PAXB1_HUMAN
ID PAXB1_HUMAN Reviewed; 917 AA.
AC Q9Y5B6; D3DSE7; Q96DU8; Q9NYQ0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=PAX3- and PAX7-binding protein 1;
DE AltName: Full=GC-rich sequence DNA-binding factor 1;
GN Name=PAXBP1; Synonyms=C21orf66, GCFC, GCFC1;
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] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, Heart, Kidney, Lung, Muscle, Placenta, and Testis;
RA Chapot-Skovsgaard F.M., Guipponi M., Lyle R., Antonarakis S.E.;
RT "Isolation and initial characterization of a putative human chromosome 21
RT transcription factor.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 132-917 (ISOFORM 1).
RX PubMed=10773462; DOI=10.1016/s0378-1119(00)00089-5;
RA Slavov D., Hattori M., Sakaki Y., Rosenthal A., Shimizu N., Minoshima S.,
RA Kudoh J., Yaspo M.-L., Ramser J., Reinhardt R., Reimer C., Clancy K.,
RA Rynditch A., Gardiner K.;
RT "Criteria for gene identification and features of genome organization:
RT analysis of 6.5 Mb of DNA sequence from human chromosome 21.";
RL Gene 247:215-232(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 489-815 (ISOFORM 2).
RA Teramoto T., Thorgeirsson S.S.;
RT "Cloning of candidate of GC-rich sequence DNA-binding factor.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-155; SER-158;
RP SER-557 AND SER-558, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-557 AND SER-558, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-154; SER-155;
RP SER-158; SER-262; SER-295; SER-557 AND SER-558, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-154; SER-155;
RP SER-262; SER-557 AND SER-558, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-155; SER-191;
RP SER-262; SER-557 AND SER-558, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP VARIANT CYS-538.
RX PubMed=28542722; DOI=10.1111/cge.13051;
RA Alharby E., Albalawi A.M., Nasir A., Alhijji S.A., Mahmood A., Ramzan K.,
RA Abdusamad F., Aljohani A., Abdelsalam O., Eldardear A., Basit S.;
RT "A homozygous potentially pathogenic variant in the PAXBP1 gene in a large
RT family with global developmental delay and myopathic hypotonia.";
RL Clin. Genet. 92:579-586(2017).
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=Q9Y5B6-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9Y5B6-2; Sequence=VSP_004267;
CC Name=3; Synonyms=C;
CC IsoId=Q9Y5B6-3; Sequence=VSP_004263, VSP_004264;
CC Name=4; Synonyms=D;
CC IsoId=Q9Y5B6-4; Sequence=VSP_004265, VSP_004266;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11707072}.
CC -!- MISCELLANEOUS: [Isoform 4]: Most abundantly expressed isoform, at mRNA
CC level according to PubMed:11707072, despite the presence of a premature
CC stop codon in the mRNA that may lead to nonsense-mediated mRNA decay.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GCF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34617.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AY033903; AAK68721.1; -; mRNA.
DR EMBL; AY033904; AAK68722.1; -; mRNA.
DR EMBL; AY033905; AAK68723.1; -; mRNA.
DR EMBL; AY033906; AAK68724.1; -; mRNA.
DR EMBL; AJ279080; CAC40813.1; -; mRNA.
DR EMBL; AJ279081; CAC40814.1; -; mRNA.
DR EMBL; CH471079; EAX09859.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09861.1; -; Genomic_DNA.
DR EMBL; AF231920; AAF72944.1; -; mRNA.
DR EMBL; AF153208; AAD34617.1; ALT_SEQ; mRNA.
DR CCDS; CCDS13619.1; -. [Q9Y5B6-1]
DR CCDS; CCDS33541.1; -. [Q9Y5B6-2]
DR RefSeq; NP_037461.2; NM_013329.3. [Q9Y5B6-2]
DR RefSeq; NP_057715.2; NM_016631.3. [Q9Y5B6-1]
DR AlphaFoldDB; Q9Y5B6; -.
DR SMR; Q9Y5B6; -.
DR BioGRID; 125115; 83.
DR CORUM; Q9Y5B6; -.
DR IntAct; Q9Y5B6; 25.
DR MINT; Q9Y5B6; -.
DR STRING; 9606.ENSP00000328992; -.
DR iPTMnet; Q9Y5B6; -.
DR MetOSite; Q9Y5B6; -.
DR PhosphoSitePlus; Q9Y5B6; -.
DR BioMuta; PAXBP1; -.
DR DMDM; 20141448; -.
DR EPD; Q9Y5B6; -.
DR jPOST; Q9Y5B6; -.
DR MassIVE; Q9Y5B6; -.
DR MaxQB; Q9Y5B6; -.
DR PaxDb; Q9Y5B6; -.
DR PeptideAtlas; Q9Y5B6; -.
DR PRIDE; Q9Y5B6; -.
DR ProteomicsDB; 86332; -. [Q9Y5B6-1]
DR ProteomicsDB; 86333; -. [Q9Y5B6-2]
DR ProteomicsDB; 86334; -. [Q9Y5B6-3]
DR ProteomicsDB; 86335; -. [Q9Y5B6-4]
DR Antibodypedia; 22645; 140 antibodies from 24 providers.
DR DNASU; 94104; -.
DR Ensembl; ENST00000290178.4; ENSP00000290178.4; ENSG00000159086.15. [Q9Y5B6-2]
DR Ensembl; ENST00000331923.9; ENSP00000328992.4; ENSG00000159086.15. [Q9Y5B6-1]
DR Ensembl; ENST00000443785.5; ENSP00000393038.1; ENSG00000159086.15. [Q9Y5B6-4]
DR Ensembl; ENST00000573680.5; ENSP00000458892.2; ENSG00000263141.5.
DR Ensembl; ENST00000574159.2; ENSP00000458262.2; ENSG00000263141.5.
DR GeneID; 94104; -.
DR KEGG; hsa:94104; -.
DR MANE-Select; ENST00000331923.9; ENSP00000328992.4; NM_016631.4; NP_057715.2.
DR UCSC; uc002yqn.3; human. [Q9Y5B6-1]
DR CTD; 94104; -.
DR DisGeNET; 94104; -.
DR GeneCards; PAXBP1; -.
DR HGNC; HGNC:13579; PAXBP1.
DR HPA; ENSG00000159086; Low tissue specificity.
DR MIM; 617621; gene.
DR neXtProt; NX_Q9Y5B6; -.
DR OpenTargets; ENSG00000159086; -.
DR PharmGKB; PA25861; -.
DR VEuPathDB; HostDB:ENSG00000159086; -.
DR eggNOG; KOG2136; Eukaryota.
DR GeneTree; ENSGT00390000000455; -.
DR HOGENOM; CLU_010846_3_0_1; -.
DR InParanoid; Q9Y5B6; -.
DR OMA; STQRTKN; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q9Y5B6; -.
DR TreeFam; TF315109; -.
DR PathwayCommons; Q9Y5B6; -.
DR SignaLink; Q9Y5B6; -.
DR BioGRID-ORCS; 94104; 520 hits in 1083 CRISPR screens.
DR ChiTaRS; PAXBP1; human.
DR GeneWiki; C21orf66; -.
DR GenomeRNAi; 94104; -.
DR Pharos; Q9Y5B6; Tbio.
DR PRO; PR:Q9Y5B6; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9Y5B6; protein.
DR Bgee; ENSG00000159086; Expressed in sural nerve and 198 other tissues.
DR ExpressionAtlas; Q9Y5B6; baseline and differential.
DR Genevisible; Q9Y5B6; HS.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
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..917
FT /note="PAX3- and PAX7-binding protein 1"
FT /id="PRO_0000087439"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..558
FT /note="Necessary and sufficient for interaction with PAX7"
FT /evidence="ECO:0000250"
FT REGION 530..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 563
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P58501"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 462..469
FT /note="VPLINELE -> SVQFRKLL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11707072"
FT /id="VSP_004263"
FT VAR_SEQ 470..917
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11707072"
FT /id="VSP_004264"
FT VAR_SEQ 503..511
FT /note="NKALMAPNL -> SQSILKTKL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11707072, ECO:0000303|Ref.2"
FT /id="VSP_004265"
FT VAR_SEQ 512..917
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11707072, ECO:0000303|Ref.2"
FT /id="VSP_004266"
FT VAR_SEQ 779..917
FT /note="LLGNFLQWYGIFSNKTLQELSIDGLLNRYILMAFQNSEYGDDSIKKAQNVIN
FT CFPKQWFMNLKGERTISQLENFCRYLVHLADTIYRNSIGCSDVEKRNARENIKQIVKLL
FT ASVRALDHAMSVASDHNVKEFKSLIEGK -> VIKPPFQRGSCPIPRRKECCSERPRRI
FT WTDRPCVVFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11707072, ECO:0000303|Ref.5"
FT /id="VSP_004267"
FT VARIANT 538
FT /note="R -> C (found in a family with global developmental
FT delay and myopathic hypotonia; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28542722"
FT /id="VAR_079417"
FT CONFLICT 692..711
FT /note="Missing (in Ref. 5; AAD34617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 917 AA; 104804 MW; 855960A1D50A7789 CRC64;
MFRKARRVNV RKRNDSEEEE RERDEEQEPP PLLPPPGTGE EAGPGGGDRA PGGESLLGPG
PSPPSALTPG LGAEAGGGFP GGAEPGNGLK PRKRPRENKE VPRASLLSFQ DEEEENEEVF
KVKKSSYSKK IVKLLKKEYK EDLEKSKIKT ELNSSAESEQ PLDKTGHVKD TNQEDGVIIS
EHGEDEMDME SEKEEEKPKT GGAFSNALSS LNVLRPGEIP DAAFIHAARK KRQMARELGD
FTPHDNEPGK GRLVREDEND ASDDEDDDEK RRIVFSVKEK SQRQKIAEEI GIEGSDDDAL
VTGEQDEELS RWEQEQIRKG INIPQVQASQ PAEVNMYYQN TYQTMPYGSS YGIPYSYTAY
GSSDAKSQKT DNTVPFKTPS NEMTPVTIDL VKKQLKDRLD SMKELHKTNR QQHEKHLQSR
VDSTRAIERL EGSSGGIGER YKFLQEMRGY VQDLLECFSE KVPLINELES AIHQLYKQRA
SRLVQRRQDD IKDESSEFSS HSNKALMAPN LDSFGRDRAL YQEHAKRRIA EREARRTRRR
QAREQTGKMA DHLEGLSSDD EETSTDITNF NLEKDRISKE SGKVFEDVLE SFYSIDCIKS
QFEAWRSKYY TSYKDAYIGL CLPKLFNPLI RLQLLTWTPL EAKCRDFENM LWFESLLFYG
CEEREQEKDD VDVALLPTIV EKVILPKLTV IAENMWDPFS TTQTSRMVGI TLKLINGYPS
VVNAENKNTQ VYLKALLLRM RRTLDDDVFM PLYPKNVLEN KNSGPYLFFQ RQFWSSVKLL
GNFLQWYGIF SNKTLQELSI DGLLNRYILM AFQNSEYGDD SIKKAQNVIN CFPKQWFMNL
KGERTISQLE NFCRYLVHLA DTIYRNSIGC SDVEKRNARE NIKQIVKLLA SVRALDHAMS
VASDHNVKEF KSLIEGK
