CHSP1_HUMAN
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 03-AUG-2022, entry version 174.
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}.
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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 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; 45.
DR IntAct; Q9Y2V2; 21.
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; Q9Y2V2; -.
DR PeptideAtlas; Q9Y2V2; -.
DR PRIDE; Q9Y2V2; -.
DR ProteomicsDB; 85909; -.
DR TopDownProteomics; Q9Y2V2; -.
DR Antibodypedia; 24559; 81 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 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; 1560417at2759; -.
DR PhylomeDB; Q9Y2V2; -.
DR TreeFam; TF324381; -.
DR PathwayCommons; Q9Y2V2; -.
DR SignaLink; Q9Y2V2; -.
DR SIGNOR; Q9Y2V2; -.
DR BioGRID-ORCS; 23589; 11 hits in 1096 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 199 other tissues.
DR ExpressionAtlas; Q9Y2V2; baseline and differential.
DR Genevisible; Q9Y2V2; HS.
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; -; 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 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
