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Q8NHM5

- KDM2B_HUMAN

UniProt

Q8NHM5 - KDM2B_HUMAN

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Protein

Lysine-specific demethylase 2B

Gene

KDM2B

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

Functioni

Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.2 Publications

Catalytic activityi

Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2.1 Publication
Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.1 Publication

Cofactori

Fe2+By similarityNote: Binds 1 Fe(2+) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei239 – 2391SubstrateBy similarity
Metal bindingi242 – 2421Iron; catalyticPROSITE-ProRule annotation
Metal bindingi244 – 2441Iron; catalyticPROSITE-ProRule annotation
Binding sitei259 – 2591SubstrateBy similarity
Metal bindingi314 – 3141Iron; catalyticPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri606 – 65247CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri659 – 72567PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. histone demethylase activity Source: BHF-UCL
  3. histone demethylase activity (H3-K36 specific) Source: UniProtKB-EC
  4. rRNA binding Source: UniProtKB-KW
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. embryonic camera-type eye morphogenesis Source: BHF-UCL
  2. forebrain development Source: BHF-UCL
  3. fourth ventricle development Source: BHF-UCL
  4. hindbrain development Source: BHF-UCL
  5. histone demethylation Source: GOC
  6. histone H2A monoubiquitination Source: UniProtKB
  7. initiation of neural tube closure Source: BHF-UCL
  8. lateral ventricle development Source: BHF-UCL
  9. midbrain development Source: BHF-UCL
  10. midbrain-hindbrain boundary morphogenesis Source: BHF-UCL
  11. negative regulation of neural precursor cell proliferation Source: BHF-UCL
  12. negative regulation of neuron apoptotic process Source: BHF-UCL
  13. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  14. spermatogenesis Source: BHF-UCL
  15. third ventricle development Source: BHF-UCL
  16. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Iron, Metal-binding, RNA-binding, rRNA-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_228178. HDMs demethylate histones.
SignaLinkiQ8NHM5.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 2B (EC:1.14.11.27)
Alternative name(s):
CXXC-type zinc finger protein 2
F-box and leucine-rich repeat protein 10
F-box protein FBL10
F-box/LRR-repeat protein 10
JmjC domain-containing histone demethylation protein 1B
Jumonji domain-containing EMSY-interactor methyltransferase motif protein
Short name:
Protein JEMMA
Protein-containing CXXC domain 2
[Histone-H3]-lysine-36 demethylase 1B
Gene namesi
Name:KDM2B
Synonyms:CXXC2, FBL10, FBXL10, JHDM1B, PCCX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:13610. KDM2B.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164721242.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13361336Lysine-specific demethylase 2BPRO_0000119853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei474 – 4741Phosphoserine1 Publication
Modified residuei477 – 4771Phosphoserine1 Publication
Modified residuei493 – 4931Phosphothreonine2 Publications
Modified residuei497 – 4971Phosphoserine1 Publication
Modified residuei975 – 9751Phosphoserine1 Publication
Modified residuei979 – 9791Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8NHM5.
PaxDbiQ8NHM5.
PRIDEiQ8NHM5.

PTM databases

PhosphoSiteiQ8NHM5.

Expressioni

Gene expression databases

BgeeiQ8NHM5.
CleanExiHS_FBXL10.
ExpressionAtlasiQ8NHM5. baseline and differential.
GenevestigatoriQ8NHM5.

Interactioni

Subunit structurei

Directly interacts with SKP1 and CUL1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BCORQ6W2J92EBI-3955564,EBI-950027

Protein-protein interaction databases

BioGridi124197. 19 interactions.
IntActiQ8NHM5. 3 interactions.
STRINGi9606.ENSP00000366271.

Structurei

Secondary structure

1
1336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi617 – 6204Combined sources
Helixi628 – 6325Combined sources
Helixi634 – 6363Combined sources
Helixi647 – 6493Combined sources
Turni663 – 6653Combined sources
Helixi671 – 6733Combined sources
Helixi677 – 6826Combined sources
Beta strandi686 – 6883Combined sources
Turni689 – 6913Combined sources
Helixi697 – 6993Combined sources
Beta strandi711 – 7133Combined sources
Beta strandi716 – 7183Combined sources
Turni720 – 7223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4O64X-ray2.13A/B/C607-723[»]
ProteinModelPortaliQ8NHM5.
SMRiQ8NHM5. Positions 66-392, 508-573, 608-723, 1068-1333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 346169JmjCPROSITE-ProRule annotationAdd
BLAST
Domaini1059 – 110547F-boxAdd
BLAST
Repeati1093 – 112028LRR 1Add
BLAST
Repeati1133 – 115422LRR 2Add
BLAST
Repeati1156 – 118227LRR 3Add
BLAST
Repeati1222 – 124726LRR 4Add
BLAST
Repeati1248 – 127730LRR 5Add
BLAST
Repeati1278 – 130225LRR 6Add
BLAST
Repeati1303 – 133634LRR 7Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili943 – 97129Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi409 – 43022Glu-richAdd
BLAST
Compositional biasi1014 – 105643Pro-richAdd
BLAST

Domaini

The JmjC domain mediates demethylation activity (By similarity). It is also required for repression of ribosomal RNA genes.By similarity

Sequence similaritiesi

Belongs to the JHDM1 histone demethylase family.Curated
Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
Contains 1 F-box domain.Curated
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 7 LRR (leucine-rich) repeats.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri606 – 65247CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri659 – 72567PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Leucine-rich repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG290496.
GeneTreeiENSGT00550000074396.
HOGENOMiHOG000007396.
InParanoidiQ8NHM5.
KOiK10276.
OMAiNAEDRMA.
OrthoDBiEOG78SQH0.
PhylomeDBiQ8NHM5.
TreeFamiTF106480.

Family and domain databases

InterProiIPR001810. F-box_dom.
IPR003347. JmjC_dom.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51184. JMJC. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8NHM5-1) [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
MAGPQMGGSA EDHPPRKRHA AEKQKKKTVI YTKCFEFESA TQRPIDRQRY
60 70 80 90 100
DENEDLSDVE EIVSVRGFSL EEKLRSQLYQ GDFVHAMEGK DFNYEYVQRE
110 120 130 140 150
ALRVPLIFRE KDGLGIKMPD PDFTVRDVKL LVGSRRLVDV MDVNTQKGTE
160 170 180 190 200
MSMSQFVRYY ETPEAQRDKL YNVISLEFSH TKLEHLVKRP TVVDLVDWVD
210 220 230 240 250
NMWPQHLKEK QTEATNAIAE MKYPKVKKYC LMSVKGCFTD FHIDFGGTSV
260 270 280 290 300
WYHVFRGGKI FWLIPPTLHN LALYEEWVLS GKQSDIFLGD RVERCQRIEL
310 320 330 340 350
KQGYTFFIPS GWIHAVYTPV DSLVFGGNIL HSFNVPMQLR IYEIEDRTRV
360 370 380 390 400
QPKFRYPFYY EMCWYVLERY VYCVTQRSHL TQEYQRESML IDAPRKPSID
410 420 430 440 450
GFSSDSWLEM EEEACDQQPQ EEEEKDEEGE GRDRAPKPPT DGSTSPTSTP
460 470 480 490 500
SEDQEALGKK PKAPALRFLK RTLSNESEES VKSTTLAVDY PKTPTGSPAT
510 520 530 540 550
EVSAKWTHLT EFELKGLKAL VEKLESLPEN KKCVPEGIED PQALLEGVKN
560 570 580 590 600
VLKEHADDDP SLAITGVPVV TWPKKTPKNR AVGRPKGKLG PASAVKLAAN
610 620 630 640 650
RTTAGARRRR TRCRKCEACL RTECGECHFC KDMKKFGGPG RMKQSCIMRQ
660 670 680 690 700
CIAPVLPHTA VCLVCGEAGK EDTVEEEEGK FNLMLMECSI CNEIIHPGCL
710 720 730 740 750
KIKESEGVVN DELPNCWECP KCNHAGKTGK QKRGPGFKYA SNLPGSLLKE
760 770 780 790 800
QKMNRDNKEG QEPAKRRSEC EEAPRRRSDE HSKKVPPDGL LRRKSDDVHL
810 820 830 840 850
RKKRKYEKPQ ELSGRKRASS LQTSPGSSSH LSPRPPLGSS LSPWWRSSLT
860 870 880 890 900
YFQQQLKPGK EDKLFRKKRR SWKNAEDRMA LANKPLRRFK QEPEDELPEA
910 920 930 940 950
PPKTRESDHS RSSSPTAGPS TEGAEGPEEK KKVKMRRKRR LPNKELSREL
960 970 980 990 1000
SKELNHEIQR TENSLANENQ QPIKSEPESE GEEPKRPPGI CERPHRFSKG
1010 1020 1030 1040 1050
LNGTPRELRH QLGPSLRSPP RVISRPPPSV SPPKCIQMER HVIRPPPISP
1060 1070 1080 1090 1100
PPDSLPLDDG AAHVMHREVW MAVFSYLSHQ DLCVCMRVCR TWNRWCCDKR
1110 1120 1130 1140 1150
LWTRIDLNHC KSITPLMLSG IIRRQPVSLD LSWTNISKKQ LSWLINRLPG
1160 1170 1180 1190 1200
LRDLVLSGCS WIAVSALCSS SCPLLRTLDV QWVEGLKDAQ MRDLLSPPTD
1210 1220 1230 1240 1250
NRPGQMDNRS KLRNIVELRL AGLDITDASL RLIIRHMPLL SKLHLSYCNH
1260 1270 1280 1290 1300
VTDQSINLLT AVGTTTRDSL TEINLSDCNK VTDQCLSFFK RCGNICHIDL
1310 1320 1330
RYCKQVTKEG CEQFIAEMSV SVQFGQVEEK LLQKLS
Length:1,336
Mass (Da):152,615
Last modified:October 1, 2002 - v1
Checksum:i3A1A17B8EA9EA953
GO
Isoform 2 (identifier: Q8NHM5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     730-730: K → KAYK
     1277-1336: DCNKVTDQCL...VEEKLLQKLS → ASLLGRVFGLQFWGICEPQARKNAGWA

Show »
Length:1,306
Mass (Da):149,034
Checksum:i3329D5375AD25930
GO
Isoform 3 (identifier: Q8NHM5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     856-868: LKPGKEDKLFRKK → Q
     1204-1204: G → GPG

Note: No experimental confirmation available.

Show »
Length:1,326
Mass (Da):151,328
Checksum:iBCBDAE3F675E017C
GO
Isoform 4 (identifier: Q8NHM5-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQ → MEAEKDSGRRL
     818-855: Missing.
     1320-1336: VSVQFGQVEEKLLQKLS → SFQGRSCSTTRLGDE

Note: No experimental confirmation available.

Show »
Length:1,265
Mass (Da):144,769
Checksum:i69C8C16EFDE3541C
GO

Sequence cautioni

The sequence AAH08735.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB55112.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB55301.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC11159.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti864 – 8641L → F in BAC11159. 1 PublicationCurated
Sequence conflicti1226 – 12261T → R in BAC11159. 1 PublicationCurated
Sequence conflicti1295 – 12951I → T in BAC11159. 1 PublicationCurated
Sequence conflicti1334 – 13341K → R in BAC11159. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4242MAGPQ…ESATQ → MEAEKDSGRRL in isoform 4. 1 PublicationVSP_043146Add
BLAST
Alternative sequencei730 – 7301K → KAYK in isoform 2. 1 PublicationVSP_011340
Alternative sequencei818 – 85538Missing in isoform 4. 1 PublicationVSP_043147Add
BLAST
Alternative sequencei856 – 86813LKPGK…LFRKK → Q in isoform 3. 1 PublicationVSP_017475Add
BLAST
Alternative sequencei1204 – 12041G → GPG in isoform 3. 1 PublicationVSP_017476
Alternative sequencei1277 – 133660DCNKV…LQKLS → ASLLGRVFGLQFWGICEPQA RKNAGWA in isoform 2. 1 PublicationVSP_011341Add
BLAST
Alternative sequencei1320 – 133617VSVQF…LQKLS → SFQGRSCSTTRLGDE in isoform 4. 1 PublicationVSP_043148Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ459424 mRNA. Translation: CAD30700.1.
AK027440 mRNA. Translation: BAB55112.1. Different initiation.
AK027692 mRNA. Translation: BAB55301.1. Different initiation.
AK074718 mRNA. Translation: BAC11159.1. Different initiation.
AK127328 mRNA. Translation: BAG54483.1.
AC048337 Genomic DNA. No translation available.
AC073650 Genomic DNA. No translation available.
AC145422 Genomic DNA. No translation available.
AL133572 mRNA. Translation: CAB63721.2.
AB031230 mRNA. Translation: BAA97672.1.
BC008735 mRNA. Translation: AAH08735.2. Different initiation.
CCDSiCCDS41849.1. [Q8NHM5-4]
CCDS41850.1. [Q8NHM5-1]
PIRiT43477.
RefSeqiNP_001005366.1. NM_001005366.1. [Q8NHM5-4]
NP_115979.3. NM_032590.4. [Q8NHM5-1]
UniGeneiHs.524800.

Genome annotation databases

EnsembliENST00000377069; ENSP00000366269; ENSG00000089094. [Q8NHM5-4]
ENST00000377071; ENSP00000366271; ENSG00000089094. [Q8NHM5-1]
ENST00000542973; ENSP00000437821; ENSG00000089094.
GeneIDi84678.
KEGGihsa:84678.
UCSCiuc001uaq.3. human. [Q8NHM5-1]
uc001uas.3. human. [Q8NHM5-4]

Polymorphism databases

DMDMi51316032.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ459424 mRNA. Translation: CAD30700.1 .
AK027440 mRNA. Translation: BAB55112.1 . Different initiation.
AK027692 mRNA. Translation: BAB55301.1 . Different initiation.
AK074718 mRNA. Translation: BAC11159.1 . Different initiation.
AK127328 mRNA. Translation: BAG54483.1 .
AC048337 Genomic DNA. No translation available.
AC073650 Genomic DNA. No translation available.
AC145422 Genomic DNA. No translation available.
AL133572 mRNA. Translation: CAB63721.2 .
AB031230 mRNA. Translation: BAA97672.1 .
BC008735 mRNA. Translation: AAH08735.2 . Different initiation.
CCDSi CCDS41849.1. [Q8NHM5-4 ]
CCDS41850.1. [Q8NHM5-1 ]
PIRi T43477.
RefSeqi NP_001005366.1. NM_001005366.1. [Q8NHM5-4 ]
NP_115979.3. NM_032590.4. [Q8NHM5-1 ]
UniGenei Hs.524800.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4O64 X-ray 2.13 A/B/C 607-723 [» ]
ProteinModelPortali Q8NHM5.
SMRi Q8NHM5. Positions 66-392, 508-573, 608-723, 1068-1333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124197. 19 interactions.
IntActi Q8NHM5. 3 interactions.
STRINGi 9606.ENSP00000366271.

PTM databases

PhosphoSitei Q8NHM5.

Polymorphism databases

DMDMi 51316032.

Proteomic databases

MaxQBi Q8NHM5.
PaxDbi Q8NHM5.
PRIDEi Q8NHM5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377069 ; ENSP00000366269 ; ENSG00000089094 . [Q8NHM5-4 ]
ENST00000377071 ; ENSP00000366271 ; ENSG00000089094 . [Q8NHM5-1 ]
ENST00000542973 ; ENSP00000437821 ; ENSG00000089094 .
GeneIDi 84678.
KEGGi hsa:84678.
UCSCi uc001uaq.3. human. [Q8NHM5-1 ]
uc001uas.3. human. [Q8NHM5-4 ]

Organism-specific databases

CTDi 84678.
GeneCardsi GC12M121866.
HGNCi HGNC:13610. KDM2B.
MIMi 609078. gene.
neXtProti NX_Q8NHM5.
PharmGKBi PA164721242.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG290496.
GeneTreei ENSGT00550000074396.
HOGENOMi HOG000007396.
InParanoidi Q8NHM5.
KOi K10276.
OMAi NAEDRMA.
OrthoDBi EOG78SQH0.
PhylomeDBi Q8NHM5.
TreeFami TF106480.

Enzyme and pathway databases

Reactomei REACT_228178. HDMs demethylate histones.
SignaLinki Q8NHM5.

Miscellaneous databases

ChiTaRSi KDM2B. human.
GenomeRNAii 84678.
NextBioi 74711.
PROi Q8NHM5.
SOURCEi Search...

Gene expression databases

Bgeei Q8NHM5.
CleanExi HS_FBXL10.
ExpressionAtlasi Q8NHM5. baseline and differential.
Genevestigatori Q8NHM5.

Family and domain databases

InterProi IPR001810. F-box_dom.
IPR003347. JmjC_dom.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
[Graphical view ]
Pfami PF00646. F-box. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view ]
SMARTi SM00256. FBOX. 1 hit.
SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS51184. JMJC. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "JEMMA (Jumonji domain, EMSY-interactor, methyltransferase motif) is a novel protein which interacts with EMSY."
    Hughes-Davies L.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-1336 (ISOFORM 1).
    Tissue: Hippocampus.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1336 (ISOFORM 3).
    Tissue: Testis.
  5. Fujino T., Hasegawa M., Shibata S., Kishimoto T., Imai S., Takano T.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 480-1336 (ISOFORM 2).
    Tissue: Fibroblast.
  6. "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 710-1336 (ISOFORM 1).
    Tissue: Brain.
  7. "Histone demethylation by a family of JmjC domain-containing proteins."
    Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., Tempst P., Zhang Y.
    Nature 439:811-816(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY.
  8. "JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes."
    Frescas D., Guardavaccaro D., Bassermann F., Koyama-Nasu R., Pagano M.
    Nature 450:309-313(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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 THR-493; SER-975 AND SER-979, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-474; SER-477; THR-493 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKDM2B_HUMAN
AccessioniPrimary (citable) accession number: Q8NHM5
Secondary accession number(s): A8MRS1
, Q8NCI2, Q96HC7, Q96SL0, Q96T03, Q9NS96, Q9UF75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2002
Last modified: November 26, 2014
This is version 122 of the entry and version 1 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. 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

External Data

Dasty 3