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Protein

Lysine-specific demethylase 6B

Gene

KDM6B

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-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation.2 Publications

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1390 – 13901IronCurated
Metal bindingi1392 – 13921IronCurated
Metal bindingi1470 – 14701IronBy similarity
Metal bindingi1575 – 15751ZincBy similarity
Metal bindingi1578 – 15781ZincBy similarity
Metal bindingi1602 – 16021ZincBy similarity
Metal bindingi1605 – 16051ZincBy similarity

GO - Molecular functioni

  1. dioxygenase activity Source: UniProtKB-KW
  2. histone demethylase activity (H3-K27 specific) Source: Reactome
  3. metal ion binding Source: UniProtKB-KW
  4. sequence-specific DNA binding Source: Ensembl

GO - Biological processi

  1. cardiac muscle cell differentiation Source: BHF-UCL
  2. cellular response to hydrogen peroxide Source: Ensembl
  3. chromatin organization Source: Reactome
  4. endothelial cell differentiation Source: BHF-UCL
  5. inflammatory response Source: UniProtKB-KW
  6. mesodermal cell differentiation Source: BHF-UCL
  7. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Inflammatory response

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
REACT_263961. HDMs demethylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 6B (EC:1.14.11.-)
Alternative name(s):
JmjC domain-containing protein 3
Jumonji domain-containing protein 3
Lysine demethylase 6B
Gene namesi
Name:KDM6B
Synonyms:JMJD3, KIAA0346
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:29012. KDM6B.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16431643Lysine-specific demethylase 6BPRO_0000292007Add
BLAST

Proteomic databases

MaxQBiO15054.
PaxDbiO15054.
PRIDEiO15054.

PTM databases

PhosphoSiteiO15054.

Expressioni

Inductioni

By 12-O-tetradecanoylphorbol-13-acetate (TPA) in myeloid leukemia cells.1 Publication

Gene expression databases

BgeeiO15054.
CleanExiHS_JMJD3.
ExpressionAtlasiO15054. baseline and differential.
GenevestigatoriO15054.

Organism-specific databases

HPAiHPA037988.

Interactioni

Subunit structurei

Interacts with TLE1 (By similarity). Component of the MLL4 complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5, and KDM6B.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033722EBI-2831260,EBI-78473

Protein-protein interaction databases

BioGridi116752. 12 interactions.
DIPiDIP-59912N.
IntActiO15054. 5 interactions.
MINTiMINT-7002224.
STRINGi9606.ENSP00000254846.

Structurei

Secondary structure

1
1643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1178 – 11814Combined sources
Beta strandi1187 – 11893Combined sources
Helixi1193 – 11953Combined sources
Helixi1199 – 12068Combined sources
Beta strandi1211 – 12177Combined sources
Helixi1218 – 12225Combined sources
Helixi1226 – 12294Combined sources
Helixi1231 – 12388Combined sources
Beta strandi1242 – 12498Combined sources
Beta strandi1261 – 12644Combined sources
Beta strandi1271 – 12766Combined sources
Helixi1277 – 128913Combined sources
Beta strandi1325 – 13339Combined sources
Helixi1337 – 134711Combined sources
Helixi1352 – 13543Combined sources
Turni1356 – 13594Combined sources
Beta strandi1363 – 13653Combined sources
Beta strandi1366 – 13683Combined sources
Turni1371 – 13733Combined sources
Beta strandi1375 – 13817Combined sources
Beta strandi1386 – 13905Combined sources
Helixi1393 – 13953Combined sources
Beta strandi1397 – 140610Combined sources
Beta strandi1408 – 14136Combined sources
Helixi1415 – 14173Combined sources
Helixi1418 – 142710Combined sources
Turni1432 – 14343Combined sources
Helixi1441 – 14466Combined sources
Beta strandi1452 – 14565Combined sources
Beta strandi1461 – 14644Combined sources
Beta strandi1469 – 148719Combined sources
Helixi1491 – 14955Combined sources
Helixi1514 – 152411Combined sources
Helixi1530 – 155728Combined sources
Beta strandi1561 – 15633Combined sources
Turni1576 – 15783Combined sources
Beta strandi1584 – 15907Combined sources
Beta strandi1598 – 16014Combined sources
Helixi1603 – 16086Combined sources
Turni1610 – 16156Combined sources
Beta strandi1617 – 16226Combined sources
Helixi1624 – 163310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XUEX-ray2.00A/B1141-1643[»]
2XXZX-ray1.80A/B1176-1505[»]
4ASKX-ray1.86A/B1141-1643[»]
ProteinModelPortaliO15054.
SMRiO15054. Positions 1157-1638.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15054.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1339 – 1502164JmjCPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi32 – 8554Pro-richAdd
BLAST
Compositional biasi195 – 906712Pro-richAdd
BLAST
Compositional biasi738 – 76427Thr-richAdd
BLAST
Compositional biasi1046 – 108237Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the UTX family.Curated
Contains 1 JmjC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG246325.
GeneTreeiENSGT00410000025758.
HOGENOMiHOG000113217.
InParanoidiO15054.
KOiK11448.
OMAiMDPLPRP.
OrthoDBiEOG7CG6Z5.
PhylomeDBiO15054.
TreeFamiTF317405.

Family and domain databases

InterProiIPR003347. JmjC_dom.
IPR029518. KDM6B.
[Graphical view]
PANTHERiPTHR14017:SF5. PTHR14017:SF5. 1 hit.
PfamiPF02373. JmjC. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEiPS51184. JMJC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 2 (identifier: O15054-2) [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
MHRAVDPPGA RAAREAFALG GLSCAGAWSS CPPHPPPRSA WLPGGRCSAS
60 70 80 90 100
IGQPPLPAPL PPSHGSSSGH PSKPYYAPGA PTPRPLHGKL ESLHGCVQAL
110 120 130 140 150
LREPAQPGLW EQLGQLYESE HDSEEATRCY HSALRYGGSF AELGPRIGRL
160 170 180 190 200
QQAQLWNFHT GSCQHRAKVL PPLEQVWNLL HLEHKRNYGA KRGGPPVKRA
210 220 230 240 250
AEPPVVQPVP PAALSGPSGE EGLSPGGKRR RGCNSEQTGL PPGLPLPPPP
260 270 280 290 300
LPPPPPPPPP PPPPLPGLAT SPPFQLTKPG LWSTLHGDAW GPERKGSAPP
310 320 330 340 350
ERQEQRHSLP HPYPYPAPAY TAHPPGHRLV PAAPPGPGPR PPGAESHGCL
360 370 380 390 400
PATRPPGSDL RESRVQRSRM DSSVSPAATT ACVPYAPSRP PGLPGTTTSS
410 420 430 440 450
SSSSSSNTGL RGVEPNPGIP GADHYQTPAL EVSHHGRLGP SAHSSRKPFL
460 470 480 490 500
GAPAATPHLS LPPGPSSPPP PPCPRLLRPP PPPAWLKGPA CRAAREDGEI
510 520 530 540 550
LEELFFGTEG PPRPAPPPLP HREGFLGPPA SRFSVGTQDS HTPPTPPTPT
560 570 580 590 600
TSSSNSNSGS HSSSPAGPVS FPPPPYLARS IDPLPRPPSP AQNPQDPPLV
610 620 630 640 650
PLTLALPPAP PSSCHQNTSG SFRRPESPRP RVSFPKTPEV GPGPPPGPLS
660 670 680 690 700
KAPQPVPPGV GELPARGPRL FDFPPTPLED QFEEPAEFKI LPDGLANIMK
710 720 730 740 750
MLDESIRKEE EQQQHEAGVA PQPPLKEPFA SLQSPFPTDT APTTTAPAVA
760 770 780 790 800
VTTTTTTTTT TTATQEEEKK PPPALPPPPP LAKFPPPSQP QPPPPPPPSP
810 820 830 840 850
ASLLKSLASV LEGQKYCYRG TGAAVSTRPG PLPTTQYSPG PPSGATALPP
860 870 880 890 900
TSAAPSAQGS PQPSASSSSQ FSTSGGPWAR ERRAGEEPVP GPMTPTQPPP
910 920 930 940 950
PLSLPPARSE SEVLEEISRA CETLVERVGR SATDPADPVD TAEPADSGTE
960 970 980 990 1000
RLLPPAQAKE EAGGVAAVSG SCKRRQKEHQ KEHRRHRRAC KDSVGRRPRE
1010 1020 1030 1040 1050
GRAKAKAKVP KEKSRRVLGN LDLQSEEIQG REKSRPDLGG ASKAKPPTAP
1060 1070 1080 1090 1100
APPSAPAPSA QPTPPSASVP GKKAREEAPG PPGVSRADML KLRSLSEGPP
1110 1120 1130 1140 1150
KELKIRLIKV ESGDKETFIA SEVEERRLRM ADLTISHCAA DVVRASRNAK
1160 1170 1180 1190 1200
VKGKFRESYL SPAQSVKPKI NTEEKLPREK LNPPTPSIYL ESKRDAFSPV
1210 1220 1230 1240 1250
LLQFCTDPRN PITVIRGLAG SLRLNLGLFS TKTLVEASGE HTVEVRTQVQ
1260 1270 1280 1290 1300
QPSDENWDLT GTRQIWPCES SRSHTTIAKY AQYQASSFQE SLQEEKESED
1310 1320 1330 1340 1350
EESEEPDSTT GTPPSSAPDP KNHHIIKFGT NIDLSDAKRW KPQLQELLKL
1360 1370 1380 1390 1400
PAFMRVTSTG NMLSHVGHTI LGMNTVQLYM KVPGSRTPGH QENNNFCSVN
1410 1420 1430 1440 1450
INIGPGDCEW FAVHEHYWET ISAFCDRHGV DYLTGSWWPI LDDLYASNIP
1460 1470 1480 1490 1500
VYRFVQRPGD LVWINAGTVH WVQATGWCNN IAWNVGPLTA YQYQLALERY
1510 1520 1530 1540 1550
EWNEVKNVKS IVPMIHVSWN VARTVKISDP DLFKMIKFCL LQSMKHCQVQ
1560 1570 1580 1590 1600
RESLVRAGKK IAYQGRVKDE PAYYCNECDV EVFNILFVTS ENGSRNTYLV
1610 1620 1630 1640
HCEGCARRRS AGLQGVVVLE QYRTEELAQA YDAFTLAPAS TSR

Note: Gene prediction based on similarity to mouse ortholog.

Length:1,643
Mass (Da):176,632
Last modified:November 30, 2010 - v4
Checksum:i8CE32AE602683BA3
GO
Isoform 1 (identifier: O15054-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1636-1636: L → LVRARRARGQRRRALGQAAGTGFGSPAAPFPEPPPAFSPQ

Show »
Length:1,682
Mass (Da):180,702
Checksum:iE4264890580649AB
GO

Sequence cautioni

The sequence BAA21572.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2543Missing in BAA21572 (PubMed:9205841).Curated
Sequence conflicti252 – 2543Missing in AAH09994 (PubMed:16625196).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti203 – 2031P → A.
Corresponds to variant rs60738318 [ dbSNP | Ensembl ].
VAR_061670
Natural varianti308 – 3081S → L.
Corresponds to variant rs2270516 [ dbSNP | Ensembl ].
VAR_032927

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1636 – 16361L → LVRARRARGQRRRALGQAAG TGFGSPAAPFPEPPPAFSPQ in isoform 1. 1 PublicationVSP_040102

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002344 mRNA. Translation: BAA21572.2. Different initiation.
AC104581 Genomic DNA. No translation available.
BC009994 mRNA. Translation: AAH09994.1.
CCDSiCCDS32552.1. [O15054-1]
RefSeqiNP_001073893.1. NM_001080424.1. [O15054-1]
XP_005256606.1. XM_005256549.1. [O15054-1]
XP_005256607.1. XM_005256550.2. [O15054-1]
XP_005256608.1. XM_005256551.1. [O15054-1]
XP_005256609.1. XM_005256552.2. [O15054-1]
XP_005256611.1. XM_005256554.2. [O15054-2]
XP_006721546.1. XM_006721483.1. [O15054-1]
UniGeneiHs.223678.

Genome annotation databases

EnsembliENST00000254846; ENSP00000254846; ENSG00000132510. [O15054-1]
ENST00000448097; ENSP00000412513; ENSG00000132510. [O15054-2]
GeneIDi23135.
KEGGihsa:23135.
UCSCiuc002giw.1. human. [O15054-1]
uc002gix.3. human. [O15054-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002344 mRNA. Translation: BAA21572.2. Different initiation.
AC104581 Genomic DNA. No translation available.
BC009994 mRNA. Translation: AAH09994.1.
CCDSiCCDS32552.1. [O15054-1]
RefSeqiNP_001073893.1. NM_001080424.1. [O15054-1]
XP_005256606.1. XM_005256549.1. [O15054-1]
XP_005256607.1. XM_005256550.2. [O15054-1]
XP_005256608.1. XM_005256551.1. [O15054-1]
XP_005256609.1. XM_005256552.2. [O15054-1]
XP_005256611.1. XM_005256554.2. [O15054-2]
XP_006721546.1. XM_006721483.1. [O15054-1]
UniGeneiHs.223678.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XUEX-ray2.00A/B1141-1643[»]
2XXZX-ray1.80A/B1176-1505[»]
4ASKX-ray1.86A/B1141-1643[»]
ProteinModelPortaliO15054.
SMRiO15054. Positions 1157-1638.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116752. 12 interactions.
DIPiDIP-59912N.
IntActiO15054. 5 interactions.
MINTiMINT-7002224.
STRINGi9606.ENSP00000254846.

Chemistry

BindingDBiO15054.
ChEMBLiCHEMBL1938211.
GuidetoPHARMACOLOGYi2685.

PTM databases

PhosphoSiteiO15054.

Proteomic databases

MaxQBiO15054.
PaxDbiO15054.
PRIDEiO15054.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254846; ENSP00000254846; ENSG00000132510. [O15054-1]
ENST00000448097; ENSP00000412513; ENSG00000132510. [O15054-2]
GeneIDi23135.
KEGGihsa:23135.
UCSCiuc002giw.1. human. [O15054-1]
uc002gix.3. human. [O15054-2]

Organism-specific databases

CTDi23135.
GeneCardsiGC17P007686.
HGNCiHGNC:29012. KDM6B.
HPAiHPA037988.
MIMi611577. gene.
neXtProtiNX_O15054.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG246325.
GeneTreeiENSGT00410000025758.
HOGENOMiHOG000113217.
InParanoidiO15054.
KOiK11448.
OMAiMDPLPRP.
OrthoDBiEOG7CG6Z5.
PhylomeDBiO15054.
TreeFamiTF317405.

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
REACT_263961. HDMs demethylate histones.

Miscellaneous databases

ChiTaRSiKDM6B. human.
EvolutionaryTraceiO15054.
GenomeRNAii23135.
NextBioi44391.
PROiO15054.
SOURCEiSearch...

Gene expression databases

BgeeiO15054.
CleanExiHS_JMJD3.
ExpressionAtlasiO15054. baseline and differential.
GenevestigatoriO15054.

Family and domain databases

InterProiIPR003347. JmjC_dom.
IPR029518. KDM6B.
[Graphical view]
PANTHERiPTHR14017:SF5. PTHR14017:SF5. 1 hit.
PfamiPF02373. JmjC. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEiPS51184. JMJC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2005) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1000-1643 (ISOFORM 2).
    Tissue: Brain.
  5. "An efficient strategy to identify early TPA-responsive genes during differentiation of HL-60 cells."
    Hu L.Y., Tepper C.G., Lo S.H., Lin W.C.
    Gene Expr. 13:179-189(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY TPA.
  6. "The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing."
    De Santa F., Totaro M.G., Prosperini E., Notarbartolo S., Testa G., Natoli G.
    Cell 130:1083-1094(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, IDENTIFICATION IN THE MLL4 COMPLEX.
  7. Cited for: FUNCTION, ENZYME ACTIVITY.
  8. "Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases."
    Hong S., Cho Y.W., Yu L.-R., Yu H., Veenstra T.D., Ge K.
    Proc. Natl. Acad. Sci. U.S.A. 104:18439-18444(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY.
  9. "Crystal structure of the human JMJD3 Jumonji domain."
    Structural genomics consortium (SGC)
    Submitted (NOV-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1176-1502 IN COMPLEX WITH NICKEL IONS AND 8-HYDROXYQUINOLINE-5-CARBOXYLIC ACID.

Entry informationi

Entry nameiKDM6B_HUMAN
AccessioniPrimary (citable) accession number: O15054
Secondary accession number(s): C9IZ40, Q96G33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: November 30, 2010
Last modified: April 1, 2015
This is version 113 of the entry and version 4 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 17
    Human chromosome 17: 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

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 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.