HNRPM_HUMAN
ID HNRPM_HUMAN Reviewed; 730 AA.
AC P52272; Q15584; Q8WZ44; Q96H56; Q9BWL9; Q9Y492;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein M;
DE Short=hnRNP M;
GN Name=HNRNPM; Synonyms=HNRPM, NAGR1;
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] (ISOFORMS 1; 2 AND 3).
RX PubMed=8441656; DOI=10.1093/nar/21.3.439;
RA Datar K.V., Dreyfuss G., Swanson M.S.;
RT "The human hnRNP M proteins: identification of a methionine/arginine-rich
RT repeat motif in ribonucleoproteins.";
RL Nucleic Acids Res. 21:439-446(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8692693; DOI=10.1093/nar/24.13.2535;
RA Gattoni R., Mahe D., Mahl P., Fischer N., Mattei M.-G., Stevenin J.,
RA Fuchs J.-P.;
RT "The human hnRNP-M proteins: structure and relation with early heat shock-
RT induced splicing arrest and chromosome mapping.";
RL Nucleic Acids Res. 24:2535-2542(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Zhao Z., Huang X., Li N., Cao X.;
RT "A new human M4 protein with deletion.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lymph, 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-17; 73-83; 222-232; 372-381; 404-410; 497-503;
RP 518-524 AND 628-650, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618 AND SER-701, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575; SER-588; SER-618 AND
RP SER-701, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-633 AND SER-637, AND
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-277 AND LYS-698, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575; SER-588; SER-618 AND
RP SER-701, AND IDENTIFICATION BY 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-432; SER-452;
RP SER-481; SER-528; SER-575; SER-588; SER-618 AND SER-701, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-86; SER-204; SER-365;
RP SER-377; SER-397; SER-432; SER-468; SER-575; SER-588; SER-618; SER-633;
RP SER-637; THR-665 AND SER-701, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-397; SER-618;
RP SER-633 AND SER-637, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-496, AND IDENTIFICATION BY MASS
RP 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 [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-83; LYS-145; LYS-388;
RP LYS-685 AND LYS-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-698, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [24]
RP INTERACTION WITH PPIA.
RX PubMed=25678563; DOI=10.1093/brain/awv005;
RA Lauranzano E., Pozzi S., Pasetto L., Stucchi R., Massignan T., Paolella K.,
RA Mombrini M., Nardo G., Lunetta C., Corbo M., Mora G., Bendotti C.,
RA Bonetto V.;
RT "Peptidylprolyl isomerase A governs TARDBP function and assembly in
RT heterogeneous nuclear ribonucleoprotein complexes.";
RL Brain 138:974-991(2015).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-83; LYS-145 AND LYS-698,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-145 AND LYS-698, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [27]
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 [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-37; LYS-69; LYS-83;
RP LYS-88; LYS-127; LYS-134; LYS-143; LYS-145; LYS-221; LYS-277; LYS-285;
RP LYS-345; LYS-381; LYS-388; LYS-651; LYS-667; LYS-685; LYS-692; LYS-698 AND
RP LYS-716, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [29]
RP STRUCTURE BY NMR OF 196-296 AND 652-730.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domains of heterogeneous nuclear
RT ribonucleoprotein M.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Pre-mRNA binding protein in vivo, binds avidly to poly(G) and
CC poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a
CC receptor for carcinoembryonic antigen in Kupffer cells, may initiate a
CC series of signaling events leading to tyrosine phosphorylation of
CC proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis
CC factor alpha cytokines.
CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638).
CC Interacts with PPIA/CYPA (PubMed:25678563).
CC {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:25678563}.
CC -!- INTERACTION:
CC P52272; Q99996-2: AKAP9; NbExp=3; IntAct=EBI-486809, EBI-9641546;
CC P52272; Q99459: CDC5L; NbExp=7; IntAct=EBI-486809, EBI-374880;
CC P52272; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-486809, EBI-745707;
CC P52272; O14964: HGS; NbExp=3; IntAct=EBI-486809, EBI-740220;
CC P52272; P52597: HNRNPF; NbExp=6; IntAct=EBI-486809, EBI-352986;
CC P52272; P31943: HNRNPH1; NbExp=3; IntAct=EBI-486809, EBI-351590;
CC P52272; Q96PV6: LENG8; NbExp=3; IntAct=EBI-486809, EBI-739546;
CC P52272; P25800: LMO1; NbExp=3; IntAct=EBI-486809, EBI-8639312;
CC P52272; P25791: LMO2; NbExp=4; IntAct=EBI-486809, EBI-739696;
CC P52272; P25791-3: LMO2; NbExp=3; IntAct=EBI-486809, EBI-11959475;
CC P52272; P43360: MAGEA6; NbExp=3; IntAct=EBI-486809, EBI-1045155;
CC P52272; O43660: PLRG1; NbExp=5; IntAct=EBI-486809, EBI-1051504;
CC P52272; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-486809, EBI-750487;
CC P52272; O95271: TNKS; NbExp=3; IntAct=EBI-486809, EBI-1105254;
CC P52272; Q92973: TNPO1; NbExp=3; IntAct=EBI-486809, EBI-286693;
CC P52272; Q13077: TRAF1; NbExp=3; IntAct=EBI-486809, EBI-359224;
CC P52272; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-486809, EBI-744794;
CC P52272; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-486809, EBI-1185167;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|Ref.5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=M4;
CC IsoId=P52272-1; Sequence=Displayed;
CC Name=2; Synonyms=M1-M2;
CC IsoId=P52272-2; Sequence=VSP_005845;
CC Name=3; Synonyms=M3;
CC IsoId=P52272-3; Sequence=Not described;
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
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DR EMBL; L03532; AAA36192.1; -; mRNA.
DR EMBL; L32611; AAL31359.1; -; mRNA.
DR EMBL; AF061832; AAC16002.1; -; mRNA.
DR EMBL; BC000138; AAH00138.2; -; mRNA.
DR EMBL; BC008895; AAH08895.2; -; mRNA.
DR EMBL; BC019580; AAH19580.1; -; mRNA.
DR CCDS; CCDS12203.1; -. [P52272-1]
DR CCDS; CCDS12204.1; -. [P52272-2]
DR PIR; S35532; S35532.
DR RefSeq; NP_005959.2; NM_005968.4. [P52272-1]
DR RefSeq; NP_112480.2; NM_031203.3. [P52272-2]
DR PDB; 2DGV; NMR; -; A=652-730.
DR PDB; 2DH9; NMR; -; A=655-730.
DR PDB; 2DO0; NMR; -; A=196-296.
DR PDB; 2OT8; X-ray; 3.10 A; C/D=41-70.
DR PDBsum; 2DGV; -.
DR PDBsum; 2DH9; -.
DR PDBsum; 2DO0; -.
DR PDBsum; 2OT8; -.
DR AlphaFoldDB; P52272; -.
DR SMR; P52272; -.
DR BioGRID; 110751; 544.
DR CORUM; P52272; -.
DR DIP; DIP-29336N; -.
DR IntAct; P52272; 154.
DR MINT; P52272; -.
DR STRING; 9606.ENSP00000325376; -.
DR GlyGen; P52272; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P52272; -.
DR MetOSite; P52272; -.
DR PhosphoSitePlus; P52272; -.
DR SwissPalm; P52272; -.
DR BioMuta; HNRNPM; -.
DR DMDM; 55977747; -.
DR REPRODUCTION-2DPAGE; IPI00383296; -.
DR UCD-2DPAGE; P52272; -.
DR CPTAC; CPTAC-385; -.
DR CPTAC; CPTAC-386; -.
DR EPD; P52272; -.
DR jPOST; P52272; -.
DR MassIVE; P52272; -.
DR MaxQB; P52272; -.
DR PaxDb; P52272; -.
DR PeptideAtlas; P52272; -.
DR PRIDE; P52272; -.
DR ProteomicsDB; 56473; -. [P52272-1]
DR ProteomicsDB; 56474; -. [P52272-2]
DR Antibodypedia; 4238; 505 antibodies from 33 providers.
DR DNASU; 4670; -.
DR Ensembl; ENST00000325495.9; ENSP00000325376.2; ENSG00000099783.12. [P52272-1]
DR Ensembl; ENST00000348943.7; ENSP00000325732.2; ENSG00000099783.12. [P52272-2]
DR GeneID; 4670; -.
DR KEGG; hsa:4670; -.
DR MANE-Select; ENST00000325495.9; ENSP00000325376.2; NM_005968.5; NP_005959.2.
DR UCSC; uc010dwd.4; human. [P52272-1]
DR CTD; 4670; -.
DR DisGeNET; 4670; -.
DR GeneCards; HNRNPM; -.
DR HGNC; HGNC:5046; HNRNPM.
DR HPA; ENSG00000099783; Low tissue specificity.
DR MIM; 160994; gene.
DR neXtProt; NX_P52272; -.
DR OpenTargets; ENSG00000099783; -.
DR PharmGKB; PA29370; -.
DR VEuPathDB; HostDB:ENSG00000099783; -.
DR eggNOG; KOG4212; Eukaryota.
DR GeneTree; ENSGT00940000154595; -.
DR HOGENOM; CLU_019566_1_0_1; -.
DR InParanoid; P52272; -.
DR OMA; MGSSFER; -.
DR OrthoDB; 1174365at2759; -.
DR PhylomeDB; P52272; -.
DR TreeFam; TF313406; -.
DR PathwayCommons; P52272; -.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR SignaLink; P52272; -.
DR SIGNOR; P52272; -.
DR BioGRID-ORCS; 4670; 583 hits in 1096 CRISPR screens.
DR ChiTaRS; HNRNPM; human.
DR EvolutionaryTrace; P52272; -.
DR GenomeRNAi; 4670; -.
DR Pharos; P52272; Tbio.
DR PRO; PR:P52272; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P52272; protein.
DR Bgee; ENSG00000099783; Expressed in tibia and 202 other tissues.
DR ExpressionAtlas; P52272; baseline and differential.
DR Genevisible; P52272; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042382; C:paraspeckles; IDA:BHF-UCL.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:BHF-UCL.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
DR CDD; cd12661; RRM3_hnRNPM; 1.
DR DisProt; DP02015; -.
DR Gene3D; 3.30.70.330; -; 3.
DR IDEAL; IID00152; -.
DR InterPro; IPR024667; HnRNP_M.
DR InterPro; IPR024666; HnRNP_M_PY-NLS.
DR InterPro; IPR034990; hnRNPM_RRM3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23003:SF6; PTHR23003:SF6; 4.
DR Pfam; PF11532; HnRNP_M_NLS; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..730
FT /note="Heterogeneous nuclear ribonucleoprotein M"
FT /id="PRO_0000081864"
FT DOMAIN 71..149
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 204..281
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 400..405
FT /note="1"
FT REPEAT 407..412
FT /note="2"
FT REPEAT 415..420
FT /note="3"
FT REPEAT 426..431
FT /note="4"
FT REPEAT 433..438
FT /note="5"
FT REPEAT 440..445
FT /note="6"
FT REPEAT 446..451
FT /note="7"
FT REPEAT 453..458
FT /note="8"
FT REPEAT 461..466
FT /note="9"
FT REPEAT 468..473
FT /note="10"
FT REPEAT 475..480
FT /note="11"
FT REPEAT 482..487
FT /note="12"
FT REPEAT 493..498
FT /note="13"
FT REPEAT 500..505
FT /note="14"
FT REPEAT 507..512
FT /note="15"
FT REPEAT 514..519
FT /note="16"
FT REPEAT 521..526
FT /note="17"
FT REPEAT 528..533
FT /note="18"
FT REPEAT 540..545
FT /note="19"
FT REPEAT 547..552
FT /note="20"
FT REPEAT 554..559
FT /note="21"
FT REPEAT 562..566
FT /note="22"
FT REPEAT 567..572
FT /note="23"
FT REPEAT 575..579
FT /note="24"
FT REPEAT 580..585
FT /note="25"
FT REPEAT 588..593
FT /note="26"
FT REPEAT 603..608
FT /note="27"
FT DOMAIN 653..729
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..608
FT /note="27 X 6 AA repeats of [GEVSTPAN]-[ILMV]-[DE]-[RH]-
FT [MLVI]-[GAV]"
FT COMPBIAS 41..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D0E1"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 277
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 496
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 665
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 672
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0E1"
FT MOD_RES 698
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 651
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 667
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 685
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 692
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 716
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 160..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8441656,
FT ECO:0000303|PubMed:8692693, ECO:0000303|Ref.3"
FT /id="VSP_005845"
FT CONFLICT 24..34
FT /note="APGVPSGNGAP -> GPACERQRGS (in Ref. 1; AAA36192)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="P -> S (in Ref. 3; AAC16002)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="E -> V (in Ref. 1; AAA36192)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="H -> C (in Ref. 3; AAC16002)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="L -> P (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:2DO0"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:2DO0"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:2DO0"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:2DO0"
FT STRAND 242..253
FT /evidence="ECO:0007829|PDB:2DO0"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:2DO0"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2DO0"
FT STRAND 654..657
FT /evidence="ECO:0007829|PDB:2DGV"
FT HELIX 666..674
FT /evidence="ECO:0007829|PDB:2DGV"
FT STRAND 679..689
FT /evidence="ECO:0007829|PDB:2DGV"
FT STRAND 691..701
FT /evidence="ECO:0007829|PDB:2DGV"
FT HELIX 702..712
FT /evidence="ECO:0007829|PDB:2DGV"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:2DH9"
SQ SEQUENCE 730 AA; 77516 MW; 1A73DD35A3501861 CRC64;
MAAGVEAAAE VAATEIKMEE ESGAPGVPSG NGAPGPKGEG ERPAQNEKRK EKNIKRGGNR
FEPYANPTKR YRAFITNIPF DVKWQSLKDL VKEKVGEVTY VELLMDAEGK SRGCAVVEFK
MEESMKKAAE VLNKHSLSGR PLKVKEDPDG EHARRAMQKV MATTGGMGMG PGGPGMITIP
PSILNNPNIP NEIIHALQAG RLGSTVFVAN LDYKVGWKKL KEVFSMAGVV VRADILEDKD
GKSRGIGTVT FEQSIEAVQA ISMFNGQLLF DRPMHVKMDE RALPKGDFFP PERPQQLPHG
LGGIGMGLGP GGQPIDANHL NKGIGMGNIG PAGMGMEGIG FGINKMGGME GPFGGGMENM
GRFGSGMNMG RINEILSNAL KRGEIIAKQG GGGGGGSVPG IERMGPGIDR LGGAGMERMG
AGLGHGMDRV GSEIERMGLV MDRMGSVERM GSGIERMGPL GLDHMASSIE RMGQTMERIG
SGVERMGAGM GFGLERMAAP IDRVGQTIER MGSGVERMGP AIERMGLSME RMVPAGMGAG
LERMGPVMDR MATGLERMGA NNLERMGLER MGANSLERMG LERMGANSLE RMGPAMGPAL
GAGIERMGLA MGGGGGASFD RAIEMERGNF GGSFAGSFGG AGGHAPGVAR KACQIFVRNL
PFDFTWKMLK DKFNECGHVL YADIKMENGK SKGCGVVKFE SPEVAERACR MMNGMKLSGR
EIDVRIDRNA
