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   27-MAR-2024, entry version 226.
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; 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; 691.
DR   CORUM; P52272; -.
DR   DIP; DIP-29336N; -.
DR   IntAct; P52272; 164.
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   CPTAC; CPTAC-385; -.
DR   CPTAC; CPTAC-386; -.
DR   EPD; P52272; -.
DR   jPOST; P52272; -.
DR   MassIVE; P52272; -.
DR   MaxQB; P52272; -.
DR   PaxDb; 9606-ENSP00000325376; -.
DR   PeptideAtlas; P52272; -.
DR   ProteomicsDB; 56473; -. [P52272-1]
DR   ProteomicsDB; 56474; -. [P52272-2]
DR   Pumba; P52272; -.
DR   Antibodypedia; 4238; 578 antibodies from 33 providers.
DR   DNASU; 4670; -.
DR   Ensembl; ENST00000325495.9; ENSP00000325376.2; ENSG00000099783.13. [P52272-1]
DR   Ensembl; ENST00000348943.7; ENSP00000325732.2; ENSG00000099783.13. [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   AGR; HGNC:5046; -.
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; FPSGMNM; -.
DR   OrthoDB; 317787at2759; -.
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; 590 hits in 1184 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 204 other cell types or tissues.
DR   ExpressionAtlas; P52272; baseline and differential.
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: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:0005681; C:spliceosomal complex; IDA:HGNC-UCL.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
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   CDD; cd12657; RRM1_hnRNPM; 1.
DR   CDD; cd12659; RRM2_hnRNPM; 1.
DR   CDD; cd12661; RRM3_hnRNPM; 1.
DR   DisProt; DP02015; -.
DR   Gene3D; 3.30.70.330; -; 3.
DR   IDEAL; IID00152; -.
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; RNA RECOGNITION MOTIF RRM DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF11532; HnRNP_M_NLS; 1.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR   PROSITE; PS50102; RRM; 3.
DR   UCD-2DPAGE; P52272; -.
DR   Genevisible; P52272; HS.
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
//