PAXB1_MOUSE
ID PAXB1_MOUSE Reviewed; 919 AA.
AC P58501; E9QNN9; Q78XY2; Q8R2W3; Q9CRB7;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=PAX3- and PAX7-binding protein 1;
DE Short=PAX3/7BP;
DE AltName: Full=GC-rich sequence DNA-binding factor 1;
GN Name=Paxbp1; Synonyms=Gcfc, Gcfc1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 65-919 (ISOFORMS 1 AND 2).
RX PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S.,
RA Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.;
RT "From PREDs and open reading frames to cDNA isolation: revisiting the human
RT chromosome 21 transcription map.";
RL Genomics 78:46-54(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 430-919 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Pancreas;
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] OF 504-919 (ISOFORM 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
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-297; SER-559; SER-560 AND
RP THR-565, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC 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 FUNCTION, INTERACTION WITH PAX3; PAX7 AND WDR5, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=22862948; DOI=10.1016/j.stem.2012.05.022;
RA Diao Y., Guo X., Li Y., Sun K., Lu L., Jiang L., Fu X., Zhu H., Sun H.,
RA Wang H., Wu Z.;
RT "Pax3/7BP is a Pax7- and Pax3-binding protein that regulates the
RT proliferation of muscle precursor cells by an epigenetic mechanism.";
RL Cell Stem Cell 11:231-241(2012).
CC -!- FUNCTION: Adapter protein linking the transcription factors PAX3 and
CC PAX7 to the histone methylation machinery and involved in myogenesis.
CC Associates with a histone methyltransferase complex that specifically
CC mediates dimethylation and trimethylation of 'Lys-4' of histone H3.
CC Mediates the recruitment of that complex to the transcription factors
CC PAX3 and PAX7 on chromatin to regulate the expression of genes involved
CC in muscle progenitor cells proliferation including ID3 and CDC20.
CC {ECO:0000269|PubMed:22862948}.
CC -!- SUBUNIT: Interacts with PAX3 and PAX7. Interacts with WDR5; associates
CC with a histone methyltransferase (HMT) complex composed at least of
CC RBBP5, ASH2L, SET1, SET2 and KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and
CC KMT2B/MLL4 through direct interaction with WDR5.
CC {ECO:0000269|PubMed:22862948}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22862948}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=P58501-1; Sequence=Displayed;
CC Name=2; Synonyms=D;
CC IsoId=P58501-2; Sequence=VSP_004268, VSP_004269;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues tested
CC including skeletal muscle. Expressed in primary myoblasts.
CC {ECO:0000269|PubMed:22862948}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GCF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14838.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAH27145.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH27145.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAB24988.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAB27645.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AC141885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY033907; AAK68725.1; -; mRNA.
DR EMBL; AY033908; AAK68726.1; -; mRNA.
DR EMBL; AK007365; BAB24988.2; ALT_SEQ; mRNA.
DR EMBL; AK011477; BAB27645.2; ALT_SEQ; mRNA.
DR EMBL; BC014838; AAH14838.2; ALT_SEQ; mRNA.
DR EMBL; BC027145; AAH27145.1; ALT_SEQ; mRNA.
DR CCDS; CCDS49908.1; -. [P58501-1]
DR RefSeq; NP_080386.3; NM_026110.2. [P58501-1]
DR AlphaFoldDB; P58501; -.
DR SMR; P58501; -.
DR BioGRID; 212138; 19.
DR STRING; 10090.ENSMUSP00000113835; -.
DR iPTMnet; P58501; -.
DR PhosphoSitePlus; P58501; -.
DR EPD; P58501; -.
DR jPOST; P58501; -.
DR MaxQB; P58501; -.
DR PaxDb; P58501; -.
DR PeptideAtlas; P58501; -.
DR PRIDE; P58501; -.
DR ProteomicsDB; 287786; -. [P58501-1]
DR ProteomicsDB; 287787; -. [P58501-2]
DR Antibodypedia; 22645; 140 antibodies from 24 providers.
DR DNASU; 67367; -.
DR Ensembl; ENSMUST00000118522; ENSMUSP00000113835; ENSMUSG00000022974. [P58501-1]
DR GeneID; 67367; -.
DR KEGG; mmu:67367; -.
DR UCSC; uc012aih.1; mouse. [P58501-1]
DR CTD; 94104; -.
DR MGI; MGI:1914617; Paxbp1.
DR VEuPathDB; HostDB:ENSMUSG00000022974; -.
DR eggNOG; KOG2136; Eukaryota.
DR GeneTree; ENSGT00390000000455; -.
DR HOGENOM; CLU_010846_3_0_1; -.
DR InParanoid; P58501; -.
DR OMA; STQRTKN; -.
DR OrthoDB; 1217358at2759; -.
DR PhylomeDB; P58501; -.
DR TreeFam; TF315109; -.
DR BioGRID-ORCS; 67367; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Paxbp1; mouse.
DR PRO; PR:P58501; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P58501; protein.
DR Bgee; ENSMUSG00000022974; Expressed in cerebellar cortex and 267 other tissues.
DR ExpressionAtlas; P58501; baseline and differential.
DR Genevisible; P58501; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0031062; P:positive regulation of histone methylation; IDA:MGI.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR InterPro; IPR012890; GCFC2-like.
DR InterPro; IPR022783; GCFC_dom.
DR PANTHER; PTHR12214; PTHR12214; 1.
DR Pfam; PF07842; GCFC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Myogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..919
FT /note="PAX3- and PAX7-binding protein 1"
FT /id="PRO_0000087440"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..560
FT /note="Necessary and sufficient for interaction with PAX7"
FT /evidence="ECO:0000269|PubMed:22862948"
FT REGION 533..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B6"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B6"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B6"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B6"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 565
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B6"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B6"
FT VAR_SEQ 505..513
FT /note="NKALMAPNL -> SQSILKIKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11707072,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_004268"
FT VAR_SEQ 514..919
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11707072,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_004269"
FT CONFLICT 70
FT /note="H -> N (in Ref. 2; AAK68725/AAK68726)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="S -> P (in Ref. 2; AAK68725/AAK68726)"
FT /evidence="ECO:0000305"
FT CONFLICT 505..506
FT /note="NK -> SQ (in Ref. 2; AAK68725)"
FT /evidence="ECO:0000305"
FT CONFLICT P58501-2:510
FT /note="K -> E (in Ref. 3; BAB24988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 919 AA; 104836 MW; B87DB648782A1CB6 CRC64;
MFRKARRVNV RKRNDSEEEE RERDEEQEPP PLLPPPASGE EPGPGGGDRA PAGESLLGPG
PLPPPPSAHH PGLGAEAGGG ISGGAEPGNG LKPRKRPREN KEVPRASLLS FQDEEEENEE
VFKVKKSSYS KKIVKLLKKE YKEDLEKSKI KTELNTAADS DQPLDKTCHA KDTNPEDGVV
ISEHGEDEMD MESEKEEEKP KAGGAFSNAL SSLNVLRPGE IPDAAFIHAA RKKRQLAREL
GDFTPHDSEP GKGRLVREDE NDASDDEDDD EKRRIVFSVK EKSQRQKIAE EIGIEGSDDD
ALVTGEQDEE LSRWEQEQIR KGINIPQVQA SQPSEVNVYY QNTYQTMPYG ASYGIPYSYT
AYGSSDAKSQ KTDNTVPFKT PSNEMAPVTI DLVKRQLKDR LDSMKELHKT NQQQHEKHLQ
SRVDSTRAIE RLEGSSGGIG ERYKFLQEMR GYVQDLLECF SEKVPLINEL ESAIHQLYKQ
RASRLVQRRQ DDIKDESSEF SSHSNKALMA PNLDSFGRDR ALYQEHAKRR IAEREARRTR
RRQAREQTGQ MADHLEGLSS DDEETSTDIT NFNLEKDRIL KESSKVFEDV LESFYSIDCI
KAQFEAWRSK YYMSYKDAYI GLCLPKLFNP LIRLQLLTWT PLEAKCRDFE TMLWFESLLF
YGCEDREQEK DEADVALLPT IVEKVILPKL TVIAETMWDP FSTTQTSRMV GITMKLINGY
PSVVNADNKN TQVYLKALLL RMRRTLDDDV FMPLYPKNVL ENKNSGPYLF FQRQFWSSVK
LLGNFLQWYG IFSNKTLQEL SIDGLLNRYI LMAFQNSEYG DDSIRKAQNV INCFPKQWFV
NLKGERTISQ LENFCRYLVH LADTIYRNSI GCSDVEKRNA RENIKQIVKL LASVRALDHA
ISVASDHNVK EVKSLIEGK
