Full text data of CARHSP1
CARHSP1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Calcium-regulated heat stable protein 1 (Calcium-regulated heat-stable protein of 24 kDa; CRHSP-24)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Calcium-regulated heat stable protein 1 (Calcium-regulated heat-stable protein of 24 kDa; CRHSP-24)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y2V2
ID CHSP1_HUMAN Reviewed; 147 AA.
AC Q9Y2V2; B2R4C3; D3DUF5; Q2YDX5; Q9BQ53;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-JAN-2004, sequence version 2.
DT 22-JAN-2014, entry version 111.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=9712905; DOI=10.1074/jbc.273.35.22738;
RA Groblewski G.E., Yoshida M., Bragado M.J., Ernst S.A., Leykam J.,
RA Williams J.A.;
RT "Purification and characterization of a novel physiological substrate
RT for calcineurin in mammalian cells.";
RL J. Biol. Chem. 273:22738-22744(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Prostate;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION AT SER-30; SER-32; SER-41 AND SER-52.
RX PubMed=15910284; DOI=10.1042/BJ20050733;
RA Auld G.C., Campbell D.G., Morrice N., Cohen P.;
RT "Identification of calcium-regulated heat-stable protein of 24 kDa
RT (CRHSP24) as a physiological substrate for PKB and RSK using
RT KESTREL.";
RL Biochem. J. 389:775-783(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32; SER-41;
RP SER-52; SER-146 AND SER-147, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-52, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, RNA-BINDING, AND MASS SPECTROMETRY.
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).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-41; THR-45 AND SER-52, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, FUNCTION, SUBCELLULAR
RP LOCATION, DNA-BINDING, AND MUTAGENESIS OF SER-41 AND HIS-76.
RX PubMed=21177848; DOI=10.1074/jbc.M110.177436;
RA Hou H., Wang F., Zhang W., Wang D., Li X., Bartlam M., Shen Y.,
RA Yao X., Rao Z.;
RT "Structure-functional analyses of CRHSP-24 plasticity and dynamics in
RT oxidative stress response.";
RL J. Biol. Chem. 286:9623-9635(2011).
CC -!- FUNCTION: Binds mRNA and regulates the stability of target mRNA.
CC Binds single-stranded DNA (in vitro).
CC -!- SUBUNIT: Homodimer. Interacts with STYX (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body. Cytoplasmic
CC granule. Note=Detected at cytoplasmic stress granules and P-
CC bodies. Detected at exosome granules where mRNA is degraded (By
CC similarity).
CC -!- PTM: Dephosphorylated by calcineurin in a Ca(2+) dependent manner
CC (By similarity). Can be phosphorylated by DYRK2 (in vitro).
CC -!- SIMILARITY: Contains 1 CSD (cold-shock) domain.
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DR EMBL; AF115345; AAD25021.1; -; mRNA.
DR EMBL; AK311777; BAG34720.1; -; mRNA.
DR EMBL; CH471112; EAW85196.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85197.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85198.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85199.1; -; Genomic_DNA.
DR EMBL; BC003366; AAH03366.1; -; mRNA.
DR EMBL; BC108283; AAI08284.1; -; mRNA.
DR RefSeq; NP_001035941.1; NM_001042476.2.
DR RefSeq; NP_001265189.1; NM_001278260.1.
DR RefSeq; NP_001265190.1; NM_001278261.1.
DR RefSeq; NP_001265191.1; NM_001278262.1.
DR RefSeq; NP_001265192.1; NM_001278263.1.
DR RefSeq; NP_001265193.1; NM_001278264.1.
DR RefSeq; NP_001265194.1; NM_001278265.1.
DR RefSeq; NP_001265195.1; NM_001278266.1.
DR RefSeq; NP_055131.2; NM_014316.3.
DR RefSeq; XP_005255286.1; XM_005255229.1.
DR RefSeq; XP_005255287.1; XM_005255230.1.
DR UniGene; Hs.632184; -.
DR PDB; 3AQQ; X-ray; 2.80 A; A/B/C/D=1-147.
DR PDBsum; 3AQQ; -.
DR ProteinModelPortal; Q9Y2V2; -.
DR SMR; Q9Y2V2; 43-141.
DR IntAct; Q9Y2V2; 6.
DR MINT; MINT-1432836; -.
DR STRING; 9606.ENSP00000311847; -.
DR PhosphoSite; Q9Y2V2; -.
DR DMDM; 41016932; -.
DR PaxDb; Q9Y2V2; -.
DR PeptideAtlas; Q9Y2V2; -.
DR PRIDE; Q9Y2V2; -.
DR DNASU; 23589; -.
DR Ensembl; ENST00000311052; ENSP00000311847; ENSG00000153048.
DR Ensembl; ENST00000396593; ENSP00000379838; ENSG00000153048.
DR Ensembl; ENST00000561530; ENSP00000455284; ENSG00000153048.
DR Ensembl; ENST00000567554; ENSP00000455855; ENSG00000153048.
DR GeneID; 23589; -.
DR KEGG; hsa:23589; -.
DR UCSC; uc002czh.2; human.
DR CTD; 23589; -.
DR GeneCards; GC16M008946; -.
DR HGNC; HGNC:17150; CARHSP1.
DR HPA; HPA051911; -.
DR neXtProt; NX_Q9Y2V2; -.
DR PharmGKB; PA38440; -.
DR eggNOG; NOG239041; -.
DR HOGENOM; HOG000059524; -.
DR HOVERGEN; HBG050947; -.
DR InParanoid; Q9Y2V2; -.
DR OMA; AMSSEPP; -.
DR OrthoDB; EOG7N63PN; -.
DR PhylomeDB; Q9Y2V2; -.
DR GeneWiki; CARHSP1; -.
DR GenomeRNAi; 23589; -.
DR NextBio; 46226; -.
DR PRO; PR:Q9Y2V2; -.
DR ArrayExpress; Q9Y2V2; -.
DR Bgee; Q9Y2V2; -.
DR CleanEx; HS_CARHSP1; -.
DR Genevestigator; Q9Y2V2; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; NAS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR019844; Cold-shock_CS.
DR InterPro; IPR011129; Cold_shock_prot.
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; COLD_SHOCK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 147 Calcium-regulated heat stable protein 1.
FT /FTId=PRO_0000100230.
FT DOMAIN 62 129 CSD.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 30 30 Phosphoserine.
FT MOD_RES 32 32 Phosphoserine.
FT MOD_RES 41 41 Phosphoserine.
FT MOD_RES 45 45 Phosphothreonine.
FT MOD_RES 52 52 Phosphoserine.
FT MOD_RES 146 146 Phosphoserine.
FT MOD_RES 147 147 Phosphoserine.
FT MUTAGEN 41 41 S->D: Reduced affinity for single-
FT stranded DNA. Abolishes location at
FT cytoplasmic stress granules.
FT MUTAGEN 76 76 H->Q: Reduced affinity for single-
FT stranded DNA.
FT CONFLICT 60 60 G -> V (in Ref. 1; AAD25021).
FT HELIX 51 59
FT STRAND 63 70
FT TURN 72 74
FT STRAND 75 84
FT STRAND 88 91
FT HELIX 92 94
FT STRAND 95 99
FT STRAND 106 113
FT STRAND 121 130
FT STRAND 133 135
SQ SEQUENCE 147 AA; 15892 MW; 83D70DAE7B1FC573 CRC64;
MSSEPPPPPQ PPTHQASVGL LDTPRSRERS PSPLRGNVVP SPLPTRRTRT FSATVRASQG
PVYKGVCKCF CRSKGHGFIT PADGGPDIFL HISDVEGEYV PVEGDEVTYK MCSIPPKNEK
LQAVEVVITH LAPGTKHETW SGHVISS
//
ID CHSP1_HUMAN Reviewed; 147 AA.
AC Q9Y2V2; B2R4C3; D3DUF5; Q2YDX5; Q9BQ53;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-JAN-2004, sequence version 2.
DT 22-JAN-2014, entry version 111.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=9712905; DOI=10.1074/jbc.273.35.22738;
RA Groblewski G.E., Yoshida M., Bragado M.J., Ernst S.A., Leykam J.,
RA Williams J.A.;
RT "Purification and characterization of a novel physiological substrate
RT for calcineurin in mammalian cells.";
RL J. Biol. Chem. 273:22738-22744(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Prostate;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION AT SER-30; SER-32; SER-41 AND SER-52.
RX PubMed=15910284; DOI=10.1042/BJ20050733;
RA Auld G.C., Campbell D.G., Morrice N., Cohen P.;
RT "Identification of calcium-regulated heat-stable protein of 24 kDa
RT (CRHSP24) as a physiological substrate for PKB and RSK using
RT KESTREL.";
RL Biochem. J. 389:775-783(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32; SER-41;
RP SER-52; SER-146 AND SER-147, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-52, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, RNA-BINDING, AND MASS SPECTROMETRY.
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).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-41; THR-45 AND SER-52, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, FUNCTION, SUBCELLULAR
RP LOCATION, DNA-BINDING, AND MUTAGENESIS OF SER-41 AND HIS-76.
RX PubMed=21177848; DOI=10.1074/jbc.M110.177436;
RA Hou H., Wang F., Zhang W., Wang D., Li X., Bartlam M., Shen Y.,
RA Yao X., Rao Z.;
RT "Structure-functional analyses of CRHSP-24 plasticity and dynamics in
RT oxidative stress response.";
RL J. Biol. Chem. 286:9623-9635(2011).
CC -!- FUNCTION: Binds mRNA and regulates the stability of target mRNA.
CC Binds single-stranded DNA (in vitro).
CC -!- SUBUNIT: Homodimer. Interacts with STYX (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body. Cytoplasmic
CC granule. Note=Detected at cytoplasmic stress granules and P-
CC bodies. Detected at exosome granules where mRNA is degraded (By
CC similarity).
CC -!- PTM: Dephosphorylated by calcineurin in a Ca(2+) dependent manner
CC (By similarity). Can be phosphorylated by DYRK2 (in vitro).
CC -!- SIMILARITY: Contains 1 CSD (cold-shock) domain.
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DR EMBL; AF115345; AAD25021.1; -; mRNA.
DR EMBL; AK311777; BAG34720.1; -; mRNA.
DR EMBL; CH471112; EAW85196.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85197.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85198.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85199.1; -; Genomic_DNA.
DR EMBL; BC003366; AAH03366.1; -; mRNA.
DR EMBL; BC108283; AAI08284.1; -; mRNA.
DR RefSeq; NP_001035941.1; NM_001042476.2.
DR RefSeq; NP_001265189.1; NM_001278260.1.
DR RefSeq; NP_001265190.1; NM_001278261.1.
DR RefSeq; NP_001265191.1; NM_001278262.1.
DR RefSeq; NP_001265192.1; NM_001278263.1.
DR RefSeq; NP_001265193.1; NM_001278264.1.
DR RefSeq; NP_001265194.1; NM_001278265.1.
DR RefSeq; NP_001265195.1; NM_001278266.1.
DR RefSeq; NP_055131.2; NM_014316.3.
DR RefSeq; XP_005255286.1; XM_005255229.1.
DR RefSeq; XP_005255287.1; XM_005255230.1.
DR UniGene; Hs.632184; -.
DR PDB; 3AQQ; X-ray; 2.80 A; A/B/C/D=1-147.
DR PDBsum; 3AQQ; -.
DR ProteinModelPortal; Q9Y2V2; -.
DR SMR; Q9Y2V2; 43-141.
DR IntAct; Q9Y2V2; 6.
DR MINT; MINT-1432836; -.
DR STRING; 9606.ENSP00000311847; -.
DR PhosphoSite; Q9Y2V2; -.
DR DMDM; 41016932; -.
DR PaxDb; Q9Y2V2; -.
DR PeptideAtlas; Q9Y2V2; -.
DR PRIDE; Q9Y2V2; -.
DR DNASU; 23589; -.
DR Ensembl; ENST00000311052; ENSP00000311847; ENSG00000153048.
DR Ensembl; ENST00000396593; ENSP00000379838; ENSG00000153048.
DR Ensembl; ENST00000561530; ENSP00000455284; ENSG00000153048.
DR Ensembl; ENST00000567554; ENSP00000455855; ENSG00000153048.
DR GeneID; 23589; -.
DR KEGG; hsa:23589; -.
DR UCSC; uc002czh.2; human.
DR CTD; 23589; -.
DR GeneCards; GC16M008946; -.
DR HGNC; HGNC:17150; CARHSP1.
DR HPA; HPA051911; -.
DR neXtProt; NX_Q9Y2V2; -.
DR PharmGKB; PA38440; -.
DR eggNOG; NOG239041; -.
DR HOGENOM; HOG000059524; -.
DR HOVERGEN; HBG050947; -.
DR InParanoid; Q9Y2V2; -.
DR OMA; AMSSEPP; -.
DR OrthoDB; EOG7N63PN; -.
DR PhylomeDB; Q9Y2V2; -.
DR GeneWiki; CARHSP1; -.
DR GenomeRNAi; 23589; -.
DR NextBio; 46226; -.
DR PRO; PR:Q9Y2V2; -.
DR ArrayExpress; Q9Y2V2; -.
DR Bgee; Q9Y2V2; -.
DR CleanEx; HS_CARHSP1; -.
DR Genevestigator; Q9Y2V2; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; NAS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR019844; Cold-shock_CS.
DR InterPro; IPR011129; Cold_shock_prot.
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; COLD_SHOCK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 147 Calcium-regulated heat stable protein 1.
FT /FTId=PRO_0000100230.
FT DOMAIN 62 129 CSD.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 30 30 Phosphoserine.
FT MOD_RES 32 32 Phosphoserine.
FT MOD_RES 41 41 Phosphoserine.
FT MOD_RES 45 45 Phosphothreonine.
FT MOD_RES 52 52 Phosphoserine.
FT MOD_RES 146 146 Phosphoserine.
FT MOD_RES 147 147 Phosphoserine.
FT MUTAGEN 41 41 S->D: Reduced affinity for single-
FT stranded DNA. Abolishes location at
FT cytoplasmic stress granules.
FT MUTAGEN 76 76 H->Q: Reduced affinity for single-
FT stranded DNA.
FT CONFLICT 60 60 G -> V (in Ref. 1; AAD25021).
FT HELIX 51 59
FT STRAND 63 70
FT TURN 72 74
FT STRAND 75 84
FT STRAND 88 91
FT HELIX 92 94
FT STRAND 95 99
FT STRAND 106 113
FT STRAND 121 130
FT STRAND 133 135
SQ SEQUENCE 147 AA; 15892 MW; 83D70DAE7B1FC573 CRC64;
MSSEPPPPPQ PPTHQASVGL LDTPRSRERS PSPLRGNVVP SPLPTRRTRT FSATVRASQG
PVYKGVCKCF CRSKGHGFIT PADGGPDIFL HISDVEGEYV PVEGDEVTYK MCSIPPKNEK
LQAVEVVITH LAPGTKHETW SGHVISS
//