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Protein

Lysine-specific demethylase 5B

Gene

KDM5B

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

Functioni

Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity).By similarity4 Publications

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi499Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi502Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi587Iron; catalyticPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri309 – 359PHD-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1176 – 1224PHD-type 2PROSITE-ProRule annotationAdd BLAST49
Zinc fingeri1484 – 1538PHD-type 3PROSITE-ProRule annotationAdd BLAST55

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000117139-MONOMER.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
R-HSA-8866911. TFAP2 (AP-2) family regulates transcription of cell cycle factors.
SIGNORiQ9UGL1.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 5B (EC:1.14.11.-)
Alternative name(s):
Cancer/testis antigen 31
Short name:
CT31
Histone demethylase JARID1B
Jumonji/ARID domain-containing protein 1B
PLU-1
Retinoblastoma-binding protein 2 homolog 1
Short name:
RBP2-H1
Gene namesi
Name:KDM5B
Synonyms:JARID1B, PLU1, RBBP2H1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18039. KDM5B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi335H → A: Slightly impairs transcription repression ability. 1 Publication1
Mutagenesisi499H → Y: Abolishes enzymatic activity. 1 Publication1
Mutagenesisi1200H → A: Impairs transcription repression ability and interaction with HDAC4. 1 Publication1

Organism-specific databases

DisGeNETi10765.
OpenTargetsiENSG00000117139.
PharmGKBiPA164721626.

Chemistry databases

GuidetoPHARMACOLOGYi2681.

Polymorphism and mutation databases

BioMutaiKDM5B.
DMDMi296439317.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002924121 – 1544Lysine-specific demethylase 5BAdd BLAST1544

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki242Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki769Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei832N6-acetyllysineBy similarity1
Modified residuei986PhosphoserineCombined sources1
Modified residuei1328PhosphoserineCombined sources1
Modified residuei1456PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UGL1.
PaxDbiQ9UGL1.
PeptideAtlasiQ9UGL1.
PRIDEiQ9UGL1.

PTM databases

iPTMnetiQ9UGL1.
PhosphoSitePlusiQ9UGL1.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in testis. Down-regulated in melanoma and glioblastoma. Up-regulated in breast cancer (at protein level).5 Publications

Gene expression databases

BgeeiENSG00000117139.
CleanExiHS_JARID1B.
ExpressionAtlasiQ9UGL1. baseline and differential.
GenevisibleiQ9UGL1. HS.

Organism-specific databases

HPAiCAB068193.
HPA027179.
HPA053723.

Interactioni

Subunit structurei

Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts with HDAC1, HDAC4, HDAC5 and HDAC7.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTCFP497118EBI-2514978,EBI-932887

Protein-protein interaction databases

BioGridi115984. 63 interactors.
DIPiDIP-53652N.
IntActiQ9UGL1. 3 interactors.
STRINGi9606.ENSP00000356234.

Structurei

Secondary structure

11544
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi39 – 42Combined sources4
Helixi45 – 56Combined sources12
Turni57 – 59Combined sources3
Beta strandi60 – 64Combined sources5
Turni78 – 80Combined sources3
Beta strandi86 – 89Combined sources4
Beta strandi96 – 98Combined sources3
Beta strandi308 – 310Combined sources3
Beta strandi313 – 315Combined sources3
Helixi319 – 323Combined sources5
Beta strandi324 – 326Combined sources3
Beta strandi328 – 331Combined sources4
Beta strandi333 – 335Combined sources3
Turni336 – 339Combined sources4
Helixi354 – 359Combined sources6
Helixi379 – 394Combined sources16
Helixi398 – 400Combined sources3
Helixi403 – 415Combined sources13
Beta strandi422 – 429Combined sources8
Beta strandi432 – 434Combined sources3
Beta strandi443 – 445Combined sources3
Helixi449 – 454Combined sources6
Beta strandi458 – 460Combined sources3
Turni461 – 466Combined sources6
Beta strandi467 – 469Combined sources3
Helixi472 – 474Combined sources3
Helixi480 – 483Combined sources4
Beta strandi486 – 490Combined sources5
Beta strandi495 – 499Combined sources5
Helixi502 – 504Combined sources3
Beta strandi506 – 515Combined sources10
Beta strandi517 – 521Combined sources5
Helixi524 – 526Combined sources3
Helixi527 – 537Combined sources11
Helixi539 – 542Combined sources4
Helixi548 – 550Combined sources3
Beta strandi552 – 554Combined sources3
Helixi558 – 563Combined sources6
Beta strandi569 – 573Combined sources5
Beta strandi578 – 581Combined sources4
Beta strandi587 – 602Combined sources16
Helixi605 – 607Combined sources3
Helixi608 – 621Combined sources14
Helixi629 – 637Combined sources9
Helixi638 – 642Combined sources5
Helixi645 – 671Combined sources27
Beta strandi676 – 679Combined sources4
Helixi682 – 684Combined sources3
Helixi687 – 689Combined sources3
Beta strandi690 – 692Combined sources3
Turni693 – 695Combined sources3
Beta strandi701 – 706Combined sources6
Helixi719 – 721Combined sources3
Helixi727 – 729Combined sources3
Beta strandi730 – 735Combined sources6
Helixi738 – 752Combined sources15
Beta strandi1495 – 1500Combined sources6
Beta strandi1502 – 1505Combined sources4
Turni1506 – 1509Combined sources4
Beta strandi1511 – 1514Combined sources4
Helixi1515 – 1518Combined sources4
Helixi1522 – 1526Combined sources5
Helixi1533 – 1537Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MA5NMR-A1487-1544[»]
2MNYNMR-A306-360[»]
2MNZNMR-A306-360[»]
5A1FX-ray2.10A26-770[»]
5A3NX-ray2.00A26-101[»]
A374-772[»]
5A3PX-ray2.01A26-101[»]
A374-770[»]
5A3TX-ray1.90A26-101[»]
A374-772[»]
5A3WX-ray2.00A26-101[»]
A374-772[»]
5FPLX-ray2.35A26-101[»]
A374-772[»]
5FPUX-ray2.24A26-101[»]
A374-772[»]
5FUNX-ray2.30A26-101[»]
A374-772[»]
5FUPX-ray2.15A26-101[»]
A374-770[»]
5FV3X-ray2.37A26-101[»]
A374-770[»]
5FYTX-ray1.87A26-101[»]
A374-770[»]
5FYUX-ray2.06A26-101[»]
A374-770[»]
5FYYX-ray2.18A26-101[»]
A374-770[»]
5FYZX-ray1.75A26-101[»]
A374-770[»]
5FZ0X-ray2.42A26-101[»]
A374-770[»]
5FZ1X-ray2.39A26-101[»]
A374-770[»]
5FZ3X-ray2.50A26-101[»]
A374-770[»]
5FZ4X-ray2.07A26-101[»]
A374-770[»]
5FZ6X-ray2.33A26-101[»]
A374-770[»]
5FZ7X-ray2.30A26-101[»]
A374-770[»]
5FZ9X-ray2.06A26-101[»]
A374-770[»]
5FZAX-ray2.10A26-101[»]
A374-770[»]
5FZBX-ray2.18A26-101[»]
A374-770[»]
5FZCX-ray2.05A26-101[»]
A374-770[»]
5FZHX-ray2.09A26-101[»]
A374-442[»]
A444-770[»]
5FZKX-ray2.05A26-101[»]
A374-770[»]
5FZLX-ray2.55A26-101[»]
A374-770[»]
5LW9X-ray2.30A26-99[»]
A374-772[»]
DisProtiDP00712.
ProteinModelPortaliQ9UGL1.
SMRiQ9UGL1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 73JmjNPROSITE-ProRule annotationAdd BLAST42
Domaini97 – 187ARIDPROSITE-ProRule annotationAdd BLAST91
Domaini453 – 619JmjCPROSITE-ProRule annotationAdd BLAST167

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1434 – 1439Poly-Lys6

Domaini

Both the JmjC domain and the JmjN domain are required for enzymatic activity.
The 2 first PHD-type zinc finger domains are required for transcription repression activity.

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 fingeri309 – 359PHD-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1176 – 1224PHD-type 2PROSITE-ProRule annotationAdd BLAST49
Zinc fingeri1484 – 1538PHD-type 3PROSITE-ProRule annotationAdd BLAST55

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1246. Eukaryota.
ENOG410XR9J. LUCA.
GeneTreeiENSGT00530000063118.
HOGENOMiHOG000290719.
InParanoidiQ9UGL1.
KOiK11446.
OMAiNECCRGK.
OrthoDBiEOG091G0RFR.
PhylomeDBiQ9UGL1.
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. 3 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: Q9UGL1-1) [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
MEAATTLHPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH
60 70 80 90 100
KIRPIAEQTG ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK
110 120 130 140 150
LNFLDQIAKY WELQGSTLKI PHVERKILDL FQLNKLVAEE GGFAVVCKDR
160 170 180 190 200
KWTKIATKMG FAPGKAVGSH IRGHYERILN PYNLFLSGDS LRCLQKPNLT
210 220 230 240 250
TDTKDKEYKP HDIPQRQSVQ PSETCPPARR AKRMRAEAMN IKIEPEETTE
260 270 280 290 300
ARTHNLRRRM GCPTPKCENE KEMKSSIKQE PIERKDYIVE NEKEKPKSRS
310 320 330 340 350
KKATNAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLI PPLHDVPKGD
360 370 380 390 400
WRCPKCLAQE CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM
410 420 430 440 450
VPTELVEKEF WRLVSTIEED VTVEYGADIA SKEFGSGFPV RDGKIKLSPE
460 470 480 490 500
EEEYLDSGWN LNNMPVMEQS VLAHITADIC GMKLPWLYVG MCFSSFCWHI
510 520 530 540 550
EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE LFVSQPDLLH
560 570 580 590 600
QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV
610 620 630 640 650
NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST
660 670 680 690 700
VQKDMAIMIE DEKALRETVR KLGVIDSERM DFELLPDDER QCVKCKTTCF
710 720 730 740 750
MSAISCSCKP GLLVCLHHVK ELCSCPPYKY KLRYRYTLDD LYPMMNALKL
760 770 780 790 800
RAESYNEWAL NVNEALEAKI NKKKSLVSFK ALIEESEMKK FPDNDLLRHL
810 820 830 840 850
RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN ELRQFVTQLY
860 870 880 890 900
ALPCVLSQTP LLKDLLNRVE DFQQHSQKLL SEETPSAAEL QDLLDVSFEF
910 920 930 940 950
DVELPQLAEM RIRLEQARWL EEVQQACLDP SSLTLDDMRR LIDLGVGLAP
960 970 980 990 1000
YSAVEKAMAR LQELLTVSEH WDDKAKSLLK ARPRHSLNSL ATAVKEIEEI
1010 1020 1030 1040 1050
PAYLPNGAAL KDSVQRARDW LQDVEGLQAG GRVPVLDTLI ELVTRGRSIP
1060 1070 1080 1090 1100
VHLNSLPRLE TLVAEVQAWK ECAVNTFLTE NSPYSLLEVL CPRCDIGLLG
1110 1120 1130 1140 1150
LKRKQRKLKE PLPNGKKKST KLESLSDLER ALTESKETAS AMATLGEARL
1160 1170 1180 1190 1200
REMEALQSLR LANEGKLLSP LQDVDIKICL CQKAPAAPMI QCELCRDAFH
1210 1220 1230 1240 1250
TSCVAVPSIS QGLRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD
1260 1270 1280 1290 1300
ALRYMIERTV NWQHRAQQLL SSGNLKFVQD RVGSGLLYSR WQASAGQVSD
1310 1320 1330 1340 1350
TNKVSQPPGT TSFSLPDDWD NRTSYLHSPF STGRSCIPLH GVSPEVNELL
1360 1370 1380 1390 1400
MEAQLLQVSL PEIQELYQTL LAKPSPAQQT DRSSPVRPSS EKNDCCRGKR
1410 1420 1430 1440 1450
DGINSLERKL KRRLEREGLS SERWERVKKM RTPKKKKIKL SHPKDMNNFK
1460 1470 1480 1490 1500
LERERSYELV RSAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV
1510 1520 1530 1540
DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTVKDA PSRK
Length:1,544
Mass (Da):175,658
Last modified:May 18, 2010 - v3
Checksum:i70A0738D9A709F61
GO
Isoform 2 (identifier: Q9UGL1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     237-237: E → ERQSLAVLPRLECSGAILAHCNLRLLDSSNSSASASQ

Show »
Length:1,580
Mass (Da):179,409
Checksum:i61B03B8A7EE16B3C
GO

Sequence cautioni

The sequence CAB63108 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78V → G in CAB63108 (PubMed:10878660).Curated1
Sequence conflicti585 – 589AYHSG → VPQW in AAD16061 (PubMed:10616211).Curated5
Sequence conflicti708C → W in AAD16061 (PubMed:10616211).Curated1
Sequence conflicti759A → P in AAD16061 (PubMed:10616211).Curated1
Sequence conflicti771N → T in AAD16061 (PubMed:10616211).Curated1
Sequence conflicti771N → T in CAB63108 (PubMed:10878660).Curated1
Sequence conflicti1182Q → R in AAD16061 (PubMed:10616211).Curated1
Sequence conflicti1293A → P in AAD16061 (PubMed:10616211).Curated1
Sequence conflicti1307P → L in AAD16061 (PubMed:10616211).Curated1
Sequence conflicti1331S → ST in AAD16061 (PubMed:10616211).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_026408237E → ERQSLAVLPRLECSGAILAH CNLRLLDSSNSSASASQ in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132440 mRNA. Translation: CAB43532.1.
AF087481 mRNA. Translation: AAD16061.1.
AJ243706 mRNA. Translation: CAB63108.1. Different initiation.
AC098934 Genomic DNA. No translation available.
AC104463 Genomic DNA. No translation available.
CCDSiCCDS30974.1. [Q9UGL1-1]
CCDS81417.1. [Q9UGL1-2]
RefSeqiNP_001300971.1. NM_001314042.1. [Q9UGL1-2]
NP_006609.3. NM_006618.4. [Q9UGL1-1]
UniGeneiHs.18891.
Hs.443650.

Genome annotation databases

EnsembliENST00000367264; ENSP00000356233; ENSG00000117139. [Q9UGL1-2]
ENST00000367265; ENSP00000356234; ENSG00000117139. [Q9UGL1-1]
GeneIDi10765.
KEGGihsa:10765.
UCSCiuc001gyf.4. human. [Q9UGL1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132440 mRNA. Translation: CAB43532.1.
AF087481 mRNA. Translation: AAD16061.1.
AJ243706 mRNA. Translation: CAB63108.1. Different initiation.
AC098934 Genomic DNA. No translation available.
AC104463 Genomic DNA. No translation available.
CCDSiCCDS30974.1. [Q9UGL1-1]
CCDS81417.1. [Q9UGL1-2]
RefSeqiNP_001300971.1. NM_001314042.1. [Q9UGL1-2]
NP_006609.3. NM_006618.4. [Q9UGL1-1]
UniGeneiHs.18891.
Hs.443650.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MA5NMR-A1487-1544[»]
2MNYNMR-A306-360[»]
2MNZNMR-A306-360[»]
5A1FX-ray2.10A26-770[»]
5A3NX-ray2.00A26-101[»]
A374-772[»]
5A3PX-ray2.01A26-101[»]
A374-770[»]
5A3TX-ray1.90A26-101[»]
A374-772[»]
5A3WX-ray2.00A26-101[»]
A374-772[»]
5FPLX-ray2.35A26-101[»]
A374-772[»]
5FPUX-ray2.24A26-101[»]
A374-772[»]
5FUNX-ray2.30A26-101[»]
A374-772[»]
5FUPX-ray2.15A26-101[»]
A374-770[»]
5FV3X-ray2.37A26-101[»]
A374-770[»]
5FYTX-ray1.87A26-101[»]
A374-770[»]
5FYUX-ray2.06A26-101[»]
A374-770[»]
5FYYX-ray2.18A26-101[»]
A374-770[»]
5FYZX-ray1.75A26-101[»]
A374-770[»]
5FZ0X-ray2.42A26-101[»]
A374-770[»]
5FZ1X-ray2.39A26-101[»]
A374-770[»]
5FZ3X-ray2.50A26-101[»]
A374-770[»]
5FZ4X-ray2.07A26-101[»]
A374-770[»]
5FZ6X-ray2.33A26-101[»]
A374-770[»]
5FZ7X-ray2.30A26-101[»]
A374-770[»]
5FZ9X-ray2.06A26-101[»]
A374-770[»]
5FZAX-ray2.10A26-101[»]
A374-770[»]
5FZBX-ray2.18A26-101[»]
A374-770[»]
5FZCX-ray2.05A26-101[»]
A374-770[»]
5FZHX-ray2.09A26-101[»]
A374-442[»]
A444-770[»]
5FZKX-ray2.05A26-101[»]
A374-770[»]
5FZLX-ray2.55A26-101[»]
A374-770[»]
5LW9X-ray2.30A26-99[»]
A374-772[»]
DisProtiDP00712.
ProteinModelPortaliQ9UGL1.
SMRiQ9UGL1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115984. 63 interactors.
DIPiDIP-53652N.
IntActiQ9UGL1. 3 interactors.
STRINGi9606.ENSP00000356234.

Chemistry databases

GuidetoPHARMACOLOGYi2681.

PTM databases

iPTMnetiQ9UGL1.
PhosphoSitePlusiQ9UGL1.

Polymorphism and mutation databases

BioMutaiKDM5B.
DMDMi296439317.

Proteomic databases

EPDiQ9UGL1.
PaxDbiQ9UGL1.
PeptideAtlasiQ9UGL1.
PRIDEiQ9UGL1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367264; ENSP00000356233; ENSG00000117139. [Q9UGL1-2]
ENST00000367265; ENSP00000356234; ENSG00000117139. [Q9UGL1-1]
GeneIDi10765.
KEGGihsa:10765.
UCSCiuc001gyf.4. human. [Q9UGL1-1]

Organism-specific databases

CTDi10765.
DisGeNETi10765.
GeneCardsiKDM5B.
H-InvDBHIX0001478.
HGNCiHGNC:18039. KDM5B.
HPAiCAB068193.
HPA027179.
HPA053723.
MIMi605393. gene.
neXtProtiNX_Q9UGL1.
OpenTargetsiENSG00000117139.
PharmGKBiPA164721626.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1246. Eukaryota.
ENOG410XR9J. LUCA.
GeneTreeiENSGT00530000063118.
HOGENOMiHOG000290719.
InParanoidiQ9UGL1.
KOiK11446.
OMAiNECCRGK.
OrthoDBiEOG091G0RFR.
PhylomeDBiQ9UGL1.
TreeFamiTF106476.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000117139-MONOMER.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
R-HSA-8866911. TFAP2 (AP-2) family regulates transcription of cell cycle factors.
SIGNORiQ9UGL1.

Miscellaneous databases

ChiTaRSiKDM5B. human.
GeneWikiiJARID1B.
GenomeRNAii10765.
PROiQ9UGL1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117139.
CleanExiHS_JARID1B.
ExpressionAtlasiQ9UGL1. baseline and differential.
GenevisibleiQ9UGL1. 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. 3 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 nameiKDM5B_HUMAN
AccessioniPrimary (citable) accession number: Q9UGL1
Secondary accession number(s): O95811, Q15752, Q9Y3Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 133 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.