MGAP_HUMAN
ID MGAP_HUMAN Reviewed; 3065 AA.
AC Q8IWI9; B9EGR5; E7ENI0; F5H7K2; Q9H8R3; Q9H9N7; Q9UG69; Q9Y4E9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 4.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=MAX gene-associated protein;
DE AltName: Full=MAX dimerization protein 5;
GN Name=MGA; Synonyms=KIAA0518, MAD5;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS SER-716
RP AND ALA-1523.
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-1134 AND 1800-2526 (ISOFORM
RP 1), AND VARIANT SER-716.
RC TISSUE=Ovary, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2416-3065 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2817-3065 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924; SER-1208 AND SER-1457,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-2910, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534; SER-1208; SER-1430;
RP SER-1457 AND SER-2541, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2921, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607; SER-851; SER-924;
RP SER-1208; SER-1457; SER-2541; SER-2921 AND SER-2978, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [14]
RP INTERACTION WITH ZMYND11.
RX PubMed=23372760; DOI=10.1371/journal.pone.0054715;
RA Kateb F., Perrin H., Tripsianes K., Zou P., Spadaccini R., Bottomley M.,
RA Franzmann T.M., Buchner J., Ansieau S., Sattler M.;
RT "Structural and functional analysis of the DEAF-1 and BS69 MYND domains.";
RL PLoS ONE 8:E54715-E54715(2013).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2265, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-460; LYS-570; LYS-1985; LYS-2113;
RP LYS-2135 AND LYS-2238, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2113; LYS-2135 AND LYS-2238, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-329; LYS-1207; LYS-1985;
RP LYS-2113; LYS-2135; LYS-2194; LYS-2238; LYS-2284 AND LYS-2413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-178; LYS-323; LYS-329;
RP LYS-349; LYS-432; LYS-460; LYS-465; LYS-482; LYS-570; LYS-613; LYS-654;
RP LYS-785; LYS-791; LYS-817; LYS-826; LYS-928; LYS-990; LYS-1091; LYS-1140;
RP LYS-1162; LYS-1199; LYS-1207; LYS-1461; LYS-1502; LYS-1985; LYS-1992;
RP LYS-2103; LYS-2113; LYS-2135; LYS-2139; LYS-2146; LYS-2159; LYS-2194;
RP LYS-2206; LYS-2238; LYS-2284; LYS-2378; LYS-2413; LYS-2457; LYS-2532;
RP LYS-2546; LYS-2629; LYS-2679; LYS-2698; LYS-2784 AND LYS-3041, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Functions as a dual-specificity transcription factor,
CC regulating the expression of both MAX-network and T-box family target
CC genes. Functions as a repressor or an activator. Binds to 5'-
CC AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate MYC-MAX
CC target genes. Suppresses transcriptional activation by MYC and inhibits
CC MYC-dependent cell transformation. Function activated by
CC heterodimerization with MAX. This heterodimerization serves the dual
CC function of both generating an E-box-binding heterodimer and
CC simultaneously blocking interaction of a corepressor (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAX. Requires dimerization with MAX for E-box
CC binding (By similarity). Component of some MLL1/MLL complex, at least
CC composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and
CC RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70,
CC INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31,
CC RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9
CC and TEX10. Interacts with ZMYND11. {ECO:0000250,
CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:23372760}.
CC -!- INTERACTION:
CC Q8IWI9; Q13185: CBX3; NbExp=3; IntAct=EBI-2815196, EBI-78176;
CC Q8IWI9; P61244: MAX; NbExp=5; IntAct=EBI-2815196, EBI-751711;
CC Q8IWI9; Q93009: USP7; NbExp=3; IntAct=EBI-2815196, EBI-302474;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IWI9-4; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IWI9-3; Sequence=VSP_060177;
CC -!- DOMAIN: Transcription repression is enhanced or dependent on the
CC presence of the T-box DNA-binding domain. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14186.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14543.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC016134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136659; AAI36660.1; -; mRNA.
DR EMBL; AK022696; BAB14186.1; ALT_INIT; mRNA.
DR EMBL; AK023360; BAB14543.1; ALT_INIT; mRNA.
DR EMBL; AB011090; BAA25444.1; -; mRNA.
DR EMBL; AL050181; CAB43310.1; -; mRNA.
DR CCDS; CCDS55959.1; -. [Q8IWI9-4]
DR CCDS; CCDS55960.1; -. [Q8IWI9-3]
DR PIR; T00081; T00081.
DR RefSeq; NP_001074010.2; NM_001080541.2. [Q8IWI9-3]
DR RefSeq; NP_001157745.1; NM_001164273.1. [Q8IWI9-4]
DR SMR; Q8IWI9; -.
DR BioGRID; 116870; 193.
DR CORUM; Q8IWI9; -.
DR DIP; DIP-57615N; -.
DR ELM; Q8IWI9; -.
DR IntAct; Q8IWI9; 104.
DR MINT; Q8IWI9; -.
DR STRING; 9606.ENSP00000219905; -.
DR CarbonylDB; Q8IWI9; -.
DR GlyConnect; 2859; 1 O-Linked glycan (1 site).
DR GlyGen; Q8IWI9; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q8IWI9; -.
DR PhosphoSitePlus; Q8IWI9; -.
DR BioMuta; MGA; -.
DR DMDM; 527504082; -.
DR EPD; Q8IWI9; -.
DR jPOST; Q8IWI9; -.
DR MassIVE; Q8IWI9; -.
DR MaxQB; Q8IWI9; -.
DR PaxDb; Q8IWI9; -.
DR PeptideAtlas; Q8IWI9; -.
DR PRIDE; Q8IWI9; -.
DR ProteomicsDB; 17160; -.
DR ProteomicsDB; 27509; -.
DR Antibodypedia; 6067; 87 antibodies from 16 providers.
DR Ensembl; ENST00000219905.13; ENSP00000219905.7; ENSG00000174197.18. [Q8IWI9-4]
DR Ensembl; ENST00000566586.6; ENSP00000456141.1; ENSG00000174197.18. [Q8IWI9-3]
DR GeneID; 23269; -.
DR KEGG; hsa:23269; -.
DR UCSC; uc010ucy.2; human. [Q8IWI9-4]
DR CTD; 23269; -.
DR DisGeNET; 23269; -.
DR GeneCards; MGA; -.
DR HGNC; HGNC:14010; MGA.
DR HPA; ENSG00000174197; Tissue enhanced (brain).
DR MalaCards; MGA; -.
DR MIM; 616061; gene.
DR neXtProt; NX_Q8IWI9; -.
DR OpenTargets; ENSG00000174197; -.
DR PharmGKB; PA134976336; -.
DR VEuPathDB; HostDB:ENSG00000174197; -.
DR eggNOG; KOG3585; Eukaryota.
DR GeneTree; ENSGT00940000156269; -.
DR HOGENOM; CLU_000469_1_0_1; -.
DR InParanoid; Q8IWI9; -.
DR OMA; FQRKATH; -.
DR OrthoDB; 1201455at2759; -.
DR TreeFam; TF106341; -.
DR PathwayCommons; Q8IWI9; -.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q8IWI9; -.
DR SIGNOR; Q8IWI9; -.
DR BioGRID-ORCS; 23269; 42 hits in 1101 CRISPR screens.
DR ChiTaRS; MGA; human.
DR GenomeRNAi; 23269; -.
DR Pharos; Q8IWI9; Tbio.
DR PRO; PR:Q8IWI9; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8IWI9; protein.
DR Bgee; ENSG00000174197; Expressed in calcaneal tendon and 206 other tissues.
DR ExpressionAtlas; Q8IWI9; baseline and differential.
DR Genevisible; Q8IWI9; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00182; TBOX; 1.
DR Gene3D; 2.60.40.820; -; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR037935; MAX_gene-associated_protein.
DR InterPro; IPR032060; MGA_dom.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR046360; T-box_DNA-bd.
DR InterPro; IPR036960; T-box_sf.
DR InterPro; IPR001699; TF_T-box.
DR InterPro; IPR018186; TF_T-box_CS.
DR PANTHER; PTHR11267; PTHR11267; 1.
DR PANTHER; PTHR11267:SF32; PTHR11267:SF32; 1.
DR Pfam; PF16059; DUF4801; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00907; T-box; 1.
DR PRINTS; PR00937; TBOX.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00425; TBOX; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS01264; TBOX_2; 1.
DR PROSITE; PS50252; TBOX_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..3065
FT /note="MAX gene-associated protein"
FT /id="PRO_0000342692"
FT DOMAIN 2423..2474
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DNA_BIND 84..260
FT /note="T-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 259..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1967..2029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2258..2316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2576..2595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2668..2709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2944..2968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1111..1147
FT /evidence="ECO:0000255"
FT COILED 2817..2841
FT /evidence="ECO:0000255"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1972..1998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2299..2316
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2577..2595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2675..2705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2265
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2910
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 2921
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 329
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 349
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 432
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 460
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 482
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 570
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 785
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 791
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 817
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 826
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 928
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 990
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1091
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1162
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1502
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1985
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1992
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2206
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2284
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2532
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2546
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2629
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2679
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2784
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 3041
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1529..1737
FT /note="Missing (in isoform 2)"
FT /id="VSP_060177"
FT VARIANT 338
FT /note="T -> A (in dbSNP:rs3803348)"
FT /id="VAR_044341"
FT VARIANT 716
FT /note="T -> S (in dbSNP:rs2178004)"
FT /id="VAR_044342"
FT VARIANT 1270
FT /note="C -> R (in dbSNP:rs17677811)"
FT /id="VAR_044343"
FT VARIANT 1523
FT /note="P -> A (in dbSNP:rs17677991)"
FT /id="VAR_057268"
FT CONFLICT 266
FT /note="K -> N (in Ref. 3; BAB14186)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="S -> R (in Ref. 3; BAB14186)"
FT /evidence="ECO:0000305"
FT CONFLICT 1383
FT /note="R -> P (in Ref. 2; AAI36660)"
FT /evidence="ECO:0000305"
FT CONFLICT 2230
FT /note="Missing (in Ref. 3; BAB14543)"
FT /evidence="ECO:0000305"
FT CONFLICT 2365
FT /note="A -> T (in Ref. 3; BAB14543)"
FT /evidence="ECO:0000305"
FT CONFLICT 2744
FT /note="P -> L (in Ref. 2; AAI36660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3065 AA; 336159 MW; 430B04B7ED92B4A8 CRC64;
MEEKQQIILA NQDGGTVAGA APTFFVILKQ PGNGKTDQGI LVTNQDACAL ASSVSSPVKS
KGKICLPADC TVGGITVTLD NNSMWNEFYH RSTEMILTKQ GRRMFPYCRY WITGLDSNLK
YILVMDISPV DNHRYKWNGR WWEPSGKAEP HVLGRVFIHP ESPSTGHYWM HQPVSFYKLK
LTNNTLDQEG HIILHSMHRY LPRLHLVPAE KAVEVIQLNG PGVHTFTFPQ TEFFAVTAYQ
NIQITQLKID YNPFAKGFRD DGLNNKPQRD GKQKNSSDQE GNNISSSSGH RVRLTEGQGS
EIQPGDLDPL SRGHETSGKG LEKTSLNIKR DFLGFMDTDS ALSEVPQLKQ EISECLIASS
FEDDSRVASP LDQNGSFNVV IKEEPLDDYD YELGECPEGV TVKQEETDEE TDVYSNSDDD
PILEKQLKRH NKVDNPEADH LSSKWLPSSP SGVAKAKMFK LDTGKMPVVY LEPCAVTRST
VKISELPDNM LSTSRKDKSS MLAELEYLPT YIENSNETAF CLGKESENGL RKHSPDLRVV
QKYPLLKEPQ WKYPDISDSI STERILDDSK DSVGDSLSGK EDLGRKRTTM LKIATAAKVV
NANQNASPNV PGKRGRPRKL KLCKAGRPPK NTGKSLISTK NTPVSPGSTF PDVKPDLEDV
DGVLFVSFES KEALDIHAVD GTTEESSSLQ ASTTNDSGYR ARISQLEKEL IEDLKTLRHK
QVIHPGLQEV GLKLNSVDPT MSIDLKYLGV QLPLAPATSF PFWNLTGTNP ASPDAGFPFV
SRTGKTNDFT KIKGWRGKFH SASASRNEGG NSESSLKNRS AFCSDKLDEY LENEGKLMET
SMGFSSNAPT SPVVYQLPTK STSYVRTLDS VLKKQSTISP STSYSLKPHS VPPVSRKAKS
QNRQATFSGR TKSSYKSILP YPVSPKQKYS HVILGDKVTK NSSGIISENQ ANNFVVPTLD
ENIFPKQISL RQAQQQQQQQ QGSRPPGLSK SQVKLMDLED CALWEGKPRT YITEERADVS
LTTLLTAQAS LKTKPIHTII RKRAPPCNND FCRLGCVCSS LALEKRQPAH CRRPDCMFGC
TCLKRKVVLV KGGSKTKHFQ RKAAHRDPVF YDTLGEEARE EEEGIREEEE QLKEKKKRKK
LEYTICETEP EQPVRHYPLW VKVEGEVDPE PVYIPTPSVI EPMKPLLLPQ PEVLSPTVKG
KLLTGIKSPR SYTPKPNPVI REEDKDPVYL YFESMMTCAR VRVYERKKED QRQPSSSSSP
SPSFQQQTSC HSSPENHNNA KEPDSEQQPL KQLTCDLEDD SDKLQEKSWK SSCNEGESSS
TSYMHQRSPG GPTKLIEIIS DCNWEEDRNK ILSILSQHIN SNMPQSLKVG SFIIELASQR
KSRGEKNPPV YSSRVKISMP SCQDQDDMAE KSGSETPDGP LSPGKMEDIS PVQTDALDSV
RERLHGGKGL PFYAGLSPAG KLVAYKRKPS SSTSGLIQVA SNAKVAASRK PRTLLPSTSN
SKMASSSGTA TNRPGKNLKA FVPAKRPIAA RPSPGGVFTQ FVMSKVGALQ QKIPGVSTPQ
TLAGTQKFSI RPSPVMVVTP VVSSEPVQVC SPVTAAVTTT TPQVFLENTT AVTPMTAISD
VETKETTYSS GATTTGVVEV SETNTSTSVT STQSTATVNL TKTTGITTPV ASVAFPKSLV
ASPSTITLPV ASTASTSLVV VTAAASSSMV TTPTSSLGSV PIILSGINGS PPVSQRPENA
AQIPVATPQV SPNTVKRAGP RLLLIPVQQG SPTLRPVSNT QLQGHRMVLQ PVRSPSGMNL
FRHPNGQIVQ LLPLHQLRGS NTQPNLQPVM FRNPGSVMGI RLPAPSKPSE TPPSSTSSSA
FSVMNPVIQA VGSSSAVNVI TQAPSLLSSG ASFVSQAGTL TLRISPPEPQ SFASKTGSET
KITYSSGGQP VGTASLIPLQ SGSFALLQLP GQKPVPSSIL QHVASLQMKR ESQNPDQKDE
TNSIKREQET KKVLQSEGEA VDPEANVIKQ NSGAATSEET LNDSLEDRGD HLDEECLPEE
GCATVKPSEH SCITGSHTDQ DYKDVNEEYG ARNRKSSKEK VAVLEVRTIS EKASNKTVQN
LSKVQHQKLG DVKVEQQKGF DNPEENSSEF PVTFKEESKF ELSGSKVMEQ QSNLQPEAKE
KECGDSLEKD RERWRKHLKG PLTRKCVGAS QECKKEADEQ LIKETKTCQE NSDVFQQEQG
ISDLLGKSGI TEDARVLKTE CDSWSRISNP SAFSIVPRRA AKSSRGNGHF QGHLLLPGEQ
IQPKQEKKGG RSSADFTVLD LEEDDEDDNE KTDDSIDEIV DVVSDYQSEE VDDVEKNNCV
EYIEDDEEHV DIETVEELSE EINVAHLKTT AAHTQSFKQP SCTHISADEK AAERSRKAPP
IPLKLKPDYW SDKLQKEAEA FAYYRRTHTA NERRRRGEMR DLFEKLKITL GLLHSSKVSK
SLILTRAFSE IQGLTDQADK LIGQKNLLTR KRNILIRKVS SLSGKTEEVV LKKLEYIYAK
QQALEAQKRK KKMGSDEFDI SPRISKQQEG SSASSVDLGQ MFINNRRGKP LILSRKKDQA
TENTSPLNTP HTSANLVMTP QGQLLTLKGP LFSGPVVAVS PDLLESDLKP QVAGSAVALP
ENDDLFMMPR IVNVTSLATE GGLVDMGGSK YPHEVPDSKP SDHLKDTVRN EDNSLEDKGR
ISSRGNRDGR VTLGPTQVFL ANKDSGYPQI VDVSNMQKAQ EFLPKKISGD MRGIQYKWKE
SESRGERVKS KDSSFHKLKM KDLKDSSIEM ELRKVTSAIE EAALDSSELL TNMEDEDDTD
ETLTSLLNEI AFLNQQLNDD SVGLAELPSS MDTEFPGDAR RAFISKVPPG SRATFQVEHL
GTGLKELPDV QGESDSISPL LLHLEDDDFS ENEKQLAEPA SEPDVLKIVI DSEIKDSLLS
NKKAIDGGKN TSGLPAEPES VSSPPTLHMK TGLENSNSTD TLWRPMPKLA PLGLKVANPS
SDADGQSLKV MPCLAPIAAK VGSVGHKMNL TGNDQEGRES KVMPTLAPVV AKLGNSGASP
SSAGK
