ID CHSP1_HUMAN Reviewed; 147 AA. AC Q9Y2V2; B2R4C3; D3DUF5; Q2YDX5; Q9BQ53; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 24-JAN-2024, entry version 182. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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 for RT 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., 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 [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]. 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [6] 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 KESTREL."; RL Biochem. J. 389:775-783(2005). RN [7] 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., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32; SER-41; SER-52; RP SER-146 AND SER-147, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-52, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] 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., Buerckstuemmer T., RA 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 [13] RP FUNCTION, RNA-BINDING, AND IDENTIFICATION BY 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-41; THR-45 AND SER-52, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32; SER-41; SER-52 RP AND SER-58, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32; SER-41 AND RP SER-52, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] 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., Yao X., RA 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. Binds CC single-stranded DNA (in vitro). {ECO:0000269|PubMed:21078874, CC ECO:0000269|PubMed:21177848}. CC -!- SUBUNIT: Homodimer. Interacts with STYX (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q9Y2V2; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-718719, EBI-357530; CC Q9Y2V2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-718719, EBI-3867333; CC Q9Y2V2; Q8NF50: DOCK8; NbExp=3; IntAct=EBI-718719, EBI-2548605; CC Q9Y2V2; Q8NF50-2: DOCK8; NbExp=3; IntAct=EBI-718719, EBI-10174653; CC Q9Y2V2; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-718719, EBI-739467; CC Q9Y2V2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-718719, EBI-10172290; CC Q9Y2V2; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-718719, EBI-10171774; CC Q9Y2V2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-718719, EBI-10172526; CC Q9Y2V2; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-718719, EBI-945833; CC Q9Y2V2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-718719, EBI-22310682; CC Q9Y2V2; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-718719, EBI-302345; CC Q9Y2V2; P30153: PPP2R1A; NbExp=3; IntAct=EBI-718719, EBI-302388; CC Q9Y2V2; Q13077: TRAF1; NbExp=3; IntAct=EBI-718719, EBI-359224; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21177848}. CC Cytoplasm, P-body {ECO:0000269|PubMed:21177848}. Cytoplasmic granule CC {ECO:0000269|PubMed:21177848}. Note=Detected at cytoplasmic stress CC granules and P-bodies. Detected at exosome granules where mRNA is CC degraded (By similarity). {ECO:0000250}. CC -!- PTM: Dephosphorylated by calcineurin in a Ca(2+) dependent manner (By CC similarity). Can be phosphorylated by DYRK2 (in vitro). {ECO:0000250, CC ECO:0000269|PubMed:15910284}. 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; 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 CCDS; CCDS10537.1; -. 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_005255229.4. DR RefSeq; XP_011520746.1; XM_011522444.2. DR PDB; 3AQQ; X-ray; 2.80 A; A/B/C/D=1-147. DR PDBsum; 3AQQ; -. DR AlphaFoldDB; Q9Y2V2; -. DR SMR; Q9Y2V2; -. DR BioGRID; 117124; 56. DR IntAct; Q9Y2V2; 22. DR MINT; Q9Y2V2; -. DR STRING; 9606.ENSP00000379838; -. DR GlyGen; Q9Y2V2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y2V2; -. DR PhosphoSitePlus; Q9Y2V2; -. DR BioMuta; CARHSP1; -. DR DMDM; 41016932; -. DR EPD; Q9Y2V2; -. DR jPOST; Q9Y2V2; -. DR MassIVE; Q9Y2V2; -. DR MaxQB; Q9Y2V2; -. DR PaxDb; 9606-ENSP00000379838; -. DR PeptideAtlas; Q9Y2V2; -. DR ProteomicsDB; 85909; -. DR Pumba; Q9Y2V2; -. DR TopDownProteomics; Q9Y2V2; -. DR Antibodypedia; 24559; 86 antibodies from 22 providers. DR DNASU; 23589; -. DR Ensembl; ENST00000311052.10; ENSP00000311847.4; ENSG00000153048.11. DR Ensembl; ENST00000396593.6; ENSP00000379838.2; ENSG00000153048.11. DR Ensembl; ENST00000561530.5; ENSP00000455284.1; ENSG00000153048.11. DR Ensembl; ENST00000567554.5; ENSP00000455855.1; ENSG00000153048.11. DR Ensembl; ENST00000610831.4; ENSP00000478055.1; ENSG00000153048.11. DR Ensembl; ENST00000611932.4; ENSP00000481550.1; ENSG00000153048.11. DR Ensembl; ENST00000614449.4; ENSP00000480542.1; ENSG00000153048.11. DR Ensembl; ENST00000618335.4; ENSP00000483591.1; ENSG00000153048.11. DR Ensembl; ENST00000619881.4; ENSP00000480144.1; ENSG00000153048.11. DR GeneID; 23589; -. DR KEGG; hsa:23589; -. DR MANE-Select; ENST00000311052.10; ENSP00000311847.4; NM_014316.4; NP_055131.2. DR UCSC; uc002czh.2; human. DR AGR; HGNC:17150; -. DR CTD; 23589; -. DR DisGeNET; 23589; -. DR GeneCards; CARHSP1; -. DR HGNC; HGNC:17150; CARHSP1. DR HPA; ENSG00000153048; Tissue enhanced (testis). DR MIM; 616885; gene. DR neXtProt; NX_Q9Y2V2; -. DR OpenTargets; ENSG00000153048; -. DR PharmGKB; PA38440; -. DR VEuPathDB; HostDB:ENSG00000153048; -. DR eggNOG; KOG3070; Eukaryota. DR GeneTree; ENSGT00390000000022; -. DR HOGENOM; CLU_139526_1_0_1; -. DR InParanoid; Q9Y2V2; -. DR OMA; THERWED; -. DR OrthoDB; 218650at2759; -. DR PhylomeDB; Q9Y2V2; -. DR TreeFam; TF324381; -. DR PathwayCommons; Q9Y2V2; -. DR SignaLink; Q9Y2V2; -. DR SIGNOR; Q9Y2V2; -. DR BioGRID-ORCS; 23589; 12 hits in 1173 CRISPR screens. DR ChiTaRS; CARHSP1; human. DR GeneWiki; CARHSP1; -. DR GenomeRNAi; 23589; -. DR Pharos; Q9Y2V2; Tbio. DR PRO; PR:Q9Y2V2; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9Y2V2; Protein. DR Bgee; ENSG00000153048; Expressed in right testis and 201 other cell types or tissues. DR ExpressionAtlas; Q9Y2V2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IEA:Ensembl. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0043186; C:P granule; ISS:UniProtKB. DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell. 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 CDD; cd04458; CSP_CDS; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR011129; CSD. DR InterPro; IPR019844; CSD_1. DR InterPro; IPR002059; CSP_DNA-bd. DR InterPro; IPR012340; NA-bd_OB-fold. DR PANTHER; PTHR12962; CALCIUM-REGULATED HEAT STABLE PROTEIN CRHSP-24-RELATED; 1. DR PANTHER; PTHR12962:SF3; CALCIUM-REGULATED HEAT-STABLE PROTEIN 1; 1. DR Pfam; PF00313; CSD; 1. DR SMART; SM00357; CSP; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS00352; CSD_1; 1. DR PROSITE; PS51857; CSD_2; 1. DR Genevisible; Q9Y2V2; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Phosphoprotein; Reference proteome; KW RNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692" FT CHAIN 2..147 FT /note="Calcium-regulated heat-stable protein 1" FT /id="PRO_0000100230" FT DOMAIN 62..129 FT /note="CSD" FT REGION 1..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15910284, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 32 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15910284, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 41 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15910284, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 45 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15910284, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 146 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MUTAGEN 41 FT /note="S->D: Reduced affinity for single-stranded DNA. FT Abolishes location at cytoplasmic stress granules." FT /evidence="ECO:0000269|PubMed:21177848" FT MUTAGEN 76 FT /note="H->Q: Reduced affinity for single-stranded DNA." FT /evidence="ECO:0000269|PubMed:21177848" FT CONFLICT 60 FT /note="G -> V (in Ref. 1; AAD25021)" FT /evidence="ECO:0000305" FT HELIX 51..59 FT /evidence="ECO:0007829|PDB:3AQQ" FT STRAND 63..70 FT /evidence="ECO:0007829|PDB:3AQQ" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:3AQQ" FT STRAND 75..84 FT /evidence="ECO:0007829|PDB:3AQQ" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:3AQQ" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:3AQQ" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:3AQQ" FT STRAND 106..113 FT /evidence="ECO:0007829|PDB:3AQQ" FT STRAND 121..130 FT /evidence="ECO:0007829|PDB:3AQQ" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:3AQQ" SQ SEQUENCE 147 AA; 15892 MW; 83D70DAE7B1FC573 CRC64; MSSEPPPPPQ PPTHQASVGL LDTPRSRERS PSPLRGNVVP SPLPTRRTRT FSATVRASQG PVYKGVCKCF CRSKGHGFIT PADGGPDIFL HISDVEGEYV PVEGDEVTYK MCSIPPKNEK LQAVEVVITH LAPGTKHETW SGHVISS //