MN1_HUMAN
ID MN1_HUMAN Reviewed; 1320 AA.
AC Q10571; A9Z1V9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Transcriptional activator MN1 {ECO:0000305};
DE AltName: Full=Probable tumor suppressor protein MN1 {ECO:0000305};
GN Name=MN1;
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 [MRNA], FUNCTION, AND INVOLVEMENT IN MENINGIOMAS.
RC TISSUE=Brain;
RX PubMed=7731706;
RA Deprez R.H.L., Riegman P.H.J., Groen N.A., Warringa U.L., van Biezen N.A.,
RA Molijn A.C., Bootsma D., de Jong P.J., Menon A.G., Kley N.A.,
RA Seizenger B.R., Zwarthoff E.C.;
RT "Cloning and characterization of MN1, a gene from chromosome 22q11, which
RT is disrupted by a balanced translocation in a meningioma.";
RL Oncogene 10:1521-1528(1995).
RN [2]
RP CHROMOSOMAL TRANSLOCATION WITH ETV6.
RX PubMed=7731705;
RA Buijs A., Sherr S., van Baal S., van Bezouw S., van der Plas D.,
RA Geurts van Kessel A., Riegman P., Lekanne Deprez R., Zwarthoff E.,
RA Hagemeijer A.;
RT "Translocation (12;22) (p13;q11) in myeloproliferative disorders results in
RT fusion of the ETS-like TEL gene on 12p13 to the MN1 gene on 22q11.";
RL Oncogene 10:1511-1519(1995).
RN [3]
RP SEQUENCE REVISION.
RA Riegmann P.H.J.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1305-1320.
RC TISSUE=Brain;
RX PubMed=9026990;
RA Dmitrenko V.V., Garifulin O.M., Shostak E.A., Smikodub A.I., Kavsan V.M.;
RT "The characteristics of different types of mRNA expressed in the human
RT brain.";
RL Cyt. Genet. 30:41-47(1996).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-950; SER-954; SER-1007 AND
RP SER-1081, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP INVOLVEMENT IN CEBALID, SUBCELLULAR LOCATION, VARIANTS CEBALID
RP 1279-GLN--THR-1320 DEL AND 1295-ARG--THR-1320 DEL, CHARACTERIZATION OF
RP VARIANTS CEBALID 1279-GLN--THR-1320 DEL AND 1295-ARG--THR-1320 DEL, TISSUE
RP SPECIFICITY, AND INTERACTION WITH PBX1; PKNOX1; ZBTB24; E2F7 AND RING1.
RX PubMed=31839203; DOI=10.1016/j.ajhg.2019.11.011;
RA Miyake N., Takahashi H., Nakamura K., Isidor B., Hiraki Y., Koshimizu E.,
RA Shiina M., Sasaki K., Suzuki H., Abe R., Kimura Y., Akiyama T.,
RA Tomizawa S.I., Hirose T., Hamanaka K., Miyatake S., Mitsuhashi S.,
RA Mizuguchi T., Takata A., Obo K., Kato M., Ogata K., Matsumoto N.;
RT "Gain-of-function MN1 truncation variants cause a recognizable syndrome
RT with craniofacial and brain abnormalities.";
RL Am. J. Hum. Genet. 106:13-25(2020).
RN [10]
RP INVOLVEMENT IN CEBALID, AND VARIANTS CEBALID 472-SER--THR-1320 DEL;
RP 1249-GLU--THR-1320 DEL; 1260-GLU--THR-1320 DEL; 1273-GLN--THR-1320 DEL;
RP 1295-ARG--THR-1320 DEL AND 1301-TRP--THR-1320 DEL.
RX PubMed=31834374; DOI=10.1093/brain/awz379;
RG University of Washington Center for Mendelian Genomics;
RA Mak C.C.Y., Doherty D., Lin A.E., Vegas N., Cho M.T., Viot G.,
RA Dimartino C., Weisfeld-Adams J.D., Lessel D., Joss S., Li C.,
RA Gonzaga-Jauregui C., Zarate Y.A., Ehmke N., Horn D., Troyer C., Kant S.G.,
RA Lee Y., Ishak G.E., Leung G., Barone Pritchard A., Yang S., Bend E.G.,
RA Filippini F., Roadhouse C., Lebrun N., Mehaffey M.G., Martin P.M.,
RA Apple B., Millan F., Puk O., Hoffer M.J.V., Henderson L.B., McGowan R.,
RA Wentzensen I.M., Pei S., Zahir F.R., Yu M., Gibson W.T., Seman A.,
RA Steeves M., Murrell J.R., Luettgen S., Francisco E., Strom T.M.,
RA Amlie-Wolf L., Kaindl A.M., Wilson W.G., Halbach S., Basel-Salmon L.,
RA Lev-El N., Denecke J., Vissers L.E.L.M., Radtke K., Chelly J., Zackai E.,
RA Friedman J.M., Bamshad M.J., Nickerson D.A., Reid R.R., Devriendt K.,
RA Chae J.H., Stolerman E., McDougall C., Powis Z., Bienvenu T., Tan T.Y.,
RA Orenstein N., Dobyns W.B., Shieh J.T., Choi M., Waggoner D., Gripp K.W.,
RA Parker M.J., Stoler J., Lyonnet S., Cormier-Daire V., Viskochil D.,
RA Hoffman T.L., Amiel J., Chung B.H.Y., Gordon C.T.;
RT "MN1 C-terminal truncation syndrome is a novel neurodevelopmental and
RT craniofacial disorder with partial rhombencephalosynapsis.";
RL Brain 143:55-68(2020).
CC -!- FUNCTION: Transcriptional activator which specifically regulates
CC expression of TBX22 in the posterior region of the developing palate.
CC Required during later stages of palate development for growth and
CC medial fusion of the palatal shelves. Promotes maturation and normal
CC function of calvarial osteoblasts, including expression of the
CC osteoclastogenic cytokine TNFSF11/RANKL. Necessary for normal
CC development of the membranous bones of the skull (By similarity). May
CC play a role in tumor suppression (Probable).
CC {ECO:0000250|UniProtKB:D3YWE6, ECO:0000305|PubMed:7731706}.
CC -!- SUBUNIT: Interacts with PBX1, PKNOX1, ZBTB24, E2F7, RING1.
CC {ECO:0000269|PubMed:31839203}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31839203}.
CC -!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues.
CC Highest expression is observed in fetal brain and skeletal muscle, and
CC adult skeletal muscle. {ECO:0000269|PubMed:31839203}.
CC -!- DISEASE: CEBALID syndrome (CEBALID) [MIM:618774]: An autosomal dominant
CC developmental disorder characterized by global developmental delay,
CC intellectual disability with severe expressive language delay,
CC craniofacial dysmorphism, and structural brain abnormalities. Most
CC patients have an atypical form of rhombencephalosynapsis, a distinctive
CC brain malformation characterized by partial or complete loss of the
CC cerebellar vermis with fusion of the cerebellar hemispheres. Other
CC frequent features include perisylvian polymicrogyria, abnormal
CC posterior clinoid processes, cerebellar hypoplasia or dysplasia, and
CC persistent trigeminal artery. {ECO:0000269|PubMed:31834374,
CC ECO:0000269|PubMed:31839203}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving MN1 may be a cause of
CC acute myeloid leukemia (AML). Translocation t(12;22)(p13;q11) with
CC ETV6. {ECO:0000269|PubMed:7731705}.
CC -!- DISEASE: Note=Defects in MN1 involved in the development of
CC meningiomas, slowly growing benign tumors derived from the arachnoidal
CC cap cells of the leptomeninges, the soft coverings of the brain and
CC spinal cord. Meningiomas are believed to be the most common primary
CC tumors of the central nervous system in man.
CC {ECO:0000269|PubMed:7731706}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MN1ID56.html";
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DR EMBL; X82209; CAA57693.2; -; mRNA.
DR EMBL; AL031591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO393416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59741.1; -; Genomic_DNA.
DR EMBL; Z70218; CAA94179.1; -; mRNA.
DR CCDS; CCDS42998.1; -.
DR RefSeq; NP_002421.3; NM_002430.2.
DR AlphaFoldDB; Q10571; -.
DR BioGRID; 110473; 29.
DR IntAct; Q10571; 3.
DR MINT; Q10571; -.
DR STRING; 9606.ENSP00000304956; -.
DR GlyGen; Q10571; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q10571; -.
DR PhosphoSitePlus; Q10571; -.
DR BioMuta; MN1; -.
DR DMDM; 215274133; -.
DR jPOST; Q10571; -.
DR MassIVE; Q10571; -.
DR MaxQB; Q10571; -.
DR PaxDb; Q10571; -.
DR PeptideAtlas; Q10571; -.
DR PRIDE; Q10571; -.
DR ProteomicsDB; 58861; -.
DR Antibodypedia; 309; 164 antibodies from 28 providers.
DR DNASU; 4330; -.
DR Ensembl; ENST00000302326.5; ENSP00000304956.4; ENSG00000169184.6.
DR GeneID; 4330; -.
DR KEGG; hsa:4330; -.
DR MANE-Select; ENST00000302326.5; ENSP00000304956.4; NM_002430.3; NP_002421.3.
DR UCSC; uc003adj.3; human.
DR CTD; 4330; -.
DR DisGeNET; 4330; -.
DR GeneCards; MN1; -.
DR GeneReviews; MN1; -.
DR HGNC; HGNC:7180; MN1.
DR HPA; ENSG00000169184; Group enriched (brain, skeletal muscle, tongue).
DR MalaCards; MN1; -.
DR MIM; 156100; gene.
DR MIM; 607174; phenotype.
DR MIM; 618774; phenotype.
DR neXtProt; NX_Q10571; -.
DR OpenTargets; ENSG00000169184; -.
DR Orphanet; 263662; Familial multiple meningioma.
DR PharmGKB; PA30893; -.
DR VEuPathDB; HostDB:ENSG00000169184; -.
DR eggNOG; ENOG502QVWY; Eukaryota.
DR GeneTree; ENSGT00390000001777; -.
DR HOGENOM; CLU_009075_0_0_1; -.
DR InParanoid; Q10571; -.
DR OMA; AWFSGPH; -.
DR OrthoDB; 923694at2759; -.
DR PhylomeDB; Q10571; -.
DR TreeFam; TF331780; -.
DR PathwayCommons; Q10571; -.
DR SignaLink; Q10571; -.
DR SIGNOR; Q10571; -.
DR BioGRID-ORCS; 4330; 9 hits in 1067 CRISPR screens.
DR ChiTaRS; MN1; human.
DR GeneWiki; MN1_(gene); -.
DR GenomeRNAi; 4330; -.
DR Pharos; Q10571; Tbio.
DR PRO; PR:Q10571; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q10571; protein.
DR Bgee; ENSG00000169184; Expressed in ganglionic eminence and 175 other tissues.
DR ExpressionAtlas; Q10571; baseline and differential.
DR Genevisible; Q10571; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IDA:UniProtKB.
DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR037644; MN1.
DR PANTHER; PTHR15821; PTHR15821; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Chromosomal rearrangement; Developmental protein;
KW Disease variant; Intellectual disability; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Tumor suppressor.
FT CHAIN 1..1320
FT /note="Transcriptional activator MN1"
FT /id="PRO_0000096521"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 950
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 382
FT /note="Q -> H (in dbSNP:rs45589338)"
FT /id="VAR_047533"
FT VARIANT 472..1320
FT /note="Missing (in CEBALID)"
FT /evidence="ECO:0000269|PubMed:31834374"
FT /id="VAR_083776"
FT VARIANT 1249..1320
FT /note="Missing (in CEBALID)"
FT /evidence="ECO:0000269|PubMed:31834374"
FT /id="VAR_083777"
FT VARIANT 1260..1320
FT /note="Missing (in CEBALID)"
FT /evidence="ECO:0000269|PubMed:31834374"
FT /id="VAR_083778"
FT VARIANT 1273..1320
FT /note="Missing (in CEBALID)"
FT /evidence="ECO:0000269|PubMed:31834374"
FT /id="VAR_083779"
FT VARIANT 1279..1320
FT /note="Missing (in CEBALID; increased protein aggregation;
FT decreased protein degradation via the ubiquitin-proteasome
FT pathway; loss of interaction with RING1; decreased
FT interaction with ZBTB24; no effect on nuclear
FT localization)"
FT /evidence="ECO:0000269|PubMed:31839203"
FT /id="VAR_083780"
FT VARIANT 1295..1320
FT /note="Missing (in CEBALID; increased protein aggregation;
FT decreased protein degradation via the ubiquitin-proteasome
FT pathway; loss of interaction with RING1; decreased
FT interaction with ZBTB24; no effect on nuclear
FT localization)"
FT /evidence="ECO:0000269|PubMed:31834374,
FT ECO:0000269|PubMed:31839203"
FT /id="VAR_083781"
FT VARIANT 1301..1320
FT /note="Missing (in CEBALID)"
FT /evidence="ECO:0000269|PubMed:31834374"
FT /id="VAR_083782"
SQ SEQUENCE 1320 AA; 136001 MW; 41CFFE16E5688B1C CRC64;
MFGLDQFEPQ VNSRNAGQGE RNFNETGLSM NTHFKAPAFH TGGPPGPVDP AMSALGEPPI
LGMNMEPYGF HARGHSELHA GGLQAQPVHG FFGGQQPHHG HPGSHHPHQH HPHFGGNFGG
PDPGASCLHG GRLLGYGGAA GGLGSQPPFA EGYEHMAESQ GPESFGPQRP GNLPDFHSSG
ASSHAVPAPC LPLDQSPNRA ASFHGLPSSS GSDSHSLEPR RVTNQGAVDS LEYNYPGEAP
SGHFDMFSPS DSEGQLPHYA AGRQVPGGAF PGASAMPRAA GMVGLSKMHA QPPQQQPQQQ
QQPQQQQQQH GVFFERFSGA RKMPVGLEPS VGSRHPLMQP PQQAPPPPQQ QPPQQPPQQQ
PPPPPGLLVR QNSCPPALPR PQQGEAGTPS GGLQDGGPML PSQHAQFEYP IHRLENRSMH
PYSEPVFSMQ HPPPQQAPNQ RLQHFDAPPY MNVAKRPRFD FPGSAGVDRC ASWNGSMHNG
ALDNHLSPSA YPGLPGEFTP PVPDSFPSGP PLQHPAPDHQ SLQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ RQNAALMIKQ MASRNQQQRL RQPNLAQLGH PGDVGQGGLV HGGPVGGLAQ
PNFEREGGST GAGRLGTFEQ QAPHLAQESA WFSGPHPPPG DLLPRRMGGS GLPADCGPHD
PSLAPPPPPG GSGVLFRGPL QEPMRMPGEG HVPALPSPGL QFGGSLGGLG QLQSPGAGVG
LPSAASERRP PPPDFATSAL GGQPGFPFGA AGRQSTPHSG PGVNSPPSAG GGGGSSGGGG
GGGAYPPQPD FQPSQRTSAS KLGALSLGSF NKPSSKDNLF GQSCLAALST ACQNMIASLG
APNLNVTFNK KNPPEGKRKL SQNETDGAAV AGNPGSDYFP GGTAPGAPGP GGPSGTSSSG
SKASGPPNPP AQGDGTSLSP NYTLESTSGN DGKPVSGGGG RGRGRRKRDS GHVSPGTFFD
KYSAAPDSGG APGVSPGQQQ ASGAAVGGSS AGETRGAPTP HEKALTSPSW GKGAELLLGD
QPDLIGSLDG GAKSDSSSPN VGEFASDEVS TSYANEDEVS SSSDNPQALV KASRSPLVTG
SPKLPPRGVG AGEHGPKAPP PALGLGIMSN STSTPDSYGG GGGPGHPGTP GLEQVRTPTS
SSGAPPPDEI HPLEILQAQI QLQRQQFSIS EDQPLGLKGG KKGECAVGAS GAQNGDSELG
SCCSEAVKSA MSTIDLDSLM AEHSAAWYMP ADKALVDSAD DDKTLAPWEK AKPQNPNSKE
AHDLPANKAS ASQPGSHLQC LSVHCTDDVG DAKARASVPT WRSLHSDISN RFGTFVAALT
