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Protein

Lysine-specific demethylase 2B

Gene

Kdm2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei208 – 2081SubstrateBy similarity
Metal bindingi211 – 2111Iron; catalyticPROSITE-ProRule annotation
Metal bindingi213 – 2131Iron; catalyticPROSITE-ProRule annotation
Binding sitei228 – 2281SubstrateBy similarity
Metal bindingi283 – 2831Iron; catalyticPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri579 – 62547CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri632 – 69867PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • histone demethylase activity Source: BHF-UCL
  • histone demethylase activity (H3-K36 specific) Source: UniProtKB-EC
  • RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  • rRNA binding Source: UniProtKB-KW
  • zinc ion binding Source: InterPro

GO - Biological processi

  • embryonic camera-type eye morphogenesis Source: BHF-UCL
  • forebrain development Source: BHF-UCL
  • fourth ventricle development Source: BHF-UCL
  • hindbrain development Source: BHF-UCL
  • histone H2A monoubiquitination Source: MGI
  • histone H3-K36 demethylation Source: MGI
  • initiation of neural tube closure Source: BHF-UCL
  • lateral ventricle development Source: BHF-UCL
  • midbrain development Source: BHF-UCL
  • midbrain-hindbrain boundary morphogenesis Source: BHF-UCL
  • negative regulation of neural precursor cell proliferation Source: BHF-UCL
  • negative regulation of neuron apoptotic process Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of cell growth Source: MGI
  • positive regulation of stem cell population maintenance Source: MGI
  • spermatogenesis Source: BHF-UCL
  • third ventricle development Source: BHF-UCL
  • 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

BRENDAi1.14.11.27. 3474.
ReactomeiR-MMU-3214842. HDMs demethylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 2B (EC:1.14.11.27)
Alternative name(s):
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
[Histone-H3]-lysine-36 demethylase 1B
Gene namesi
Name:Kdm2b
Synonyms:Fbl10, Fbxl10, Jhdm1b, Kiaa3014
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1354737. Kdm2b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13091309Lysine-specific demethylase 2BPRO_0000119854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei447 – 4471PhosphoserineBy similarity
Modified residuei450 – 4501PhosphoserineBy similarity
Modified residuei466 – 4661PhosphothreonineBy similarity
Modified residuei470 – 4701PhosphoserineBy similarity
Cross-linki863 – 863Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei948 – 9481PhosphoserineBy similarity
Modified residuei952 – 9521PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6P1G2.
MaxQBiQ6P1G2.
PaxDbiQ6P1G2.
PRIDEiQ6P1G2.

PTM databases

iPTMnetiQ6P1G2.
PhosphoSiteiQ6P1G2.

Expressioni

Gene expression databases

BgeeiQ6P1G2.
CleanExiMM_FBXL10.
ExpressionAtlasiQ6P1G2. baseline and differential.
GenevisibleiQ6P1G2. MM.

Interactioni

Subunit structurei

Directly interacts with SKP1 and CUL1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Rnf2Q9CQJ44EBI-1216214,EBI-927321

Protein-protein interaction databases

BioGridi205978. 19 interactions.
DIPiDIP-46351N.
IntActiQ6P1G2. 11 interactions.
STRINGi10090.ENSMUSP00000038229.

Structurei

3D structure databases

ProteinModelPortaliQ6P1G2.
SMRiQ6P1G2. Positions 35-361, 481-546, 581-696.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 315169JmjCPROSITE-ProRule annotationAdd
BLAST
Domaini1032 – 107847F-boxAdd
BLAST
Repeati1106 – 112722LRR 1Add
BLAST
Repeati1129 – 115527LRR 2Add
BLAST
Repeati1195 – 122026LRR 3Add
BLAST
Repeati1221 – 125030LRR 4Add
BLAST
Repeati1251 – 127525LRR 5Add
BLAST
Repeati1276 – 130934LRR 6Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili916 – 94429Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi378 – 40326Glu-richAdd
BLAST

Domaini

The JmjC domain mediates demethylation activity. It is also required for repression of ribosomal RNA genes (By similarity).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 6 LRR (leucine-rich) repeats.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri579 – 62547CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri632 – 69867PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1633. Eukaryota.
KOG1947. Eukaryota.
ENOG410XQXU. LUCA.
GeneTreeiENSGT00550000074396.
HOGENOMiHOG000007396.
InParanoidiQ6P1G2.
KOiK10276.
OMAiEEACDQQ.
OrthoDBiEOG78SQH0.
PhylomeDBiQ6P1G2.
TreeFamiTF106480.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR003347. JmjC_dom.
IPR032675. L_dom-like.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF16866. PHD_4. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00367. LRR_CC. 5 hits.
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. AlignAdd to basket

Isoform 1 (identifier: Q6P1G2-1) [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
MEAEKDSGRR LRAIDRQRYD ENEDLSDVEE IVSVRGFSLE EKLRSQLYQG
60 70 80 90 100
DFVHAMEGKD FNYEYVQREA LRVPLVFRDK DGLGIKMPDP DFTVRDVKLL
110 120 130 140 150
VGSRRLVDVM DVNTQKGTEM SMSQFVRYYE TPEAQRDKLY NVISLEFSHT
160 170 180 190 200
KLEHLVKRPT VVDLVDWVDN MWPQHLKEKQ TEATNALAEM KYPKVKKYCL
210 220 230 240 250
MSVKGCFTDF HIDFGGTSVW YHVFRGGKIF WLIPPTLHNL ALYEEWVLSG
260 270 280 290 300
KQSDIFLGDR VERCQRIELK QGYTFFIPSG WIHAVYTPVD SLVFGGNILH
310 320 330 340 350
SFNVPMQLRI YEIEDRTRVQ PKFRYPFYYE MCWYVLERYV YCVTQRSYLT
360 370 380 390 400
QEYQRELMLI DAPRKTSVDG FSSDSWLDME EESCEQQPQE EEEEEEDKEE
410 420 430 440 450
EGDGADKTPK PPTDDPTSPT STPPEDQDST GKKPKAPAIR FLKRTLSNES
460 470 480 490 500
EESVKSTSMP TDDPKTPTGS PATEVSTKWT HLTEFELKGL KALVEKLESL
510 520 530 540 550
PENKKCVPEG IEDPQALLEG VKNVLKEHVD DDPTLAITGV PVVSWPKKTA
560 570 580 590 600
KNRVVGRPKG KLGPASAVKL AANRTTAGAR RRRTRCRKCE ACLRTECGEC
610 620 630 640 650
HFCKDMKKFG GPGRMKQSCI MRQCIAPVLP HTAVCLVCGE AGKEDTVEEE
660 670 680 690 700
EGKFNLMLME CSICNEIIHP GCLKIKESEG VVNDELPNCW ECPKCNHAGK
710 720 730 740 750
TGKQKRGPGF KYASNLPGSL LKEQKMNRDN KEGQEPAKRR SECEEAPRRR
760 770 780 790 800
SDEHPKKVPA DGILRRKSDD VHLRRKRKYE KPQELSGRKR ASSLQTSPGS
810 820 830 840 850
SSHLSPRPPL GSSLSPWWRS SLTYFQQQLK PGKEDKLFRK KRRSWKNAED
860 870 880 890 900
RLSLANKPLR RFKQEPEDDL PEAPPKTRES DQSRSSSPTA GPSTEGAEGP
910 920 930 940 950
EEKKKVKMRR KRRLVNKELS KELSKELNHE IQKTESTLAH ESQQPIKSEP
960 970 980 990 1000
ESENDEPKRP LSHCERPHRF SKGLNGTPRE LRHSLGPGLR SPPRVMSRPP
1010 1020 1030 1040 1050
PSASPPKCIQ MERHVIRPPP ISPPPDSLPL DDGAAHVMHR EVWMAVFSYL
1060 1070 1080 1090 1100
SHRDLCVCMR VCRTWNRWCC DKRLWTRIDL NRCKSITPLM LSGIIRRQPV
1110 1120 1130 1140 1150
SLDLSWTNIS KKQLSWLINR LPGLRDLVLS GCSWIAVSAL CSSSCPLLRT
1160 1170 1180 1190 1200
LDVQWVEGLK DAQMRDLLSP PTDNRPGQMD NRSKLRNIVE LRLAGLDITD
1210 1220 1230 1240 1250
VSLRLIIRHM PLLSKLQLSY CNHINDQSIN LLTAVGTTTR DSLTEVNLSD
1260 1270 1280 1290 1300
CNKVTDLCLS FFKRCGNICH IDLRYCKQVT KEGCEQFIAE MSVSVQFGQV

EEKLLQKLS
Length:1,309
Mass (Da):149,733
Last modified:July 5, 2004 - v1
Checksum:i5BD203C3535C4D88
GO
Isoform 2 (identifier: Q6P1G2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-533: Missing.
     534-551: TLAITGVPVVSWPKKTAK → MAMSVSAEDDDYESEPDQ

Show »
Length:776
Mass (Da):88,005
Checksum:iEA6E56115E4B550E
GO
Isoform 3 (identifier: Q6P1G2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     627-656: PVLPHTAVCLVCGEAGKEDTVEEEEGKFNL → VSAQKAQAGLMQGLPAICPALGLLCGMGEV
     657-1309: Missing.

Note: No experimental confirmation available.
Show »
Length:656
Mass (Da):74,951
Checksum:iF2917493A7697ED2
GO
Isoform 4 (identifier: Q6P1G2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-1196: Missing.

Note: No experimental confirmation available.
Show »
Length:114
Mass (Da):12,956
Checksum:iFF378CEB4B3674FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti461 – 4611T → M in BAC98289 (PubMed:14621295).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 533533Missing in isoform 2. 1 PublicationVSP_011342Add
BLAST
Alternative sequencei2 – 11961195Missing in isoform 4. 1 PublicationVSP_019003Add
BLAST
Alternative sequencei534 – 55118TLAIT…KKTAK → MAMSVSAEDDDYESEPDQ in isoform 2. 1 PublicationVSP_011343Add
BLAST
Alternative sequencei627 – 65630PVLPH…GKFNL → VSAQKAQAGLMQGLPAICPA LGLLCGMGEV in isoform 3. 1 PublicationVSP_017477Add
BLAST
Alternative sequencei657 – 1309653Missing in isoform 3. 1 PublicationVSP_017478Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012952 mRNA. Translation: BAB28568.2.
AK043352 mRNA. Translation: BAE20639.1.
BC057622 mRNA. Translation: AAH57622.1.
BC065090 mRNA. Translation: AAH65090.1.
AK129479 mRNA. Translation: BAC98289.1.
AF176524 mRNA. Translation: AAF09133.1.
CCDSiCCDS19657.1. [Q6P1G2-2]
CCDS39259.1. [Q6P1G2-1]
RefSeqiNP_001003953.1. NM_001003953.2. [Q6P1G2-1]
NP_038938.1. NM_013910.2. [Q6P1G2-2]
UniGeneiMm.86406.

Genome annotation databases

EnsembliENSMUST00000031435; ENSMUSP00000031435; ENSMUSG00000029475. [Q6P1G2-2]
ENSMUST00000046073; ENSMUSP00000038229; ENSMUSG00000029475. [Q6P1G2-1]
GeneIDi30841.
KEGGimmu:30841.
UCSCiuc008zmq.2. mouse. [Q6P1G2-2]
uc008zms.3. mouse. [Q6P1G2-1]
uc008zmu.2. mouse. [Q6P1G2-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012952 mRNA. Translation: BAB28568.2.
AK043352 mRNA. Translation: BAE20639.1.
BC057622 mRNA. Translation: AAH57622.1.
BC065090 mRNA. Translation: AAH65090.1.
AK129479 mRNA. Translation: BAC98289.1.
AF176524 mRNA. Translation: AAF09133.1.
CCDSiCCDS19657.1. [Q6P1G2-2]
CCDS39259.1. [Q6P1G2-1]
RefSeqiNP_001003953.1. NM_001003953.2. [Q6P1G2-1]
NP_038938.1. NM_013910.2. [Q6P1G2-2]
UniGeneiMm.86406.

3D structure databases

ProteinModelPortaliQ6P1G2.
SMRiQ6P1G2. Positions 35-361, 481-546, 581-696.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205978. 19 interactions.
DIPiDIP-46351N.
IntActiQ6P1G2. 11 interactions.
STRINGi10090.ENSMUSP00000038229.

PTM databases

iPTMnetiQ6P1G2.
PhosphoSiteiQ6P1G2.

Proteomic databases

EPDiQ6P1G2.
MaxQBiQ6P1G2.
PaxDbiQ6P1G2.
PRIDEiQ6P1G2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031435; ENSMUSP00000031435; ENSMUSG00000029475. [Q6P1G2-2]
ENSMUST00000046073; ENSMUSP00000038229; ENSMUSG00000029475. [Q6P1G2-1]
GeneIDi30841.
KEGGimmu:30841.
UCSCiuc008zmq.2. mouse. [Q6P1G2-2]
uc008zms.3. mouse. [Q6P1G2-1]
uc008zmu.2. mouse. [Q6P1G2-3]

Organism-specific databases

CTDi84678.
MGIiMGI:1354737. Kdm2b.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1633. Eukaryota.
KOG1947. Eukaryota.
ENOG410XQXU. LUCA.
GeneTreeiENSGT00550000074396.
HOGENOMiHOG000007396.
InParanoidiQ6P1G2.
KOiK10276.
OMAiEEACDQQ.
OrthoDBiEOG78SQH0.
PhylomeDBiQ6P1G2.
TreeFamiTF106480.

Enzyme and pathway databases

BRENDAi1.14.11.27. 3474.
ReactomeiR-MMU-3214842. HDMs demethylate histones.

Miscellaneous databases

PROiQ6P1G2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P1G2.
CleanExiMM_FBXL10.
ExpressionAtlasiQ6P1G2. baseline and differential.
GenevisibleiQ6P1G2. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR003347. JmjC_dom.
IPR032675. L_dom-like.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF16866. PHD_4. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00367. LRR_CC. 5 hits.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Cerebellum and Embryo.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1309 (ISOFORM 1).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1011-1309 (ISOFORMS 1/2).
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiKDM2B_MOUSE
AccessioniPrimary (citable) accession number: Q6P1G2
Secondary accession number(s): Q3V396
, Q6PFD0, Q6ZPE8, Q9CSF7, Q9QZN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.