HMGA1_MOUSE
ID HMGA1_MOUSE Reviewed; 107 AA.
AC P17095; Q91WV2; Q924L7; Q924L8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=High mobility group protein HMG-I/HMG-Y;
DE Short=HMG-I(Y);
DE AltName: Full=High mobility group AT-hook protein 1;
DE Short=High mobility group protein A1;
GN Name=Hmga1; Synonyms=Hmgi, Hmgiy;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HMG-Y).
RX PubMed=3192537; DOI=10.1016/s0021-9258(19)81364-9;
RA Johnson K.R., Lehn D.A., Elton T.S., Barr P.J., Reeves R.;
RT "Complete murine cDNA sequence, genomic structure, and tissue expression of
RT the high mobility group protein HMG-I(Y).";
RL J. Biol. Chem. 263:18338-18342(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS HMG-I AND HMG-Y).
RC STRAIN=BALB/cJ;
RX PubMed=11410365; DOI=10.1016/s0378-1119(01)00500-5;
RA Pedulla M.L., Treff N.R., Resar L.M.S., Reeves R.;
RT "Sequence and analysis of the murine Hmgiy (Hmga1) gene locus.";
RL Gene 271:51-58(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HMG-Y).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HMG-I).
RC STRAIN=FVB/N; TISSUE=Colon;
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 PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, ACETYLATION AT SER-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=1429598; DOI=10.1016/s0021-9258(18)41698-5;
RA Ferranti P., Malorni A., Marino G., Pucci P., Goodwin G.H., Manfioletti G.,
RA Giancotti V.;
RT "Mass spectrometric analysis of the HMGY protein from Lewis lung carcinoma.
RT Identification of phosphorylation sites.";
RL J. Biol. Chem. 267:22486-22489(1992).
RN [6]
RP INTERACTION WITH HIPK2, AND PHOSPHORYLATION.
RX PubMed=11593421; DOI=10.1038/sj.onc.1204635;
RA Pierantoni G.M., Fedele M., Pentimalli F., Benvenuto G., Pero R.,
RA Viglietto G., Santoro M., Chiariotti L., Fusco A.;
RT "High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase
RT protein which inhibits cell growth.";
RL Oncogene 20:6132-6141(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53; SER-99; SER-102 AND
RP SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53; SER-99; SER-102 AND
RP SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-7 AND LYS-15, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP 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: HMG-I/Y bind preferentially to the minor groove of A+T rich
CC regions in double-stranded DNA. It is suggested that these proteins
CC could function in nucleosome phasing and in the 3'-end processing of
CC mRNA transcripts. They are also involved in the transcription
CC regulation of genes containing, or in close proximity to A+T-rich
CC regions.
CC -!- SUBUNIT: Interacts with HIPK2. {ECO:0000269|PubMed:11593421}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=HMG-I; Synonyms=HMGA1a;
CC IsoId=P17095-2; Sequence=Displayed;
CC Name=HMG-Y; Synonyms=HMGA1b, HMGI-E;
CC IsoId=P17095-1; Sequence=VSP_012406;
CC -!- PTM: Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2.
CC Phosphorylation may modulate DNA-binding affinity (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Methylation at Arg-58 is mutually exclusive with methylation at
CC Arg-60. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HMGA family. {ECO:0000305}.
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DR EMBL; J04179; AAA37820.1; -; mRNA.
DR EMBL; AF285780; AAK66158.1; -; Genomic_DNA.
DR EMBL; AF285780; AAK66159.1; -; Genomic_DNA.
DR EMBL; AK010617; BAB27065.1; -; mRNA.
DR EMBL; BC013455; AAH13455.1; -; mRNA.
DR CCDS; CCDS28564.1; -. [P17095-2]
DR CCDS; CCDS49010.1; -. [P17095-2]
DR CCDS; CCDS50044.1; -. [P17095-1]
DR PIR; A31895; A31895.
DR RefSeq; NP_001020598.1; NM_001025427.3. [P17095-2]
DR RefSeq; NP_001034445.1; NM_001039356.2. [P17095-2]
DR RefSeq; NP_001159948.1; NM_001166476.1. [P17095-2]
DR RefSeq; NP_001159949.1; NM_001166477.1. [P17095-1]
DR RefSeq; NP_001160007.1; NM_001166535.1. [P17095-2]
DR RefSeq; NP_001160008.1; NM_001166536.1. [P17095-2]
DR RefSeq; NP_001160009.1; NM_001166537.1. [P17095-1]
DR RefSeq; NP_001160011.1; NM_001166539.1. [P17095-1]
DR RefSeq; NP_001160012.1; NM_001166540.1. [P17095-1]
DR RefSeq; NP_001160013.1; NM_001166541.1. [P17095-1]
DR RefSeq; NP_001160014.1; NM_001166542.1. [P17095-1]
DR RefSeq; NP_057869.2; NM_016660.3. [P17095-2]
DR AlphaFoldDB; P17095; -.
DR BMRB; P17095; -.
DR BioGRID; 200340; 8.
DR BioGRID; 226328; 2.
DR DIP; DIP-53N; -.
DR IntAct; P17095; 3.
DR STRING; 10090.ENSMUSP00000100667; -.
DR iPTMnet; P17095; -.
DR PhosphoSitePlus; P17095; -.
DR EPD; P17095; -.
DR jPOST; P17095; -.
DR PaxDb; P17095; -.
DR PeptideAtlas; P17095; -.
DR PRIDE; P17095; -.
DR ProteomicsDB; 273186; -. [P17095-2]
DR ProteomicsDB; 273187; -. [P17095-1]
DR TopDownProteomics; P17095-1; -. [P17095-1]
DR TopDownProteomics; P17095-2; -. [P17095-2]
DR Antibodypedia; 29318; 405 antibodies from 39 providers.
DR DNASU; 15361; -.
DR Ensembl; ENSMUST00000105046; ENSMUSP00000100667; ENSMUSG00000078249. [P17095-2]
DR Ensembl; ENSMUST00000114888; ENSMUSP00000110538; ENSMUSG00000046711. [P17095-1]
DR Ensembl; ENSMUST00000118570; ENSMUSP00000114101; ENSMUSG00000046711. [P17095-1]
DR Ensembl; ENSMUST00000118599; ENSMUSP00000113015; ENSMUSG00000046711. [P17095-2]
DR Ensembl; ENSMUST00000119486; ENSMUSP00000113916; ENSMUSG00000046711. [P17095-2]
DR Ensembl; ENSMUST00000231358; ENSMUSP00000155876; ENSMUSG00000046711. [P17095-1]
DR Ensembl; ENSMUST00000231825; ENSMUSP00000156327; ENSMUSG00000046711. [P17095-1]
DR Ensembl; ENSMUST00000231874; ENSMUSP00000156199; ENSMUSG00000046711. [P17095-2]
DR Ensembl; ENSMUST00000232013; ENSMUSP00000155886; ENSMUSG00000046711. [P17095-2]
DR Ensembl; ENSMUST00000232265; ENSMUSP00000156173; ENSMUSG00000046711. [P17095-2]
DR Ensembl; ENSMUST00000232552; ENSMUSP00000156044; ENSMUSG00000046711. [P17095-1]
DR GeneID; 111241; -.
DR GeneID; 15361; -.
DR KEGG; mmu:111241; -.
DR KEGG; mmu:15361; -.
DR UCSC; uc008boz.2; mouse. [P17095-2]
DR CTD; 111241; -.
DR CTD; 3159; -.
DR MGI; MGI:96160; Hmga1.
DR VEuPathDB; HostDB:ENSMUSG00000046711; -.
DR VEuPathDB; HostDB:ENSMUSG00000078249; -.
DR eggNOG; ENOG502S5JW; Eukaryota.
DR GeneTree; ENSGT00730000111329; -.
DR HOGENOM; CLU_138888_0_0_1; -.
DR InParanoid; P17095; -.
DR OMA; HKKKQGP; -.
DR PhylomeDB; P17095; -.
DR TreeFam; TF351623; -.
DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR BioGRID-ORCS; 111241; 1 hit in 75 CRISPR screens.
DR BioGRID-ORCS; 15361; 3 hits in 110 CRISPR screens.
DR ChiTaRS; Hmga1; mouse.
DR PRO; PR:P17095; -.
DR Proteomes; UP000000589; Chromosome 11.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P17095; protein.
DR Bgee; ENSMUSG00000046711; Expressed in epiblast (generic) and 151 other tissues.
DR ExpressionAtlas; P17095; baseline and differential.
DR Genevisible; P17095; MM.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0035985; C:senescence-associated heterochromatin focus; ISS:UniProtKB.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:BHF-UCL.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:BHF-UCL.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISS:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISS:UniProtKB.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030527; F:structural constituent of chromatin; TAS:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0090402; P:oncogene-induced cell senescence; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR000116; HMGA.
DR InterPro; IPR031079; HMGA1_chordates.
DR InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
DR PANTHER; PTHR23341:SF6; PTHR23341:SF6; 1.
DR PRINTS; PR00929; ATHOOK.
DR PRINTS; PR00930; HIGHMOBLTYIY.
DR SMART; SM00384; AT_hook; 3.
DR PROSITE; PS00354; HMGI_Y; 3.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Alternative splicing; Chromosome;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1429598,
FT ECO:0007744|PubMed:23806337"
FT CHAIN 2..107
FT /note="High mobility group protein HMG-I/HMG-Y"
FT /id="PRO_0000206709"
FT DNA_BIND 21..31
FT /note="A.T hook 1"
FT DNA_BIND 53..63
FT /note="A.T hook 2"
FT DNA_BIND 78..89
FT /note="A.T hook 3"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..77
FT /note="Interaction with HIPK2"
FT /evidence="ECO:0000269|PubMed:11593421"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:1429598,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 8
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 9
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 9
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 26
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 26
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 26
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 36
FT /note="Phosphoserine; by HIPK2 and CDC2"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 53
FT /note="Phosphothreonine; by HIPK2 and CDC2"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 58
FT /note="Asymmetric dimethylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 58
FT /note="Omega-N-methylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 60
FT /note="Asymmetric dimethylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 60
FT /note="Omega-N-methylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1429598,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1429598,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:17622165,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1429598,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:17622165,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT VAR_SEQ 35..45
FT /note="Missing (in isoform HMG-Y)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:3192537"
FT /id="VSP_012406"
FT CONFLICT 106
FT /note="E -> G (in Ref. 2; AAK66158/AAK66159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 107 AA; 11614 MW; 4EC39386611959FC CRC64;
MSESGSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR
PKGSKNKGAA KTRKVTTAPG RKPRGRPKKL EKEEEEGISQ ESSEEEQ
