ID   CSDC2_HUMAN             Reviewed;         153 AA.
AC   Q9Y534; Q8ND37;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Cold shock domain-containing protein C2;
DE   AltName: Full=RNA-binding protein PIPPin;
GN   Name=CSDC2; Synonyms=PIPPIN;
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].
RA   Hattori A., Seki N., Hayashi A., Kozuma S., Miyajima N., Muramatsu M.,
RA   Saito T.;
RT   "Human RNA-binding protein PIPPin.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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).
CC   -!- FUNCTION: RNA-binding factor which binds specifically to the very 3'-
CC       UTR ends of both histone H1 and H3.3 mRNAs, encompassing the
CC       polyadenylation signal. Might play a central role in the negative
CC       regulation of histone variant synthesis in the developing brain (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9Y534; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1763657, EBI-6509505;
CC       Q9Y534; P50222: MEOX2; NbExp=3; IntAct=EBI-1763657, EBI-748397;
CC       Q9Y534; A8K7B7: PPP2R1A; NbExp=5; IntAct=EBI-1763657, EBI-10174513;
CC       Q9Y534; P30153: PPP2R1A; NbExp=6; IntAct=EBI-1763657, EBI-302388;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=PIPPin-RNA complexes are located to the nucleus. {ECO:0000250}.
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DR   EMBL; AB027011; BAA84704.1; -; mRNA.
DR   EMBL; CR456457; CAG30343.1; -; mRNA.
DR   EMBL; AL834417; CAD39079.2; -; mRNA.
DR   EMBL; AL023553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC067113; AAH67113.1; -; mRNA.
DR   CCDS; CCDS14019.1; -.
DR   RefSeq; NP_055275.1; NM_014460.3.
DR   AlphaFoldDB; Q9Y534; -.
DR   SMR; Q9Y534; -.
DR   BioGRID; 118102; 3.
DR   IntAct; Q9Y534; 5.
DR   STRING; 9606.ENSP00000302485; -.
DR   iPTMnet; Q9Y534; -.
DR   PhosphoSitePlus; Q9Y534; -.
DR   BioMuta; CSDC2; -.
DR   DMDM; 32129852; -.
DR   EPD; Q9Y534; -.
DR   MassIVE; Q9Y534; -.
DR   MaxQB; Q9Y534; -.
DR   PaxDb; Q9Y534; -.
DR   PeptideAtlas; Q9Y534; -.
DR   PRIDE; Q9Y534; -.
DR   ProteomicsDB; 86281; -.
DR   Antibodypedia; 310; 146 antibodies from 23 providers.
DR   DNASU; 27254; -.
DR   Ensembl; ENST00000306149.12; ENSP00000302485.7; ENSG00000172346.15.
DR   GeneID; 27254; -.
DR   KEGG; hsa:27254; -.
DR   MANE-Select; ENST00000306149.12; ENSP00000302485.7; NM_014460.4; NP_055275.1.
DR   UCSC; uc003bak.2; human.
DR   CTD; 27254; -.
DR   DisGeNET; 27254; -.
DR   GeneCards; CSDC2; -.
DR   HGNC; HGNC:30359; CSDC2.
DR   HPA; ENSG00000172346; Tissue enhanced (adrenal gland, heart muscle, ovary).
DR   MIM; 617689; gene.
DR   neXtProt; NX_Q9Y534; -.
DR   OpenTargets; ENSG00000172346; -.
DR   PharmGKB; PA142672071; -.
DR   VEuPathDB; HostDB:ENSG00000172346; -.
DR   eggNOG; KOG3070; Eukaryota.
DR   GeneTree; ENSGT00390000000022; -.
DR   HOGENOM; CLU_139526_1_0_1; -.
DR   InParanoid; Q9Y534; -.
DR   OMA; PVWPIFP; -.
DR   OrthoDB; 1560417at2759; -.
DR   PhylomeDB; Q9Y534; -.
DR   TreeFam; TF324381; -.
DR   PathwayCommons; Q9Y534; -.
DR   SignaLink; Q9Y534; -.
DR   BioGRID-ORCS; 27254; 19 hits in 1086 CRISPR screens.
DR   ChiTaRS; CSDC2; human.
DR   GeneWiki; CSDC2; -.
DR   GenomeRNAi; 27254; -.
DR   Pharos; Q9Y534; Tbio.
DR   PRO; PR:Q9Y534; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9Y534; protein.
DR   Bgee; ENSG00000172346; Expressed in apex of heart and 140 other tissues.
DR   ExpressionAtlas; Q9Y534; baseline and differential.
DR   Genevisible; Q9Y534; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
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   Cytoplasm; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..153
FT                   /note="Cold shock domain-containing protein C2"
FT                   /id="PRO_0000100351"
FT   DOMAIN          68..135
FT                   /note="CSD"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63430"
SQ   SEQUENCE   153 AA;  16786 MW;  F0CB947289356E93 CRC64;
     MTSESTSPPV VPPLHSPKSP VWPTFPFHRE GSRVWERGGV PPRDLPSPLP TKRTRTYSAT
     ARASAGPVFK GVCKQFSRSQ GHGFITPENG SEDIFVHVSD IEGEYVPVEG DEVTYKMCPI
     PPKNQKFQAV EVVLTQLAPH TPHETWSGQV VGS