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Q8BW72

- KDM4A_MOUSE

UniProt

Q8BW72 - KDM4A_MOUSE

Protein

Lysine-specific demethylase 4A

Gene

Kdm4a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively By similarity.By similarity

    Cofactori

    Binds 1 Fe2+ ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei132 – 1321Alpha-ketoglutarateBy similarity
    Metal bindingi188 – 1881Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi190 – 1901Iron; catalyticPROSITE-ProRule annotation
    Binding sitei198 – 1981Alpha-ketoglutarateBy similarity
    Binding sitei206 – 2061Alpha-ketoglutarateBy similarity
    Metal bindingi234 – 2341ZincBy similarity
    Metal bindingi240 – 2401ZincBy similarity
    Metal bindingi276 – 2761Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi306 – 3061ZincBy similarity
    Metal bindingi308 – 3081ZincBy similarity
    Binding sitei945 – 9451Histone H3K4me3By similarity
    Binding sitei967 – 9671Histone H3K4me3By similarity
    Binding sitei973 – 9731Histone H3K4me3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri709 – 76759PHD-type 1Add
    BLAST
    Zinc fingeri829 – 88557PHD-type 2Add
    BLAST

    GO - Molecular functioni

    1. histone demethylase activity (H3-K36 specific) Source: Ensembl
    2. methylated histone binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cardiac muscle hypertrophy in response to stress Source: MGI
    2. negative regulation of transcription, DNA-templated Source: Ensembl
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 4A (EC:1.14.11.-)
    Alternative name(s):
    JmjC domain-containing histone demethylation protein 3A
    Jumonji domain-containing protein 2A
    Gene namesi
    Name:Kdm4a
    Synonyms:Jhdm3a, Jmjd2, Jmjd2a, Kiaa0677
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:2446210. Kdm4a.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. cytoplasm Source: Ensembl
    3. nucleolus Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10641063Lysine-specific demethylase 4APRO_0000183173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Post-translational modificationi

    Ubiquitinated by RNF8 and RNF168 following DNA damage, leading to its degradation. Degradation promotes accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited By similarity.By similarity

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    PaxDbiQ8BW72.
    PRIDEiQ8BW72.

    PTM databases

    PhosphoSiteiQ8BW72.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    BgeeiQ8BW72.
    CleanExiMM_JMJD2A.
    GenevestigatoriQ8BW72.

    Interactioni

    Subunit structurei

    Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3. Interacts with RB and NCOR1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi230999. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BW72.
    SMRiQ8BW72. Positions 3-355, 733-770, 821-869, 898-1011.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 5643JmjNPROSITE-ProRule annotationAdd
    BLAST
    Domaini142 – 308167JmjCPROSITE-ProRule annotationAdd
    BLAST
    Domaini897 – 95458Tudor 1Add
    BLAST
    Domaini955 – 101157Tudor 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni597 – 63842Interaction with NCOR1By similarityAdd
    BLAST

    Domaini

    The 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue (H3K4me). Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' (H3K4me3) is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are also able to bind trimethylated histone H3 'Lys-9' (H3K9me3), di- and trimethylated H4 'Lys-20' (H4K20me2 and H4K20me3). Has high affinity for H4K20me2, blocking recruitment of proteins such as TP53BP1 By similarity.By similarity

    Sequence similaritiesi

    Belongs to the JHDM3 histone demethylase family.Curated
    Contains 1 JmjC domain.PROSITE-ProRule annotation
    Contains 1 JmjN domain.PROSITE-ProRule annotation
    Contains 2 PHD-type zinc fingers.Curated
    Contains 2 Tudor domains.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri709 – 76759PHD-type 1Add
    BLAST
    Zinc fingeri829 – 88557PHD-type 2Add
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5141.
    GeneTreeiENSGT00530000063342.
    HOVERGENiHBG080483.
    InParanoidiA2A8L8.
    KOiK06709.
    OMAiRKRTAGC.
    OrthoDBiEOG7TQV03.
    TreeFamiTF106449.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR003347. JmjC_dom.
    IPR003349. TF_JmjN.
    IPR002999. Tudor.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF02373. JmjC. 1 hit.
    PF02375. JmjN. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    SM00249. PHD. 2 hits.
    SM00333. TUDOR. 2 hits.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BW72-1) [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

    MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP     50
    KEWKPRTSYD DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI 100
    ANSDKYCTPR YSEFEELERK YWKNLTFNPP IYGADVNGTL YEQHVDEWNI 150
    GRLKTILDLV EKESGITIEG VNTPYLYFGM WKTSFAWHTE DMDLYSINYL 200
    HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH KMTLISPLML 250
    KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATRRWIEYG 300
    KQAVLCSCRK DMVKISMDVF VRRFQPERYK LWKAGKDSMV IDHTLPTPEA 350
    AEFLKDSGGL TPRAGSEECP EEDVEAADQG EEGDVKRSLA KHRIGTKRHR 400
    VCLEIPQEVS QSELFPKEEL SSGQYEMTEC PATLAPVRPT HSSVRQVEDS 450
    LPFPDYSDPT EVKFEELKNV KLEEEDEEDE PEAAALDLSV NPASVGGRLV 500
    FSGSKKKSSS SLGSTSSQDS VSSDSETAES VSCQGQEKTG VLTVHSYARG 550
    DGKAATGEPS VKKKRSAPRS ISEQELAEVA DEYMLSLEEN KKTKGRRQPL 600
    SKLPRHHPLV LQECGSDDET SEQLTPEEEA EETEAWAKPL SQLWQNRPPN 650
    FEAEKEFNEI MAQQAPHCAV CMIFQTYHQV EFGAFSQSCG DASEPAAQTQ 700
    RTKPLIPEMC FTTTGCSTDI NLSTPYLEED GTSMLVSCKK CSVRVHASCY 750
    GVPPAKASEE WMCSRCSANA LEEDCCLCSL RGGALQRAND DRWVHVSCAV 800
    AILEARFVNI AERSPVDVSK IPLPRFKLKC VFCKKRRKRN AGCCVQCSHG 850
    RCPTAFHVSC AQAAGVMMQP DDWPFVVFIT CFRHKIPNLE RAKGALLSIT 900
    AGQKVISKHK NGRFYQCEVV RLTTETFYEV NFDDGSFSDN LYPEDIVSQD 950
    CLQLGPPAEG EVVQVRWTDG QVYGAKFVAS HPIQMYQVEF EDGSQLVVKR 1000
    DDVYTLDEEL PKRVKSRLSV ASDMRFNEIF TEKEVKQEKK RQRVINSRYR 1050
    EDYIEPALYR AIME 1064
    Length:1,064
    Mass (Da):120,334
    Last modified:July 27, 2011 - v3
    Checksum:i92FB3E363FDF9E7D
    GO
    Isoform 2 (identifier: Q8BW72-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         948-1033: SQDCLQLGPP...MRFNEIFTEK → MSESGFWQHF...ISDQIISNSI
         1034-1064: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,033
    Mass (Da):115,963
    Checksum:iA0485D01A1AEDF4D
    GO

    Sequence cautioni

    The sequence BAC97997.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti339 – 3391M → T in BAC97997. (PubMed:14621295)Curated
    Sequence conflicti339 – 3391M → T in BAE26217. (PubMed:16141072)Curated
    Sequence conflicti339 – 3391M → T in AAH28866. (PubMed:15489334)Curated
    Sequence conflicti1007 – 10071D → G in BAE26776. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei948 – 103386SQDCL…IFTEK → MSESGFWQHFGSSGTSSCYC RLDDCGLFACPWSVSKQKEP LFPGSLSRKSGHAGALSFPE EFRGVSVPCSPLKYAYISDQ IISNSI in isoform 2. 1 PublicationVSP_016144Add
    BLAST
    Alternative sequencei1034 – 106431Missing in isoform 2. 1 PublicationVSP_016145Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK129187 mRNA. Translation: BAC97997.1. Different initiation.
    AK054095 mRNA. Translation: BAC35653.1.
    AK136085 mRNA. Translation: BAE22812.1.
    AK145066 mRNA. Translation: BAE26217.1.
    AK145947 mRNA. Translation: BAE26776.1.
    AL626764 Genomic DNA. Translation: CAM27385.1.
    BC028866 mRNA. Translation: AAH28866.1.
    CCDSiCCDS51282.1. [Q8BW72-1]
    RefSeqiNP_001155295.1. NM_001161823.1. [Q8BW72-1]
    NP_759014.2. NM_172382.2.
    XP_006503073.1. XM_006503010.1. [Q8BW72-1]
    UniGeneiMm.234234.

    Genome annotation databases

    EnsembliENSMUST00000097911; ENSMUSP00000095524; ENSMUSG00000033326. [Q8BW72-1]
    ENSMUST00000106403; ENSMUSP00000102011; ENSMUSG00000033326. [Q8BW72-1]
    ENSMUST00000106406; ENSMUSP00000102014; ENSMUSG00000033326. [Q8BW72-1]
    GeneIDi230674.
    KEGGimmu:230674.
    UCSCiuc008ujn.2. mouse. [Q8BW72-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK129187 mRNA. Translation: BAC97997.1 . Different initiation.
    AK054095 mRNA. Translation: BAC35653.1 .
    AK136085 mRNA. Translation: BAE22812.1 .
    AK145066 mRNA. Translation: BAE26217.1 .
    AK145947 mRNA. Translation: BAE26776.1 .
    AL626764 Genomic DNA. Translation: CAM27385.1 .
    BC028866 mRNA. Translation: AAH28866.1 .
    CCDSi CCDS51282.1. [Q8BW72-1 ]
    RefSeqi NP_001155295.1. NM_001161823.1. [Q8BW72-1 ]
    NP_759014.2. NM_172382.2.
    XP_006503073.1. XM_006503010.1. [Q8BW72-1 ]
    UniGenei Mm.234234.

    3D structure databases

    ProteinModelPortali Q8BW72.
    SMRi Q8BW72. Positions 3-355, 733-770, 821-869, 898-1011.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230999. 4 interactions.

    PTM databases

    PhosphoSitei Q8BW72.

    Proteomic databases

    PaxDbi Q8BW72.
    PRIDEi Q8BW72.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000097911 ; ENSMUSP00000095524 ; ENSMUSG00000033326 . [Q8BW72-1 ]
    ENSMUST00000106403 ; ENSMUSP00000102011 ; ENSMUSG00000033326 . [Q8BW72-1 ]
    ENSMUST00000106406 ; ENSMUSP00000102014 ; ENSMUSG00000033326 . [Q8BW72-1 ]
    GeneIDi 230674.
    KEGGi mmu:230674.
    UCSCi uc008ujn.2. mouse. [Q8BW72-1 ]

    Organism-specific databases

    CTDi 9682.
    MGIi MGI:2446210. Kdm4a.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5141.
    GeneTreei ENSGT00530000063342.
    HOVERGENi HBG080483.
    InParanoidi A2A8L8.
    KOi K06709.
    OMAi RKRTAGC.
    OrthoDBi EOG7TQV03.
    TreeFami TF106449.

    Miscellaneous databases

    ChiTaRSi Kdm4A. mouse.
    NextBioi 380043.
    PROi Q8BW72.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BW72.
    CleanExi MM_JMJD2A.
    Genevestigatori Q8BW72.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR003347. JmjC_dom.
    IPR003349. TF_JmjN.
    IPR002999. Tudor.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF02373. JmjC. 1 hit.
    PF02375. JmjN. 1 hit.
    [Graphical view ]
    SMARTi SM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    SM00249. PHD. 2 hits.
    SM00333. TUDOR. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 1).
      Tissue: Embryonic tail.
    2. "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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Embryo, Mammary gland, Oviduct and Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Colon.
    5. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 499-505, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    6. "JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2)."
      Zhang D., Yoon H.-G., Wong J.
      Mol. Cell. Biol. 25:6404-6414(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiKDM4A_MOUSE
    AccessioniPrimary (citable) accession number: Q8BW72
    Secondary accession number(s): A2A8L8
    , Q3UKM5, Q3UM81, Q3UWV2, Q6ZQ72, Q8K137
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 106 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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

    External Data

    Dasty 3