PABP1_MOUSE
ID PABP1_MOUSE Reviewed; 636 AA.
AC P29341; Q99L36;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Polyadenylate-binding protein 1;
DE Short=PABP-1;
DE Short=Poly(A)-binding protein 1;
GN Name=Pabpc1; Synonyms=Pabp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=1630930; DOI=10.1093/nar/20.13.3519;
RA Wang M.-Y., Cutler M., Karimpour I., Kleene K.C.;
RT "Nucleotide sequence of a mouse testis poly(A) binding protein cDNA.";
RL Nucleic Acids Res. 20:3519-3519(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, Skin, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary tumor;
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 IN A MRNP COMPLEX WITH YBX2.
RX PubMed=10076007; DOI=10.1093/nar/27.7.1747;
RA Herbert T.P., Hecht N.B.;
RT "The mouse Y-box protein, MSY2, is associated with a kinase on non-
RT polysomal mouse testicular mRNAs.";
RL Nucleic Acids Res. 27:1747-1753(1999).
RN [6]
RP INTERACTION WITH CSDE1.
RX PubMed=15314026; DOI=10.1101/gad.1219104;
RA Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S.,
RA Kahvejian A., Sonenberg N., Shyu A.-B.;
RT "UNR, a new partner of poly(A)-binding protein, plays a key role in
RT translationally coupled mRNA turnover mediated by the c-fos major coding-
RT region determinant.";
RL Genes Dev. 18:2010-2023(2004).
RN [7]
RP INTERACTION WITH TENT2.
RX PubMed=17927953; DOI=10.1016/j.bbrc.2007.09.096;
RA Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T., Kimura M.,
RA Kashiwabara S., Baba T.;
RT "Disruption of mouse poly(A) polymerase mGLD-2 does not alter
RT polyadenylation status in oocytes and somatic cells.";
RL Biochem. Biophys. Res. Commun. 364:14-19(2007).
RN [8]
RP INTERACTION WITH PIWIL1.
RX PubMed=19020299; DOI=10.1095/biolreprod.108.072553;
RA Kimura M., Ishida K., Kashiwabara S., Baba T.;
RT "Characterization of two cytoplasmic poly(A)-binding proteins, PABPC1 and
RT PABPC2, in mouse spermatogenic cells.";
RL Biol. Reprod. 80:545-554(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-419; ARG-475; ARG-493 AND
RP ARG-506, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA, including that of its own
CC transcript, and regulates processes of mRNA metabolism such as pre-mRNA
CC splicing and mRNA stability. Its function in translational initiation
CC regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can
CC probably bind to cytoplasmic RNA sequences other than poly(A) in vivo.
CC Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to
CC MYC stability by binding to m6A-containing MYC mRNAs. Involved in
CC translationally coupled mRNA turnover. Implicated with other RNA-
CC binding proteins in the cytoplasmic deadenylation/translational and
CC decay interplay of the FOS mRNA mediated by the major coding-region
CC determinant of instability (mCRD) domain. Involved in regulation of
CC nonsense-mediated decay (NMD) of mRNAs containing premature stop
CC codons; for the recognition of premature termination codons (PTC) and
CC initiation of NMD a competitive interaction between UPF1 and PABPC1
CC with the ribosome-bound release factors is proposed. By binding to long
CC poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and
CC hence contribute to mRNA stability. {ECO:0000250|UniProtKB:P11940}.
CC -!- SUBUNIT: May form homodimers. Component of a multisubunit
CC autoregulatory ribonucleoprotein complex (ARC), at least composed of
CC IGF2BP1, PABPC1 and CSDE1. Directly interacts with IGF2BP1. Part of a
CC complex associated with the FOS mCRD domain and consisting of HNRPD,
CC SYNCRIP, PAIP1 and CSDE1/UNR. Interacts with PAIP1 and PAIP2 (via the
CC PABPC1-interacting motifs PAM1 and PAM2). Interacts with PAIP1 with a
CC 1:1 stoichiometry and with PAIP2 with a 1:2 stoichiometry (By
CC similarity). The interaction with CSDE1 is direct and RNA-independent
CC (PubMed:15314026). Found in a mRNP complex with YBX2 (PubMed:10076007).
CC Interacts with TENT2/GLD2 (PubMed:17927953). Identified in the
CC spliceosome C complex. Identified in a mRNP complex, at least composed
CC of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2,
CC STAU1, STAU2, SYNCRIP and YBX1. The interaction with DDX3X is direct
CC and RNA-independent. This interaction increases in stressed cells and
CC decreases during cell recovery. Identified in a IGF2BP1-dependent mRNP
CC granule complex containing untranslated mRNAs. Interacts with NXF1/TAP
CC (By similarity). Interacts with PIWIL1 (PubMed:19020299). Interacts
CC with AGO1, AGO2, GSPT1 and GSPT2. Interacts with LARP4B. Interacts (via
CC the second and third RRM domains and the C-terminus) with PAIP2B (via
CC central acidic portion and C-terminus). Forms a complex with LARP1 and
CC SHFL. Interacts with LARP4. Interacts with ZFC3H1 in a RNase-sensitive
CC manner. Interacts with TRIM71 (via NHL repeats) in an RNA-dependent
CC manner. Interacts with TENT5C; the interaction has no effect on TENT5C
CC poly(A) polymerase function. Interacts with G3BP1 and G3BP2 (By
CC similarity). Interacts with ENDOV; the interaction is RNA-dependent and
CC stimulates ENDOV activity (By similarity). Interacts with UPF1; the
CC interaction is RNA-dependent (By similarity). Interacts with IGF2BP2
CC and IGF2BP3. May interact with SETX. {ECO:0000250|UniProtKB:P11940,
CC ECO:0000269|PubMed:10076007, ECO:0000269|PubMed:15314026,
CC ECO:0000269|PubMed:17927953, ECO:0000269|PubMed:19020299}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11940}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P11940}. Nucleus
CC {ECO:0000250|UniProtKB:P11940}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P11940}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs (By similarity). Shuttles
CC between the cytoplasm and the nucleus (By similarity). During stress
CC and in the absence of DDX3X, localizes to the nucleus (By similarity).
CC At the leading edge of migrating fibroblasts, colocalizes with DDX3X
CC (By similarity). Relocalizes to cytoplasmic stress granules upon
CC cellular stress where it colocalizes with ENDOV (By similarity).
CC {ECO:0000250|UniProtKB:P11940}.
CC -!- DOMAIN: The RNA-binding domains RRM1 and RRM2 and the C-terminus (last
CC 138 amino acids) regions interact respectively with the PABPC1-
CC interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
CC {ECO:0000250|UniProtKB:P11940}.
CC -!- DOMAIN: The RNA-binding domains RRM2 and RRM3 and the C-terminus (last
CC 138 amino acids) regions interact with the PABPC1-interacting motif-1
CC (PAM1) and -2 (PAM2) of PAIP2, respectively.
CC {ECO:0000250|UniProtKB:P11940}.
CC -!- PTM: Phosphorylated by MAPKAPK2. {ECO:0000250|UniProtKB:P11940}.
CC -!- PTM: Methylated by CARM1. Arg-493 is dimethylated, probably to
CC asymmetric dimethylarginine (By similarity).
CC {ECO:0000250|UniProtKB:P11940}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; X65553; CAA46522.1; -; mRNA.
DR EMBL; AK044829; BAC32110.1; -; mRNA.
DR EMBL; AK133196; BAE21553.1; -; mRNA.
DR EMBL; AK159703; BAE35302.1; -; mRNA.
DR EMBL; AK159733; BAE35327.1; -; mRNA.
DR EMBL; AK160968; BAE36120.1; -; mRNA.
DR EMBL; AK161123; BAE36203.1; -; mRNA.
DR EMBL; AK161671; BAE36522.1; -; mRNA.
DR EMBL; AK168466; BAE40360.1; -; mRNA.
DR EMBL; CH466541; EDL08818.1; -; Genomic_DNA.
DR EMBL; BC003870; AAH03870.1; -; mRNA.
DR EMBL; BC011207; AAH11207.1; -; mRNA.
DR EMBL; BC023145; AAH23145.1; -; mRNA.
DR EMBL; BC046233; AAH46233.1; -; mRNA.
DR CCDS; CCDS27431.1; -.
DR PIR; I48718; I48718.
DR RefSeq; NP_032800.2; NM_008774.3.
DR RefSeq; XP_011243641.1; XM_011245339.2.
DR AlphaFoldDB; P29341; -.
DR BMRB; P29341; -.
DR SMR; P29341; -.
DR BioGRID; 202010; 161.
DR ComplexPortal; CPX-1078; mCRD-poly(A)-bridging complex.
DR DIP; DIP-32127N; -.
DR IntAct; P29341; 36.
DR MINT; P29341; -.
DR STRING; 10090.ENSMUSP00000001809; -.
DR iPTMnet; P29341; -.
DR PhosphoSitePlus; P29341; -.
DR SwissPalm; P29341; -.
DR REPRODUCTION-2DPAGE; P29341; -.
DR EPD; P29341; -.
DR jPOST; P29341; -.
DR MaxQB; P29341; -.
DR PaxDb; P29341; -.
DR PeptideAtlas; P29341; -.
DR PRIDE; P29341; -.
DR ProteomicsDB; 287760; -.
DR DNASU; 18458; -.
DR Ensembl; ENSMUST00000001809; ENSMUSP00000001809; ENSMUSG00000022283.
DR GeneID; 18458; -.
DR KEGG; mmu:18458; -.
DR UCSC; uc007vmx.2; mouse.
DR CTD; 26986; -.
DR MGI; MGI:1349722; Pabpc1.
DR VEuPathDB; HostDB:ENSMUSG00000022283; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000153773; -.
DR HOGENOM; CLU_012062_22_2_1; -.
DR InParanoid; P29341; -.
DR OMA; SHAEQKD; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; P29341; -.
DR TreeFam; TF300458; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-429947; Deadenylation of mRNA.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 18458; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Pabpc1; mouse.
DR PRO; PR:P29341; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P29341; protein.
DR Bgee; ENSMUSG00000022283; Expressed in embryonic post-anal tail and 226 other tissues.
DR ExpressionAtlas; P29341; baseline and differential.
DR Genevisible; P29341; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; ISO:MGI.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF63570; SSF63570; 1.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Cytoplasm; Methylation; mRNA processing;
KW mRNA splicing; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Spliceosome.
FT CHAIN 1..636
FT /note="Polyadenylate-binding protein 1"
FT /id="PRO_0000081699"
FT DOMAIN 11..89
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 99..175
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 191..268
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 294..370
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 542..619
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 166..289
FT /note="CSDE1-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 299
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 385
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 419
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 432
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 436
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 455
FT /note="Omega-N-methylated arginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 460
FT /note="Omega-N-methylated arginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 475
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 481
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 493
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 493
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 493
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 506
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 512
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 518
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT CONFLICT 176
FT /note="R -> Q (in Ref. 1; CAA46522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 70671 MW; E5BB6D5BA4F86CB7 CRC64;
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ
QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS
AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE
AELGARAKEF TNVYIKNFGE DMDDERLKEL FGKFGPALSV KVMTDESGKS KGFGFVSFER
HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT
KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY QPAPPSGYFM AAIPQTQNRA
AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ
RVANTSTQTM GPRPAAAAAA ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ
GQEPLTASML ASAPPQEQKQ MLGERLFPLI QAMHPSLAGK ITGMLLEIDN SELLHMLESP
ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV
