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 09-DEC-2015, entry version 164. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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- RT rich 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 RT shock-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 RT project: 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 RP SPLICEOSOMAL 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 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- RT like modifier substrates."; RL J. Biol. Chem. 280:5004-5012(2005). RN [8] 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575; SER-588; SER-618 RP AND SER-701, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-633 AND RP SER-637, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND IDENTIFICATION RP BY 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 [13] 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., RA Walther T.C., 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575; SER-588; SER-618 RP AND SER-701, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] 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., RA Buerckstuemmer T., 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 [16] 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 RP IDENTIFICATION 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-397; SER-618; RP SER-633 AND SER-637, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-83; LYS-145; RP LYS-388; LYS-685 AND LYS-698, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE 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 [20] 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., RA Ayoub D., 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 [21] 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 RT nuclear ribonucleoprotein M."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: Pre-mRNA binding protein in vivo, binds avidly to CC poly(G) and poly(U) RNA homopolymers in vitro. Involved in CC splicing. Acts as a receptor for carcinoembryonic antigen in CC Kupffer cells, may initiate a series of signaling events leading CC to tyrosine phosphorylation of proteins and induction of IL-1 CC alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines. CC -!- SUBUNIT: Identified in the spliceosome C complex. CC {ECO:0000269|PubMed:11991638}. CC -!- INTERACTION: CC Q99996-2:AKAP9; NbExp=3; IntAct=EBI-486809, EBI-9641546; CC Q99459:CDC5L; NbExp=7; IntAct=EBI-486809, EBI-374880; CC Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-486809, EBI-1185167; CC Q8NEA9:GMCL1P1; NbExp=3; IntAct=EBI-486809, EBI-745707; CC P52597:HNRNPF; NbExp=3; IntAct=EBI-486809, EBI-352986; CC P25791:LMO2; NbExp=4; IntAct=EBI-486809, EBI-739696; CC O43660:PLRG1; NbExp=5; IntAct=EBI-486809, EBI-1051504; CC Q8WW24:TEKT4; NbExp=3; IntAct=EBI-486809, EBI-750487; 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 CC 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}. CC -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains. CC {ECO:0000255|PROSITE-ProRule:PRU00176}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Hs.465808; -. DR UniGene; Hs.666214; -. 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 ProteinModelPortal; P52272; -. DR SMR; P52272; 74-147, 196-296, 652-730. DR BioGrid; 110751; 230. DR DIP; DIP-29336N; -. DR IntAct; P52272; 61. DR MINT; MINT-4999200; -. DR STRING; 9606.ENSP00000325376; -. DR PhosphoSite; P52272; -. DR BioMuta; HNRNPM; -. DR DMDM; 55977747; -. DR REPRODUCTION-2DPAGE; IPI00383296; -. DR UCD-2DPAGE; P52272; -. DR MaxQB; P52272; -. DR PaxDb; P52272; -. DR PRIDE; P52272; -. DR Ensembl; ENST00000325495; ENSP00000325376; ENSG00000099783. [P52272-1] DR Ensembl; ENST00000348943; ENSP00000325732; ENSG00000099783. [P52272-2] DR GeneID; 4670; -. DR UCSC; uc010dwd.3; human. [P52272-2] DR UCSC; uc010dwe.3; human. [P52272-1] DR CTD; 4670; -. DR GeneCards; HNRNPM; -. DR H-InvDB; HIX0137462; -. DR HGNC; HGNC:5046; HNRNPM. DR HPA; CAB016113; -. DR HPA; HPA024344; -. DR MIM; 160994; gene. DR neXtProt; NX_P52272; -. DR PharmGKB; PA29370; -. DR eggNOG; KOG4212; Eukaryota. DR eggNOG; COG0724; LUCA. DR GeneTree; ENSGT00410000025635; -. DR HOGENOM; HOG000231932; -. DR HOVERGEN; HBG054880; -. DR InParanoid; P52272; -. DR OMA; GMNKMGG; -. DR OrthoDB; EOG7ZSHSK; -. DR PhylomeDB; P52272; -. DR TreeFam; TF313406; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA. DR ChiTaRS; HNRNPM; human. DR EvolutionaryTrace; P52272; -. DR GenomeRNAi; 4670; -. DR NextBio; 17994; -. DR PRO; PR:P52272; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; P52272; -. DR CleanEx; HS_HNRNPM; -. DR ExpressionAtlas; P52272; baseline and differential. DR Genevisible; P52272; HS. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0016020; C:membrane; IDA: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:0042382; C:paraspeckles; IDA:BHF-UCL. DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC. DR GO; GO:0003823; F:antigen binding; IEA:Ensembl. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; NAS:HGNC. DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:BHF-UCL. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. DR GO; GO:0008380; P:RNA splicing; TAS:Reactome. DR Gene3D; 3.30.70.330; -; 3. DR InterPro; IPR024667; HnRNP_M. DR InterPro; IPR024666; HnRNP_M_PY-NLS. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR23003:SF6; PTHR23003:SF6; 3. DR Pfam; PF11532; HnRNP_M; 1. DR Pfam; PF00076; RRM_1; 3. DR SMART; SM00360; RRM; 3. DR PROSITE; PS50102; RRM; 3. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Direct protein sequencing; Isopeptide bond; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Ribonucleoprotein; RNA-binding; Spliceosome; Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:22223895, FT ECO:0000269|Ref.5}. FT CHAIN 2 730 Heterogeneous nuclear ribonucleoprotein FT M. FT /FTId=PRO_0000081864. FT DOMAIN 71 149 RRM 1. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT DOMAIN 204 281 RRM 2. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT REPEAT 400 405 1. FT REPEAT 407 412 2. FT REPEAT 415 420 3. FT REPEAT 426 431 4. FT REPEAT 433 438 5. FT REPEAT 440 445 6. FT REPEAT 446 451 7. FT REPEAT 453 458 8. FT REPEAT 461 466 9. FT REPEAT 468 473 10. FT REPEAT 475 480 11. FT REPEAT 482 487 12. FT REPEAT 493 498 13. FT REPEAT 500 505 14. FT REPEAT 507 512 15. FT REPEAT 514 519 16. FT REPEAT 521 526 17. FT REPEAT 528 533 18. FT REPEAT 540 545 19. FT REPEAT 547 552 20. FT REPEAT 554 559 21. FT REPEAT 562 567 22. FT REPEAT 567 572 23. FT REPEAT 575 580 24. FT REPEAT 580 585 25. FT REPEAT 588 593 26. FT REPEAT 603 608 27. FT DOMAIN 653 729 RRM 3. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT REGION 400 608 27 X 6 AA repeats of [GEVSTPAN]-[ILMV]- FT [DE]-[RH]-[MLVI]-[GAV]. FT COMPBIAS 390 396 Poly-Gly. FT COMPBIAS 612 616 Poly-Gly. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:22223895, FT ECO:0000269|Ref.5}. FT MOD_RES 29 29 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 134 134 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9D0E1}. FT MOD_RES 277 277 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 365 365 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 397 397 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 432 432 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 452 452 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 468 468 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 481 481 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 528 528 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 575 575 Phosphoserine. FT {ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 588 588 Phosphoserine. FT {ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 618 618 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 633 633 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 637 637 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 672 672 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9D0E1}. FT MOD_RES 698 698 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 701 701 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT CROSSLNK 17 17 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 83 83 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 145 145 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 685 685 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 698 698 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:25218447}. FT VAR_SEQ 160 198 Missing (in isoform 2). FT {ECO:0000303|PubMed:8441656, FT ECO:0000303|PubMed:8692693, FT ECO:0000303|Ref.3}. FT /FTId=VSP_005845. FT CONFLICT 24 34 APGVPSGNGAP -> GPACERQRGS (in Ref. 1; FT AAA36192). {ECO:0000305}. FT CONFLICT 34 34 P -> S (in Ref. 3; AAC16002). FT {ECO:0000305}. FT CONFLICT 51 51 E -> V (in Ref. 1; AAA36192). FT {ECO:0000305}. FT CONFLICT 152 152 H -> C (in Ref. 3; AAC16002). FT {ECO:0000305}. FT CONFLICT 527 527 L -> P (in Ref. 1 and 3). {ECO:0000305}. FT STRAND 206 210 {ECO:0000244|PDB:2DO0}. FT HELIX 217 224 {ECO:0000244|PDB:2DO0}. FT TURN 225 227 {ECO:0000244|PDB:2DO0}. FT STRAND 230 237 {ECO:0000244|PDB:2DO0}. FT STRAND 242 253 {ECO:0000244|PDB:2DO0}. FT HELIX 254 264 {ECO:0000244|PDB:2DO0}. FT STRAND 275 278 {ECO:0000244|PDB:2DO0}. FT STRAND 654 657 {ECO:0000244|PDB:2DGV}. FT HELIX 666 674 {ECO:0000244|PDB:2DGV}. FT STRAND 679 689 {ECO:0000244|PDB:2DGV}. FT STRAND 691 701 {ECO:0000244|PDB:2DGV}. FT HELIX 702 712 {ECO:0000244|PDB:2DGV}. FT STRAND 725 727 {ECO:0000244|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 //