ID PAX7_HUMAN Reviewed; 505 AA. AC P23759; E9PFV9; Q0VA99; Q2PJS5; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 24-JUN-2015, sequence version 4. DT 24-JAN-2024, entry version 219. DE RecName: Full=Paired box protein Pax-7; DE AltName: Full=HuP1; GN Name=PAX7; Synonyms=HUP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). RX PubMed=9339373; DOI=10.1006/geno.1997.4915; RA Vorobyov E., Mertsalov I., Dockhorn-Dworniczak B., Dworniczak B., Horst J.; RT "The genomic organization and the full coding region of the human PAX7 RT gene."; RL Genomics 45:168-174(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=16830101; DOI=10.1007/s00239-005-0163-7; RA Vorobyov E., Horst J.; RT "Getting the proto-Pax by the tail."; RL J. Mol. Evol. 63:153-164(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-467 (ISOFORMS 1/3). RX PubMed=7527137; DOI=10.1093/nar/22.22.4574; RA Schaefer B.W., Czerny T., Bernasconi M., Genini M., Busslinger M.; RT "Molecular cloning and characterization of a human PAX-7 cDNA expressed in RT normal and neoplastic myocytes."; RL Nucleic Acids Res. 22:4574-4582(1994). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-195 (ISOFORM 2). RX PubMed=2501086; DOI=10.1002/j.1460-2075.1989.tb03490.x; RA Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.; RT "Conservation of the paired domain in metazoans and its structure in three RT isolated human genes."; RL EMBO J. 8:1183-1190(1989). RN [8] RP INVOLVEMENT IN RMS2, AND CHROMOSOMAL TRANSLOCATION WITH FOXO1. RX PubMed=8187070; RA Davis R.J., D'Cruz C.M., Lovell M.A., Biegel J.A., Barr F.G.; RT "Fusion of PAX7 to FKHR by the variant t(1;13)(p36;q14) translocation in RT alveolar rhabdomyosarcoma."; RL Cancer Res. 54:2869-2872(1994). RN [9] RP INTERACTION WITH DAXX. RX PubMed=10393185; DOI=10.1093/emboj/18.13.3702; RA Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.; RT "The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor RT hDaxx."; RL EMBO J. 18:3702-3711(1999). RN [10] RP FUNCTION, VARIANTS CMYP19 CYS-56; 74-ARG--TYR-505 DEL AND 145-ARG--TYR-505 RP DEL, AND CHARACTERIZATION OF VARIANT CMYP19 145-ARG--TYR-505 DEL. RX PubMed=31092906; DOI=10.1038/s41436-019-0532-z; RA Feichtinger R.G., Mucha B.E., Hengel H., Orfi Z., Makowski C., Dort J., RA D'Anjou G., Nguyen T.T.M., Buchert R., Juenger H., Freisinger P., RA Baumeister S., Schoser B., Ahting U., Keimer R., Nguyen C.E., Fabre P., RA Gauthier J., Miguet M., Lopes F., AlHakeem A., AlHashem A., Tabarki B., RA Kandaswamy K.K., Bauer P., Steinbacher P., Prokisch H., Sturm M., RA Strom T.M., Ellezam B., Mayr J.A., Schoels L., Michaud J.L., Campeau P.M., RA Haack T.B., Dumont N.A.; RT "Biallelic variants in the transcription factor PAX7 are a new genetic RT cause of myopathy."; RL Genet. Med. 21:2521-2531(2019). CC -!- FUNCTION: Transcription factor that is involved in the regulation of CC muscle stem cells proliferation, playing a role in myogenesis and CC muscle regeneration. {ECO:0000269|PubMed:31092906}. CC -!- SUBUNIT: Can bind to DNA as a heterodimer with PAX3. Interacts with CC PAXBP1; the interaction links PAX7 to a WDR5-containing histone CC methyltransferase complex (By similarity). Interacts with DAXX CC (PubMed:10393185). {ECO:0000250|UniProtKB:P47239, CC ECO:0000269|PubMed:10393185}. CC -!- INTERACTION: CC P23759-2; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-12859446, EBI-8643161; CC P23759-2; Q99828: CIB1; NbExp=3; IntAct=EBI-12859446, EBI-372594; CC P23759-2; Q8WUE5: CT55; NbExp=3; IntAct=EBI-12859446, EBI-6873363; CC P23759-2; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-12859446, EBI-748420; CC P23759-2; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-12859446, EBI-10241353; CC P23759-2; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-12859446, EBI-746778; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P47239}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=3; CC IsoId=P23759-3; Sequence=Displayed; CC Name=1; Synonyms=Long; CC IsoId=P23759-1; Sequence=VSP_057679; CC Name=2; Synonyms=Short; CC IsoId=P23759-2; Sequence=VSP_057678, VSP_057679; CC -!- DISEASE: Rhabdomyosarcoma 2 (RMS2) [MIM:268220]: A form of CC rhabdomyosarcoma, a highly malignant tumor of striated muscle derived CC from primitive mesenchymal cells and exhibiting differentiation along CC rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently CC occurring soft tissue sarcomas and the most common in children. It CC occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal CC rhabdomyosarcomas. {ECO:0000269|PubMed:8187070}. Note=The gene CC represented in this entry is involved in disease pathogenesis. A CC chromosomal aberration involving PAX7 is found in rhabdomyosarcoma. CC Translocation t(1;13)(p36;q14) with FOXO1. The resulting protein is a CC transcriptional activator. {ECO:0000269|PubMed:8187070}. CC -!- DISEASE: Congenital myopathy 19 (CMYP19) [MIM:618578]: An autosomal CC recessive muscular disorder characterized by infantile onset of CC progressive muscular atrophy, hypotonia, ptosis, scoliosis and CC dysmorphic facial features. Disease severity is variable, ranging from CC mild to severe. {ECO:0000269|PubMed:31092906}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}. 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; X96743; CAA65520.1; -; mRNA. DR EMBL; X96744; CAA65521.1; -; Genomic_DNA. DR EMBL; X15042; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X15250; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X15251; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96745; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96746; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96747; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96748; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96744; CAA65522.1; -; Genomic_DNA. DR EMBL; X15042; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X15250; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X15251; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X96745; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X96746; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X96747; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X96748; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; DQ322591; ABC48797.1; -; mRNA. DR EMBL; AL021528; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471134; EAW94853.1; -; Genomic_DNA. DR EMBL; BC121165; AAI21166.1; -; mRNA. DR EMBL; BC121166; AAI21167.1; -; mRNA. DR EMBL; Z35141; CAA84513.1; -; mRNA. DR CCDS; CCDS186.1; -. [P23759-1] DR CCDS; CCDS44074.1; -. [P23759-3] DR CCDS; CCDS44075.1; -. [P23759-2] DR PIR; S78502; S78502. DR RefSeq; NP_001128726.1; NM_001135254.1. [P23759-3] DR RefSeq; NP_002575.1; NM_002584.2. [P23759-1] DR RefSeq; NP_039236.1; NM_013945.2. [P23759-2] DR AlphaFoldDB; P23759; -. DR SMR; P23759; -. DR BioGRID; 111115; 123. DR IntAct; P23759; 120. DR MINT; P23759; -. DR STRING; 9606.ENSP00000364524; -. DR GlyGen; P23759; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P23759; -. DR PhosphoSitePlus; P23759; -. DR BioMuta; PAX7; -. DR DMDM; 8247951; -. DR MassIVE; P23759; -. DR PaxDb; 9606-ENSP00000364524; -. DR PeptideAtlas; P23759; -. DR ProteomicsDB; 54149; -. [P23759-2] DR Antibodypedia; 14724; 835 antibodies from 41 providers. DR DNASU; 5081; -. DR Ensembl; ENST00000375375.7; ENSP00000364524.3; ENSG00000009709.12. [P23759-1] DR Ensembl; ENST00000400661.3; ENSP00000383502.3; ENSG00000009709.12. [P23759-2] DR Ensembl; ENST00000420770.7; ENSP00000403389.2; ENSG00000009709.12. [P23759-3] DR GeneID; 5081; -. DR KEGG; hsa:5081; -. DR MANE-Select; ENST00000420770.7; ENSP00000403389.2; NM_001135254.2; NP_001128726.1. DR UCSC; uc001bay.3; human. [P23759-3] DR AGR; HGNC:8621; -. DR CTD; 5081; -. DR DisGeNET; 5081; -. DR GeneCards; PAX7; -. DR HGNC; HGNC:8621; PAX7. DR HPA; ENSG00000009709; Tissue enhanced (skeletal muscle, tongue). DR MalaCards; PAX7; -. DR MIM; 167410; gene. DR MIM; 268220; phenotype. DR MIM; 618578; phenotype. DR neXtProt; NX_P23759; -. DR OpenTargets; ENSG00000009709; -. DR Orphanet; 99756; Alveolar rhabdomyosarcoma. DR PharmGKB; PA32961; -. DR VEuPathDB; HostDB:ENSG00000009709; -. DR eggNOG; KOG0849; Eukaryota. DR GeneTree; ENSGT00940000156759; -. DR HOGENOM; CLU_019281_8_0_1; -. DR InParanoid; P23759; -. DR OMA; SECLAPW; -. DR OrthoDB; 5398393at2759; -. DR TreeFam; TF351610; -. DR PathwayCommons; P23759; -. DR SignaLink; P23759; -. DR SIGNOR; P23759; -. DR BioGRID-ORCS; 5081; 18 hits in 1175 CRISPR screens. DR ChiTaRS; PAX7; human. DR GeneWiki; PAX7; -. DR GenomeRNAi; 5081; -. DR Pharos; P23759; Tbio. DR PRO; PR:P23759; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P23759; Protein. DR Bgee; ENSG00000009709; Expressed in olfactory segment of nasal mucosa and 48 other cell types or tissues. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central. DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc. DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW. DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd00086; homeodomain; 1. DR CDD; cd00131; PAX; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR003654; OAR_dom. DR InterPro; IPR043182; PAIRED_DNA-bd_dom. DR InterPro; IPR001523; Paired_dom. DR InterPro; IPR022106; Pax7_C. DR InterPro; IPR043565; PAX_fam. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR45636; PAIRED BOX PROTEIN PAX-6-RELATED-RELATED; 1. DR PANTHER; PTHR45636:SF26; PAIRED BOX PROTEIN PAX-7; 1. DR Pfam; PF00046; Homeodomain; 1. DR Pfam; PF00292; PAX; 1. DR Pfam; PF12360; Pax7; 1. DR PRINTS; PR00027; PAIREDBOX. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS50803; OAR; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. DR Genevisible; P23759; HS. PE 1: Evidence at protein level; KW Alternative splicing; Chromosomal rearrangement; Developmental protein; KW Disease variant; DNA-binding; Homeobox; Myogenesis; Nucleus; Paired box; KW Proto-oncogene; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..505 FT /note="Paired box protein Pax-7" FT /id="PRO_0000050194" FT DNA_BIND 34..163 FT /note="Paired" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT DNA_BIND 217..276 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 27..210 FT /note="Sufficient to mediate interaction with PAXBP1" FT /evidence="ECO:0000250|UniProtKB:P47239" FT REGION 37..93 FT /note="PAI subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT REGION 113..163 FT /note="RED subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT REGION 167..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 389..409 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 479..491 FT /note="OAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00138" FT VAR_SEQ 151..152 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_057678" FT VAR_SEQ 468..505 FT /note="TAVDYLAKNVSLSTQRRMKLGEHSAVLGLLPVETGQAY -> SECLVPWASP FT VPIPSPTPRASCLFMESYKVVSGWGMSISQMEKLKSSQMEQFT (in isoform 1 FT and isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9339373" FT /id="VSP_057679" FT VARIANT 56 FT /note="R -> C (in CMYP19; dbSNP:rs1392068839)" FT /evidence="ECO:0000269|PubMed:31092906" FT /id="VAR_083265" FT VARIANT 74..505 FT /note="Missing (in CMYP19)" FT /evidence="ECO:0000269|PubMed:31092906" FT /id="VAR_083266" FT VARIANT 145..505 FT /note="Missing (in CMYP19; loss-of-function variant FT resulting in a reduced muscle stem cell pool; the protein FT is not detected in patient muscle)" FT /evidence="ECO:0000269|PubMed:31092906" FT /id="VAR_083267" FT CONFLICT 468 FT /note="T -> S (in Ref. 2; ABC48797)" FT /evidence="ECO:0000305" SQ SEQUENCE 505 AA; 55119 MW; E51CF8B3E8D4C3D9 CRC64; MAALPGTVPR MMRPAPGQNY PRTGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPRQVA TPDVEKKIEE YKRENPGMFS WEIRDRLLKD GHCDRSTVPS GLVSSISRVL RIKFGKKEEE DEADKKEDDG EKKAKHSIDG ILGDKGNRLD EGSDVESEPD LPLKRKQRRS RTTFTAEQLE ELEKAFERTH YPDIYTREEL AQRTKLTEAR VQVWFSNRRA RWRKQAGANQ LAAFNHLLPG GFPPTGMPTL PPYQLPDSTY PTTTISQDGG STVHRPQPLP PSTMHQGGLA AAAAAADTSS AYGARHSFSS YSDSFMNPAA PSNHMNPVSN GLSPQVMSIL GNPSAVPPQP QADFSISPLH GGLDSATSIS ASCSQRADSI KPGDSLPTSQ AYCPPTYSTT GYSVDPVAGY QYGQYGQTAV DYLAKNVSLS TQRRMKLGEH SAVLGLLPVE TGQAY //