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NPAS2_HUMAN
ID   NPAS2_HUMAN             Reviewed;         824 AA.
AC   Q99743; Q4ZFV9; Q53SQ3; Q86V96; Q99629;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 3.
DT   03-AUG-2022, entry version 197.
DE   RecName: Full=Neuronal PAS domain-containing protein 2;
DE            Short=Neuronal PAS2;
DE   AltName: Full=Basic-helix-loop-helix-PAS protein MOP4;
DE   AltName: Full=Class E basic helix-loop-helix protein 9;
DE            Short=bHLHe9;
DE   AltName: Full=Member of PAS protein 4;
DE   AltName: Full=PAS domain-containing protein 4;
GN   Name=NPAS2; Synonyms=BHLHE9, MOP4, PASD4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-394 AND LEU-471.
RX   PubMed=9012850; DOI=10.1073/pnas.94.2.713;
RA   Zhou Y.-D., Barnard M., Tian H., Li X., Ring H.Z., Francke U., Shelton J.,
RA   Richardson J., Russell D.W., McKnight S.L.;
RT   "Molecular characterization of two mammalian bHLH-PAS domain proteins
RT   selectively expressed in the central nervous system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:713-718(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-394.
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-626, AND VARIANT ALA-394.
RX   PubMed=9079689; DOI=10.1074/jbc.272.13.8581;
RA   Hogenesch J.B., Chan W.K., Jackiw V.H., Brown R.C., Gu Y.-Z.,
RA   Pray-Grant M., Perdew G.H., Bradfield C.A.;
RT   "Characterization of a subset of the basic-helix-loop-helix-PAS superfamily
RT   that interacts with components of the dioxin signaling pathway.";
RL   J. Biol. Chem. 272:8581-8593(1997).
RN   [5]
RP   FUNCTION.
RX   PubMed=11441147; DOI=10.1126/science.1060699;
RA   Reick M., Garcia J.A., Dudley C., McKnight S.L.;
RT   "NPAS2: an analog of clock operative in the mammalian forebrain.";
RL   Science 293:506-509(2001).
RN   [6]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=11441146; DOI=10.1126/science.1060698;
RA   Rutter J., Reick M., Wu L.C., McKnight S.L.;
RT   "Regulation of clock and NPAS2 DNA binding by the redox state of NAD
RT   cofactors.";
RL   Science 293:510-514(2001).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NCOA3; KAT2B; CREBBP
RP   AND EP300.
RX   PubMed=14645221; DOI=10.1074/jbc.m311973200;
RA   Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
RA   Chakravarti D., FitzGerald G.A., McNamara P.;
RT   "Histone acetyltransferase-dependent chromatin remodeling and the vascular
RT   clock.";
RL   J. Biol. Chem. 279:7091-7097(2004).
RN   [8]
RP   FUNCTION.
RX   PubMed=18439826; DOI=10.1016/j.cub.2008.04.012;
RA   Hampp G., Ripperger J.A., Houben T., Schmutz I., Blex C., Perreau-Lenz S.,
RA   Brunk I., Spanagel R., Ahnert-Hilger G., Meijer J.H., Albrecht U.;
RT   "Regulation of monoamine oxidase A by circadian-clock components implies
RT   clock influence on mood.";
RL   Curr. Biol. 18:678-683(2008).
RN   [9]
RP   FUNCTION.
RX   PubMed=18819933; DOI=10.1158/1541-7786.mcr-07-2094;
RA   Hoffman A.E., Zheng T., Ba Y., Zhu Y.;
RT   "The circadian gene NPAS2, a putative tumor suppressor, is involved in DNA
RT   damage response.";
RL   Mol. Cancer Res. 6:1461-1468(2008).
RN   [10]
RP   REVIEW.
RX   PubMed=23303907; DOI=10.1152/physrev.00016.2012;
RA   Eckel-Mahan K., Sassone-Corsi P.;
RT   "Metabolism and the circadian clock converge.";
RL   Physiol. Rev. 93:107-135(2013).
RN   [11]
RP   ASSOCIATION OF VARIANT LEU-471 WITH SAD.
RX   PubMed=12655319; DOI=10.1038/sj.npp.1300121;
RA   Johansson C., Willeit M., Smedh C., Ekholm J., Paunio T., Kieseppa T.,
RA   Lichtermann D., Praschak-Rieder N., Neumeister A., Nilsson L.G., Kasper S.,
RA   Peltonen L., Adolfsson R., Schalling M., Partonen T.;
RT   "Circadian clock-related polymorphisms in seasonal affective disorder and
RT   their relevance to diurnal preference.";
RL   Neuropsychopharmacology 28:734-739(2003).
RN   [12]
RP   VARIANT ALA-394.
RX   PubMed=17096334; DOI=10.1002/ijc.22321;
RA   Zhu Y., Leaderer D., Guss C., Brown H.N., Zhang Y., Boyle P., Stevens R.G.,
RA   Hoffman A., Qin Q., Han X., Zheng T.;
RT   "Ala394Thr polymorphism in the clock gene NPAS2: a circadian modifier for
RT   the risk of non-Hodgkin's lymphoma.";
RL   Int. J. Cancer 120:432-435(2007).
RN   [13]
RP   VARIANT ALA-394.
RX   PubMed=17453337; DOI=10.1007/s10549-007-9565-0;
RA   Zhu Y., Stevens R.G., Leaderer D., Hoffman A., Holford T., Zhang Y.,
RA   Brown H.N., Zheng T.;
RT   "Non-synonymous polymorphisms in the circadian gene NPAS2 and breast cancer
RT   risk.";
RL   Breast Cancer Res. Treat. 107:421-425(2008).
CC   -!- FUNCTION: Transcriptional activator which forms a core component of the
CC       circadian clock. The circadian clock, an internal time-keeping system,
CC       regulates various physiological processes through the generation of
CC       approximately 24 hour circadian rhythms in gene expression, which are
CC       translated into rhythms in metabolism and behavior. It is derived from
CC       the Latin roots 'circa' (about) and 'diem' (day) and acts as an
CC       important regulator of a wide array of physiological functions
CC       including metabolism, sleep, body temperature, blood pressure,
CC       endocrine, immune, cardiovascular, and renal function. Consists of two
CC       major components: the central clock, residing in the suprachiasmatic
CC       nucleus (SCN) of the brain, and the peripheral clocks that are present
CC       in nearly every tissue and organ system. Both the central and
CC       peripheral clocks can be reset by environmental cues, also known as
CC       Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the
CC       central clock is light, which is sensed by retina and signals directly
CC       to the SCN. The central clock entrains the peripheral clocks through
CC       neuronal and hormonal signals, body temperature and feeding-related
CC       cues, aligning all clocks with the external light/dark cycle. Circadian
CC       rhythms allow an organism to achieve temporal homeostasis with its
CC       environment at the molecular level by regulating gene expression to
CC       create a peak of protein expression once every 24 hours to control when
CC       a particular physiological process is most active with respect to the
CC       solar day. Transcription and translation of core clock components
CC       (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and
CC       CRY2) plays a critical role in rhythm generation, whereas delays
CC       imposed by post-translational modifications (PTMs) are important for
CC       determining the period (tau) of the rhythms (tau refers to the period
CC       of a rhythm and is the length, in time, of one complete cycle). A
CC       diurnal rhythm is synchronized with the day/night cycle, while the
CC       ultradian and infradian rhythms have a period shorter and longer than
CC       24 hours, respectively. Disruptions in the circadian rhythms contribute
CC       to the pathology of cardiovascular diseases, cancer, metabolic
CC       syndromes and aging. A transcription/translation feedback loop (TTFL)
CC       forms the core of the molecular circadian clock mechanism.
CC       Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2,
CC       form the positive limb of the feedback loop, act in the form of a
CC       heterodimer and activate the transcription of core clock genes and
CC       clock-controlled genes (involved in key metabolic processes), harboring
CC       E-box elements (5'-CACGTG-3') within their promoters. The core clock
CC       genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form
CC       the negative limb of the feedback loop and interact with the
CC       CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its
CC       activity and thereby negatively regulating their own expression. This
CC       heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G,
CC       which form a second feedback loop and which activate and repress
CC       ARNTL/BMAL1 transcription, respectively. The NPAS2-ARNTL/BMAL1
CC       heterodimer positively regulates the expression of MAOA, F7 and LDHA
CC       and modulates the circadian rhythm of daytime contrast sensitivity by
CC       regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1)
CC       in the retina. NPAS2 plays an important role in sleep homeostasis and
CC       in maintaining circadian behaviors in normal light/dark and feeding
CC       conditions and in the effective synchronization of feeding behavior
CC       with scheduled food availability. Regulates the gene transcription of
CC       key metabolic pathways in the liver and is involved in DNA damage
CC       response by regulating several cell cycle and DNA repair genes.
CC       Controls the circadian rhythm of NR0B2 expression by binding
CC       rhythmically to its promoter (By similarity). Mediates the diurnal
CC       variation in the expression of GABARA1 receptor in the brain and
CC       contributes to the regulation of anxiety-like behaviors and GABAergic
CC       neurotransmission in the ventral striatum (By similarity).
CC       {ECO:0000250|UniProtKB:P97460, ECO:0000269|PubMed:11441146,
CC       ECO:0000269|PubMed:11441147, ECO:0000269|PubMed:14645221,
CC       ECO:0000269|PubMed:18439826, ECO:0000269|PubMed:18819933}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P97460};
CC   -!- ACTIVITY REGULATION: Carbon monoxide (CO) and the redox state of the
CC       cell can modulate the transcriptional activity of the NPAS2-ARNTL/BMAL1
CC       heterodimer. NADH and NADPH enhance the DNA-binding activity of the
CC       heterodimer whereas CO binds the heme group in NPAS2 and inhibits the
CC       DNA-binding activity of the heterodimer.
CC       {ECO:0000250|UniProtKB:P97460}.
CC   -!- SUBUNIT: Component of the circadian clock oscillator which includes the
CC       CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D
CC       and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA binding
CC       requires dimerization with another bHLH protein. Forms a heterodimer
CC       with ARNTL/BMAL1 and this heterodimerization is required for E-box-
CC       dependent transactivation. Interacts with NCOA3, KAT2B, CREBBP and
CC       EP300. {ECO:0000269|PubMed:14645221}.
CC   -!- INTERACTION:
CC       Q99743; O00327-8: ARNTL; NbExp=10; IntAct=EBI-3932727, EBI-11991546;
CC       Q99743; Q8WYA1-3: ARNTL2; NbExp=10; IntAct=EBI-3932727, EBI-12268276;
CC       Q99743; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-3932727, EBI-953896;
CC       Q99743; P22607: FGFR3; NbExp=3; IntAct=EBI-3932727, EBI-348399;
CC       Q99743; Q14957: GRIN2C; NbExp=3; IntAct=EBI-3932727, EBI-8285963;
CC       Q99743; Q0VD86: INCA1; NbExp=3; IntAct=EBI-3932727, EBI-6509505;
CC       Q99743; O43639: NCK2; NbExp=6; IntAct=EBI-3932727, EBI-713635;
CC       Q99743; Q96IV0: NGLY1; NbExp=3; IntAct=EBI-3932727, EBI-6165879;
CC       Q99743; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-3932727, EBI-2514383;
CC       Q99743; Q9Y649; NbExp=3; IntAct=EBI-3932727, EBI-25900580;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC       ECO:0000269|PubMed:14645221}.
CC   -!- POLYMORPHISM: Variants in NPAS2 show a susceptibility to seasonal
CC       affective disorder (SAD) [MIM:608516]. SAD is a depressive condition
CC       resulting from seasonal changes, and with diurnal preference.
CC       {ECO:0000269|PubMed:9012850}.
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DR   EMBL; U77970; AAB47250.1; -; mRNA.
DR   EMBL; AC016738; AAY14822.1; -; Genomic_DNA.
DR   EMBL; AC092168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC106891; AAX88966.1; -; Genomic_DNA.
DR   EMBL; BC051351; AAH51351.2; -; mRNA.
DR   EMBL; BC072383; AAH72383.1; -; mRNA.
DR   EMBL; U51625; AAC51211.1; -; mRNA.
DR   CCDS; CCDS2048.1; -.
DR   RefSeq; NP_002509.2; NM_002518.3.
DR   AlphaFoldDB; Q99743; -.
DR   SMR; Q99743; -.
DR   BioGRID; 110923; 39.
DR   CORUM; Q99743; -.
DR   DIP; DIP-60821N; -.
DR   IntAct; Q99743; 27.
DR   STRING; 9606.ENSP00000338283; -.
DR   iPTMnet; Q99743; -.
DR   PhosphoSitePlus; Q99743; -.
DR   BioMuta; NPAS2; -.
DR   DMDM; 311033423; -.
DR   jPOST; Q99743; -.
DR   MassIVE; Q99743; -.
DR   PaxDb; Q99743; -.
DR   PeptideAtlas; Q99743; -.
DR   PRIDE; Q99743; -.
DR   ProteomicsDB; 78454; -.
DR   Antibodypedia; 32870; 247 antibodies from 31 providers.
DR   DNASU; 4862; -.
DR   Ensembl; ENST00000335681.10; ENSP00000338283.5; ENSG00000170485.17.
DR   GeneID; 4862; -.
DR   KEGG; hsa:4862; -.
DR   MANE-Select; ENST00000335681.10; ENSP00000338283.5; NM_002518.4; NP_002509.2.
DR   UCSC; uc002tap.2; human.
DR   CTD; 4862; -.
DR   DisGeNET; 4862; -.
DR   GeneCards; NPAS2; -.
DR   HGNC; HGNC:7895; NPAS2.
DR   HPA; ENSG00000170485; Low tissue specificity.
DR   MIM; 603347; gene.
DR   MIM; 608516; phenotype.
DR   neXtProt; NX_Q99743; -.
DR   OpenTargets; ENSG00000170485; -.
DR   PharmGKB; PA31696; -.
DR   VEuPathDB; HostDB:ENSG00000170485; -.
DR   eggNOG; KOG3561; Eukaryota.
DR   GeneTree; ENSGT00940000160744; -.
DR   HOGENOM; CLU_010044_2_2_1; -.
DR   InParanoid; Q99743; -.
DR   OMA; RPCRMPL; -.
DR   OrthoDB; 205871at2759; -.
DR   PhylomeDB; Q99743; -.
DR   TreeFam; TF324568; -.
DR   PathwayCommons; Q99743; -.
DR   Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-400253; Circadian Clock.
DR   Reactome; R-HSA-9707616; Heme signaling.
DR   SignaLink; Q99743; -.
DR   SIGNOR; Q99743; -.
DR   BioGRID-ORCS; 4862; 16 hits in 1093 CRISPR screens.
DR   ChiTaRS; NPAS2; human.
DR   GeneWiki; NPAS2; -.
DR   GenomeRNAi; 4862; -.
DR   Pharos; Q99743; Tbio.
DR   PRO; PR:Q99743; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q99743; protein.
DR   Bgee; ENSG00000170485; Expressed in lower esophagus mucosa and 186 other tissues.
DR   ExpressionAtlas; Q99743; baseline and differential.
DR   Genevisible; Q99743; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:1990513; C:CLOCK-BMAL transcription complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0051879; F:Hsp90 protein binding; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR   GO; GO:2000987; P:positive regulation of behavioral fear response; ISS:UniProtKB.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0051775; P:response to redox state; IDA:UniProtKB.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR001067; Nuc_translocat.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00785; NCTRNSLOCATR.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   1: Evidence at protein level;
KW   Activator; Biological rhythms; DNA damage; DNA-binding; Heme; Iron;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..824
FT                   /note="Neuronal PAS domain-containing protein 2"
FT                   /id="PRO_0000127406"
FT   DOMAIN          9..59
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          82..152
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          237..307
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          311..354
FT                   /note="PAC"
FT   REGION          1..61
FT                   /note="Sufficient for heterodimer formation with
FT                   ARNTL/BMAL1, E-box binding and for the effect of NADPH"
FT                   /evidence="ECO:0000250|UniProtKB:P97460"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..790
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..805
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..824
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         119
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P97460"
FT   BINDING         171
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P97460"
FT   VARIANT         394
FT                   /note="T -> A (associated with non-Hodgkin's lymphoma and
FT                   breast cancer risk; dbSNP:rs2305160)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17096334, ECO:0000269|PubMed:17453337,
FT                   ECO:0000269|PubMed:9012850, ECO:0000269|PubMed:9079689"
FT                   /id="VAR_029078"
FT   VARIANT         471
FT                   /note="S -> L (susceptibility to seasonal affective
FT                   disorder (SAD) and diurnal preference; dbSNP:rs11541353)"
FT                   /evidence="ECO:0000269|PubMed:9012850"
FT                   /id="VAR_029079"
FT   CONFLICT        51
FT                   /note="K -> E (in Ref. 4; AAC51211)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="S -> G (in Ref. 4; AAC51211)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="K -> T (in Ref. 1; AAB47250)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   824 AA;  91791 MW;  679919FCDD3AFDEB CRC64;
     MDEDEKDRAK RASRNKSEKK RRDQFNVLIK ELSSMLPGNT RKMDKTTVLE KVIGFLQKHN
     EVSAQTEICD IQQDWKPSFL SNEEFTQLML EALDGFIIAV TTDGSIIYVS DSITPLLGHL
     PSDVMDQNLL NFLPEQEHSE VYKILSSHML VTDSPSPEYL KSDSDLEFYC HLLRGSLNPK
     EFPTYEYIKF VGNFRSYNNV PSPSCNGFDN TLSRPCRVPL GKEVCFIATV RLATPQFLKE
     MCIVDEPLEE FTSRHSLEWK FLFLDHRAPP IIGYLPFEVL GTSGYDYYHI DDLELLARCH
     QHLMQFGKGK SCCYRFLTKG QQWIWLQTHY YITYHQWNSK PEFIVCTHSV VSYADVRVER
     RQELALEDPP SEALHSSALK DKGSSLEPRQ HFNTLDVGAS GLNTSHSPSA SSRSSHKSSH
     TAMSEPTSTP TKLMAEASTP ALPRSATLPQ ELPVPGLSQA ATMPAPLPSP SSCDLTQQLL
     PQTVLQSTPA PMAQFSAQFS MFQTIKDQLE QRTRILQANI RWQQEELHKI QEQLCLVQDS
     NVQMFLQQPA VSLSFSSTQR PEAQQQLQQR SAAVTQPQLG AGPQLPGQIS SAQVTSQHLL
     RESSVISTQG PKPMRSSQLM QSSGRSGSSL VSPFSSATAA LPPSLNLTTP ASTSQDASQC
     QPSPDFSHDR QLRLLLSQPI QPMMPGSCDA RQPSEVSRTG RQVKYAQSQT VFQNPDAHPA
     NSSSAPMPVL LMGQAVLHPS FPASQPSPLQ PAQARQQPPQ HYLQVQAPTS LHSEQQDSLL
     LSTYSQQPGT LGYPQPPPAQ PQPLRPPRRV SSLSESSGLQ QPPR
 
 
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