CAPR1_HUMAN
ID CAPR1_HUMAN Reviewed; 709 AA.
AC Q14444; A6NMY7; D3DR06; Q15074; Q6IMN4; Q6IMN7; Q9BV09;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Caprin-1;
DE AltName: Full=Cell cycle-associated protein 1;
DE AltName: Full=Cytoplasmic activation- and proliferation-associated protein 1;
DE AltName: Full=GPI-anchored membrane protein 1;
DE AltName: Full=GPI-anchored protein p137;
DE Short=GPI-p137;
DE Short=p137GPI;
DE AltName: Full=Membrane component chromosome 11 surface marker 1;
DE AltName: Full=RNA granule protein 105;
GN Name=CAPRIN1; Synonyms=GPIAP1, GPIP137, M11S1, RNG105;
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] (ISOFORM 1), AND VARIANT ASP-263.
RC TISSUE=Colon;
RX PubMed=7657653; DOI=10.1074/jbc.270.35.20717;
RA Ellis J.A., Luzio J.P.;
RT "Identification and characterization of a novel protein (p137) which
RT transcytoses bidirectionally in Caco-2 cells.";
RL J. Biol. Chem. 270:20717-20723(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
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] (ISOFORM 1).
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-72.
RX PubMed=8786113; DOI=10.1006/geno.1996.0099;
RA Gessler M., Klant B., Tsaoussidou S., Ellis J.A., Luzio J.P.;
RT "The gene encoding the GPI-anchored membrane protein p137GPI (M11S1) maps
RT to human chromosome 11p13 and is highly conserved in the mouse.";
RL Genomics 32:169-170(1996).
RN [6]
RP PROTEIN SEQUENCE OF 56-63; 88-110; 115-125; 148-158; 298-310 AND 634-660,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP MULTIMERIZATION.
RX PubMed=14764709; DOI=10.4049/jimmunol.172.4.2389;
RA Grill B., Wilson G.M., Zhang K.-X., Wang B., Doyonnas R., Quadroni M.,
RA Schrader J.W.;
RT "Activation/division of lymphocytes results in increased levels of
RT cytoplasmic activation/proliferation-associated protein-1: prototype of a
RT new family of proteins.";
RL J. Immunol. 172:2389-2400(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH G3BP1, MRNA-BINDING, AND
RP MUTAGENESIS OF ARG-612; ARG-633 AND ARG-690.
RX PubMed=17210633; DOI=10.1128/mcb.02300-06;
RA Solomon S., Xu Y., Wang B., David M.D., Schubert P., Kennedy D.,
RA Schrader J.W.;
RT "Distinct structural features of caprin-1 mediate its interaction with
RT G3BP-1 and its induction of phosphorylation of eukaryotic translation
RT initiation factor 2alpha, entry to cytoplasmic stress granules, and
RT selective interaction with a subset of mRNAs.";
RL Mol. Cell. Biol. 27:2324-2342(2007).
RN [9]
RP IDENTIFICATION.
RX PubMed=20516077; DOI=10.1074/jbc.m110.108944;
RA Shiina N., Tokunaga M.;
RT "RNA granule protein 140 (RNG140), a paralog of RNG105 localized to
RT distinct RNA granules in neuronal dendrites in the adult vertebrate
RT brain.";
RL J. Biol. Chem. 285:24260-24269(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP 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 INTERACTION WITH PQBP1.
RX PubMed=21933836; DOI=10.1093/hmg/ddr430;
RA Kunde S.A., Musante L., Grimme A., Fischer U., Mueller E., Wanker E.E.,
RA Kalscheuer V.M.;
RT "The X-chromosome-linked intellectual disability protein PQBP1 is a
RT component of neuronal RNA granules and regulates the appearance of stress
RT granules.";
RL Hum. Mol. Genet. 20:4916-4931(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT PRO-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE 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 GLYCOSYLATION.
RX PubMed=22967762; DOI=10.1016/j.bbagen.2012.08.024;
RA Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F.,
RA Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.;
RT "Characterization of O-GlcNAc cycling and proteomic identification of
RT differentially O-GlcNAcylated proteins during G1/S transition.";
RL Biochim. Biophys. Acta 1820:1839-1848(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-343, AND
RP 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 [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-626; ARG-633; ARG-640 AND
RP ARG-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
RX PubMed=28733330; DOI=10.1042/bcj20170354;
RA Copsey A.C., Cooper S., Parker R., Lineham E., Lapworth C., Jallad D.,
RA Sweet S., Morley S.J.;
RT "The helicase, DDX3X, interacts with poly(A)-binding protein 1 (PABP1) and
RT caprin-1 at the leading edge of migrating fibroblasts and is required for
RT efficient cell spreading.";
RL Biochem. J. 474:3109-3120(2017).
CC -!- FUNCTION: May regulate the transport and translation of mRNAs of
CC proteins involved in synaptic plasticity in neurons and cell
CC proliferation and migration in multiple cell types. Binds directly and
CC selectively to MYC and CCND2 RNAs. In neuronal cells, directly binds to
CC several mRNAs associated with RNA granules, including BDNF, CAMK2A,
CC CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not
CC to rRNAs. {ECO:0000269|PubMed:17210633}.
CC -!- SUBUNIT: May form homomultimers (PubMed:14764709). Interacts with
CC G3BP1; interaction is direct and takes place in cytoplasmic RNA
CC granules (PubMed:17210633). Interacts with PQBP1 (PubMed:21933836).
CC Interacts with DDX3X (PubMed:28733330). {ECO:0000269|PubMed:14764709,
CC ECO:0000269|PubMed:17210633, ECO:0000269|PubMed:21933836,
CC ECO:0000269|PubMed:28733330}.
CC -!- INTERACTION:
CC Q14444; Q13283: G3BP1; NbExp=5; IntAct=EBI-1047080, EBI-1047359;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28733330}.
CC Cell projection, dendrite {ECO:0000250|UniProtKB:Q5M9G3}. Cell
CC projection, lamellipodium {ECO:0000269|PubMed:28733330}.
CC Note=Associated with RNA granules. At the leading edge of migrating
CC fibroblasts, colocalizes with DDX3X (PubMed:28733330).
CC {ECO:0000269|PubMed:28733330}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14444-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14444-2; Sequence=VSP_032687;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000269|PubMed:22967762}.
CC -!- MISCELLANEOUS: Overexpression induces the formation of cytoplasmic
CC stress granules and EIF2A phosphorylation through a mechanism that
CC depends on its ability to bind mRNA.
CC -!- SIMILARITY: Belongs to the caprin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a GPI-anchored membrane protein.
CC {ECO:0000305|PubMed:7657653}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA88096.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z48042; CAA88096.1; ALT_FRAME; mRNA.
DR EMBL; AC090469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68177.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68178.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68179.1; -; Genomic_DNA.
DR EMBL; BC001731; AAH01731.2; -; mRNA.
DR EMBL; X89572; CAA61751.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK001101; DAA01118.1; -; mRNA.
DR EMBL; BK001104; DAA01121.1; -; mRNA.
DR EMBL; BR000867; FAA00692.1; -; mRNA.
DR CCDS; CCDS31453.1; -. [Q14444-1]
DR CCDS; CCDS31454.1; -. [Q14444-2]
DR PIR; A57352; A57352.
DR RefSeq; NP_005889.3; NM_005898.4. [Q14444-1]
DR RefSeq; NP_976240.1; NM_203364.2. [Q14444-2]
DR RefSeq; XP_016873238.1; XM_017017749.1.
DR PDB; 4WBE; X-ray; 2.05 A; A/B/C=132-251.
DR PDB; 4WBP; X-ray; 2.50 A; A/B=132-251.
DR PDB; 6TA7; X-ray; 1.93 A; G/H=356-386.
DR PDBsum; 4WBE; -.
DR PDBsum; 4WBP; -.
DR PDBsum; 6TA7; -.
DR AlphaFoldDB; Q14444; -.
DR SMR; Q14444; -.
DR BioGRID; 110252; 221.
DR CORUM; Q14444; -.
DR IntAct; Q14444; 65.
DR MINT; Q14444; -.
DR STRING; 9606.ENSP00000340329; -.
DR ChEMBL; CHEMBL4295821; -.
DR GlyGen; Q14444; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; Q14444; -.
DR MetOSite; Q14444; -.
DR PhosphoSitePlus; Q14444; -.
DR SwissPalm; Q14444; -.
DR BioMuta; CAPRIN1; -.
DR DMDM; 182676426; -.
DR CPTAC; CPTAC-37; -.
DR CPTAC; CPTAC-38; -.
DR EPD; Q14444; -.
DR jPOST; Q14444; -.
DR MassIVE; Q14444; -.
DR MaxQB; Q14444; -.
DR PaxDb; Q14444; -.
DR PeptideAtlas; Q14444; -.
DR PRIDE; Q14444; -.
DR ProteomicsDB; 59992; -. [Q14444-1]
DR ProteomicsDB; 59993; -. [Q14444-2]
DR Antibodypedia; 12960; 334 antibodies from 32 providers.
DR DNASU; 4076; -.
DR Ensembl; ENST00000341394.9; ENSP00000340329.4; ENSG00000135387.21. [Q14444-1]
DR Ensembl; ENST00000389645.7; ENSP00000374296.3; ENSG00000135387.21. [Q14444-2]
DR Ensembl; ENST00000530820.5; ENSP00000434204.1; ENSG00000135387.21. [Q14444-2]
DR Ensembl; ENST00000532820.5; ENSP00000434150.1; ENSG00000135387.21. [Q14444-1]
DR GeneID; 4076; -.
DR KEGG; hsa:4076; -.
DR MANE-Select; ENST00000341394.9; ENSP00000340329.4; NM_005898.5; NP_005889.3.
DR UCSC; uc001mvg.4; human. [Q14444-1]
DR CTD; 4076; -.
DR DisGeNET; 4076; -.
DR GeneCards; CAPRIN1; -.
DR HGNC; HGNC:6743; CAPRIN1.
DR HPA; ENSG00000135387; Low tissue specificity.
DR MIM; 601178; gene.
DR neXtProt; NX_Q14444; -.
DR OpenTargets; ENSG00000135387; -.
DR PharmGKB; PA30508; -.
DR VEuPathDB; HostDB:ENSG00000135387; -.
DR eggNOG; ENOG502QUGC; Eukaryota.
DR GeneTree; ENSGT00940000153438; -.
DR InParanoid; Q14444; -.
DR OMA; VEQNYFK; -.
DR OrthoDB; 382856at2759; -.
DR PhylomeDB; Q14444; -.
DR TreeFam; TF329471; -.
DR PathwayCommons; Q14444; -.
DR SignaLink; Q14444; -.
DR SIGNOR; Q14444; -.
DR BioGRID-ORCS; 4076; 64 hits in 1081 CRISPR screens.
DR ChiTaRS; CAPRIN1; human.
DR GeneWiki; CAPRIN1; -.
DR GenomeRNAi; 4076; -.
DR Pharos; Q14444; Tbio.
DR PRO; PR:Q14444; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q14444; protein.
DR Bgee; ENSG00000135387; Expressed in cortical plate and 211 other tissues.
DR ExpressionAtlas; Q14444; baseline and differential.
DR Genevisible; Q14444; HS.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR IDEAL; IID00668; -.
DR InterPro; IPR028816; Caprin.
DR InterPro; IPR022070; Caprin-1_C.
DR InterPro; IPR041637; Caprin-1_dimer.
DR PANTHER; PTHR22922; PTHR22922; 1.
DR Pfam; PF12287; Caprin-1_C; 1.
DR Pfam; PF18293; Caprin-1_dimer; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Coiled coil; Cytoplasm; Differentiation; Direct protein sequencing;
KW Glycoprotein; Methylation; Phosphoprotein; Protein synthesis inhibitor;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..709
FT /note="Caprin-1"
FT /id="PRO_0000087549"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..381
FT /note="G3BP1-binding"
FT REGION 417..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..94
FT /evidence="ECO:0000255"
FT COILED 125..153
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q60865"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 626
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 633
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 640
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 698
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 698
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 690..709
FT /note="RGGPPRPNRGMPQMNTQQVN -> NILWW (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032687"
FT VARIANT 263
FT /note="A -> D (in dbSNP:rs1132973)"
FT /evidence="ECO:0000269|PubMed:7657653"
FT /id="VAR_042425"
FT VARIANT 588
FT /note="Q -> H (in dbSNP:rs12282627)"
FT /id="VAR_042426"
FT VARIANT 616
FT /note="R -> H (in dbSNP:rs11552285)"
FT /id="VAR_042427"
FT MUTAGEN 612
FT /note="R->A: Major reduction in MYC and CCND2 RNA-binding;
FT when associated with A-633 and A-690."
FT /evidence="ECO:0000269|PubMed:17210633"
FT MUTAGEN 633
FT /note="R->A: Major reduction in MYC and CCND2 RNA-binding;
FT when associated with A-612 and A-690."
FT /evidence="ECO:0000269|PubMed:17210633"
FT MUTAGEN 690
FT /note="R->A: Major reduction in MYC and CCND2 RNA-binding;
FT when associated with A-612 and A-633."
FT /evidence="ECO:0000269|PubMed:17210633"
FT CONFLICT 370
FT /note="Y -> D (in Ref. 1; CAA88096)"
FT /evidence="ECO:0000305"
FT HELIX 133..158
FT /evidence="ECO:0007829|PDB:4WBE"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:4WBE"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4WBE"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:4WBE"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:4WBE"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:4WBE"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4WBP"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:4WBE"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4WBE"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6TA7"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:6TA7"
SQ SEQUENCE 709 AA; 78366 MW; 56F5BC188CA3A2D4 CRC64;
MPSATSHSGS GSKSSGPPPP SGSSGSEAAA GAGAAAPASQ HPATGTGAVQ TEAMKQILGV
IDKKLRNLEK KKGKLDDYQE RMNKGERLNQ DQLDAVSKYQ EVTNNLEFAK ELQRSFMALS
QDIQKTIKKT ARREQLMREE AEQKRLKTVL ELQYVLDKLG DDEVRTDLKQ GLNGVPILSE
EELSLLDEFY KLVDPERDMS LRLNEQYEHA SIHLWDLLEG KEKPVCGTTY KVLKEIVERV
FQSNYFDSTH NHQNGLCEEE EAASAPAVED QVPEAEPEPA EEYTEQSEVE STEYVNRQFM
AETQFTSGEK EQVDEWTVET VEVVNSLQQQ PQAASPSVPE PHSLTPVAQA DPLVRRQRVQ
DLMAQMQGPY NFIQDSMLDF ENQTLDPAIV SAQPMNPTQN MDMPQLVCPP VHSESRLAQP
NQVPVQPEAT QVPLVSSTSE GYTASQPLYQ PSHATEQRPQ KEPIDQIQAT ISLNTDQTTA
SSSLPAASQP QVFQAGTSKP LHSSGINVNA APFQSMQTVF NMNAPVPPVN EPETLKQQNQ
YQASYNQSFS SQPHQVEQTE LQQEQLQTVV GTYHGSPDQS HQVTGNHQQP PQQNTGFPRS
NQPYYNSRGV SRGGSRGARG LMNGYRGPAN GFRGGYDGYR PSFSNTPNSG YTQSQFSAPR
DYSGYQRDGY QQNFKRGSGQ SGPRGAPRGR GGPPRPNRGM PQMNTQQVN
