HM20A_MOUSE
ID HM20A_MOUSE Reviewed; 346 AA.
AC Q9DC33; Q3LSF9; Q6NV87; Q8BSK1; Q8C3C1; Q8CAA0; Q9CYG2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=High mobility group protein 20A;
DE AltName: Full=HMG box-containing protein 20A;
DE AltName: Full=HMG domain-containing protein HMGX1;
DE AltName: Full=Inhibitor of BRAF35;
DE Short=iBRAF;
GN Name=Hmg20a; Synonyms=Ibraf;
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 1).
RX PubMed=10773667; DOI=10.1159/000015486;
RA Sumoy L., Carim-Todd L., Escarceller M., Nadal M., Gratacos M.,
RA Pujana M.A., Estivill X., Peral B.;
RT "HMG20A and HMG20B map to human chromosomes 15q24 and 19p13.3 and
RT constitute a distinct class of HMG-box genes with ubiquitous expression.";
RL Cytogenet. Cell Genet. 88:62-67(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND FUNCTION.
RC STRAIN=C57BL/6J;
RX PubMed=16227968; DOI=10.1038/ncb1312;
RA Wynder C., Hakimi M.-A., Epstein J.A., Shilatifard A., Shiekhattar R.;
RT "Recruitment of MLL by HMG-domain protein iBRAF promotes neural
RT differentiation.";
RL Nat. Cell Biol. 7:1113-1117(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Hypothalamus, Lung, Thymus, and Wolffian duct;
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] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Pancreas;
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 [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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 INTERACTION WITH DTNB.
RX PubMed=20530487; DOI=10.1074/jbc.m109.090654;
RA Artegiani B., Labbaye C., Sferra A., Quaranta M.T., Torreri P., Macchia G.,
RA Ceccarini M., Petrucci T.C., Macioce P.;
RT "The interaction with HMG20a/b proteins suggests a potential role for beta-
RT dystrobrevin in neuronal differentiation.";
RL J. Biol. Chem. 285:24740-24750(2010).
CC -!- FUNCTION: Plays a role in neuronal differentiation as chromatin-
CC associated protein. Acts as inhibitor of HMG20B. Overcomes the
CC repressive effects of the neuronal silencer REST and induces the
CC activation of neuronal-specific genes. Involved in the recruitment of
CC the histone methyltransferase KMT2A/MLL1 and consequent increased
CC methylation of histone H3 lysine 4. {ECO:0000269|PubMed:16227968}.
CC -!- SUBUNIT: Interacts with DTNB. {ECO:0000269|PubMed:20530487}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9DC33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DC33-2; Sequence=VSP_018627;
CC Name=3;
CC IsoId=Q9DC33-3; Sequence=VSP_018625, VSP_018626;
CC Name=4;
CC IsoId=Q9DC33-4; Sequence=VSP_018623, VSP_018624;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Detected in mature neurons.
CC {ECO:0000269|PubMed:16227968}.
CC -!- DEVELOPMENTAL STAGE: Detected at 16.5 dpc in the outer cortex of the
CC developing brain. {ECO:0000269|PubMed:16227968}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA26278.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ182735; ABA26278.1; ALT_INIT; mRNA.
DR EMBL; AK004596; BAB23397.1; -; mRNA.
DR EMBL; AK017716; BAB30892.1; -; mRNA.
DR EMBL; AK032790; BAC28023.1; -; mRNA.
DR EMBL; AK039222; BAC30283.1; -; mRNA.
DR EMBL; AK086346; BAC39652.1; -; mRNA.
DR EMBL; AK134213; BAE22054.1; -; mRNA.
DR EMBL; BC013804; AAH13804.1; -; mRNA.
DR EMBL; BC068257; AAH68257.1; -; mRNA.
DR CCDS; CCDS23208.1; -. [Q9DC33-1]
DR RefSeq; NP_080088.1; NM_025812.2. [Q9DC33-1]
DR RefSeq; XP_006511431.1; XM_006511368.2.
DR AlphaFoldDB; Q9DC33; -.
DR SMR; Q9DC33; -.
DR BioGRID; 211774; 12.
DR IntAct; Q9DC33; 1.
DR STRING; 10090.ENSMUSP00000034879; -.
DR iPTMnet; Q9DC33; -.
DR PhosphoSitePlus; Q9DC33; -.
DR EPD; Q9DC33; -.
DR jPOST; Q9DC33; -.
DR MaxQB; Q9DC33; -.
DR PaxDb; Q9DC33; -.
DR PeptideAtlas; Q9DC33; -.
DR PRIDE; Q9DC33; -.
DR ProteomicsDB; 273176; -. [Q9DC33-1]
DR ProteomicsDB; 273177; -. [Q9DC33-2]
DR ProteomicsDB; 273178; -. [Q9DC33-3]
DR ProteomicsDB; 273179; -. [Q9DC33-4]
DR Antibodypedia; 1449; 331 antibodies from 33 providers.
DR DNASU; 66867; -.
DR Ensembl; ENSMUST00000034879; ENSMUSP00000034879; ENSMUSG00000032329. [Q9DC33-1]
DR Ensembl; ENSMUST00000214869; ENSMUSP00000150382; ENSMUSG00000032329. [Q9DC33-4]
DR Ensembl; ENSMUST00000215269; ENSMUSP00000149698; ENSMUSG00000032329. [Q9DC33-1]
DR Ensembl; ENSMUST00000217518; ENSMUSP00000149359; ENSMUSG00000032329. [Q9DC33-2]
DR GeneID; 66867; -.
DR KEGG; mmu:66867; -.
DR UCSC; uc009ptb.1; mouse. [Q9DC33-4]
DR UCSC; uc009ptc.1; mouse. [Q9DC33-3]
DR UCSC; uc009ptd.1; mouse. [Q9DC33-2]
DR UCSC; uc009pte.1; mouse. [Q9DC33-1]
DR CTD; 10363; -.
DR MGI; MGI:1914117; Hmg20a.
DR VEuPathDB; HostDB:ENSMUSG00000032329; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000158464; -.
DR HOGENOM; CLU_060006_0_0_1; -.
DR InParanoid; Q9DC33; -.
DR OMA; MDTIDSY; -.
DR OrthoDB; 1458939at2759; -.
DR PhylomeDB; Q9DC33; -.
DR TreeFam; TF106440; -.
DR BioGRID-ORCS; 66867; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Hmg20a; mouse.
DR PRO; PR:Q9DC33; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DC33; protein.
DR Bgee; ENSMUSG00000032329; Expressed in humerus cartilage element and 267 other tissues.
DR ExpressionAtlas; Q9DC33; baseline and differential.
DR Genevisible; Q9DC33; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Coiled coil; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..346
FT /note="High mobility group protein 20A"
FT /id="PRO_0000238650"
FT DNA_BIND 102..170
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 228..272
FT /evidence="ECO:0000255"
FT COMPBIAS 38..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 79..101
FT /note="QRSKRGGWSKGRKRKKPLRDSNA -> VSEHLLSLSTAASKAMGMQGGIE
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018623"
FT VAR_SEQ 102..346
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018624"
FT VAR_SEQ 150..180
FT /note="RYLDEADRDKERYMKELEQYQKTEAYKVFSR -> VMVPASGVSLGFDYISQ
FT IVWGAGEIWGLGHA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018625"
FT VAR_SEQ 181..346
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018626"
FT VAR_SEQ 303..346
FT /note="SGEIPTVDTIDSYMNRLHSIILANPQDNENFIATVREVVNRLDR -> NVIL
FT SEVSGRESGEDGDGVLFTLVLMWRSRSVSQEEKRRGKKNPVKIFSAVWACLKSQHSGGR
FT GRKISVSSRPACPT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018627"
FT CONFLICT 294
FT /note="S -> C (in Ref. 3; BAC30283)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="P -> T (in Ref. 3; BAB30892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 39917 MW; D57502BEFD3C0026 CRC64;
MESLMASSTL PPLFADEDGS KESNDLATSG LTHPEGPYGS AATSTTNPEF VEDLSQGQLL
QSEASNAVEG NEQRPEDEQR SKRGGWSKGR KRKKPLRDSN APKSPLTGYV RFMNERREQL
RAKRPEVPFP EITRMLGNEW SKLPPEEKQR YLDEADRDKE RYMKELEQYQ KTEAYKVFSR
KTQDRQKGKS HRQDAARQAT HDHEKETEVK ERSVFDIPIF TEEFLNHSKA REAELRQLRK
SNMEFEERNA ALQKHVESMR TAVEKLEVDV IQERSRNTVL QQHLETLRQM LTSSFASMPL
PGSGEIPTVD TIDSYMNRLH SIILANPQDN ENFIATVREV VNRLDR
