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Q8NB78

- KDM1B_HUMAN

UniProt

Q8NB78 - KDM1B_HUMAN

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Protein

Lysine-specific histone demethylase 1B

Gene

KDM1B

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

Functioni

Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4 (By similarity).By similarity

Cofactori

FAD.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri133 – 19361CW-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi383 – 43957FADSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. flavin adenine dinucleotide binding Source: Ensembl
  3. histone demethylase activity (H3-dimethyl-K4 specific) Source: UniProtKB
  4. histone demethylase activity (H3-monomethyl-K4 specific) Source: UniProtKB
  5. oxidoreductase activity Source: UniProtKB-KW
  6. zinc ion binding Source: Ensembl

GO - Biological processi

  1. DNA methylation involved in gamete generation Source: Ensembl
  2. histone H3-K4 demethylation Source: UniProtKB
  3. multicellular organismal development Source: UniProtKB-KW
  4. regulation of DNA methylation Source: UniProtKB
  5. regulation of gene expression by genetic imprinting Source: UniProtKB
  6. regulation of transcription, DNA-templated Source: UniProtKB-KW
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Oxidoreductase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

FAD, Flavoprotein, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific histone demethylase 1B (EC:1.-.-.-)
Alternative name(s):
Flavin-containing amine oxidase domain-containing protein 1
Lysine-specific histone demethylase 2
Gene namesi
Name:KDM1B
Synonyms:AOF1, C6orf193, LSD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:21577. KDM1B.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162379723.
PA165617946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 822822Lysine-specific histone demethylase 1BPRO_0000247336Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine3 Publications
Modified residuei247 – 2471Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8NB78.
PaxDbiQ8NB78.
PRIDEiQ8NB78.

PTM databases

PhosphoSiteiQ8NB78.

Expressioni

Gene expression databases

BgeeiQ8NB78.
CleanExiHS_AOF1.
ExpressionAtlasiQ8NB78. baseline and differential.
GenevestigatoriQ8NB78.

Organism-specific databases

HPAiHPA031269.
HPA055597.

Interactioni

Subunit structurei

Does not form a complex with RCOR1/CoREST.By similarity

Protein-protein interaction databases

BioGridi128743. 14 interactions.
IntActiQ8NB78. 1 interaction.
STRINGi9606.ENSP00000297792.

Structurei

Secondary structure

1
822
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 555
Beta strandi70 – 723
Beta strandi75 – 773
Beta strandi82 – 865
Beta strandi89 – 924
Helixi93 – 1008
Helixi104 – 1063
Helixi107 – 11610
Turni117 – 1204
Helixi127 – 1348
Beta strandi139 – 1413
Turni145 – 1473
Beta strandi150 – 1523
Helixi161 – 1666
Beta strandi173 – 1753
Beta strandi180 – 1823
Helixi184 – 1863
Helixi192 – 1954
Helixi199 – 2035
Beta strandi211 – 2133
Helixi217 – 2193
Helixi225 – 2273
Helixi267 – 2693
Beta strandi286 – 2883
Helixi291 – 2966
Helixi298 – 3003
Helixi305 – 32016
Helixi328 – 3314
Helixi332 – 3343
Helixi341 – 35818
Beta strandi361 – 3633
Helixi371 – 3733
Helixi378 – 3803
Beta strandi384 – 3885
Helixi392 – 40413
Beta strandi407 – 4115
Beta strandi413 – 4175
Beta strandi427 – 4304
Beta strandi432 – 4354
Beta strandi438 – 4403
Helixi446 – 4549
Beta strandi458 – 4603
Beta strandi467 – 4693
Helixi477 – 49721
Helixi498 – 5003
Helixi503 – 5053
Helixi509 – 52315
Helixi530 – 54718
Turni551 – 5533
Turni556 – 5605
Helixi561 – 5644
Beta strandi572 – 5743
Helixi580 – 5878
Beta strandi592 – 5954
Beta strandi598 – 6025
Beta strandi604 – 6129
Beta strandi617 – 6259
Helixi629 – 6346
Beta strandi637 – 6415
Helixi645 – 6539
Beta strandi654 – 6574
Beta strandi660 – 6656
Helixi672 – 6754
Beta strandi679 – 6835
Beta strandi686 – 6883
Turni689 – 6924
Beta strandi693 – 7008
Beta strandi708 – 7136
Helixi716 – 7205
Turni721 – 7233
Helixi726 – 74015
Turni741 – 7433
Beta strandi750 – 7545
Helixi757 – 7593
Turni761 – 7633
Beta strandi766 – 7716
Helixi777 – 7837
Turni787 – 7893
Beta strandi790 – 7923
Helixi795 – 7973
Beta strandi799 – 8013
Helixi805 – 82117

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FWEX-ray2.13A30-822[»]
4FWFX-ray2.70A30-822[»]
4FWJX-ray2.90A/B30-822[»]
4GU0X-ray3.10A/B/C/D51-822[»]
4GU1X-ray2.94A/B51-822[»]
4GURX-ray2.51A51-822[»]
4GUSX-ray2.23A51-822[»]
4GUTX-ray2.00A51-822[»]
4GUUX-ray2.30A51-822[»]
4HSUX-ray1.99A51-822[»]
ProteinModelPortaliQ8NB78.
SMRiQ8NB78. Positions 49-822.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini275 – 37399SWIRMPROSITE-ProRule annotationAdd
BLAST

Domaini

The SWIRM domain may act as an anchor site for a histone tail.By similarity

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated
Contains 1 CW-type zinc finger.PROSITE-ProRule annotation
Contains 1 SWIRM domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri133 – 19361CW-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG1231.
GeneTreeiENSGT00530000062888.
HOGENOMiHOG000230870.
HOVERGENiHBG079963.
InParanoidiQ8NB78.
OrthoDBiEOG7X9G66.
PhylomeDBiQ8NB78.
TreeFamiTF352593.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR009057. Homeodomain-like.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
IPR011124. Znf_CW.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
PF07496. zf-CW. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS50934. SWIRM. 1 hit.
PS51050. ZF_CW. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8NB78-1) [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
MATPRGRTKK KASFDHSPDS LPLRSSGRQA KKKATETTDE DEDGGSEKKY
60 70 80 90 100
RKCEKAGCTA TCPVCFASAS ERCAKNGYTS RWYHLSCGEH FCNECFDHYY
110 120 130 140 150
RSHKDGYDKY TTWKKIWTSN GKTEPSPKAF MADQQLPYWV QCTKPECRKW
160 170 180 190 200
RQLTKEIQLT PQIAKTYRCG MKPNTAIKPE TSDHCSLPED LRVLEVSNHW
210 220 230 240 250
WYSMLILPPL LKDSVAAPLL SAYYPDCVGM SPSCTSTNRA AATGNASPGK
260 270 280 290 300
LEHSKAALSV HVPGMNRYFQ PFYQPNECGK ALCVRPDVME LDELYEFPEY
310 320 330 340 350
SRDPTMYLAL RNLILALWYT NCKEALTPQK CIPHIIVRGL VRIRCVQEVE
360 370 380 390 400
RILYFMTRKG LINTGVLSVG ADQYLLPKDY HNKSVIIIGA GPAGLAAARQ
410 420 430 440 450
LHNFGIKVTV LEAKDRIGGR VWDDKSFKGV TVGRGAQIVN GCINNPVALM
460 470 480 490 500
CEQLGISMHK FGERCDLIQE GGRITDPTID KRMDFHFNAL LDVVSEWRKD
510 520 530 540 550
KTQLQDVPLG EKIEEIYKAF IKESGIQFSE LEGQVLQFHL SNLEYACGSN
560 570 580 590 600
LHQVSARSWD HNEFFAQFAG DHTLLTPGYS VIIEKLAEGL DIQLKSPVQC
610 620 630 640 650
IDYSGDEVQV TTTDGTGYSA QKVLVTVPLA LLQKGAIQFN PPLSEKKMKA
660 670 680 690 700
INSLGAGIIE KIALQFPYRF WDSKVQGADF FGHVPPSASK RGLFAVFYDM
710 720 730 740 750
DPQKKHSVLM SVIAGEAVAS VRTLDDKQVL QQCMATLREL FKEQEVPDPT
760 770 780 790 800
KYFVTRWSTD PWIQMAYSFV KTGGSGEAYD IIAEDIQGTV FFAGEATNRH
810 820
FPQTVTGAYL SGVREASKIA AF
Length:822
Mass (Da):92,098
Last modified:January 11, 2011 - v3
Checksum:i6C0A9BD6B2CEA2EA
GO
Isoform 2 (identifier: Q8NB78-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     192-323: Missing.
     453-552: Missing.

Note: No experimental confirmation available.

Show »
Length:590
Mass (Da):65,717
Checksum:iAFDC638DFD727A9E
GO
Isoform 4 (identifier: Q8NB78-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-647: Missing.

Note: No experimental confirmation available.

Show »
Length:175
Mass (Da):19,428
Checksum:i5571123B00CDE9E8
GO

Sequence cautioni

The sequence BAC03663.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti651 – 6511I → T in BAC86124. (PubMed:14702039)Curated
Sequence conflicti794 – 7952Missing in CAH10499. (PubMed:17974005)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 647647Missing in isoform 4. 1 PublicationVSP_019963Add
BLAST
Alternative sequencei192 – 323132Missing in isoform 2. 1 PublicationVSP_019964Add
BLAST
Alternative sequencei453 – 552100Missing in isoform 2. 1 PublicationVSP_019965Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK091217 mRNA. Translation: BAC03612.1.
AK091428 mRNA. Translation: BAC03663.1. Different initiation.
AK125318 mRNA. Translation: BAC86124.1.
AL589723, AL031774 Genomic DNA. Translation: CAM14159.1.
AL589723, AL031774 Genomic DNA. Translation: CAM14160.1.
AL031774, AL589723 Genomic DNA. Translation: CAM28216.1.
AL031774, AL589723 Genomic DNA. Translation: CAM28217.1.
CH471087 Genomic DNA. Translation: EAW55401.1.
CR627410 mRNA. Translation: CAH10499.1.
CCDSiCCDS34343.1. [Q8NB78-2]
RefSeqiNP_694587.3. NM_153042.3. [Q8NB78-2]
XP_005248983.1. XM_005248926.1. [Q8NB78-1]
UniGeneiHs.709336.

Genome annotation databases

EnsembliENST00000297792; ENSP00000297792; ENSG00000165097. [Q8NB78-2]
GeneIDi221656.
KEGGihsa:221656.
UCSCiuc003ncn.1. human. [Q8NB78-2]
uc003nco.1. human. [Q8NB78-1]
uc003ncp.1. human. [Q8NB78-4]

Polymorphism databases

DMDMi317373434.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK091217 mRNA. Translation: BAC03612.1 .
AK091428 mRNA. Translation: BAC03663.1 . Different initiation.
AK125318 mRNA. Translation: BAC86124.1 .
AL589723 , AL031774 Genomic DNA. Translation: CAM14159.1 .
AL589723 , AL031774 Genomic DNA. Translation: CAM14160.1 .
AL031774 , AL589723 Genomic DNA. Translation: CAM28216.1 .
AL031774 , AL589723 Genomic DNA. Translation: CAM28217.1 .
CH471087 Genomic DNA. Translation: EAW55401.1 .
CR627410 mRNA. Translation: CAH10499.1 .
CCDSi CCDS34343.1. [Q8NB78-2 ]
RefSeqi NP_694587.3. NM_153042.3. [Q8NB78-2 ]
XP_005248983.1. XM_005248926.1. [Q8NB78-1 ]
UniGenei Hs.709336.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4FWE X-ray 2.13 A 30-822 [» ]
4FWF X-ray 2.70 A 30-822 [» ]
4FWJ X-ray 2.90 A/B 30-822 [» ]
4GU0 X-ray 3.10 A/B/C/D 51-822 [» ]
4GU1 X-ray 2.94 A/B 51-822 [» ]
4GUR X-ray 2.51 A 51-822 [» ]
4GUS X-ray 2.23 A 51-822 [» ]
4GUT X-ray 2.00 A 51-822 [» ]
4GUU X-ray 2.30 A 51-822 [» ]
4HSU X-ray 1.99 A 51-822 [» ]
ProteinModelPortali Q8NB78.
SMRi Q8NB78. Positions 49-822.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128743. 14 interactions.
IntActi Q8NB78. 1 interaction.
STRINGi 9606.ENSP00000297792.

Chemistry

BindingDBi Q8NB78.
ChEMBLi CHEMBL1938208.

PTM databases

PhosphoSitei Q8NB78.

Polymorphism databases

DMDMi 317373434.

Proteomic databases

MaxQBi Q8NB78.
PaxDbi Q8NB78.
PRIDEi Q8NB78.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297792 ; ENSP00000297792 ; ENSG00000165097 . [Q8NB78-2 ]
GeneIDi 221656.
KEGGi hsa:221656.
UCSCi uc003ncn.1. human. [Q8NB78-2 ]
uc003nco.1. human. [Q8NB78-1 ]
uc003ncp.1. human. [Q8NB78-4 ]

Organism-specific databases

CTDi 221656.
GeneCardsi GC06P018156.
H-InvDB HIX0005608.
HGNCi HGNC:21577. KDM1B.
HPAi HPA031269.
HPA055597.
MIMi 613081. gene.
neXtProti NX_Q8NB78.
PharmGKBi PA162379723.
PA165617946.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1231.
GeneTreei ENSGT00530000062888.
HOGENOMi HOG000230870.
HOVERGENi HBG079963.
InParanoidi Q8NB78.
OrthoDBi EOG7X9G66.
PhylomeDBi Q8NB78.
TreeFami TF352593.

Miscellaneous databases

GenomeRNAii 221656.
NextBioi 91405.
PROi Q8NB78.
SOURCEi Search...

Gene expression databases

Bgeei Q8NB78.
CleanExi HS_AOF1.
ExpressionAtlasi Q8NB78. baseline and differential.
Genevestigatori Q8NB78.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR002937. Amino_oxidase.
IPR009057. Homeodomain-like.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
IPR011124. Znf_CW.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
PF07496. zf-CW. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
PROSITEi PS50934. SWIRM. 1 hit.
PS51050. ZF_CW. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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] (ISOFORMS 2 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-822 (ISOFORM 1).
    Tissue: Brain and Tongue.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-822 (ISOFORM 1).
    Tissue: Cervix.
  5. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-17 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiKDM1B_HUMAN
AccessioniPrimary (citable) accession number: Q8NB78
Secondary accession number(s): A2A2C5
, A2A2C6, Q5TGV3, Q6AI15, Q6ZUU4, Q8N258, Q96EL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 103 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 6
    Human chromosome 6: 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