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CIART_HUMAN
ID   CIART_HUMAN             Reviewed;         385 AA.
AC   Q8N365; B2RD43; D3DV01; Q8N795; Q96MG6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Circadian-associated transcriptional repressor;
DE   AltName: Full=ChIP-derived repressor of network oscillator;
DE            Short=Chrono;
DE   AltName: Full=Computationally highlighted repressor of the network oscillator;
GN   Name=CIART; Synonyms=C1orf51;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Skeletal muscle, and Subthalamic nucleus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Brain;
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Testis;
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   [5]
RP   INTERACTION WITH ARNTL.
RX   PubMed=24385426; DOI=10.1074/jbc.m113.534651;
RA   Annayev Y., Adar S., Chiou Y.Y., Lieb J., Sancar A., Ye R.;
RT   "Gene model 129 (Gm129) encodes a novel transcriptional repressor that
RT   modulates circadian gene expression.";
RL   J. Biol. Chem. 289:5013-5024(2014).
CC   -!- FUNCTION: Transcriptional repressor which forms a negative regulatory
CC       component of the circadian clock and acts independently of the
CC       circadian transcriptional repressors: CRY1, CRY2 and BHLHE41. In a
CC       histone deacetylase-dependent manner represses the transcriptional
CC       activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Abrogates the
CC       interaction of ARNTL/BMAL1 with the transcriptional coactivator CREBBP
CC       and can repress the histone acetyl-transferase activity of the CLOCK-
CC       ARNTL/BMAL1 heterodimer, reducing histone acetylation of its target
CC       genes. Rhythmically binds the E-box elements (5'-CACGTG-3') on
CC       circadian gene promoters and its occupancy shows circadian oscillation
CC       antiphasic to ARNTL/BMAL1. Interacts with the glucocorticoid receptor
CC       (NR3C1) and contributes to the repressive function in the
CC       glucocorticoid response (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PER2, CRY2, BHLHE41, HDAC1 and NR3C1 (By
CC       similarity). Interacts with ARNTL/BMAL1. {ECO:0000250,
CC       ECO:0000269|PubMed:24385426}.
CC   -!- INTERACTION:
CC       Q8N365; P55212: CASP6; NbExp=3; IntAct=EBI-10265133, EBI-718729;
CC       Q8N365; O75553: DAB1; NbExp=3; IntAct=EBI-10265133, EBI-7875264;
CC       Q8N365; P13473-2: LAMP2; NbExp=3; IntAct=EBI-10265133, EBI-21591415;
CC       Q8N365; Q13952-2: NFYC; NbExp=3; IntAct=EBI-10265133, EBI-11956831;
CC       Q8N365; Q9WTL8: Arntl; Xeno; NbExp=6; IntAct=EBI-10265133, EBI-644534;
CC       Q8N365; O54943: Per2; Xeno; NbExp=4; IntAct=EBI-10265133, EBI-1266779;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body
CC       {ECO:0000250}. Note=Co-localizes with the CLOCK-ARNTL/BMAL1 heterodimer
CC       in the PML body. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N365-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N365-2; Sequence=VSP_020743, VSP_020744;
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DR   EMBL; AK056960; BAB71326.1; -; mRNA.
DR   EMBL; AK098755; BAC05404.1; -; mRNA.
DR   EMBL; AK315397; BAG37790.1; -; mRNA.
DR   EMBL; AL138795; CAI22816.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53560.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53564.1; -; Genomic_DNA.
DR   EMBL; BC027999; AAH27999.1; -; mRNA.
DR   EMBL; BC047238; AAH47238.1; -; mRNA.
DR   CCDS; CCDS949.1; -. [Q8N365-1]
DR   RefSeq; NP_001287767.1; NM_001300838.1. [Q8N365-1]
DR   RefSeq; NP_001287769.1; NM_001300840.1.
DR   RefSeq; NP_001287770.1; NM_001300841.1.
DR   RefSeq; NP_653298.1; NM_144697.3. [Q8N365-1]
DR   AlphaFoldDB; Q8N365; -.
DR   BioGRID; 127153; 18.
DR   DIP; DIP-60822N; -.
DR   IntAct; Q8N365; 12.
DR   STRING; 9606.ENSP00000290363; -.
DR   iPTMnet; Q8N365; -.
DR   PhosphoSitePlus; Q8N365; -.
DR   BioMuta; CIART; -.
DR   EPD; Q8N365; -.
DR   MassIVE; Q8N365; -.
DR   PaxDb; Q8N365; -.
DR   PeptideAtlas; Q8N365; -.
DR   PRIDE; Q8N365; -.
DR   ProteomicsDB; 71767; -. [Q8N365-1]
DR   ProteomicsDB; 71768; -. [Q8N365-2]
DR   Antibodypedia; 34023; 147 antibodies from 21 providers.
DR   DNASU; 148523; -.
DR   Ensembl; ENST00000290363.6; ENSP00000290363.5; ENSG00000159208.16. [Q8N365-1]
DR   Ensembl; ENST00000369095.5; ENSP00000358091.1; ENSG00000159208.16. [Q8N365-1]
DR   GeneID; 148523; -.
DR   KEGG; hsa:148523; -.
DR   MANE-Select; ENST00000290363.6; ENSP00000290363.5; NM_144697.4; NP_653298.1.
DR   UCSC; uc001euh.4; human. [Q8N365-1]
DR   CTD; 148523; -.
DR   GeneCards; CIART; -.
DR   HGNC; HGNC:25200; CIART.
DR   HPA; ENSG00000159208; Low tissue specificity.
DR   MIM; 615782; gene.
DR   neXtProt; NX_Q8N365; -.
DR   OpenTargets; ENSG00000159208; -.
DR   PharmGKB; PA134921053; -.
DR   VEuPathDB; HostDB:ENSG00000159208; -.
DR   eggNOG; ENOG502RZ6H; Eukaryota.
DR   GeneTree; ENSGT00390000018360; -.
DR   HOGENOM; CLU_060548_0_0_1; -.
DR   InParanoid; Q8N365; -.
DR   OMA; GPHCHSL; -.
DR   OrthoDB; 972715at2759; -.
DR   PhylomeDB; Q8N365; -.
DR   TreeFam; TF332541; -.
DR   PathwayCommons; Q8N365; -.
DR   SignaLink; Q8N365; -.
DR   BioGRID-ORCS; 148523; 14 hits in 1044 CRISPR screens.
DR   GenomeRNAi; 148523; -.
DR   Pharos; Q8N365; Tbio.
DR   PRO; PR:Q8N365; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q8N365; protein.
DR   Bgee; ENSG00000159208; Expressed in oocyte and 143 other tissues.
DR   ExpressionAtlas; Q8N365; baseline and differential.
DR   Genevisible; Q8N365; HS.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   InterPro; IPR031373; Ciart.
DR   PANTHER; PTHR35441; PTHR35441; 1.
DR   Pfam; PF15673; Ciart; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Biological rhythms; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..385
FT                   /note="Circadian-associated transcriptional repressor"
FT                   /id="PRO_0000251193"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         123
FT                   /note="C -> D (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_020743"
FT   VAR_SEQ         124..385
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_020744"
FT   CONFLICT        187
FT                   /note="M -> L (in Ref. 1; BAB71326)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   385 AA;  41443 MW;  3242FA7CA663493E CRC64;
     MDSPSSVSSY SSYSLSSSFP TSPVNSDFGF PSDSEREDKG AHGPRPDTVG QRGGSRPSPG
     PIRCRHRSKV SGNQHTPSHP KQRGSASPMA GSGAKRSRDG ELETSLNTQG CTTEGDLLFA
     QKCKELQGFI PPLTDLLNGL KMGRFERGLS SFQQSVAMDR IQRIVGVLQK PQMGERYLGT
     LLQVEGMLKT WFPQIAAQKS SLGGGKHQLT KHFPSHHSDS AASSPASPME KMDQTQLGHL
     ALKPKQPWHL TQWPAMNLTW IHTTPICNPP LSSPGTISFS HGPLGTGTGI GVILFLQHGV
     QPFTHSAPTT PVPPTTASPV IPGEPMKLSG EGPRCYSLPV TLPSDWSYTL SPPSLPTLAR
     KMTIGHREQQ RSHPPVAADA HLLNL
 
 
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