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P16951

- ATF2_MOUSE

UniProt

P16951 - ATF2_MOUSE

Protein

Cyclic AMP-dependent transcription factor ATF-2

Gene

Atf2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type By similarity.By similarity

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri7 – 3125C2H2-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cAMP response element binding Source: Ensembl
    2. cAMP response element binding protein binding Source: Ensembl
    3. chromatin binding Source: MGI
    4. DNA binding Source: MGI
    5. histone acetyltransferase activity Source: UniProtKB
    6. metal ion binding Source: UniProtKB-KW
    7. protein binding Source: UniProtKB
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    9. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
    10. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. adipose tissue development Source: MGI
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. fat cell differentiation Source: MGI
    4. intra-S DNA damage checkpoint Source: UniProtKB
    5. outflow tract morphogenesis Source: MGI
    6. positive regulation of mitochondrial membrane permeability involved in apoptotic process Source: UniProtKB
    7. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    8. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    9. positive regulation of transforming growth factor beta2 production Source: MGI
    10. regulation of transcription, DNA-templated Source: UniProtKB
    11. response to osmotic stress Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Transferase

    Keywords - Biological processi

    DNA damage, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_204811. Activation of the AP-1 family of transcription factors.
    REACT_226917. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclic AMP-dependent transcription factor ATF-2 (EC:2.3.1.48)
    Short name:
    cAMP-dependent transcription factor ATF-2
    Alternative name(s):
    Activating transcription factor 2
    MXBP protein
    cAMP response element-binding protein CRE-BP1
    Gene namesi
    Name:Atf2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:109349. Atf2.

    Subcellular locationi

    Nucleus. Cytoplasm By similarity. Mitochondrion outer membrane By similarity
    Note: Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress and in disease states. Localizes at the mitochondrial outer membrane in response to genotoxic stress. Phosphorylation at Thr-34 is required for its nuclear localization and negatively regulates its mitochondrial localization. Colocalizes with the MRN complex in the IR-induced foci (IRIF) By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. membrane Source: MGI
    3. mitochondrial outer membrane Source: UniProtKB
    4. nucleus Source: MGI
    5. site of double-strand break Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 487487Cyclic AMP-dependent transcription factor ATF-2PRO_0000076578Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei34 – 341Phosphothreonine; by PKC/PRKCHBy similarity
    Modified residuei44 – 441Phosphoserine; by VRK1By similarity
    Modified residuei51 – 511Phosphothreonine; by MAPK11 and MAPK141 Publication
    Modified residuei53 – 531Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK31 Publication
    Modified residuei55 – 551Phosphothreonine; by VRK1By similarity
    Modified residuei72 – 721PhosphoserineBy similarity
    Modified residuei94 – 941PhosphoserineBy similarity
    Modified residuei98 – 981PhosphothreonineBy similarity
    Modified residuei103 – 1031Phosphoserine; by PKC/PRKCA and PKC/PRKCBBy similarity
    Modified residuei310 – 3101PhosphoserineBy similarity
    Modified residuei322 – 3221Phosphoserine; by PKC/PRKCA and PKC/PRKCBBy similarity
    Modified residuei339 – 3391N6-acetyllysineBy similarity
    Modified residuei349 – 3491Phosphoserine; by PKC/PRKCA and PKC/PRKCBBy similarity
    Modified residuei356 – 3561N6-acetyllysineBy similarity
    Modified residuei472 – 4721Phosphoserine; by ATMBy similarity
    Modified residuei480 – 4801Phosphoserine; by ATMBy similarity

    Post-translational modificationi

    Phosphorylation of Thr-51 by MAPK14 and MAPK11, and at Thr-53 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity By similarity. Phosphorylated by PLK3 following hyperosmotic stress. Also phosphorylated and activated by JNK and CaMK4 By similarity. Phosphorylation at Ser-44, Thr-55 and Ser-103 activates its transcriptional activity By similarity. ATM-mediated phosphorylation at Ser-472 and Ser-480 stimulates its function in DNA damage response. Phosphorylation at Thr-51 or Thr-53 enhances its histone acetyltransferase (HAT) activity.By similarity1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP16951.
    PaxDbiP16951.
    PRIDEiP16951.

    PTM databases

    PhosphoSiteiP16951.

    Expressioni

    Gene expression databases

    ArrayExpressiP16951.
    BgeeiP16951.
    CleanExiMM_ATF2.
    GenevestigatoriP16951.

    Interactioni

    Subunit structurei

    Binds DNA as a dimer and can form a homodimer in the absence of DNA. Can form a heterodimer with JUN. Heterodimerization is essential for its transcriptional activity. Interacts with SMAD3 and SMAD4. Interacts with the HK1/VDAC1 complex. Interacts with NBN, MRE11A, XPO1, KAT5 and CUL3 By similarity. Binds through its N-terminal region to UTF1 which acts as a coactivator of ATF2 transcriptional activity.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi198233. 12 interactions.
    IntActiP16951. 5 interactions.
    MINTiMINT-189465.

    Structurei

    3D structure databases

    ProteinModelPortaliP16951.
    SMRiP16951. Positions 1-38, 336-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini334 – 39764bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni278 – 2814Essential for its histone acetyltransferase activityBy similarity
    Regioni336 – 35621Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni362 – 39029Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi387 – 39610Nuclear export signalBy similarity

    Sequence similaritiesi

    Belongs to the bZIP family. ATF subfamily.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation
    Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri7 – 3125C2H2-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG306955.
    GeneTreeiENSGT00390000020106.
    HOGENOMiHOG000220894.
    HOVERGENiHBG004300.
    InParanoidiP16951.
    KOiK04450.
    OMAiTPIIRNK.
    PhylomeDBiP16951.

    Family and domain databases

    Gene3Di3.30.160.60. 1 hit.
    InterProiIPR004827. bZIP.
    IPR016378. TF_cAMP-dep.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF003153. ATF2_CRE-BP1. 1 hit.
    SMARTiSM00338. BRLZ. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P16951-1) [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

    MSDDKPFLCT APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RNDSVIVADQ    50
    TPTPTRFLKN CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI 100
    IRSKIEEPSV VETTHQDSPL PHPESTTSDE KEVPLAQTAQ PTSAIVRPAS 150
    LQVPNVLLTS SDSSVIIQQA VPSPTSSTVI TQAPSSNRPI VPVPGPFPLL 200
    LHLPNGQTMP VAIPASITSS NVHVPAAVPL VRPVTMVPSV PGIPGPSSPQ 250
    PVQSEAKMRL KAALTQQHPP VTNGDTVKGH GSGLVRTQSE ESRPQSLQQP 300
    ATSTTETPAS PAHTTPQTQN TSGRRRRAAN EDPDEKRRKF LERNRAAASR 350
    CRQKRKVWVQ SLEKKAEDLS SLNGQLQSEV TLLRNEVAQL KQLLLAHKDC 400
    PVTAMQKKSG YHTADKDDSS EDLSVPSSPH TEAIQHSSVS TSNGVSSTSK 450
    AEAVATSVLT QMADQSTEPA LSQIVMAPPS QAQPSGS 487
    Length:487
    Mass (Da):52,298
    Last modified:May 30, 2000 - v2
    Checksum:iF9CDEC3BC3119ACB
    GO
    Isoform 2 (identifier: P16951-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         132-229: Missing.

    Show »
    Length:389
    Mass (Da):42,345
    Checksum:i770AD65EA6114F10
    GO
    Isoform 3 (identifier: P16951-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-48: MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVA → MHCPWVWP

    Show »
    Length:447
    Mass (Da):48,002
    Checksum:i35A0751C1627D682
    GO

    Sequence cautioni

    The sequence AAB21128.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAB21129.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti482 – 4876AQPSGS → HSPQEVD in AAB21128. (PubMed:11471062)Curated
    Sequence conflicti482 – 4876AQPSGS → HSPQEVD in AAB21129. (PubMed:11471062)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4848MSDDK…SVIVA → MHCPWVWP in isoform 3. CuratedVSP_000589Add
    BLAST
    Alternative sequencei132 – 22998Missing in isoform 2. CuratedVSP_000590Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF483482 mRNA. Translation: AAL90756.1.
    AF483483 mRNA. Translation: AAL90757.1.
    S76657 mRNA. Translation: AAB21128.1. Different initiation.
    S76659 mRNA. Translation: AAB21129.1. Different initiation.
    S76655 mRNA. Translation: AAB21127.1.
    M31629 mRNA. Translation: AAA39780.1.
    CCDSiCCDS16134.1. [P16951-1]
    CCDS16135.1. [P16951-3]
    CCDS71076.1. [P16951-2]
    PIRiA42026.
    C42026.
    RefSeqiNP_001020264.1. NM_001025093.2. [P16951-1]
    XP_006498655.1. XM_006498592.1. [P16951-1]
    XP_006498656.1. XM_006498593.1. [P16951-1]
    XP_006498657.1. XM_006498594.1. [P16951-1]
    XP_006498658.1. XM_006498595.1. [P16951-1]
    XP_006498659.1. XM_006498596.1. [P16951-1]
    XP_006543929.1. XM_006543866.1. [P16951-1]
    UniGeneiMm.209903.

    Genome annotation databases

    EnsembliENSMUST00000055833; ENSMUSP00000058521; ENSMUSG00000027104. [P16951-1]
    ENSMUST00000090802; ENSMUSP00000088311; ENSMUSG00000027104. [P16951-3]
    ENSMUST00000100009; ENSMUSP00000097588; ENSMUSG00000027104. [P16951-1]
    ENSMUST00000112007; ENSMUSP00000107638; ENSMUSG00000027104. [P16951-3]
    ENSMUST00000112010; ENSMUSP00000107641; ENSMUSG00000027104. [P16951-3]
    ENSMUST00000112016; ENSMUSP00000107647; ENSMUSG00000027104. [P16951-2]
    ENSMUST00000112017; ENSMUSP00000107648; ENSMUSG00000027104. [P16951-1]
    GeneIDi102641666.
    11909.
    KEGGimmu:102641666.
    mmu:11909.
    UCSCiuc008kdd.1. mouse. [P16951-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF483482 mRNA. Translation: AAL90756.1 .
    AF483483 mRNA. Translation: AAL90757.1 .
    S76657 mRNA. Translation: AAB21128.1 . Different initiation.
    S76659 mRNA. Translation: AAB21129.1 . Different initiation.
    S76655 mRNA. Translation: AAB21127.1 .
    M31629 mRNA. Translation: AAA39780.1 .
    CCDSi CCDS16134.1. [P16951-1 ]
    CCDS16135.1. [P16951-3 ]
    CCDS71076.1. [P16951-2 ]
    PIRi A42026.
    C42026.
    RefSeqi NP_001020264.1. NM_001025093.2. [P16951-1 ]
    XP_006498655.1. XM_006498592.1. [P16951-1 ]
    XP_006498656.1. XM_006498593.1. [P16951-1 ]
    XP_006498657.1. XM_006498594.1. [P16951-1 ]
    XP_006498658.1. XM_006498595.1. [P16951-1 ]
    XP_006498659.1. XM_006498596.1. [P16951-1 ]
    XP_006543929.1. XM_006543866.1. [P16951-1 ]
    UniGenei Mm.209903.

    3D structure databases

    ProteinModelPortali P16951.
    SMRi P16951. Positions 1-38, 336-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198233. 12 interactions.
    IntActi P16951. 5 interactions.
    MINTi MINT-189465.

    Chemistry

    ChEMBLi CHEMBL2176797.

    PTM databases

    PhosphoSitei P16951.

    Proteomic databases

    MaxQBi P16951.
    PaxDbi P16951.
    PRIDEi P16951.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000055833 ; ENSMUSP00000058521 ; ENSMUSG00000027104 . [P16951-1 ]
    ENSMUST00000090802 ; ENSMUSP00000088311 ; ENSMUSG00000027104 . [P16951-3 ]
    ENSMUST00000100009 ; ENSMUSP00000097588 ; ENSMUSG00000027104 . [P16951-1 ]
    ENSMUST00000112007 ; ENSMUSP00000107638 ; ENSMUSG00000027104 . [P16951-3 ]
    ENSMUST00000112010 ; ENSMUSP00000107641 ; ENSMUSG00000027104 . [P16951-3 ]
    ENSMUST00000112016 ; ENSMUSP00000107647 ; ENSMUSG00000027104 . [P16951-2 ]
    ENSMUST00000112017 ; ENSMUSP00000107648 ; ENSMUSG00000027104 . [P16951-1 ]
    GeneIDi 102641666.
    11909.
    KEGGi mmu:102641666.
    mmu:11909.
    UCSCi uc008kdd.1. mouse. [P16951-1 ]

    Organism-specific databases

    CTDi 1386.
    MGIi MGI:109349. Atf2.

    Phylogenomic databases

    eggNOGi NOG306955.
    GeneTreei ENSGT00390000020106.
    HOGENOMi HOG000220894.
    HOVERGENi HBG004300.
    InParanoidi P16951.
    KOi K04450.
    OMAi TPIIRNK.
    PhylomeDBi P16951.

    Enzyme and pathway databases

    Reactomei REACT_204811. Activation of the AP-1 family of transcription factors.
    REACT_226917. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi ATF2. mouse.
    NextBioi 279971.
    PROi P16951.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16951.
    Bgeei P16951.
    CleanExi MM_ATF2.
    Genevestigatori P16951.

    Family and domain databases

    Gene3Di 3.30.160.60. 1 hit.
    InterProi IPR004827. bZIP.
    IPR016378. TF_cAMP-dep.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003153. ATF2_CRE-BP1. 1 hit.
    SMARTi SM00338. BRLZ. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
      Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
      Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: ILS and ISS.
    2. "Functionally distinct isoforms of the CRE-BP DNA-binding protein mediate activity of a T-cell-specific enhancer."
      Georgopoulos K., Morgan B.A., Moore D.D.
      Mol. Cell. Biol. 12:747-757(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-487, ALTERNATIVE SPLICING.
    3. "mXBP/CRE-BP2 and c-Jun form a complex which binds to the cyclic AMP, but not to the 12-O-tetradecanoylphorbol-13-acetate, response element."
      Ivashkiv L.B., Liou H.-C., Kara C.J., Lamph W.W., Verma I.M., Glimcher L.H.
      Mol. Cell. Biol. 10:1609-1621(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-487.
    4. "UTF1, a novel transcriptional coactivator expressed in pluripotent embryonic stem cells and extra-embryonic cells."
      Okuda A., Fukushima A., Nishimoto M., Orimo A., Yamagishi T., Nabeshima Y., Kuro-o M., Nabeshima Y., Boon K., Keaveney M., Stunnenberg H.G., Muramatsu M.
      EMBO J. 17:2019-2032(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UTF1.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 AND THR-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiATF2_MOUSE
    AccessioniPrimary (citable) accession number: P16951
    Secondary accession number(s): Q64089, Q64090, Q64091
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 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

    External Data

    Dasty 3