HNRPM_MOUSE
ID HNRPM_MOUSE Reviewed; 729 AA.
AC Q9D0E1; Q6P1B2; Q99JQ0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein M;
DE Short=hnRNP M;
GN Name=Hnrnpm; Synonyms=Hnrpm;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 449-455, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-700, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-671 AND LYS-697, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Identified in the spliceosome C complex (By similarity).
CC Interacts with PPIA/CYPA (By similarity).
CC {ECO:0000250|UniProtKB:P52272}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D0E1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D0E1-2; Sequence=VSP_011933;
CC -!- PTM: Sumoylated. {ECO:0000250}.
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; AK011521; BAB27675.1; -; mRNA.
DR EMBL; BC005758; AAH05758.1; -; mRNA.
DR EMBL; BC065172; AAH65172.1; -; mRNA.
DR CCDS; CCDS37570.1; -. [Q9D0E1-1]
DR CCDS; CCDS50068.1; -. [Q9D0E1-2]
DR RefSeq; NP_001103383.1; NM_001109913.1. [Q9D0E1-2]
DR RefSeq; NP_084080.1; NM_029804.3. [Q9D0E1-1]
DR AlphaFoldDB; Q9D0E1; -.
DR SMR; Q9D0E1; -.
DR BioGRID; 218411; 46.
DR CORUM; Q9D0E1; -.
DR IntAct; Q9D0E1; 10.
DR MINT; Q9D0E1; -.
DR STRING; 10090.ENSMUSP00000120115; -.
DR iPTMnet; Q9D0E1; -.
DR PhosphoSitePlus; Q9D0E1; -.
DR SwissPalm; Q9D0E1; -.
DR EPD; Q9D0E1; -.
DR jPOST; Q9D0E1; -.
DR MaxQB; Q9D0E1; -.
DR PaxDb; Q9D0E1; -.
DR PeptideAtlas; Q9D0E1; -.
DR PRIDE; Q9D0E1; -.
DR ProteomicsDB; 273313; -. [Q9D0E1-1]
DR ProteomicsDB; 273314; -. [Q9D0E1-2]
DR Antibodypedia; 4238; 505 antibodies from 33 providers.
DR DNASU; 76936; -.
DR Ensembl; ENSMUST00000087582; ENSMUSP00000084864; ENSMUSG00000059208. [Q9D0E1-2]
DR Ensembl; ENSMUST00000148178; ENSMUSP00000120115; ENSMUSG00000059208. [Q9D0E1-1]
DR GeneID; 76936; -.
DR KEGG; mmu:76936; -.
DR UCSC; uc008bze.2; mouse. [Q9D0E1-1]
DR CTD; 4670; -.
DR MGI; MGI:1926465; Hnrnpm.
DR VEuPathDB; HostDB:ENSMUSG00000059208; -.
DR eggNOG; KOG4212; Eukaryota.
DR GeneTree; ENSGT00940000154595; -.
DR HOGENOM; CLU_019566_1_0_1; -.
DR InParanoid; Q9D0E1; -.
DR OMA; MGSSFER; -.
DR PhylomeDB; Q9D0E1; -.
DR TreeFam; TF313406; -.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 76936; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Hnrnpm; mouse.
DR PRO; PR:Q9D0E1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D0E1; protein.
DR Bgee; ENSMUSG00000059208; Expressed in embryonic post-anal tail and 264 other tissues.
DR ExpressionAtlas; Q9D0E1; baseline and differential.
DR Genevisible; Q9D0E1; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042382; C:paraspeckles; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990405; F:protein antigen binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:1904591; P:positive regulation of protein import; ISO:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
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 Gene3D; 3.30.70.330; -; 3.
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 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:0000250|UniProtKB:P52272"
FT CHAIN 2..729
FT /note="Heterogeneous nuclear ribonucleoprotein M"
FT /id="PRO_0000081865"
FT DOMAIN 70..148
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 203..280
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 399..404
FT /note="1"
FT REPEAT 406..411
FT /note="2"
FT REPEAT 414..419
FT /note="3"
FT REPEAT 425..430
FT /note="4"
FT REPEAT 432..437
FT /note="5"
FT REPEAT 439..444
FT /note="6"
FT REPEAT 445..450
FT /note="7"
FT REPEAT 452..457
FT /note="8"
FT REPEAT 460..465
FT /note="9"
FT REPEAT 467..472
FT /note="10"
FT REPEAT 474..479
FT /note="11"
FT REPEAT 481..486
FT /note="12"
FT REPEAT 492..497
FT /note="13"
FT REPEAT 499..504
FT /note="14"
FT REPEAT 506..511
FT /note="15"
FT REPEAT 513..518
FT /note="16"
FT REPEAT 520..525
FT /note="17"
FT REPEAT 527..532
FT /note="18"
FT REPEAT 539..544
FT /note="19"
FT REPEAT 546..551
FT /note="20"
FT REPEAT 553..558
FT /note="21"
FT REPEAT 561..566
FT /note="22"
FT REPEAT 567..571
FT /note="23"
FT REPEAT 574..579
FT /note="24"
FT REPEAT 580..584
FT /note="25"
FT REPEAT 587..592
FT /note="26"
FT REPEAT 602..607
FT /note="27"
FT DOMAIN 652..728
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..607
FT /note="27 X 6 AA repeats of [GEVSTPAN]-[ILMV]-[DE]-[RH]-
FT [MLVI]-[GAV]"
FT COMPBIAS 40..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 133
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 276
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 495
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 664
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 671
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 697
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 284
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 344
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 380
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 387
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 650
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 666
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 684
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 691
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 715
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT VAR_SEQ 159..197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011933"
FT CONFLICT 357
FT /note="E -> G (in Ref. 2; AAH05758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 77649 MW; D42650B419362D6B CRC64;
MAAGVEAAAE VAATEPKMEE ESGAPCVPSG NGAPGPKGEE RPTQNEKRKE KNIKRGGNRF
EPYSNPTKRY RAFITNIPFD VKWQSLKDLV KEKVGEVTYV ELLMDAEGKS RGCAVVEFKM
EESMKKAAEV LNKHSLSGRP LKVKEDPDGE HARRAMQKVM ATTGGMGMGP GGPGMINIPP
SILNNPNIPN EIIHALQAGR LGSTVFVANL DYKVGWKKLK EVFSMAGVVV RADILEDKDG
KSRGIGIVTF EQSIEAVQAI SMFNGQLLFD RPMHVKMDER ALPKGDFFPP ERPQQLPHGL
GGIGMGLGPG GQPIDANHLS KGIGMGNLGP AGMGMEGIGF GINKIGGMEG PFGGGMENMG
RFGSGMNMGR INEILSNALK RGEIIAKQGG GGAGGSVPGI ERMGPGIDRI SGAGMERMGA
GLGHGMDRVG SEIERMGLVM DRMGSVERMG SSIERMGPLG LDHMASSIER MGQTMERIGS
GVERMGAGMG FGLERMAAPI DRVGQTIERM GSGVERMGPA IERMGLSMDR MVPTGMGASL
ERMGPVMDRM ATGLERMGAN NLERMGLERM GANSLERMGL ERMGANSLER MGPAMGPALG
AGIERMGLAM GGAGGASFDR AIEMERGNFG GSFAGSFGGA GGHAPGVARK ACQIFVRNLP
FDFTWKMLKD KFNECGHVLY ADIKMENGKS KGCGVVKFES PEVAERACRM MNGMKLSGRE
IDVRIDRNA
