HNRPQ_MOUSE
ID HNRPQ_MOUSE Reviewed; 623 AA.
AC Q7TMK9; O88991; Q2YDV8; Q68ED6; Q80YV6; Q8BGP1; Q8C5K6; Q8CGC2; Q91ZR0;
AC Q99KU9; Q9QYF4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein Q;
DE Short=hnRNP Q;
DE AltName: Full=Glycine- and tyrosine-rich RNA-binding protein;
DE Short=GRY-RBP;
DE AltName: Full=NS1-associated protein 1;
DE AltName: Full=Synaptotagmin-binding, cytoplasmic RNA-interacting protein;
DE AltName: Full=pp68;
GN Name=Syncrip; Synonyms=Hnrpq, Nsap1, Nsap1l;
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] (ISOFORM 1).
RA Du G., Pan M., Zhou Y., Chen J., Yao H., Yuan J., Qiang B.;
RT "Cloning of human and mouse GRY-RBP cDNA.";
RL Chin. Sci. Bull. 45:343-349(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 257-282, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH SYT7;
RP SYT8 AND SYT9.
RC STRAIN=ddY; TISSUE=Brain, and Cerebellum;
RX PubMed=10734137; DOI=10.1074/jbc.275.13.9823;
RA Mizutani A., Fukuda M., Ibata K., Shiraishi Y., Mikoshiba K.;
RT "SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
RT ribonucleoprotein R, interacts with ubiquitous synaptotagmin isoforms.";
RL J. Biol. Chem. 275:9823-9831(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Medulla oblongata;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Embryo, Embryonic brain, Kidney, Mammary tumor, and Retina;
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 [MRNA] OF 66-561 (ISOFORM 2).
RA Zhou M., Raschke W.C.;
RT "Mus musculus RRM RNA binding protein, NSAP1.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, PHOSPHORYLATION
RP AT TYROSINE RESIDUES, AND ASSOCIATION WITH POLYSOMES.
RC TISSUE=Adipocyte;
RX PubMed=11994298; DOI=10.1074/jbc.m202556200;
RA Hresko R.C., Mueckler M.;
RT "Identification of pp68 as the tyrosine-phosphorylated form of
RT SYNCRIP/NSAP1. A cytoplasmic RNA-binding protein.";
RL J. Biol. Chem. 277:25233-25238(2002).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=9847309; DOI=10.1128/jvi.73.1.72-80.1999;
RA Harris C.E., Boden R.A., Astell C.R.;
RT "A novel heterogeneous nuclear ribonucleoprotein-like protein interacts
RT with NS1 of the minute virus of mice.";
RL J. Virol. 73:72-80(1999).
RN [8]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH SMN.
RX PubMed=11773003; DOI=10.1093/hmg/11.1.93;
RA Rossoll W., Kroening A.-K., Ohndorf U.-M., Steegborn C., Jablonka S.,
RA Sendtner M.;
RT "Specific interaction of Smn, the spinal muscular atrophy determining gene
RT product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA processing
RT in motor axons?";
RL Hum. Mol. Genet. 11:93-105(2002).
RN [9]
RP IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19470752; DOI=10.1128/mcb.00296-09;
RA Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
RT "Three proteins of the U7-specific Sm ring function as the molecular ruler
RT to determine the site of 3'-end processing in mammalian histone pre-mRNA.";
RL Mol. Cell. Biol. 29:4045-4056(2009).
RN [10]
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).
CC -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) implicated in
CC mRNA processing mechanisms. Component of the CRD-mediated complex that
CC promotes MYC mRNA stability. Isoform 1 and isoform 2 are associated in
CC vitro with pre-mRNA, splicing intermediates and mature mRNA protein
CC complexes. Isoform 1 binds to apoB mRNA AU-rich sequences (By
CC similarity). Isoform 1 is part of the APOB mRNA editosome complex and
CC may modulate the postranscriptional C to U RNA-editing of the APOB mRNA
CC through either by binding to A1CF (APOBEC1 complementation factor), to
CC APOBEC1 or to RNA itself (By similarity). May be 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 (By similarity). Interacts in
CC vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 2
CC may be involved in cytoplasmic vesicle-based mRNA transport through
CC interaction with synaptotagmins. {ECO:0000250}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the
CC coding region determinant (CRD)-mediated complex, composed of DHX9,
CC HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a mRNP complex, at
CC least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1,
CC PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP
CC granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1,
CC HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8,
CC IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3,
CC RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, YBX1 and untranslated mRNAs.
CC Interacts with GTPBP1 (By similarity). Isoform 1 is a component of the
CC APOB mRNA editosome complex. Isoform 1 interacts with APOBEC1 and A1CF.
CC Part of a complex associated with the FOS mCRD domain and consisting of
CC PABPC1, PAIP1, CSDE1/UNR, HNRPD and SYNCRIP. Isoform 2 interacts with
CC HNRPR. Interacts with POLR2A hyperphosphorylated C-terminal domain.
CC Interacts with HABP4 (By similarity). Identified in a histone pre-mRNA
CC complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and
CC YBX1. Isoform 1 and isoform 2 interact with SMN. Isoform 2 interacts
CC through its C-terminal domain with SYT7, SYT8 and SYT9. The non-
CC phosphorylated and phosphorylated forms are colocalized with PAIP1 in
CC polysomes. {ECO:0000250|UniProtKB:O60506, ECO:0000269|PubMed:10734137,
CC ECO:0000269|PubMed:11773003, ECO:0000269|PubMed:19470752}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10734137,
CC ECO:0000269|PubMed:11994298}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:O43390}. Microsome
CC {ECO:0000269|PubMed:11994298}. Cytoplasm {ECO:0000269|PubMed:10734137}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs (By similarity). Isoforms 1 and 2 are expressed predominantly in
CC the nucleoplasm. According to PubMed:10734137, isoform 2 is
CC predominantly found in cytoplasm. The tyrosine phosphorylated form
CC bound to RNA is found in microsomes. {ECO:0000250|UniProtKB:O43390,
CC ECO:0000269|PubMed:10734137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TMK9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TMK9-2; Sequence=VSP_009585, VSP_009586;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, spleen, lung,
CC liver, skeletal muscle, adipocytes, kidney and testis.
CC {ECO:0000269|PubMed:10734137, ECO:0000269|PubMed:11773003,
CC ECO:0000269|PubMed:9847309}.
CC -!- DEVELOPMENTAL STAGE: Expressed in spinal cord at 14 dpc and onwards.
CC {ECO:0000269|PubMed:11773003}.
CC -!- DOMAIN: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-box)
CC may be involved in RNA-binding and protein-protein interactions. It is
CC methylated by PRMT1, and essential for nuclear localization (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine. The membrane-bound form found in
CC microsomes is phosphorylated in vitro by insulin receptor tyrosine
CC kinase (INSR). Phosphorylation is inhibited upon binding to RNA,
CC whereas the cytoplasmic form is poorly phosphorylated.
CC {ECO:0000269|PubMed:11994298}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice site
CC and to an exon inclusion. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55863.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH58807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF093821; AAC62511.1; -; mRNA.
DR EMBL; AB035725; BAA88342.1; -; mRNA.
DR EMBL; AK034845; BAC28852.1; -; mRNA.
DR EMBL; AK077588; BAC36880.1; -; mRNA.
DR EMBL; AK078158; BAC37152.1; -; mRNA.
DR EMBL; BC004001; AAH04001.1; ALT_SEQ; mRNA.
DR EMBL; BC041148; AAH41148.2; -; mRNA.
DR EMBL; BC050079; AAH50079.2; -; mRNA.
DR EMBL; BC055863; AAH55863.1; ALT_INIT; mRNA.
DR EMBL; BC058807; AAH58807.1; ALT_INIT; mRNA.
DR EMBL; BC080309; AAH80309.1; -; mRNA.
DR EMBL; BC108363; AAI08364.2; -; mRNA.
DR EMBL; AF408434; AAL11726.1; -; mRNA.
DR CCDS; CCDS23388.1; -. [Q7TMK9-2]
DR CCDS; CCDS57686.1; -. [Q7TMK9-1]
DR RefSeq; NP_001271257.1; NM_001284328.1.
DR RefSeq; NP_001298042.1; NM_001311113.1.
DR RefSeq; NP_062640.2; NM_019666.2. [Q7TMK9-1]
DR RefSeq; NP_062770.1; NM_019796.5. [Q7TMK9-2]
DR AlphaFoldDB; Q7TMK9; -.
DR SMR; Q7TMK9; -.
DR BioGRID; 207955; 104.
DR ComplexPortal; CPX-1078; mCRD-poly(A)-bridging complex.
DR ComplexPortal; CPX-1089; CRD-mediated mRNA stability complex.
DR ComplexPortal; CPX-1098; C-to-U editosome complex. [Q7TMK9-1]
DR IntAct; Q7TMK9; 6.
DR MINT; Q7TMK9; -.
DR STRING; 10090.ENSMUSP00000063744; -.
DR iPTMnet; Q7TMK9; -.
DR PhosphoSitePlus; Q7TMK9; -.
DR SwissPalm; Q7TMK9; -.
DR REPRODUCTION-2DPAGE; IPI00406117; -.
DR EPD; Q7TMK9; -.
DR jPOST; Q7TMK9; -.
DR MaxQB; Q7TMK9; -.
DR PaxDb; Q7TMK9; -.
DR PeptideAtlas; Q7TMK9; -.
DR PRIDE; Q7TMK9; -.
DR ProteomicsDB; 273373; -. [Q7TMK9-1]
DR ProteomicsDB; 273374; -. [Q7TMK9-2]
DR Antibodypedia; 18610; 298 antibodies from 37 providers.
DR DNASU; 56403; -.
DR Ensembl; ENSMUST00000069221; ENSMUSP00000063744; ENSMUSG00000032423. [Q7TMK9-2]
DR Ensembl; ENSMUST00000173801; ENSMUSP00000133649; ENSMUSG00000032423. [Q7TMK9-1]
DR GeneID; 56403; -.
DR KEGG; mmu:56403; -.
DR UCSC; uc009qyo.2; mouse. [Q7TMK9-2]
DR UCSC; uc009qyq.2; mouse. [Q7TMK9-1]
DR CTD; 10492; -.
DR MGI; MGI:1891690; Syncrip.
DR VEuPathDB; HostDB:ENSMUSG00000032423; -.
DR eggNOG; KOG0117; Eukaryota.
DR GeneTree; ENSGT00940000153511; -.
DR InParanoid; Q7TMK9; -.
DR OMA; KAMEGMN; -.
DR PhylomeDB; Q7TMK9; -.
DR TreeFam; TF314932; -.
DR BioGRID-ORCS; 56403; 6 hits in 76 CRISPR screens.
DR ChiTaRS; Syncrip; mouse.
DR PRO; PR:Q7TMK9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q7TMK9; protein.
DR Bgee; ENSMUSG00000032423; Expressed in ureter smooth muscle and 277 other tissues.
DR ExpressionAtlas; Q7TMK9; baseline and differential.
DR Genevisible; Q7TMK9; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0097452; C:GAIT complex; ISO:MGI.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045293; C:mRNA editing complex; IC:ComplexPortal.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1990635; C:proximal dendrite; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:0016556; P:mRNA modification; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0090367; P:negative regulation of mRNA modification; ISO:MGI.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:MGI.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; IC:ComplexPortal.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12483; RRM1_hnRNPQ; 1.
DR CDD; cd12489; RRM2_hnRNPQ; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR041337; hnRNP_Q_AcD.
DR InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR InterPro; IPR034544; hnRNPQ_RRM1.
DR InterPro; IPR034548; hnRNPQ_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF18360; hnRNP_Q_AcD; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Isopeptide bond; Methylation; Microsome;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT CHAIN 2..623
FT /note="Heterogeneous nuclear ribonucleoprotein Q"
FT /id="PRO_0000081868"
FT DOMAIN 162..241
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 243..325
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 338..408
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 448..450
FT /note="1-1"
FT REPEAT 451..453
FT /note="1-2"
FT REPEAT 460..464
FT /note="2-1"
FT REPEAT 469..472
FT /note="2-2"
FT REPEAT 478..480
FT /note="1-3"
FT REPEAT 485..488
FT /note="2-3"
FT REPEAT 498..500
FT /note="1-4"
FT REPEAT 526..528
FT /note="1-5"
FT REPEAT 539..541
FT /note="1-6"
FT REPEAT 554..556
FT /note="1-7"
FT REPEAT 557..559
FT /note="1-8"
FT REGION 400..561
FT /note="Interaction with APOBEC1"
FT /evidence="ECO:0000250"
FT REGION 448..559
FT /note="8 X 3 AA repeats of R-G-G"
FT REGION 460..488
FT /note="3 X 4 AA repeats of Y-Y-G-Y"
FT REGION 497..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..549
FT /note="Interaction with SMN"
FT /evidence="ECO:0000250"
FT MOTIF 564..578
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 574..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 363
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 373
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 444
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 444
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 496
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 510
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 518
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 518
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 526
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 526
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 536
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 536
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 539
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 539
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT CROSSLNK 607
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT VAR_SEQ 550..562
FT /note="VRGARGGRGGNVG -> QGKGVEAGPDLLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10734137,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.5"
FT /id="VSP_009585"
FT VAR_SEQ 563..623
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10734137,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.5"
FT /id="VSP_009586"
FT CONFLICT 143
FT /note="K -> E (in Ref. 4; AAH58807)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="M -> T (in Ref. 4; AAH50079)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="L -> LTGL (in Ref. 1; AAC62511)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="V -> A (in Ref. 1; AAC62511)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="L -> Q (in Ref. 1; AAC62511)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="T -> A (in Ref. 1; AAC62511)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="K -> N (in Ref. 3; BAC37152)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="Q -> K (in Ref. 3; BAC37152)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="Q -> H (in Ref. 3; BAC37152)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="G -> A (in Ref. 1; AAC62511)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="Missing (in Ref. 1; AAC62511)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="N -> H (in Ref. 1; AAC62511)"
FT /evidence="ECO:0000305"
FT CONFLICT Q7TMK9-2:549..550
FT /note="GQ -> G (in Ref. 2; BAA88342 and 4; AAH41148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 69633 MW; 8139FF9E2C8FB304 CRC64;
MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER
AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD
EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP
LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV
ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA
QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT EEILEKSFSQ
FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN IEIVFAKPPD QKRKERKAQR
QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG
YEDPYYGYED FQVGARGRGG RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG
GAQQQRGRGV RGARGGRGGN VGGKRKADGY NQPDTKRRQT NNQNWGSQPI AQQPLQGGDH
SGNYGYKSEN QEFYQDTFGQ QWK
