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O08785

- CLOCK_MOUSE

UniProt

O08785 - CLOCK_MOUSE

Protein

Circadian locomoter output cycles protein kaput

Gene

Clock

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner ARNTL/BMAL1. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-ARNTL/BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1 and also genes implicated in glucose and lipid metabolism. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. May play a role in spermatogenesis; contributes to the chromatoid body assembly and physiology. The CLOCK-ARNTL2/BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1.28 Publications

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

    Enzyme regulationi

    The redox state of the cell can modulate the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer; NADH and NADPH enhance the DNA-binding activity of the heterodimer.By similarity

    GO - Molecular functioni

    1. chromatin DNA binding Source: UniProtKB
    2. core promoter binding Source: UniProtKB
    3. core promoter sequence-specific DNA binding Source: UniProtKB
    4. DNA binding Source: UniProtKB
    5. E-box binding Source: UniProtKB
    6. histone acetyltransferase activity Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    10. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
    11. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
    12. sequence-specific DNA binding Source: UniProtKB
    13. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    14. signal transducer activity Source: InterPro
    15. transcription factor binding Source: MGI

    GO - Biological processi

    1. cellular response to ionizing radiation Source: Ensembl
    2. circadian regulation of gene expression Source: UniProtKB
    3. circadian rhythm Source: UniProtKB
    4. DNA damage checkpoint Source: Ensembl
    5. histone acetylation Source: GOC
    6. negative regulation of glucocorticoid receptor signaling pathway Source: UniProtKB
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. positive regulation of inflammatory response Source: UniProtKB
    9. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    10. positive regulation of transcription, DNA-templated Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    12. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    13. regulation of hair cycle Source: UniProtKB
    14. regulation of insulin secretion Source: UniProtKB
    15. regulation of transcription, DNA-templated Source: UniProtKB
    16. regulation of type B pancreatic cell development Source: UniProtKB
    17. response to redox state Source: UniProtKB
    18. spermatogenesis Source: UniProtKB
    19. transcription from RNA polymerase II promoter Source: GOC

    Keywords - Molecular functioni

    Activator, Acyltransferase, Transferase

    Keywords - Biological processi

    Biological rhythms, DNA damage, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_115781. Bmal1:Clock,Npas2 activates circadian gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_198620. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_226917. HATs acetylate histones.
    REACT_24972. Circadian Clock.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Circadian locomoter output cycles protein kaput (EC:2.3.1.48)
    Short name:
    mCLOCK
    Gene namesi
    Name:Clock
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:99698. Clock.

    Subcellular locationi

    Nucleus. Chromosome. Cytoplasm
    Note: Localizes to sites of DNA damage in a H2AX-independent manner By similarity. Shuffling between the cytoplasm and the nucleus is under circadian regulation and is ARNTL/BMAL1-dependent. Phosphorylated form located in the nucleus predominantly between C12 and C21. Nonphosphorylated form found only in the cytoplasm. Sequestered to the cytoplasm in the presence of ID2.By similarity

    GO - Cellular componenti

    1. chromatoid body Source: UniProtKB
    2. chromosome Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: Reactome
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB
    7. transcription factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381S → D: Significant decrease in transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer. Significant decrease in transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer, reduced nuclear localization and DNA-binding; when associated with D-42. 1 Publication
    Mutagenesisi42 – 421S → D: Significant decrease in transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer. Significant decrease in transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer, reduced nuclear localization and DNA-binding; when associated with D-38. 1 Publication
    Mutagenesisi57 – 571L → E: Reduced ARNTL/BMAL1 binding. Abolishes transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer. Abolishes regulation of circadian clock. 1 Publication
    Mutagenesisi67 – 671K → R: Decrease in sumoylation and its transcriptional activity. Abolishes sumoylation and interaction with ESR1 and decrease in its transcriptional activity; when associated with R-851. 1 Publication
    Mutagenesisi74 – 741L → E: Reduced ARNTL/BMAL1 binding. Abolishes transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer. 1 Publication
    Mutagenesisi284 – 2841W → A: Reduced ARNTL/BMAL1 binding. Slightly reduced transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer. 1 Publication
    Mutagenesisi427 – 4271S → A: Significant loss of phosphorylation. 2 Publications
    Mutagenesisi431 – 4311S → A: Significant loss of phosphorylation. 1 Publication
    Mutagenesisi656 – 6561P → A: Reduces histone acetyltransferase activity; when associated with A-658 and A-659. 1 Publication
    Mutagenesisi658 – 6581Y → A: Reduces histone acetyltransferase activity; when associated with A-656 and A-659. 1 Publication
    Mutagenesisi659 – 6591N → A: Reduces histone acetyltransferase activity; when associated with A-656 and A-658. 1 Publication
    Mutagenesisi669 – 6691G → A: Reduces histone acetyltransferase activity; when associated with A-670 and A-672. 1 Publication
    Mutagenesisi670 – 6701S → A: Reduces histone acetyltransferase activity; when associated with A-669 and A-672. 1 Publication
    Mutagenesisi672 – 6721V → A: Reduces histone acetyltransferase activity; when associated with A-669 and A-670. 1 Publication
    Mutagenesisi851 – 8511K → R: Decrease in sumoylation and its transcriptional activity. Abolishes sumoylation and interaction with ESR1 and decrease in its transcriptional activity; when associated with R-67. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 855855Circadian locomoter output cycles protein kaputPRO_0000127164Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381Phosphoserine1 Publication
    Modified residuei42 – 421Phosphoserine1 Publication
    Cross-linki67 – 67Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
    Modified residuei408 – 4081Phosphoserine1 Publication
    Modified residuei427 – 4271Phosphoserine; by GSK3-beta2 Publications
    Modified residuei431 – 4311Phosphoserine1 Publication
    Modified residuei451 – 4511Phosphothreonine; by CDK51 Publication
    Modified residuei461 – 4611Phosphothreonine; by CDK51 Publication
    Cross-linki851 – 851Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)

    Post-translational modificationi

    Ubiquitinated, leading to its proteasomal degradation.
    O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-ARNTL/BMAL1 heterodimer thereby increasing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2/3 and CRY1/2.2 Publications
    Phosphorylation is dependent on the CLOCK-ARNTL/BMAL1 heterodimer formation. Phosphorylation enhances the transcriptional activity, alters the subcellular localization and decreases the stability of the heterodimer by promoting its degradation. Phosphorylation shows circadian variations in the liver: the hyperphosphorylated form peaks at midnight (CT18), while the hypophosphorylated form is abundant throughout the day. May be phosphorylated by CSNK1D and CKSN1E.7 Publications
    Sumoylation enhances its transcriptional activity and interaction with ESR1, resulting in up-regulation of ESR1 activity. Estrogen stimulates sumoylation. Desumoylation by SENP1 negatively regulates its transcriptional activity.1 Publication

    Keywords - PTMi

    Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO08785.
    PRIDEiO08785.

    PTM databases

    PhosphoSiteiO08785.

    Expressioni

    Tissue specificityi

    Expressed equally in brain, eye, testes, ovaries, liver, heart, lung, kidney. In the brain, expression is abundant in the suprachiasmatic nuclei (SCN), in the pyriform cortex, and in the hippocampus. Low expression throughout the rest of the brain. Expression does not appear to undergo circadian oscillations.3 Publications

    Inductioni

    In the SCN, nuclear expression is lowest between CT7 and CT13. Cytoplasmic expression is highest at these times. In liver, peak levels from CT21 to CT3. Expression of both phosphorylated and unphosphorylated forms of ARNTL/BMAL1 with other circadian clock proteins occurs between CT15 and CT18. Expression in the heart oscillates in a circadian manner.3 Publications

    Gene expression databases

    ArrayExpressiO08785.
    BgeeiO08785.
    CleanExiMM_CLOCK.
    GenevestigatoriO08785.

    Interactioni

    Subunit structurei

    Component of the circadian clock oscillator which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA binding requires dimerization with another bHLH protein. Forms a heterodimer with ARNTL/BMAL1 and this heterodimerization is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and for phosphorylation of both CLOCK and ARNTL/BMAL1. Interacts with PER1, PER2 and CRY1. Interaction with PER and CRY proteins requires translocation to the nucleus. Interaction of the CLOCK-ARNTL/BMAL1 heterodimer with PER or CRY inhibits transcription activation. Interaction of the CLOCK-ARNTL/BMAL1 with CRY1 is independent of DNA but with PER2 is off DNA. Interacts with CIPC. Interacts with NR3C1 in a ligand-dependent fashion. Interacts with RELA/p65, EIF4E, PIWIL1, DDX4 and MGEA5. The CLOCK-ARNTL/BMAL1 heterodimer interacts with GSK3B. Interacts with ESR1 and estrogen stimulates this interaction. Interacts with the complex p35/CDK5. Interacts with KAT2B, CREBBP and EP300. Interacts with ID1, ID2 and ID3. Interacts with MTA1.17 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ArntlQ9WTL824EBI-79859,EBI-644534
    Cry1P977847EBI-79859,EBI-1266607
    Csnk1eQ9JMK22EBI-79859,EBI-771709
    CSNK2BP678702EBI-79859,EBI-348169From a different organism.
    NR1D2Q149952EBI-79859,EBI-6144053From a different organism.
    Per2O5494310EBI-79859,EBI-1266779
    PPP1CAP621362EBI-79859,EBI-357253From a different organism.
    PPP1CBP621402EBI-79859,EBI-352350From a different organism.
    PPP1CCP368732EBI-79859,EBI-356283From a different organism.
    PPP2R1BP301542EBI-79859,EBI-357094From a different organism.
    PPP2R5DQ147382EBI-79859,EBI-396563From a different organism.
    PrkcaP204443EBI-79859,EBI-6976815
    RORBQ927532EBI-79859,EBI-6144615From a different organism.
    RORCP514492EBI-79859,EBI-3908771From a different organism.
    Sirt1Q923E411EBI-79859,EBI-1802585

    Protein-protein interaction databases

    BioGridi198756. 16 interactions.
    DIPiDIP-30958N.
    IntActiO08785. 28 interactions.
    MINTiMINT-4654078.

    Structurei

    Secondary structure

    1
    855
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 5917
    Beta strandi63 – 653
    Helixi70 – 8819
    Helixi94 – 963
    Helixi107 – 11711
    Beta strandi120 – 1267
    Beta strandi129 – 1346
    Helixi138 – 1425
    Helixi146 – 1494
    Helixi154 – 1574
    Helixi160 – 1623
    Helixi163 – 17210
    Beta strandi179 – 1813
    Helixi183 – 1853
    Helixi187 – 1893
    Beta strandi190 – 1989
    Beta strandi204 – 2063
    Beta strandi210 – 22112
    Beta strandi249 – 25911
    Beta strandi262 – 2665
    Beta strandi270 – 2723
    Beta strandi275 – 2806
    Beta strandi284 – 2896
    Helixi294 – 2974
    Helixi301 – 3044
    Helixi309 – 3124
    Helixi315 – 33117
    Beta strandi332 – 3354
    Beta strandi339 – 3424
    Beta strandi346 – 35914
    Turni361 – 3633
    Beta strandi366 – 37510
    Helixi378 – 3836

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4F3LX-ray2.27A26-384[»]
    DisProtiDP00734.
    ProteinModelPortaliO08785.
    SMRiO08785. Positions 31-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 8451bHLHPROSITE-ProRule annotationAdd
    BLAST
    Domaini107 – 17771PAS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini262 – 33271PAS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini336 – 37944PACAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni371 – 854484Interaction with NR3C1Add
    BLAST
    Regioni514 – 56451Implicated in the circadian rhythmicityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi32 – 4716Nuclear localization signal1 PublicationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi484 – 855372Gln-richAdd
    BLAST
    Compositional biasi740 – 7456Poly-Gln
    Compositional biasi751 – 7599Poly-Gln
    Compositional biasi762 – 7698Poly-Gln
    Compositional biasi828 – 83710Poly-Gln

    Domaini

    Contains a Gln-rich C-terminal domain which could correspond to the transactivation domain.

    Sequence similaritiesi

    Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
    Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG300360.
    GeneTreeiENSGT00650000092935.
    HOGENOMiHOG000234382.
    HOVERGENiHBG050997.
    InParanoidiO08785.
    KOiK02223.
    OMAiTPINMQG.
    OrthoDBiEOG71G9T7.
    PhylomeDBiO08785.
    TreeFamiTF324568.

    Family and domain databases

    Gene3Di4.10.280.10. 1 hit.
    InterProiIPR011598. bHLH_dom.
    IPR001067. Nuc_translocat.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    [Graphical view]
    PfamiPF00010. HLH. 1 hit.
    PF00989. PAS. 1 hit.
    [Graphical view]
    PRINTSiPR00785. NCTRNSLOCATR.
    SMARTiSM00353. HLH. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 2 hits.
    [Graphical view]
    SUPFAMiSSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 2 hits.
    PROSITEiPS50888. BHLH. 1 hit.
    PS50112. PAS. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: O08785-1) [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

    MVFTVSCSKM SSIVDRDDSS IFDGLVEEDD KDKAKRVSRN KSEKKRRDQF    50
    NVLIKELGSM LPGNARKMDK STVLQKSIDF LRKHKETTAQ SDASEIRQDW 100
    KPTFLSNEEF TQLMLEALDG FFLAIMTDGS IIYVSESVTS LLEHLPSDLV 150
    DQSIFNFIPE GEHSEVYKIL STHLLESDSL TPEYLKSKNQ LEFCCHMLRG 200
    TIDPKEPSTY EYVRFIGNFK SLTSVSTSTH NGFEGTIQRT HRPSYEDRVC 250
    FVATVRLATP QFIKEMCTVE EPNEEFTSRH SLEWKFLFLD HRAPPIIGYL 300
    PFEVLGTSGY DYYHVDDLEN LAKCHEHLMQ YGKGKSCYYR FLTKGQQWIW 350
    LQTHYYITYH QWNSRPEFIV CTHTVVSYAE VRAERRRELG IEESLPETAA 400
    DKSQDSGSDN RINTVSLKEA LERFDHSPTP SASSRSSRKS SHTAVSDPSS 450
    TPTKIPTDTS TPPRQHLPAH EKMTQRRSSF SSQSINSQSV GPSLTQPAMS 500
    QAANLPIPQG MSQFQFSAQL GAMQHLKDQL EQRTRMIEAN IHRQQEELRK 550
    IQEQLQMVHG QGLQMFLQQS NPGLNFGSVQ LSSGNSNIQQ LTPVNMQGQV 600
    VPANQVQSGH ISTGQHMIQQ QTLQSTSTQQ SQQSVMSGHS QQTSLPSQTP 650
    STLTAPLYNT MVISQPAAGS MVQIPSSMPQ NSTQSATVTT FTQDRQIRFS 700
    QGQQLVTKLV TAPVACGAVM VPSTMLMGQV VTAYPTFATQ QQQAQTLSVT 750
    QQQQQQQQQP PQQQQQQQQS SQEQQLPSVQ QPAQAQLGQP PQQFLQTSRL 800
    LHGNPSTQLI LSAAFPLQQS TFPPSHHQQH QPQQQQQLPR HRTDSLTDPS 850
    KVQPQ 855
    Length:855
    Mass (Da):96,393
    Last modified:July 1, 1997 - v1
    Checksum:i9864D947049742F4
    GO
    Isoform Short (identifier: O08785-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         484-513: Missing.

    Show »
    Length:825
    Mass (Da):93,371
    Checksum:iFABAE927F765B680
    GO

    Polymorphismi

    The naturally-occurring CLOCK variant, missing exon 19 (deletion of AA 514-564) due to an A-->T nucleotide transversion in a splice donor site, forms a heterodimer with DNA, but fails to activate transcription. Homozygous CLOCK mutants have a circadian rhythm that is increased from 3 to 4 hours and usually the circadian rhythmicity is lost at constant darkness. Expression of CLOCK is also reduced. There also exists an alternative spliced CLOCK variant missing both exon 18 and exon 19 (AA 484-564).

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei484 – 51330Missing in isoform Short. 1 PublicationVSP_002103Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000998 mRNA. Translation: AAC53200.1.
    AF146793 Genomic DNA. Translation: AAD30565.1.
    CCDSiCCDS19360.1. [O08785-1]
    RefSeqiNP_001276755.1. NM_001289826.1. [O08785-1]
    NP_031741.1. NM_007715.6. [O08785-1]
    XP_006534807.1. XM_006534744.1. [O08785-1]
    UniGeneiMm.3552.
    Mm.392894.

    Genome annotation databases

    EnsembliENSMUST00000075159; ENSMUSP00000074656; ENSMUSG00000029238. [O08785-1]
    GeneIDi12753.
    KEGGimmu:12753.
    UCSCiuc008xuq.1. mouse. [O08785-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000998 mRNA. Translation: AAC53200.1 .
    AF146793 Genomic DNA. Translation: AAD30565.1 .
    CCDSi CCDS19360.1. [O08785-1 ]
    RefSeqi NP_001276755.1. NM_001289826.1. [O08785-1 ]
    NP_031741.1. NM_007715.6. [O08785-1 ]
    XP_006534807.1. XM_006534744.1. [O08785-1 ]
    UniGenei Mm.3552.
    Mm.392894.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4F3L X-ray 2.27 A 26-384 [» ]
    DisProti DP00734.
    ProteinModelPortali O08785.
    SMRi O08785. Positions 31-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198756. 16 interactions.
    DIPi DIP-30958N.
    IntActi O08785. 28 interactions.
    MINTi MINT-4654078.

    PTM databases

    PhosphoSitei O08785.

    Proteomic databases

    PaxDbi O08785.
    PRIDEi O08785.

    Protocols and materials databases

    DNASUi 12753.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075159 ; ENSMUSP00000074656 ; ENSMUSG00000029238 . [O08785-1 ]
    GeneIDi 12753.
    KEGGi mmu:12753.
    UCSCi uc008xuq.1. mouse. [O08785-1 ]

    Organism-specific databases

    CTDi 9575.
    MGIi MGI:99698. Clock.

    Phylogenomic databases

    eggNOGi NOG300360.
    GeneTreei ENSGT00650000092935.
    HOGENOMi HOG000234382.
    HOVERGENi HBG050997.
    InParanoidi O08785.
    KOi K02223.
    OMAi TPINMQG.
    OrthoDBi EOG71G9T7.
    PhylomeDBi O08785.
    TreeFami TF324568.

    Enzyme and pathway databases

    Reactomei REACT_115781. Bmal1:Clock,Npas2 activates circadian gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_198620. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_226917. HATs acetylate histones.
    REACT_24972. Circadian Clock.

    Miscellaneous databases

    NextBioi 282092.
    PROi O08785.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08785.
    Bgeei O08785.
    CleanExi MM_CLOCK.
    Genevestigatori O08785.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    InterProi IPR011598. bHLH_dom.
    IPR001067. Nuc_translocat.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    [Graphical view ]
    Pfami PF00010. HLH. 1 hit.
    PF00989. PAS. 1 hit.
    [Graphical view ]
    PRINTSi PR00785. NCTRNSLOCATR.
    SMARTi SM00353. HLH. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 2 hits.
    PROSITEi PS50888. BHLH. 1 hit.
    PS50112. PAS. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional identification of the mouse circadian clock gene by transgenic BAC rescue."
      Antoch M.P., Song E.J., Chang A.M., Vitaterna M.H., Zhao Y., Wilsbacher L.D., Sangoram A.M., King D.P., Pinto L.H., Takahashi J.S.
      Cell 89:655-667(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Strain: 129.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT), TISSUE SPECIFICITY, IDENTIFICATION OF CLOCK VARIANT.
      Strain: C57BL/6 X BALB/c.
      Tissue: Suprachiasmatic nucleus.
    3. "The mouse Clock locus: sequence and comparative analysis of 204 kb from mouse chromosome 5."
      Wilsbacher L.D., Sangoram A.M., Antoch M.P., Takahashi J.S.
      Genome Res. 10:1928-1940(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    4. Cited for: INTERACTION WITH ARNTL.
    5. "Posttranslational mechanisms regulate the mammalian circadian clock."
      Lee C., Etchegaray J.-P., Cagampang F.R.A., Loudon A.S.I., Reppert S.M.
      Cell 107:855-867(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARNTL; PER1; PER2; CRY1; CRY2 AND CSNK1E, PHOSPHORYLATION, SUBCELLULAR LOCATION, INDUCTION.
    6. "BMAL1-dependent circadian oscillation of nuclear CLOCK: posttranslational events induced by dimerization of transcriptional activators of the mammalian clock system."
      Kondratov R.V., Chernov M.V., Kondratova A.A., Gorbacheva V.Y., Gudkov A.V., Antoch M.P.
      Genes Dev. 17:1921-1932(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARNTL, PHOSPHORYLATION, SUBCELLULAR LOCATION, INDUCTION.
    7. "Regulation of the PAI-1 promoter by circadian clock components: differential activation by BMAL1 and BMAL2."
      Schoenhard J.A., Smith L.H., Painter C.A., Eren M., Johnson C.H., Vaughan D.E.
      J. Mol. Cell. Cardiol. 35:473-481(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: FUNCTION.
    9. "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
      Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
      J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Circadian regulator CLOCK is a histone acetyltransferase."
      Doi M., Hirayama J., Sassone-Corsi P.
      Cell 125:497-508(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-656; TYR-658; ASN-659; GLY-669; SER-670 AND VAL-672, FUNCTION, CATALYTIC ACTIVITY.
    11. "BMAL1 shuttling controls transactivation and degradation of the CLOCK/BMAL1 heterodimer."
      Kwon I., Lee J., Chang S.H., Jung N.C., Lee B.J., Son G.H., Kim K., Lee K.H.
      Mol. Cell. Biol. 26:7318-7330(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ARNTL, UBIQUITINATION, PROTEASOMAL DEGRADATION.
    12. "CIPC is a mammalian circadian clock protein without invertebrate homologues."
      Zhao W.N., Malinin N., Yang F.C., Staknis D., Gekakis N., Maier B., Reischl S., Kramer A., Weitz C.J.
      Nat. Cell Biol. 9:268-275(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CIPC.
    13. "CLOCK and NPAS2 have overlapping roles in the suprachiasmatic circadian clock."
      DeBruyne J.P., Weaver D.R., Reppert S.M.
      Nat. Neurosci. 10:543-545(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "CLOCK-mediated acetylation of BMAL1 controls circadian function."
      Hirayama J., Sahar S., Grimaldi B., Tamaru T., Takamatsu K., Nakahata Y., Sassone-Corsi P.
      Nature 450:1086-1090(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACETYLATION OF ARNTL/BMAL1.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "Interaction of circadian clock proteins PER2 and CRY with BMAL1 and CLOCK."
      Langmesser S., Tallone T., Bordon A., Rusconi S., Albrecht U.
      BMC Mol. Biol. 9:41-41(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PER2.
    17. "Evidence for an overlapping role of CLOCK and NPAS2 transcription factors in liver circadian oscillators."
      Bertolucci C., Cavallari N., Colognesi I., Aguzzi J., Chen Z., Caruso P., Foa A., Tosini G., Bernardi F., Pinotti M.
      Mol. Cell. Biol. 28:3070-3075(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "A serine cluster mediates BMAL1-dependent CLOCK phosphorylation and degradation."
      Spengler M.L., Kuropatwinski K.K., Schumer M., Antoch M.P.
      Cell Cycle 8:4138-4146(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-427 AND SER-431, MUTAGENESIS OF SER-427 AND SER-431, INTERACTION WITH GSK3B AND ARNTL.
    19. "Circadian rhythm transcription factor CLOCK regulates the transcriptional activity of the glucocorticoid receptor by acetylating its hinge region lysine cluster: potential physiological implications."
      Nader N., Chrousos G.P., Kino T.
      FASEB J. 23:1572-1583(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NR3C1.
    20. "Preferential inhibition of BMAL2-CLOCK activity by PER2 reemphasizes its negative role and a positive role of BMAL2 in the circadian transcription."
      Sasaki M., Yoshitane H., Du N.H., Okano T., Fukada Y.
      J. Biol. Chem. 284:25149-25159(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Roles of CLOCK phosphorylation in suppression of E-box-dependent transcription."
      Yoshitane H., Takao T., Satomi Y., Du N.H., Okano T., Fukada Y.
      Mol. Cell. Biol. 29:3675-3686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, PHOSPHORYLATION AT SER-38; SER-42 AND SER-427, MUTAGENESIS OF SER-38; SER-42 AND SER-427.
    22. "Circadian control of the NAD+ salvage pathway by CLOCK-SIRT1."
      Nakahata Y., Sahar S., Astarita G., Kaluzova M., Sassone-Corsi P.
      Science 324:654-657(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "CLOCK regulates circadian rhythms of hepatic glycogen synthesis through transcriptional activation of Gys2."
      Doi R., Oishi K., Ishida N.
      J. Biol. Chem. 285:22114-22121(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "The transcriptional repressor ID2 can interact with the canonical clock components CLOCK and BMAL1 and mediate inhibitory effects on mPer1 expression."
      Ward S.M., Fernando S.J., Hou T.Y., Duffield G.E.
      J. Biol. Chem. 285:38987-39000(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ID1; ID2 AND ID3.
    25. Cited for: FUNCTION.
    26. Cited for: FUNCTION.
    27. "cAMP-response element (CRE)-mediated transcription by activating transcription factor-4 (ATF4) is essential for circadian expression of the Period2 gene."
      Koyanagi S., Hamdan A.M., Horiguchi M., Kusunose N., Okamoto A., Matsunaga N., Ohdo S.
      J. Biol. Chem. 286:32416-32423(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. "Deficiency in core circadian protein Bmal1 is associated with a prothrombotic and vascular phenotype."
      Somanath P.R., Podrez E.A., Chen J., Ma Y., Marchant K., Antoch M., Byzova T.V.
      J. Cell. Physiol. 226:132-140(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "The period of the circadian oscillator is primarily determined by the balance between casein kinase 1 and protein phosphatase 1."
      Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.
      Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CSNK1D AND CKSN1E.
    30. "Diurnal expression of the thrombopoietin gene is regulated by CLOCK."
      Tracey C.J., Pan X., Catterson J.H., Harmar A.J., Hussain M.M., Hartley P.S.
      J. Thromb. Haemost. 10:662-669(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    31. "Circadian Dbp transcription relies on highly dynamic BMAL1-CLOCK interaction with E boxes and requires the proteasome."
      Stratmann M., Suter D.M., Molina N., Naef F., Schibler U.
      Mol. Cell 48:277-287(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    32. "Circadian proteins CLOCK and BMAL1 in the chromatoid body, a RNA processing granule of male germ cells."
      Peruquetti R.L., de Mateo S., Sassone-Corsi P.
      PLoS ONE 7:E42695-E42695(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH EIF4E; PIWIL1 AND DDX4.
    33. Cited for: FUNCTION, INTERACTION WITH RELA/P65.
    34. "A role for the circadian clock protein Per1 in the regulation of aldosterone levels and renal Na+ retention."
      Richards J., Cheng K.Y., All S., Skopis G., Jeffers L., Lynch I.J., Wingo C.S., Gumz M.L.
      Am. J. Physiol. 305:F1697-F1704(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PER1, TISSUE SPECIFICITY.
    35. "Mechanism of the circadian clock in physiology."
      Richards J., Gumz M.L.
      Am. J. Physiol. 304:R1053-R1064(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    36. "The molecular clock regulates circadian transcription of tissue factor gene."
      Oishi K., Koyanagi S., Ohkura N.
      Biochem. Biophys. Res. Commun. 431:332-335(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    37. "Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock."
      Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K., Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.
      Cell Metab. 17:291-302(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, INTERACTION WITH MGEA5.
    38. "O-GlcNAc signaling entrains the circadian clock by inhibiting BMAL1/CLOCK ubiquitination."
      Li M.D., Ruan H.B., Hughes M.E., Lee J.S., Singh J.P., Jones S.P., Nitabach M.N., Yang X.
      Cell Metab. 17:303-310(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, UBIQUITINATION.
    39. "A role for clock genes in sleep homeostasis."
      Franken P.
      Curr. Opin. Neurobiol. 23:864-872(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    40. "Cyclin-dependent kinase 5 (Cdk5) regulates the function of CLOCK protein by direct phosphorylation."
      Kwak Y., Jeong J., Lee S., Park Y.U., Lee S.A., Han D.H., Kim J.H., Ohshima T., Mikoshiba K., Suh Y.H., Cho S., Park S.K.
      J. Biol. Chem. 288:36878-36889(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-451 AND THR-461, INTERACTION WITH THE COMPLEX P35/CDK5.
    41. Cited for: FUNCTION.
    42. "p75 neurotrophin receptor is a clock gene that regulates oscillatory components of circadian and metabolic networks."
      Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F., Sassone-Corsi P., Ptacek L.J., Akassoglou K.
      J. Neurosci. 33:10221-10234(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    43. "Metastasis-associated protein 1 is an integral component of the circadian molecular machinery."
      Li D.Q., Pakala S.B., Reddy S.D., Peng S., Balasenthil S., Deng C.X., Lee C.C., Rea M.A., Kumar R.
      Nat. Commun. 4:2545-2545(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MTA1.
    44. "CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the transcriptional activity of estrogen receptor-alpha."
      Li S., Wang M., Ao X., Chang A.K., Yang C., Zhao F., Bi H., Liu Y., Xiao L., Wu H.
      Oncogene 32:4883-4891(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-67 AND LYS-851, DESUMOYLATION, INTERACTION WITH ESR1, MUTAGENESIS OF LYS-67 AND LYS-851.
    45. "Metabolism and the circadian clock converge."
      Eckel-Mahan K., Sassone-Corsi P.
      Physiol. Rev. 93:107-135(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    46. "Clock upregulates intercellular adhesion molecule-1 expression and promotes mononuclear cells adhesion to endothelial cells."
      Gao Y., Meng D., Sun N., Zhu Z., Zhao R., Lu C., Chen S., Hua L., Qian R.
      Biochem. Biophys. Res. Commun. 443:586-591(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    47. "CLOCK:BMAL1 is a pioneer-like transcription factor."
      Menet J.S., Pescatore S., Rosbash M.
      Genes Dev. 28:8-13(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    48. "CLOCK/BMAL1 regulates circadian change of mouse hepatic insulin sensitivity via SIRT1."
      Zhou B., Zhang Y., Zhang F., Xia Y., Liu J., Huang R., Wang Y., Hu Y., Wu J., Dai C., Wang H., Tu Y., Peng X., Wang Y., Zhai Q.
      Hepatology 59:2196-2206(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    49. "Gene model 129 (Gm129) encodes a novel transcriptional repressor that modulates circadian gene expression."
      Annayev Y., Adar S., Chiou Y.Y., Lieb J., Sancar A., Ye R.
      J. Biol. Chem. 289:5013-5024(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    50. "Modulation of glucocorticoid receptor induction properties by core circadian clock proteins."
      Han D.H., Lee Y.J., Kim K., Kim C.J., Cho S.
      Mol. Cell. Endocrinol. 383:170-180(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN GR REPRESSION.
    51. "Molecular architecture of the mammalian circadian clock."
      Partch C.L., Green C.B., Takahashi J.S.
      Trends Cell Biol. 24:90-99(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    52. "Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex."
      Huang N., Chelliah Y., Shan Y., Taylor C.A., Yoo S.H., Partch C., Green C.B., Zhang H., Takahashi J.S.
      Science 337:189-194(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 26-384 IN COMPLEX WITH ARNTL, FUNCTION, INTERACTION WITH ARNTL/BMAL1, MUTAGENESIS OF LEU-57; LEU-74 AND TRP-284.

    Entry informationi

    Entry nameiCLOCK_MOUSE
    AccessioniPrimary (citable) accession number: O08785
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 148 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3