ID   Q9UG93_HUMAN            Unreviewed;       369 AA.
AC   Q9UG93;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   04-NOV-2026, entry version 104.
DE   RecName: Full=Cold shock domain-containing protein E1 {ECO:0000256|ARBA:ARBA00069501};
DE   Flags: Fragment;
GN   Name=DKFZp586J0620 {ECO:0000313|EMBL:CAB43294.1};
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 {ECO:0000313|EMBL:CAB43294.1};
RN   [1] {ECO:0000313|EMBL:CAB43294.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Uterus {ECO:0000313|EMBL:CAB43294.1};
RA   Wambutt R., Heubner D., Mewes H.W., Gassenhuber J., Wiemann S.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding protein involved in translationally coupled mRNA
CC       turnover. Implicated with other RNA-binding proteins in the cytoplasmic
CC       deadenylation/translational and decay interplay of the FOS mRNA
CC       mediated by the major coding-region determinant of instability (mCRD)
CC       domain. Required for efficient formation of stress granules.
CC       {ECO:0000256|ARBA:ARBA00057277}.
CC   -!- SUBUNIT: Component of a multi subunit autoregulatory ribonucleoprotein
CC       complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1.
CC       Interacts with STRAP. Part of a complex associated with the FOS mCRD
CC       domain and consisting of PABPC1, PAIP1, HNRPD and SYNCRIP. The
CC       interaction with PABPC1 is direct and RNA-independent. Interacts with
CC       EIF4ENIF1/4E-T. {ECO:0000256|ARBA:ARBA00065656}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}. Cytoplasm, Stress granule
CC       {ECO:0000256|ARBA:ARBA00004210}.
CC   -!- SIMILARITY: Belongs to the UNR family. {ECO:0000256|ARBA:ARBA00044751}.
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DR   EMBL; AL050150; CAB43294.1; -; mRNA.
DR   AlphaFoldDB; Q9UG93; -.
DR   PeptideAtlas; Q9UG93; -.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd04458; CSP_CDS; 1.
DR   FunFam; 2.40.50.140:FF:000093; cold shock domain-containing protein E1 isoform X1; 1.
DR   FunFam; 2.40.50.140:FF:000133; cold shock domain-containing protein E1 isoform X1; 1.
DR   FunFam; 2.40.50.140:FF:000136; cold shock domain-containing protein E1 isoform X1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 3.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR019844; CSD_CS.
DR   InterPro; IPR002059; CSD_DNA-bd.
DR   InterPro; IPR056400; CSDE1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR024642; SUZ-C.
DR   PANTHER; PTHR12913:SF1; COLD SHOCK DOMAIN-CONTAINING PROTEIN E1; 1.
DR   PANTHER; PTHR12913; UNR PROTEIN N-RAS UPSTREAM GENE PROTEIN; 1.
DR   Pfam; PF00313; CSD; 2.
DR   Pfam; PF23456; CSDE1; 2.
DR   Pfam; PF12901; SUZ-C; 1.
DR   SMART; SM00357; CSP; 2.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR   PROSITE; PS00352; CSD_1; 1.
DR   PROSITE; PS51857; CSD_2; 4.
DR   PROSITE; PS51938; SUZ_C; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          13..80
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          89..152
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          185..243
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          244..308
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          319..360
FT                   /note="SUZ-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51938"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAB43294.1"
SQ   SEQUENCE   369 AA;  40595 MW;  93F0AD858E4D2C11 CRC64;
     GTVEKEATFS NPKTTSPNKG KEKEAEDGII AYDDCGVKLT IAFQAKDVEG STSPQIGDKV
     EFSISDKQRP GQQVATCVRL LGRNSNSKRL LGYVATLKDN FGFIETANHD KEIFFHYSEF
     SGDVDSLELG DMVEYSLSKG KGNKVSAEKV NKTHSVNGIT EEADPTIYSG KVIRPLRSVD
     PTQTEYQGMI EIVEEGDMKG EVYPFGIVGM ANKGDCLQKG ESVKFQLCVL GQNAQTMAYN
     ITPLRRATVE CVKDQFGFIN YEVGDSKKLF FHVKEVQDGI ELQAGDEVEF SVILNQRTGK
     CSACNVWRVC EGPKAVAAPR PDRLVNRLKN ITLDDASAPR LMVLRQPRGP DNSMGFGAER
     KIRQAGVID
//