Full text data of HNRNPC
HNRNPC
(HNRPC)
[Confidence: low (only semi-automatic identification from reviews)]
Heterogeneous nuclear ribonucleoproteins C1/C2; hnRNP C1/C2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heterogeneous nuclear ribonucleoproteins C1/C2; hnRNP C1/C2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P07910
ID HNRPC_HUMAN Reviewed; 306 AA.
AC P07910; D3DS19; D3DS22; P22628; Q53EX2; Q59FD3; Q5FWE8; Q86SF8;
read moreAC Q86U45; Q96HK7; Q96HM4; Q96IY5; Q9BTS3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 4.
DT 22-JAN-2014, entry version 178.
DE RecName: Full=Heterogeneous nuclear ribonucleoproteins C1/C2;
DE Short=hnRNP C1/C2;
GN Name=HNRNPC; Synonyms=HNRPC;
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] (ISOFORM C2).
RX PubMed=2557628; DOI=10.1073/pnas.86.24.9788;
RA Burd C.G., Swanson M.S., Goerlach M., Dreyfuss G.;
RT "Primary structures of the heterogeneous nuclear ribonucleoprotein A2,
RT B1, and C2 proteins: a diversity of RNA binding proteins is generated
RT by small peptide inserts.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C1).
RX PubMed=3110598;
RA Swanson M.S., Nakagawa T.Y., Levan K., Dreyfuss G.;
RT "Primary structure of human nuclear ribonucleoprotein particle C
RT proteins: conservation of sequence and domain structures in
RT heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins.";
RL Mol. Cell. Biol. 7:1731-1739(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1 AND 3).
RC TISSUE=Neuroblastoma, and Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1; C2 AND 4).
RC TISSUE=Bone marrow, Brain, Chondrosarcoma, Eye, and Placenta;
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 [7]
RP PROTEIN SEQUENCE OF 2-12; 18-39; 43-61; 74-89; 143-151; 188-198 AND
RP 205-216, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Cooper W.N., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 18-39; 51-61; 74-89 AND 207-216, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, AND CHARACTERIZATION.
RX PubMed=2587210; DOI=10.1093/nar/17.21.8441;
RA Merrill B.M., Barnett S.F., Lestourgeon W.M., Williams K.R.;
RT "Primary structure differences between proteins C1 and C2 of HeLa 40S
RT nuclear ribonucleoprotein particles.";
RL Nucleic Acids Res. 17:8441-8449(1989).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8264621;
RA Huang M., Rech J.E., Northington S.J., Flicker P.F., Mayeda A.,
RA Krainer A.R., LeStourgeon W.M.;
RT "The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and
RT nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein
RT particles.";
RL Mol. Cell. Biol. 14:518-533(1994).
RN [11]
RP FUNCTION.
RX PubMed=7567451; DOI=10.1093/nar/23.17.3419;
RA Sebillon P., Beldjord C., Kaplan J.-C., Brody E., Marie J.;
RT "A T to G mutation in the polypyrimidine tract of the second intron of
RT the human beta-globin gene reduces in vitro splicing efficiency:
RT evidence for an increased hnRNP C interaction.";
RL Nucleic Acids Res. 23:3419-3425(1995).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [13]
RP PHOSPHORYLATION AT SER-253; SER-260 AND SER-299, AND MASS
RP SPECTROMETRY.
RX PubMed=12564933; DOI=10.1021/bi0268091;
RA Stone J.R., Maki J.L., Collins T.;
RT "Basal and hydrogen peroxide stimulated sites of phosphorylation in
RT heterogeneous nuclear ribonucleoprotein C1/C2.";
RL Biochemistry 42:1301-1308(2003).
RN [14]
RP FUNCTION.
RX PubMed=12509468; DOI=10.1128/MCB.23.2.708-720.2003;
RA Kim J.H., Paek K.Y., Choi K., Kim T.-D., Hahm B., Kim K.-T.,
RA Jang S.K.;
RT "Heterogeneous nuclear ribonucleoprotein C modulates translation of c-
RT myc mRNA in a cell cycle phase-dependent manner.";
RL Mol. Cell. Biol. 23:708-720(2003).
RN [15]
RP MUTAGENESIS OF LYS-197 AND LYS-250, AND SUMOYLATION AT LYS-250.
RX PubMed=15082759; DOI=10.1128/MCB.24.9.3623-3632.2004;
RA Vassileva M.T., Matunis M.J.;
RT "SUMO modification of heterogeneous nuclear ribonucleoproteins.";
RL Mol. Cell. Biol. 24:3623-3632(2004).
RN [16]
RP FUNCTION.
RX PubMed=16010978; DOI=10.1007/s11010-005-7644-2;
RA Shetty S.;
RT "Regulation of urokinase receptor mRNA stability by hnRNP C in lung
RT epithelial cells.";
RL Mol. Cell. Biochem. 272:107-118(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-233; SER-253
RP AND SER-260, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [20]
RP INTERACTION WITH IGF2BP1.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-260, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-233 AND
RP SER-241, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-108
RP (ISOFORMS 4 AND C1), 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-253; SER-260;
RP SER-299 AND SER-306, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109; SER-113; SER-115;
RP SER-233; SER-253 AND SER-260, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-260 AND
RP SER-299, AND MASS 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 [28]
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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-166; SER-233;
RP SER-241; SER-253; SER-260; SER-299 AND SER-306, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-107 (ISOFORMS 4 AND C1), 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 [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [31]
RP STRUCTURE BY NMR OF 1-94.
RX PubMed=1385725; DOI=10.1021/bi00142a013;
RA Witteking M., Goerlach M., Friedrichs M., Dreyfuss G., Mueller L.;
RT "1H, 13C, and 15N NMR assignments and global folding pattern of the
RT RNA-binding domain of the human hnRNP C proteins.";
RL Biochemistry 31:6254-6265(1992).
RN [32]
RP STRUCTURE BY NMR OF 1-94.
RX PubMed=1380452;
RA Goerlach M., Witteking M., Beckman R.A., Mueller L., Dreyfuss G.;
RT "Interaction of the RNA-binding domain of the hnRNP C proteins with
RT RNA.";
RL EMBO J. 11:3289-3295(1992).
RN [33]
RP STRUCTURE BY NMR OF 193-220, AND SUBUNIT.
RX PubMed=11162094; DOI=10.1006/jmbi.2000.4331;
RA Shahied L., Braswell E.H., LeStourgeon W.M., Krezel A.M.;
RT "An antiparallel four-helix bundle orients the high-affinity RNA
RT binding sites in hnRNP C: a mechanism for RNA chaperonin activity.";
RL J. Mol. Biol. 305:817-828(2001).
RN [34]
RP STRUCTURE BY NMR OF 8-92.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in HNRPC protein.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [35]
RP STRUCTURE BY NMR OF 193-220, AND SUBUNIT.
RX PubMed=15936032; DOI=10.1016/j.jmb.2005.05.002;
RA Whitson S.R., LeStourgeon W.M., Krezel A.M.;
RT "Solution structure of the symmetric coiled coil tetramer formed by
RT the oligomerization domain of hnRNP C: implications for biological
RT function.";
RL J. Mol. Biol. 350:319-337(2005).
CC -!- FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP
CC particles. Single HNRNPC tetramers bind 230-240 nucleotides.
CC Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role
CC in the early steps of spliceosome assembly and pre-mRNA splicing.
CC Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and
CC modulates the stability and the level of translation of bound mRNA
CC molecules.
CC -!- SUBUNIT: Tetramer composed of 3 copies of isoform C1 and 1 copy of
CC isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise
CC to a 19S complex that interacts with HNRNPA2B1 tetramers.
CC Component of the 40S hnRNP particle. Identified in the spliceosome
CC C complex. Interacts with IGF2BP1.
CC -!- INTERACTION:
CC Self; NbExp=4; IntAct=EBI-357966, EBI-357966;
CC P78362:SRPK2; NbExp=2; IntAct=EBI-357966, EBI-593303;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-357966, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Component of ribonucleosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=C2;
CC IsoId=P07910-1; Sequence=Displayed;
CC Name=C1;
CC IsoId=P07910-2; Sequence=VSP_005831;
CC Note=Contains a phosphoserine at position 107. Contains a
CC phosphoserine at position 108;
CC Name=3;
CC IsoId=P07910-3; Sequence=VSP_019225;
CC Name=4;
CC IsoId=P07910-4; Sequence=VSP_005831, VSP_019226;
CC Note=Contains a phosphoserine at position 107. Contains a
CC phosphoserine at position 108;
CC -!- PTM: Phosphorylated on Ser-260 and Ser-299 in resting cells.
CC Phosphorylated on Ser-253 and on 1 serine residue in the poly-Ser
CC stretch at position 238 in response to hydrogen peroxide.
CC -!- PTM: Sumoylated. Sumoylation reduces affinity for mRNA.
CC -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92764.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; M29063; AAA36576.1; -; mRNA.
DR EMBL; M16342; AAA52680.1; -; mRNA.
DR EMBL; BX161480; CAD61934.1; -; mRNA.
DR EMBL; BX247961; CAD62300.1; -; mRNA.
DR EMBL; BX247992; CAD62326.1; -; mRNA.
DR EMBL; AB209527; BAD92764.1; ALT_INIT; mRNA.
DR EMBL; AK223517; BAD97237.1; -; mRNA.
DR EMBL; CH471078; EAW66392.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66393.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66394.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66395.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66396.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66399.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66400.1; -; Genomic_DNA.
DR EMBL; BC003394; AAH03394.1; -; mRNA.
DR EMBL; BC007052; AAH07052.1; -; mRNA.
DR EMBL; BC008364; AAH08364.1; -; mRNA.
DR EMBL; BC008423; AAH08423.1; -; mRNA.
DR EMBL; BC066932; AAH66932.1; -; mRNA.
DR EMBL; BC089438; AAH89438.1; -; mRNA.
DR EMBL; BC108658; AAI08659.1; -; mRNA.
DR EMBL; BC103758; AAI03759.1; -; mRNA.
DR PIR; A26885; A26885.
DR PIR; C34504; C34504.
DR RefSeq; NP_001070910.1; NM_001077442.1.
DR RefSeq; NP_001070911.1; NM_001077443.1.
DR RefSeq; NP_004491.2; NM_004500.3.
DR RefSeq; NP_112604.2; NM_031314.2.
DR RefSeq; XP_005267634.1; XM_005267577.1.
DR RefSeq; XP_005267635.1; XM_005267578.1.
DR UniGene; Hs.508848; -.
DR UniGene; Hs.675546; -.
DR PDB; 1TXP; NMR; -; A/B/C/D=194-220.
DR PDB; 1WF2; NMR; -; A=1-92.
DR PDB; 3LN4; X-ray; 1.30 A; C=102-117.
DR PDBsum; 1TXP; -.
DR PDBsum; 1WF2; -.
DR PDBsum; 3LN4; -.
DR ProteinModelPortal; P07910; -.
DR SMR; P07910; 2-92.
DR DIP; DIP-29854N; -.
DR IntAct; P07910; 68.
DR MINT; MINT-4999718; -.
DR ChEMBL; CHEMBL2216742; -.
DR PhosphoSite; P07910; -.
DR DMDM; 108935845; -.
DR SWISS-2DPAGE; P07910; -.
DR PaxDb; P07910; -.
DR PRIDE; P07910; -.
DR DNASU; 3183; -.
DR Ensembl; ENST00000320084; ENSP00000319690; ENSG00000092199.
DR Ensembl; ENST00000420743; ENSP00000404848; ENSG00000092199.
DR Ensembl; ENST00000430246; ENSP00000442816; ENSG00000092199.
DR Ensembl; ENST00000449098; ENSP00000404559; ENSG00000092199.
DR Ensembl; ENST00000553300; ENSP00000450544; ENSG00000092199.
DR Ensembl; ENST00000554455; ENSP00000451291; ENSG00000092199.
DR Ensembl; ENST00000554969; ENSP00000450725; ENSG00000092199.
DR Ensembl; ENST00000555883; ENSP00000450629; ENSG00000092199.
DR Ensembl; ENST00000556628; ENSP00000451652; ENSG00000092199.
DR Ensembl; ENST00000556897; ENSP00000451176; ENSG00000092199.
DR Ensembl; ENST00000557201; ENSP00000452276; ENSG00000092199.
DR GeneID; 3183; -.
DR KEGG; hsa:3183; -.
DR UCSC; uc001vzy.3; human.
DR CTD; 3183; -.
DR GeneCards; GC14M021677; -.
DR HGNC; HGNC:5035; HNRNPC.
DR HPA; CAB005223; -.
DR MIM; 164020; gene.
DR neXtProt; NX_P07910; -.
DR PharmGKB; PA162391217; -.
DR eggNOG; NOG311712; -.
DR HOVERGEN; HBG002302; -.
DR InParanoid; P07910; -.
DR KO; K12884; -.
DR OMA; FSSPVEM; -.
DR OrthoDB; EOG7KWSK9; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; HNRNPC; human.
DR EvolutionaryTrace; P07910; -.
DR GeneWiki; HNRNPC; -.
DR GenomeRNAi; 3183; -.
DR NextBio; 12634; -.
DR PRO; PR:P07910; -.
DR ArrayExpress; P07910; -.
DR Bgee; P07910; -.
DR Genevestigator; P07910; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; NAS:HGNC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017347; hnRNP_C_Raly.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 306 Heterogeneous nuclear ribonucleoproteins
FT C1/C2.
FT /FTId=PRO_0000081844.
FT DOMAIN 16 87 RRM.
FT MOTIF 155 161 Nuclear localization signal (Potential).
FT COMPBIAS 181 303 Asp/Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 109 109 Phosphothreonine.
FT MOD_RES 113 113 Phosphoserine.
FT MOD_RES 115 115 Phosphoserine.
FT MOD_RES 162 162 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 233 233 Phosphoserine.
FT MOD_RES 241 241 Phosphoserine.
FT MOD_RES 253 253 Phosphoserine.
FT MOD_RES 260 260 Phosphoserine.
FT MOD_RES 299 299 Phosphoserine.
FT MOD_RES 306 306 Phosphoserine.
FT CROSSLNK 250 250 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT VAR_SEQ 39 119 KYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQV
FT LDINLAAEPKVNRGKAGVKRSAAEMYGSVTEHPSPSPLLS
FT -> N (in isoform 3).
FT /FTId=VSP_019225.
FT VAR_SEQ 108 120 Missing (in isoform C1 and isoform 4).
FT /FTId=VSP_005831.
FT VAR_SEQ 153 195 Missing (in isoform 4).
FT /FTId=VSP_019226.
FT VARIANT 167 167 R -> Q (in dbSNP:rs3272).
FT /FTId=VAR_052224.
FT MUTAGEN 197 197 K->R: No effect on sumoylation.
FT MUTAGEN 250 250 K->R: Loss of sumoylation.
FT CONFLICT 110 110 E -> G (in Ref. 6; AAH08423).
FT CONFLICT 217 217 I -> M (in Ref. 1 and 2).
FT CONFLICT 224 224 Q -> R (in Ref. 6; AAH08364).
FT CONFLICT 244 244 K -> R (in Ref. 6; AAH08364).
FT CONFLICT 254 254 E -> G (in Ref. 6; AAH07052).
FT CONFLICT 303 306 EDDS -> G (in Ref. 1 and 2).
FT STRAND 18 23
FT TURN 25 27
FT HELIX 30 35
FT STRAND 43 49
FT STRAND 51 59
FT HELIX 60 68
FT TURN 69 72
FT STRAND 81 84
FT HELIX 194 216
SQ SEQUENCE 306 AA; 33670 MW; 17BBC78690C69C5C CRC64;
MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE
RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVTE HPSPSPLLSS
SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR
GSSKSGKLKG DDLQAIKKEL TQIKQKVDSL LENLEKIEKE QSKQAVEMKN DKSEEEQSSS
SVKKDETNVK MESEGGADDS AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA
NGEDDS
//
ID HNRPC_HUMAN Reviewed; 306 AA.
AC P07910; D3DS19; D3DS22; P22628; Q53EX2; Q59FD3; Q5FWE8; Q86SF8;
read moreAC Q86U45; Q96HK7; Q96HM4; Q96IY5; Q9BTS3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 4.
DT 22-JAN-2014, entry version 178.
DE RecName: Full=Heterogeneous nuclear ribonucleoproteins C1/C2;
DE Short=hnRNP C1/C2;
GN Name=HNRNPC; Synonyms=HNRPC;
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] (ISOFORM C2).
RX PubMed=2557628; DOI=10.1073/pnas.86.24.9788;
RA Burd C.G., Swanson M.S., Goerlach M., Dreyfuss G.;
RT "Primary structures of the heterogeneous nuclear ribonucleoprotein A2,
RT B1, and C2 proteins: a diversity of RNA binding proteins is generated
RT by small peptide inserts.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C1).
RX PubMed=3110598;
RA Swanson M.S., Nakagawa T.Y., Levan K., Dreyfuss G.;
RT "Primary structure of human nuclear ribonucleoprotein particle C
RT proteins: conservation of sequence and domain structures in
RT heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins.";
RL Mol. Cell. Biol. 7:1731-1739(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1 AND 3).
RC TISSUE=Neuroblastoma, and Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1; C2 AND 4).
RC TISSUE=Bone marrow, Brain, Chondrosarcoma, Eye, and Placenta;
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 [7]
RP PROTEIN SEQUENCE OF 2-12; 18-39; 43-61; 74-89; 143-151; 188-198 AND
RP 205-216, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Cooper W.N., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 18-39; 51-61; 74-89 AND 207-216, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, AND CHARACTERIZATION.
RX PubMed=2587210; DOI=10.1093/nar/17.21.8441;
RA Merrill B.M., Barnett S.F., Lestourgeon W.M., Williams K.R.;
RT "Primary structure differences between proteins C1 and C2 of HeLa 40S
RT nuclear ribonucleoprotein particles.";
RL Nucleic Acids Res. 17:8441-8449(1989).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8264621;
RA Huang M., Rech J.E., Northington S.J., Flicker P.F., Mayeda A.,
RA Krainer A.R., LeStourgeon W.M.;
RT "The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and
RT nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein
RT particles.";
RL Mol. Cell. Biol. 14:518-533(1994).
RN [11]
RP FUNCTION.
RX PubMed=7567451; DOI=10.1093/nar/23.17.3419;
RA Sebillon P., Beldjord C., Kaplan J.-C., Brody E., Marie J.;
RT "A T to G mutation in the polypyrimidine tract of the second intron of
RT the human beta-globin gene reduces in vitro splicing efficiency:
RT evidence for an increased hnRNP C interaction.";
RL Nucleic Acids Res. 23:3419-3425(1995).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [13]
RP PHOSPHORYLATION AT SER-253; SER-260 AND SER-299, AND MASS
RP SPECTROMETRY.
RX PubMed=12564933; DOI=10.1021/bi0268091;
RA Stone J.R., Maki J.L., Collins T.;
RT "Basal and hydrogen peroxide stimulated sites of phosphorylation in
RT heterogeneous nuclear ribonucleoprotein C1/C2.";
RL Biochemistry 42:1301-1308(2003).
RN [14]
RP FUNCTION.
RX PubMed=12509468; DOI=10.1128/MCB.23.2.708-720.2003;
RA Kim J.H., Paek K.Y., Choi K., Kim T.-D., Hahm B., Kim K.-T.,
RA Jang S.K.;
RT "Heterogeneous nuclear ribonucleoprotein C modulates translation of c-
RT myc mRNA in a cell cycle phase-dependent manner.";
RL Mol. Cell. Biol. 23:708-720(2003).
RN [15]
RP MUTAGENESIS OF LYS-197 AND LYS-250, AND SUMOYLATION AT LYS-250.
RX PubMed=15082759; DOI=10.1128/MCB.24.9.3623-3632.2004;
RA Vassileva M.T., Matunis M.J.;
RT "SUMO modification of heterogeneous nuclear ribonucleoproteins.";
RL Mol. Cell. Biol. 24:3623-3632(2004).
RN [16]
RP FUNCTION.
RX PubMed=16010978; DOI=10.1007/s11010-005-7644-2;
RA Shetty S.;
RT "Regulation of urokinase receptor mRNA stability by hnRNP C in lung
RT epithelial cells.";
RL Mol. Cell. Biochem. 272:107-118(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-233; SER-253
RP AND SER-260, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [20]
RP INTERACTION WITH IGF2BP1.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-260, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-233 AND
RP SER-241, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-108
RP (ISOFORMS 4 AND C1), 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-253; SER-260;
RP SER-299 AND SER-306, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109; SER-113; SER-115;
RP SER-233; SER-253 AND SER-260, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-260 AND
RP SER-299, AND MASS 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 [28]
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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-166; SER-233;
RP SER-241; SER-253; SER-260; SER-299 AND SER-306, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-107 (ISOFORMS 4 AND C1), 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 [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [31]
RP STRUCTURE BY NMR OF 1-94.
RX PubMed=1385725; DOI=10.1021/bi00142a013;
RA Witteking M., Goerlach M., Friedrichs M., Dreyfuss G., Mueller L.;
RT "1H, 13C, and 15N NMR assignments and global folding pattern of the
RT RNA-binding domain of the human hnRNP C proteins.";
RL Biochemistry 31:6254-6265(1992).
RN [32]
RP STRUCTURE BY NMR OF 1-94.
RX PubMed=1380452;
RA Goerlach M., Witteking M., Beckman R.A., Mueller L., Dreyfuss G.;
RT "Interaction of the RNA-binding domain of the hnRNP C proteins with
RT RNA.";
RL EMBO J. 11:3289-3295(1992).
RN [33]
RP STRUCTURE BY NMR OF 193-220, AND SUBUNIT.
RX PubMed=11162094; DOI=10.1006/jmbi.2000.4331;
RA Shahied L., Braswell E.H., LeStourgeon W.M., Krezel A.M.;
RT "An antiparallel four-helix bundle orients the high-affinity RNA
RT binding sites in hnRNP C: a mechanism for RNA chaperonin activity.";
RL J. Mol. Biol. 305:817-828(2001).
RN [34]
RP STRUCTURE BY NMR OF 8-92.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in HNRPC protein.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [35]
RP STRUCTURE BY NMR OF 193-220, AND SUBUNIT.
RX PubMed=15936032; DOI=10.1016/j.jmb.2005.05.002;
RA Whitson S.R., LeStourgeon W.M., Krezel A.M.;
RT "Solution structure of the symmetric coiled coil tetramer formed by
RT the oligomerization domain of hnRNP C: implications for biological
RT function.";
RL J. Mol. Biol. 350:319-337(2005).
CC -!- FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP
CC particles. Single HNRNPC tetramers bind 230-240 nucleotides.
CC Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role
CC in the early steps of spliceosome assembly and pre-mRNA splicing.
CC Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and
CC modulates the stability and the level of translation of bound mRNA
CC molecules.
CC -!- SUBUNIT: Tetramer composed of 3 copies of isoform C1 and 1 copy of
CC isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise
CC to a 19S complex that interacts with HNRNPA2B1 tetramers.
CC Component of the 40S hnRNP particle. Identified in the spliceosome
CC C complex. Interacts with IGF2BP1.
CC -!- INTERACTION:
CC Self; NbExp=4; IntAct=EBI-357966, EBI-357966;
CC P78362:SRPK2; NbExp=2; IntAct=EBI-357966, EBI-593303;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-357966, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Component of ribonucleosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=C2;
CC IsoId=P07910-1; Sequence=Displayed;
CC Name=C1;
CC IsoId=P07910-2; Sequence=VSP_005831;
CC Note=Contains a phosphoserine at position 107. Contains a
CC phosphoserine at position 108;
CC Name=3;
CC IsoId=P07910-3; Sequence=VSP_019225;
CC Name=4;
CC IsoId=P07910-4; Sequence=VSP_005831, VSP_019226;
CC Note=Contains a phosphoserine at position 107. Contains a
CC phosphoserine at position 108;
CC -!- PTM: Phosphorylated on Ser-260 and Ser-299 in resting cells.
CC Phosphorylated on Ser-253 and on 1 serine residue in the poly-Ser
CC stretch at position 238 in response to hydrogen peroxide.
CC -!- PTM: Sumoylated. Sumoylation reduces affinity for mRNA.
CC -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92764.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; M29063; AAA36576.1; -; mRNA.
DR EMBL; M16342; AAA52680.1; -; mRNA.
DR EMBL; BX161480; CAD61934.1; -; mRNA.
DR EMBL; BX247961; CAD62300.1; -; mRNA.
DR EMBL; BX247992; CAD62326.1; -; mRNA.
DR EMBL; AB209527; BAD92764.1; ALT_INIT; mRNA.
DR EMBL; AK223517; BAD97237.1; -; mRNA.
DR EMBL; CH471078; EAW66392.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66393.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66394.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66395.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66396.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66399.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66400.1; -; Genomic_DNA.
DR EMBL; BC003394; AAH03394.1; -; mRNA.
DR EMBL; BC007052; AAH07052.1; -; mRNA.
DR EMBL; BC008364; AAH08364.1; -; mRNA.
DR EMBL; BC008423; AAH08423.1; -; mRNA.
DR EMBL; BC066932; AAH66932.1; -; mRNA.
DR EMBL; BC089438; AAH89438.1; -; mRNA.
DR EMBL; BC108658; AAI08659.1; -; mRNA.
DR EMBL; BC103758; AAI03759.1; -; mRNA.
DR PIR; A26885; A26885.
DR PIR; C34504; C34504.
DR RefSeq; NP_001070910.1; NM_001077442.1.
DR RefSeq; NP_001070911.1; NM_001077443.1.
DR RefSeq; NP_004491.2; NM_004500.3.
DR RefSeq; NP_112604.2; NM_031314.2.
DR RefSeq; XP_005267634.1; XM_005267577.1.
DR RefSeq; XP_005267635.1; XM_005267578.1.
DR UniGene; Hs.508848; -.
DR UniGene; Hs.675546; -.
DR PDB; 1TXP; NMR; -; A/B/C/D=194-220.
DR PDB; 1WF2; NMR; -; A=1-92.
DR PDB; 3LN4; X-ray; 1.30 A; C=102-117.
DR PDBsum; 1TXP; -.
DR PDBsum; 1WF2; -.
DR PDBsum; 3LN4; -.
DR ProteinModelPortal; P07910; -.
DR SMR; P07910; 2-92.
DR DIP; DIP-29854N; -.
DR IntAct; P07910; 68.
DR MINT; MINT-4999718; -.
DR ChEMBL; CHEMBL2216742; -.
DR PhosphoSite; P07910; -.
DR DMDM; 108935845; -.
DR SWISS-2DPAGE; P07910; -.
DR PaxDb; P07910; -.
DR PRIDE; P07910; -.
DR DNASU; 3183; -.
DR Ensembl; ENST00000320084; ENSP00000319690; ENSG00000092199.
DR Ensembl; ENST00000420743; ENSP00000404848; ENSG00000092199.
DR Ensembl; ENST00000430246; ENSP00000442816; ENSG00000092199.
DR Ensembl; ENST00000449098; ENSP00000404559; ENSG00000092199.
DR Ensembl; ENST00000553300; ENSP00000450544; ENSG00000092199.
DR Ensembl; ENST00000554455; ENSP00000451291; ENSG00000092199.
DR Ensembl; ENST00000554969; ENSP00000450725; ENSG00000092199.
DR Ensembl; ENST00000555883; ENSP00000450629; ENSG00000092199.
DR Ensembl; ENST00000556628; ENSP00000451652; ENSG00000092199.
DR Ensembl; ENST00000556897; ENSP00000451176; ENSG00000092199.
DR Ensembl; ENST00000557201; ENSP00000452276; ENSG00000092199.
DR GeneID; 3183; -.
DR KEGG; hsa:3183; -.
DR UCSC; uc001vzy.3; human.
DR CTD; 3183; -.
DR GeneCards; GC14M021677; -.
DR HGNC; HGNC:5035; HNRNPC.
DR HPA; CAB005223; -.
DR MIM; 164020; gene.
DR neXtProt; NX_P07910; -.
DR PharmGKB; PA162391217; -.
DR eggNOG; NOG311712; -.
DR HOVERGEN; HBG002302; -.
DR InParanoid; P07910; -.
DR KO; K12884; -.
DR OMA; FSSPVEM; -.
DR OrthoDB; EOG7KWSK9; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; HNRNPC; human.
DR EvolutionaryTrace; P07910; -.
DR GeneWiki; HNRNPC; -.
DR GenomeRNAi; 3183; -.
DR NextBio; 12634; -.
DR PRO; PR:P07910; -.
DR ArrayExpress; P07910; -.
DR Bgee; P07910; -.
DR Genevestigator; P07910; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; NAS:HGNC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017347; hnRNP_C_Raly.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 306 Heterogeneous nuclear ribonucleoproteins
FT C1/C2.
FT /FTId=PRO_0000081844.
FT DOMAIN 16 87 RRM.
FT MOTIF 155 161 Nuclear localization signal (Potential).
FT COMPBIAS 181 303 Asp/Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 109 109 Phosphothreonine.
FT MOD_RES 113 113 Phosphoserine.
FT MOD_RES 115 115 Phosphoserine.
FT MOD_RES 162 162 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 233 233 Phosphoserine.
FT MOD_RES 241 241 Phosphoserine.
FT MOD_RES 253 253 Phosphoserine.
FT MOD_RES 260 260 Phosphoserine.
FT MOD_RES 299 299 Phosphoserine.
FT MOD_RES 306 306 Phosphoserine.
FT CROSSLNK 250 250 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT VAR_SEQ 39 119 KYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQV
FT LDINLAAEPKVNRGKAGVKRSAAEMYGSVTEHPSPSPLLS
FT -> N (in isoform 3).
FT /FTId=VSP_019225.
FT VAR_SEQ 108 120 Missing (in isoform C1 and isoform 4).
FT /FTId=VSP_005831.
FT VAR_SEQ 153 195 Missing (in isoform 4).
FT /FTId=VSP_019226.
FT VARIANT 167 167 R -> Q (in dbSNP:rs3272).
FT /FTId=VAR_052224.
FT MUTAGEN 197 197 K->R: No effect on sumoylation.
FT MUTAGEN 250 250 K->R: Loss of sumoylation.
FT CONFLICT 110 110 E -> G (in Ref. 6; AAH08423).
FT CONFLICT 217 217 I -> M (in Ref. 1 and 2).
FT CONFLICT 224 224 Q -> R (in Ref. 6; AAH08364).
FT CONFLICT 244 244 K -> R (in Ref. 6; AAH08364).
FT CONFLICT 254 254 E -> G (in Ref. 6; AAH07052).
FT CONFLICT 303 306 EDDS -> G (in Ref. 1 and 2).
FT STRAND 18 23
FT TURN 25 27
FT HELIX 30 35
FT STRAND 43 49
FT STRAND 51 59
FT HELIX 60 68
FT TURN 69 72
FT STRAND 81 84
FT HELIX 194 216
SQ SEQUENCE 306 AA; 33670 MW; 17BBC78690C69C5C CRC64;
MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE
RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVTE HPSPSPLLSS
SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR
GSSKSGKLKG DDLQAIKKEL TQIKQKVDSL LENLEKIEKE QSKQAVEMKN DKSEEEQSSS
SVKKDETNVK MESEGGADDS AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA
NGEDDS
//
MIM
164020
*RECORD*
*FIELD* NO
164020
*FIELD* TI
*164020 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN C; HNRNPC
;;HNRPC
NUCLEAR RIBONUCLEOPROTEIN PARTICLE C1 PROTEIN, INCLUDED;;
read moreNUCLEAR RIBONUCLEOPROTEIN PARTICLE C2 PROTEIN, INCLUDED
*FIELD* TX
DESCRIPTION
The primary nuclear transcripts of RNA polymerase II, some of which are
precursors to cytoplasmic mRNA (pre-mRNA), are collectively referred to
as heterogeneous nuclear RNAs (hnRNAs). At least 20 of these proteins,
designated A1 (34 kD) through U (120 kD), are present in abundance. In
the nucleus they are found in association with a specific set of
proteins to form ribonucleoprotein (hnRNP) particles. In vertebrates,
the C proteins, C1 and C2, are major constituents of these particles.
The 2 are antigenically closely related phosphoproteins, which bind
tightly to RNA in vitro (Nakagawa et al., 1986).
CLONING
Nakagawa et al. (1986) cloned cDNA for the hnRNA C proteins. Genomic
blot analysis showed homologous DNA sequences across eukaryotes from
human to yeast, indicating that the hnRNA C proteins are members of a
conserved gene family. Burd et al. (1989) reported the complete primary
structure of the hnRNP proteins A2, B1, and C2; A1, C1, and L had
previously been sequenced. They suggested that the C1 and C2 proteins
are produced by alternative splicing of a single gene transcript.
Merrill et al. (1989) found that C1 and C2 differ by the presence of a
13-amino acid insert in C2, after either glycine-106 or serine-107 of
C1. The additional 13 amino acids account for the molecular mass
difference of C2 on SDS polyacrylamide gel electrophoresis. Otherwise C1
and C2 are identical; furthermore, the 3-prime and 5-prime untranslated
portions of the 2 mRNAs are identical (Swanson et al., 1987).
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the HNRNPC
gene to chromosome 14 (TMAP RH70234).
GENE FUNCTION
Locus control regions (LCRs) are regulatory DNA sequences located many
kilobases away from their cognate promoters. Mahajan et al. (2005) found
that an LCR-associated remodeling complex (LARC) purified from a human
erythroleukemia cell line exists as a single homogeneous complex of
hnRNP C1 and C2, the chromatin remodeling SWI/SNF complex (see 600014),
and the nucleosome remodeling and deacetylating (NURD; see 603526)/MECP1
(156535) complex.
Chen et al. (2006) purified the nuclear response element-binding protein
(REBiP) identified by Chen et al. (2003) in a patient with vitamin
D-dependent rickets type 2B (VDDR2B; 600785) and found a tryptic
fragment bearing 100% sequence identity with the human hnRNP C1 and C2
proteins (164020). Tryptic peptide sequencing followed by Western blot
analysis confirmed that cells from the VDDR2B patient overexpressed a
pair of anti-hnRNP C1/C2-reactive proteins of 39-40 kD, compatible with
the hnRNPC1 and the slightly larger hnRNPC2. When overexpressed in
vitamin D-responsive cells, cDNAs for both C1 and C2 inhibited VDR
(vitamin D receptor; 601769)-VDRE (vitamin D response element)-directed
transactivation by 23% and 42%, respectively (p less than 0.005 for
both). In contrast, transient expression of an hnRNP C1/C2 small
interfering RNA (siRNA) increased VDR transactivation by 39% (p less
than 0.005). Chromatin immunoprecipitation studies revealed the presence
of REBiP in vitamin D-responsive human cells and indicated that the
normal pattern of 1,25-dihydroxy vitamin D-initiated cyclical movement
of the VDR on and off the VDRE is legislated by competitive, reciprocal
occupancy of the VDRE by hnRNP C1/C2. The temporal and reciprocal
pattern of VDR and hnRNP C1/C2 interaction with the VDRE was lost in
VDDR2B cells overexpressing the hnRNP C1/C2 REBiP. Chen et al. (2006)
stated that their work provided further evidence that hnRNPs are able to
influence gene transcription itself by acting as binding proteins for
hormone response elements and suggested that hnRNP C1/C2 may be a key
determinant of the temporal patterns of VDRE occupancy.
*FIELD* RF
1. Burd, C. G.; Swanson, M. S.; Gorlach, M.; Dreyfuss, G.: Primary
structures of the heterogeneous nuclear ribonucleoprotein A2, B1,
and C2 proteins: a diversity of RNA binding proteins is generated
by small peptide inserts. Proc. Nat. Acad. Sci. 86: 9788-9792, 1989.
2. Chen, H.; Hewison, M.; Adams, J. S.: Functional characterization
of heterogeneous nuclear ribonuclear protein C1/C2 in vitamin D resistance:
a novel response element-binding protein. J. Biol. Chem. 281: 39114-39120,
2006.
3. Chen, H.; Hewison, M.; Hu, B.; Adams, J. S.: Heterogeneous nuclear
ribonucleoprotein (hnRNP) binding to hormone response elements: a
cause of vitamin D resistance. Proc. Nat. Acad. Sci. 100: 6109-6114,
2003.
4. Mahajan, M. C.; Narlikar, G. J.; Boyapaty, G.; Kingston, R. E.;
Weissman, S. M.: Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1,
and SWI/SNF form a chromatin remodeling complex at the beta-globin
locus control region. Proc. Nat. Acad. Sci. 102: 15012-15017, 2005.
5. Merrill, B. M.; Barnett, S. F.; LeStourgeon, W. M.; Williams, K.
R.: Primary structure differences between proteins C1 and C2 of HeLa
40S nuclear ribonucleoprotein particles. Nucleic Acids Res. 17:
8441-8449, 1989.
6. Nakagawa, T. Y.; Swanson, M. S.; Wold, B. J.; Dreyfuss, G.: Molecular
cloning of cDNA for the nuclear ribonucleoprotein particle C proteins:
a conserved gene family. Proc. Nat. Acad. Sci. 83: 2007-2011, 1986.
7. Swanson, M. S.; Nakagawa, T. Y.; LeVan, K.; Dreyfuss, G.: Primary
structure of human nuclear ribonucleoprotein particle C proteins:
conservation of sequence and domain structures in heterogeneous nuclear
RNA, mRNA, and pre-rRNA-binding proteins. Molec. Cell. Biol. 7:
1731-1739, 1987.
*FIELD* CN
Marla J. F. O'Neill - updated: 03/23/2010
Patricia A. Hartz - updated: 1/27/2006
Alan F. Scott - edited: 12/9/1996
*FIELD* CD
Victor A. McKusick: 6/25/1986
*FIELD* ED
carol: 03/23/2010
wwang: 8/27/2008
wwang: 1/24/2007
mgross: 2/1/2006
terry: 1/27/2006
dkim: 9/11/1998
mark: 9/8/1997
mark: 12/9/1996
carol: 2/24/1993
carol: 11/9/1992
supermim: 3/16/1992
supermim: 3/20/1990
carol: 1/16/1990
supermim: 1/12/1990
*RECORD*
*FIELD* NO
164020
*FIELD* TI
*164020 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN C; HNRNPC
;;HNRPC
NUCLEAR RIBONUCLEOPROTEIN PARTICLE C1 PROTEIN, INCLUDED;;
read moreNUCLEAR RIBONUCLEOPROTEIN PARTICLE C2 PROTEIN, INCLUDED
*FIELD* TX
DESCRIPTION
The primary nuclear transcripts of RNA polymerase II, some of which are
precursors to cytoplasmic mRNA (pre-mRNA), are collectively referred to
as heterogeneous nuclear RNAs (hnRNAs). At least 20 of these proteins,
designated A1 (34 kD) through U (120 kD), are present in abundance. In
the nucleus they are found in association with a specific set of
proteins to form ribonucleoprotein (hnRNP) particles. In vertebrates,
the C proteins, C1 and C2, are major constituents of these particles.
The 2 are antigenically closely related phosphoproteins, which bind
tightly to RNA in vitro (Nakagawa et al., 1986).
CLONING
Nakagawa et al. (1986) cloned cDNA for the hnRNA C proteins. Genomic
blot analysis showed homologous DNA sequences across eukaryotes from
human to yeast, indicating that the hnRNA C proteins are members of a
conserved gene family. Burd et al. (1989) reported the complete primary
structure of the hnRNP proteins A2, B1, and C2; A1, C1, and L had
previously been sequenced. They suggested that the C1 and C2 proteins
are produced by alternative splicing of a single gene transcript.
Merrill et al. (1989) found that C1 and C2 differ by the presence of a
13-amino acid insert in C2, after either glycine-106 or serine-107 of
C1. The additional 13 amino acids account for the molecular mass
difference of C2 on SDS polyacrylamide gel electrophoresis. Otherwise C1
and C2 are identical; furthermore, the 3-prime and 5-prime untranslated
portions of the 2 mRNAs are identical (Swanson et al., 1987).
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the HNRNPC
gene to chromosome 14 (TMAP RH70234).
GENE FUNCTION
Locus control regions (LCRs) are regulatory DNA sequences located many
kilobases away from their cognate promoters. Mahajan et al. (2005) found
that an LCR-associated remodeling complex (LARC) purified from a human
erythroleukemia cell line exists as a single homogeneous complex of
hnRNP C1 and C2, the chromatin remodeling SWI/SNF complex (see 600014),
and the nucleosome remodeling and deacetylating (NURD; see 603526)/MECP1
(156535) complex.
Chen et al. (2006) purified the nuclear response element-binding protein
(REBiP) identified by Chen et al. (2003) in a patient with vitamin
D-dependent rickets type 2B (VDDR2B; 600785) and found a tryptic
fragment bearing 100% sequence identity with the human hnRNP C1 and C2
proteins (164020). Tryptic peptide sequencing followed by Western blot
analysis confirmed that cells from the VDDR2B patient overexpressed a
pair of anti-hnRNP C1/C2-reactive proteins of 39-40 kD, compatible with
the hnRNPC1 and the slightly larger hnRNPC2. When overexpressed in
vitamin D-responsive cells, cDNAs for both C1 and C2 inhibited VDR
(vitamin D receptor; 601769)-VDRE (vitamin D response element)-directed
transactivation by 23% and 42%, respectively (p less than 0.005 for
both). In contrast, transient expression of an hnRNP C1/C2 small
interfering RNA (siRNA) increased VDR transactivation by 39% (p less
than 0.005). Chromatin immunoprecipitation studies revealed the presence
of REBiP in vitamin D-responsive human cells and indicated that the
normal pattern of 1,25-dihydroxy vitamin D-initiated cyclical movement
of the VDR on and off the VDRE is legislated by competitive, reciprocal
occupancy of the VDRE by hnRNP C1/C2. The temporal and reciprocal
pattern of VDR and hnRNP C1/C2 interaction with the VDRE was lost in
VDDR2B cells overexpressing the hnRNP C1/C2 REBiP. Chen et al. (2006)
stated that their work provided further evidence that hnRNPs are able to
influence gene transcription itself by acting as binding proteins for
hormone response elements and suggested that hnRNP C1/C2 may be a key
determinant of the temporal patterns of VDRE occupancy.
*FIELD* RF
1. Burd, C. G.; Swanson, M. S.; Gorlach, M.; Dreyfuss, G.: Primary
structures of the heterogeneous nuclear ribonucleoprotein A2, B1,
and C2 proteins: a diversity of RNA binding proteins is generated
by small peptide inserts. Proc. Nat. Acad. Sci. 86: 9788-9792, 1989.
2. Chen, H.; Hewison, M.; Adams, J. S.: Functional characterization
of heterogeneous nuclear ribonuclear protein C1/C2 in vitamin D resistance:
a novel response element-binding protein. J. Biol. Chem. 281: 39114-39120,
2006.
3. Chen, H.; Hewison, M.; Hu, B.; Adams, J. S.: Heterogeneous nuclear
ribonucleoprotein (hnRNP) binding to hormone response elements: a
cause of vitamin D resistance. Proc. Nat. Acad. Sci. 100: 6109-6114,
2003.
4. Mahajan, M. C.; Narlikar, G. J.; Boyapaty, G.; Kingston, R. E.;
Weissman, S. M.: Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1,
and SWI/SNF form a chromatin remodeling complex at the beta-globin
locus control region. Proc. Nat. Acad. Sci. 102: 15012-15017, 2005.
5. Merrill, B. M.; Barnett, S. F.; LeStourgeon, W. M.; Williams, K.
R.: Primary structure differences between proteins C1 and C2 of HeLa
40S nuclear ribonucleoprotein particles. Nucleic Acids Res. 17:
8441-8449, 1989.
6. Nakagawa, T. Y.; Swanson, M. S.; Wold, B. J.; Dreyfuss, G.: Molecular
cloning of cDNA for the nuclear ribonucleoprotein particle C proteins:
a conserved gene family. Proc. Nat. Acad. Sci. 83: 2007-2011, 1986.
7. Swanson, M. S.; Nakagawa, T. Y.; LeVan, K.; Dreyfuss, G.: Primary
structure of human nuclear ribonucleoprotein particle C proteins:
conservation of sequence and domain structures in heterogeneous nuclear
RNA, mRNA, and pre-rRNA-binding proteins. Molec. Cell. Biol. 7:
1731-1739, 1987.
*FIELD* CN
Marla J. F. O'Neill - updated: 03/23/2010
Patricia A. Hartz - updated: 1/27/2006
Alan F. Scott - edited: 12/9/1996
*FIELD* CD
Victor A. McKusick: 6/25/1986
*FIELD* ED
carol: 03/23/2010
wwang: 8/27/2008
wwang: 1/24/2007
mgross: 2/1/2006
terry: 1/27/2006
dkim: 9/11/1998
mark: 9/8/1997
mark: 12/9/1996
carol: 2/24/1993
carol: 11/9/1992
supermim: 3/16/1992
supermim: 3/20/1990
carol: 1/16/1990
supermim: 1/12/1990