CHSP1_MOUSE
ID CHSP1_MOUSE Reviewed; 148 AA.
AC Q9CR86;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Calcium-regulated heat stable protein 1;
DE AltName: Full=Calcium-regulated heat-stable protein of 24 kDa;
DE Short=CRHSP-24;
GN Name=Carhsp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RA Lee S.-H., Williams J.;
RT "Identification and regulation of the phosphorylation sites on the novel
RT calcineurin substrate CRHSP-24.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-33 AND SER-42, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-33, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-33 AND SER-42, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, RNA-BINDING, PHOSPHORYLATION, DEPHOSPHORYLATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21078874; DOI=10.1128/mcb.00775-10;
RA Pfeiffer J.R., McAvoy B.L., Fecteau R.E., Deleault K.M., Brooks S.A.;
RT "CARHSP1 is required for effective tumor necrosis factor alpha mRNA
RT stabilization and localizes to processing bodies and exosomes.";
RL Mol. Cell. Biol. 31:277-286(2011).
CC -!- FUNCTION: Binds mRNA and regulates the stability of target mRNA.
CC {ECO:0000269|PubMed:21078874}.
CC -!- SUBUNIT: Homodimer. Interacts with STYX (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21078874}.
CC Cytoplasm, P-body {ECO:0000269|PubMed:21078874}. Cytoplasmic granule
CC {ECO:0000269|PubMed:21078874}. Note=Detected at cytoplasmic stress
CC granules and P-bodies. Detected at exosome granules where mRNA is
CC degraded.
CC -!- PTM: Can be phosphorylated by DYRK2 (in vitro). Dephosphorylated by
CC calcineurin in a Ca(2+) dependent manner (By similarity).
CC {ECO:0000250}.
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DR EMBL; AF414101; AAL07470.1; -; mRNA.
DR EMBL; AK004711; BAB23495.1; -; mRNA.
DR EMBL; AK002853; BAB22408.1; -; mRNA.
DR EMBL; AK003926; BAB23077.1; -; mRNA.
DR EMBL; BC011225; AAH11225.1; -; mRNA.
DR CCDS; CCDS27942.1; -.
DR RefSeq; NP_080097.1; NM_025821.2.
DR RefSeq; XP_006522409.2; XM_006522346.2.
DR AlphaFoldDB; Q9CR86; -.
DR SMR; Q9CR86; -.
DR BioGRID; 206625; 2.
DR STRING; 10090.ENSMUSP00000008537; -.
DR iPTMnet; Q9CR86; -.
DR PhosphoSitePlus; Q9CR86; -.
DR CPTAC; non-CPTAC-4023; -.
DR EPD; Q9CR86; -.
DR jPOST; Q9CR86; -.
DR MaxQB; Q9CR86; -.
DR PaxDb; Q9CR86; -.
DR PRIDE; Q9CR86; -.
DR ProteomicsDB; 281468; -.
DR Antibodypedia; 24559; 81 antibodies from 22 providers.
DR DNASU; 52502; -.
DR Ensembl; ENSMUST00000008537; ENSMUSP00000008537; ENSMUSG00000008393.
DR GeneID; 52502; -.
DR KEGG; mmu:52502; -.
DR UCSC; uc007yct.1; mouse.
DR CTD; 23589; -.
DR MGI; MGI:1196368; Carhsp1.
DR VEuPathDB; HostDB:ENSMUSG00000008393; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00390000000022; -.
DR HOGENOM; CLU_139526_1_0_1; -.
DR InParanoid; Q9CR86; -.
DR OMA; YKGICKC; -.
DR OrthoDB; 1560417at2759; -.
DR PhylomeDB; Q9CR86; -.
DR TreeFam; TF324381; -.
DR BioGRID-ORCS; 52502; 3 hits in 69 CRISPR screens.
DR ChiTaRS; Carhsp1; mouse.
DR PRO; PR:Q9CR86; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CR86; protein.
DR Bgee; ENSMUSG00000008393; Expressed in lens of camera-type eye and 256 other tissues.
DR ExpressionAtlas; Q9CR86; baseline and differential.
DR Genevisible; Q9CR86; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00313; CSD; 1.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT CHAIN 2..148
FT /note="Calcium-regulated heat stable protein 1"
FT /id="PRO_0000100231"
FT DOMAIN 63..130
FT /note="CSD"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
SQ SEQUENCE 148 AA; 16062 MW; 117F3FE85D11BC93 CRC64;
MSSEPPPPPL QPPTHQTSVG LLDTPRTRDR SPSPLRGNVV PSPLPTRRTR TFSATVRASQ
GPVYKGVCKC FCRSKGHGFI TPADGGPDIF LHISDVEGEY VPVEGDEVTY KMCSIPPKNE
KLQAVEVVIT HLAPGTKHET WSGHVISN
