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;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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