
5IVJX-ray1.57A1-588[»]
5IVVX-ray1.85A1-588[»]
5IVYX-ray1.45A1-588[»]
5IW0X-ray1.63A1-588[»]
5IWFX-ray2.29A1-588[»]
5K4LX-ray3.18A/B12-797[»]
DisProtiDP00713.
ProteinModelPortaliP29375.
SMRiP29375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29375.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 60JmjNPROSITE-ProRule annotationAdd BLAST42
Domaini84 – 174ARIDPROSITE-ProRule annotationAdd BLAST91
Domaini437 – 603JmjCPROSITE-ProRule annotationAdd BLAST167

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1623 – 1690Interaction with LMO21 PublicationAdd BLAST68

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi419 – 423GSGFP motifBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1492 – 1587Lys-richAdd BLAST96

Domaini

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

Sequence similaritiesi

Belongs to the JARID1 histone demethylase family.Curated
Contains 1 ARID domain.PROSITE-ProRule annotation
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation
Contains 3 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri293 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1161 – 1218PHD-type 2PROSITE-ProRule annotationAdd BLAST58
Zinc fingeri1607 – 1661PHD-type 3PROSITE-ProRule annotationAdd BLAST55

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1246. Eukaryota.
ENOG410XR9J. LUCA.
GeneTreeiENSGT00530000063118.
HOGENOMiHOG000290719.
InParanoidiP29375.
KOiK11446.
PhylomeDBiP29375.
TreeFamiTF106476.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
3.30.40.10. 3 hits.
InterProiIPR001606. ARID_dom.
IPR003347. JmjC_dom.
IPR003349. JmjN.
IPR013637. Lys_sp_deMease-like_dom.
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]
PfamiPF01388. 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]
SMARTiSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 3 hits.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
SSF57903. SSF57903. 3 hits.
PROSITEiPS51011. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P29375-1) [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

        10         20         30         40         50
MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK
60 70 80 90 100
IRPPKDWQPP FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL
110 120 130 140 150
QGSTLKIPVV ERKILDLYAL SKIVASKGGF EMVTKEKKWS KVGSRLGYLP
160 170 180 190 200
GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPNLDLKE KVEPEVLSTD
210 220 230 240 250
TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ IFGAGPKVVG
260 270 280 290 300
LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG
310 320 330 340 350
RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE
360 370 380 390 400
AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS
410 420 430 440 450
IEEDVIVEYG ADISSKDFGS GFPVKDGRRK ILPEEEEYAL SGWNLNNMPV
460 470 480 490 500
LEQSVLAHIN VDISGMKVPW LYVGMCFSSF CWHIEDHWSY SINYLHWGEP
510 520 530 540 550
KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM NPNVLMEHGV
560 570 580 590 600
PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN
610 620 630 640 650
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR
660 670 680 690 700
ESVVQMGVLM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL
710 720 730 740 750
YHPTDLCPCP MQKKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL
760 770 780 790 800
SANFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCASVAQL
810 820 830 840 850
LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI SQARQVKNLL
860 870 880 890 900
DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ
910 920 930 940 950
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT
960 970 980 990 1000
VSERWEEKAK VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK
1010 1020 1030 1040 1050
AREWTAKVEA IQSGSNYAYL EQLESLSAKG RPIPVRLEAL PQVESQVAAA
1060 1070 1080 1090 1100
RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKELIEKE
1110 1120 1130 1140 1150
KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA MHSLRAANLA
1160 1170 1180 1190 1200
KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG
1210 1220 1230 1240 1250
SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT
1260 1270 1280 1290 1300
ERAMSWQDRA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL
1310 1320 1330 1340 1350
QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPRQTMDYDD EETDSDEDIR
1360 1370 1380 1390 1400
ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH
1410 1420 1430 1440 1450
AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM
1460 1470 1480 1490 1500
VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD
1510 1520 1530 1540 1550
SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK
1560 1570 1580 1590 1600
LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA
1610 1620 1630 1640 1650
EESDDENAVC AAQNCQRPCK DKVDWVQCDG GCDEWFHQVC VGVSPEMAEN
1660 1670 1680 1690
EDYICINCAK KQGPVSPGPA PPPSFIMSYK LPMEDLKETS
Length:1,690
Mass (Da):192,095
Last modified:November 25, 2008 - v3
Checksum:iFCF6DC22DEF001DF
GO
Isoform 2 (identifier: P29375-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,636
Mass (Da):186,289
Checksum:iF308F907C2F899E0
GO

Sequence cautioni

The sequence AAB28544 differs from that shown. Reason: Frameshift at several positions.Curated
The sequence BAE06081 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1411Q → QVFFGK in AAB28544 (PubMed:8414517).Curated1
Sequence conflicti1547E → K in AAB28544 (PubMed:8414517).Curated1
Sequence conflicti1612 – 1614AQN → EPD in AAB28544 (PubMed:8414517).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032984865M → T.Corresponds to variant rs11062385dbSNPEnsembl.1
Natural variantiVAR_0329851190P → A.Corresponds to variant rs2229353dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0357461623 – 1690VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2. 1 PublicationAdd BLAST68

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41736.1. [P29375-1]
PIRiI78879.
RefSeqiNP_001036068.1. NM_001042603.2. [P29375-1]
UniGeneiHs.76272.

Genome annotation databases

EnsembliENST00000399788; ENSP00000382688; ENSG00000073614. [P29375-1]
GeneIDi5927.
KEGGihsa:5927.
UCSCiuc001qif.3. human. [P29375-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41736.1. [P29375-1]
PIRiI78879.
RefSeqiNP_001036068.1. NM_001042603.2. [P29375-1]
UniGeneiHs.76272.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JXJNMR-A85-175[»]
2KGGNMR-A1609-1659[»]
2KGINMR-A1609-1659[»]
3GL6X-ray1.90A1609-1659[»]
5C11X-ray2.80A1609-1659[»]
5CEHX-ray3.14A12-797[»]
5E6HX-ray2.24A1-588[»]
5ISLX-ray1.69A1-588[»]
5IVBX-ray1.39A1-588[»]
5IVCX-ray1.57A1-588[»]
5IVEX-ray1.78A1-588[»]
5IVFX-ray1.68A1-588[»]
5IVJX-ray1.57A1-588[»]
5IVVX-ray1.85A1-588[»]
5IVYX-ray1.45A1-588[»]
5IW0X-ray1.63A1-588[»]
5IWFX-ray2.29A1-588[»]
5K4LX-ray3.18A/B12-797[»]
DisProtiDP00713.
ProteinModelPortaliP29375.
SMRiP29375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111862. 27 interactors.
DIPiDIP-472N.
IntActiP29375. 10 interactors.
STRINGi9606.ENSP00000382688.

Chemistry databases

BindingDBiP29375.
ChEMBLiCHEMBL2424504.
GuidetoPHARMACOLOGYi2680.

PTM databases

iPTMnetiP29375.
PhosphoSitePlusiP29375.
SwissPalmiP29375.

Polymorphism and mutation databases

BioMutaiKDM5A.
DMDMi215274124.

Proteomic databases

EPDiP29375.
MaxQBiP29375.
PaxDbiP29375.
PeptideAtlasiP29375.
PRIDEiP29375.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000399788; ENSP00000382688; ENSG00000073614. [P29375-1]
GeneIDi5927.
KEGGihsa:5927.
UCSCiuc001qif.3. human. [P29375-1]

Organism-specific databases

CTDi5927.
DisGeNETi5927.
GeneCardsiKDM5A.
H-InvDBHIX0010308.
HGNCiHGNC:9886. KDM5A.
HPAiHPA006201.
MIMi180202. gene.
neXtProtiNX_P29375.
OpenTargetsiENSG00000073614.
PharmGKBiPA34250.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1246. Eukaryota.
ENOG410XR9J. LUCA.
GeneTreeiENSGT00530000063118.
HOGENOMiHOG000290719.
InParanoidiP29375.
KOiK11446.
PhylomeDBiP29375.
TreeFamiTF106476.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000073614-MONOMER.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
SIGNORiP29375.

Miscellaneous databases

ChiTaRSiKDM5A. human.
EvolutionaryTraceiP29375.
GeneWikiiJARID1A.
GenomeRNAii5927.
PROiP29375.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000073614.
CleanExiHS_JARID1A.
HS_RBP2.
ExpressionAtlasiP29375. baseline and differential.
GenevisibleiP29375. HS.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
3.30.40.10. 3 hits.
InterProiIPR001606. ARID_dom.
IPR003347. JmjC_dom.
IPR003349. JmjN.
IPR013637. Lys_sp_deMease-like_dom.
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]
PfamiPF01388. 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]
SMARTiSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 3 hits.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
SSF57903. SSF57903. 3 hits.
PROSITEiPS51011. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiKDM5A_HUMAN
AccessioniPrimary (citable) accession number: P29375
Secondary accession number(s): A8MV76, Q4LE72, Q86XZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 171 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.