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P29375

- KDM5A_HUMAN

UniProt

P29375 - KDM5A_HUMAN

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Protein

Lysine-specific demethylase 5A

Gene

KDM5A

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi483 – 4831Iron; catalyticPROSITE-ProRule annotation
Metal bindingi486 – 4861Iron; catalyticPROSITE-ProRule annotation
Metal bindingi571 – 5711Iron; catalyticPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri293 – 34351PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1161 – 121858PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1607 – 166155PHD-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. DNA binding Source: GDB
  3. 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 Source: InterPro
  4. sequence-specific DNA binding transcription factor activity Source: ProtInc
  5. transcription coactivator activity Source: UniProtKB
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. circadian regulation of gene expression Source: UniProtKB
  3. multicellular organismal development Source: UniProtKB-KW
  4. negative regulation of histone deacetylase activity Source: UniProtKB
  5. positive regulation of transcription, DNA-templated Source: UniProtKB
  6. transcription from RNA polymerase II promoter Source: ProtInc
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

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
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9886. KDM5A.

Subcellular locationi

Nucleusnucleolus 2 Publications. Nucleus By similarity
Note: Occupies promoters of genes involved in RNA metabolism and mitochondrial function.By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34250.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16901690Lysine-specific demethylase 5APRO_0000200584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1111 – 11111Phosphoserine3 Publications
Modified residuei1331 – 13311Phosphoserine1 Publication
Modified residuei1598 – 15981Phosphoserine1 Publication
Modified residuei1603 – 16031Phosphoserine1 Publication
Modified residuei1666 – 16661Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29375.
PaxDbiP29375.
PRIDEiP29375.

PTM databases

PhosphoSiteiP29375.

Expressioni

Gene expression databases

BgeeiP29375.
CleanExiHS_JARID1A.
HS_RBP2.
ExpressionAtlasiP29375. baseline and differential.
GenevestigatoriP29375.

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. 22 interactions.
DIPiDIP-472N.
IntActiP29375. 3 interactions.
STRINGi9606.ENSP00000382688.

Structurei

Secondary structure

1
1690
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 10117
Helixi118 – 12811
Helixi131 – 1366
Helixi139 – 1468
Helixi154 – 1629
Turni163 – 1664
Helixi167 – 1737
Beta strandi1620 – 16278
Beta strandi1629 – 16324
Beta strandi1635 – 16373
Helixi1639 – 16413
Helixi1645 – 16506
Turni1656 – 16583

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXJNMR-A85-175[»]
2KGGNMR-A1609-1659[»]
2KGINMR-A1609-1659[»]
3GL6X-ray1.90A1609-1659[»]
DisProtiDP00713.
ProteinModelPortaliP29375.
SMRiP29375. Positions 18-81, 84-175, 260-585, 1162-1217, 1608-1659.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29375.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 6042JmjNPROSITE-ProRule annotationAdd
BLAST
Domaini84 – 17491ARIDPROSITE-ProRule annotationAdd
BLAST
Domaini437 – 603167JmjCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1623 – 169068Interaction with LMO21 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi419 – 4235GSGFP motifBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1492 – 158796Lys-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri293 – 34351PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1161 – 121858PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1607 – 166155PHD-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG327026.
GeneTreeiENSGT00530000063118.
HOGENOMiHOG000290719.
InParanoidiP29375.
KOiK11446.
OMAiCVAHYRR.
OrthoDBiEOG7D85VK.
PhylomeDBiP29375.
TreeFamiTF106476.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
3.30.40.10. 3 hits.
InterProiIPR001606. 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]
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. Align

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 AAB28544.1 differs from that shown. Reason: Frameshift at several positions.
The sequence BAE06081.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1411 – 14111Q → QVFFGK in AAB28544. (PubMed:8414517)Curated
Sequence conflicti1547 – 15471E → K in AAB28544. (PubMed:8414517)Curated
Sequence conflicti1612 – 16143AQN → EPD in AAB28544. (PubMed:8414517)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti865 – 8651M → T.
Corresponds to variant rs11062385 [ dbSNP | Ensembl ].
VAR_032984
Natural varianti1190 – 11901P → A.
Corresponds to variant rs2229353 [ dbSNP | Ensembl ].
VAR_032985

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1623 – 169068VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2. 1 PublicationVSP_035746Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.1. human. [P29375-1]

Polymorphism databases

DMDMi215274124.

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:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS41736.1. [P29375-1 ]
PIRi I78879.
RefSeqi NP_001036068.1. NM_001042603.2. [P29375-1 ]
UniGenei Hs.76272.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
DisProti DP00713.
ProteinModelPortali P29375.
SMRi P29375. Positions 18-81, 84-175, 260-585, 1162-1217, 1608-1659.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111862. 22 interactions.
DIPi DIP-472N.
IntActi P29375. 3 interactions.
STRINGi 9606.ENSP00000382688.

Chemistry

ChEMBLi CHEMBL2424504.
GuidetoPHARMACOLOGYi 2680.

PTM databases

PhosphoSitei P29375.

Polymorphism databases

DMDMi 215274124.

Proteomic databases

MaxQBi P29375.
PaxDbi P29375.
PRIDEi P29375.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000399788 ; ENSP00000382688 ; ENSG00000073614 . [P29375-1 ]
GeneIDi 5927.
KEGGi hsa:5927.
UCSCi uc001qif.1. human. [P29375-1 ]

Organism-specific databases

CTDi 5927.
GeneCardsi GC12M000389.
H-InvDB HIX0010308.
HGNCi HGNC:9886. KDM5A.
HPAi HPA006201.
MIMi 180202. gene.
neXtProti NX_P29375.
PharmGKBi PA34250.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG327026.
GeneTreei ENSGT00530000063118.
HOGENOMi HOG000290719.
InParanoidi P29375.
KOi K11446.
OMAi CVAHYRR.
OrthoDBi EOG7D85VK.
PhylomeDBi P29375.
TreeFami TF106476.

Miscellaneous databases

ChiTaRSi KDM5A. human.
EvolutionaryTracei P29375.
GeneWikii JARID1A.
GenomeRNAii 5927.
NextBioi 23088.
PROi P29375.
SOURCEi Search...

Gene expression databases

Bgeei P29375.
CleanExi HS_JARID1A.
HS_RBP2.
ExpressionAtlasi P29375. baseline and differential.
Genevestigatori P29375.

Family and domain databases

Gene3Di 1.10.150.60. 1 hit.
3.30.40.10. 3 hits.
InterProi 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 ]
Pfami 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 ]
SMARTi SM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 3 hits.
[Graphical view ]
SUPFAMi SSF46774. SSF46774. 1 hit.
SSF57903. SSF57903. 3 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. 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. 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. "Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences the circadian clock."
    DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J., Panda S.
    Science 333:1881-1885(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARNTL AND CLOCK.
  19. "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].

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: October 29, 2014
This is version 148 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

External Data

Dasty 3