ID A0A2Y9PAP7_DELLE Unreviewed; 3114 AA.
AC A0A2Y9PAP7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=MAX gene-associated protein isoform X2 {ECO:0000313|RefSeq:XP_022443099.1, ECO:0000313|RefSeq:XP_022443100.1};
GN Name=MGA {ECO:0000313|RefSeq:XP_022443099.1,
GN ECO:0000313|RefSeq:XP_022443100.1, ECO:0000313|RefSeq:XP_022443101.1,
GN ECO:0000313|RefSeq:XP_022443102.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022443100.1};
RN [1] {ECO:0000313|RefSeq:XP_022443099.1, ECO:0000313|RefSeq:XP_022443100.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022443099.1,
RC ECO:0000313|RefSeq:XP_022443100.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00201}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00201}.
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DR RefSeq; XP_022443099.1; XM_022587391.2.
DR RefSeq; XP_022443100.1; XM_022587392.2.
DR RefSeq; XP_022443101.1; XM_022587393.2.
DR RefSeq; XP_022443102.1; XM_022587394.2.
DR STRING; 9749.A0A2Y9PAP7; -.
DR OrthoDB; 5323209at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0071339; C:MLL1 complex; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd18911; bHLHzip_MGA; 1.
DR CDD; cd20195; T-box_MGA-like; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR Gene3D; 2.60.40.820; Transcription factor, T-box; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR013788; Hemocyanin/hexamerin.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR037935; MAX_gene-associated_bHLHzip.
DR InterPro; IPR032060; MGA_dom.
DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
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:SF32; MAX GENE-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR11267; T-BOX PROTEIN-RELATED; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF16059; MGA_dom; 1.
DR Pfam; PF00907; T-box; 1.
DR PRINTS; PR00937; TBOX.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00425; TBOX; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
DR PROSITE; PS01264; TBOX_2; 1.
DR PROSITE; PS50252; TBOX_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00201};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00201}; Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 79..260
FT /note="T-box"
FT /evidence="ECO:0000259|PROSITE:PS50252"
FT DOMAIN 2473..2524
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 259..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1534..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1778..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1945..1974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2016..2095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2187..2214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2307..2362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2580..2609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2625..2645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2990..3014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1112..1143
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2019..2040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2055..2069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2199..2214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2347..2362
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2594..2609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2627..2645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3114 AA; 341335 MW; 2827FE4B8562668B CRC64;
MEEKQQIILA NQDGGTVAGA APTFFVILKQ PGNGKTDQGI LVTNRDACAL ASSVSSPGKS
KGKICLPADC TVGGITVTLD NNSMWNEFYH RSTEMILTKQ GRRMFPYCRY WITGLDSNMK
YILVMDISPV DNHRYKWNGR WWEPSGKAEP HVLGRVFIHP ESPSTGHYWM HQPVSFYKLK
LTNNTLDQEG HIILHSMHRY LPRLHLVPAE KATEVIQLNG PGVHTFTFPQ TEFFAVTAYQ
NIQITQLKID YNPFAKGFRD DGLNSKPQRD GKQKNSSDQE GNSVPSSPGQ RVRLTEGEGS
EIQLTDSDPL LRGHEASCKG LEKPSLNVKR DFLGFMDIDS ALGEVPQLKQ EVSESLVGNN
FEDGSHVTSP LNPNENFNVV IKEEPLDDYE YELGECPEGV TVKQEETDEE TDVYSNSDDD
PILEKQLKRH NKADKLEADH PSSKWLLPNS PSGVAKAKMF KLDAGKMPVV YLEPCAVTKS
TVKISELPDN MLATSRKDRT SALTELDYLP TYIENSNETG FCLGKESENG LRRHSPDLRV
VQKYPSLKDP QWKYPDISDS MNTEKILDGS KSSVGDSFLG KEDLGRKKSM LKISTASKTV
NANQNAPPNV PGKRGRPRKL KLSKAGRPPK NTGKSLTSTK NTPMGPGSTF PDVKPDLEDV
DGVLFVSFES KEALDIHAVD GTTEESSSLQ ASVTNDPGCR ARIFQLEKEL IEDLKALRHK
QVIHPGLQEV GLKLNSVDPA MSIDLKYLGV QLPLAPATSF PFWNLTGTNP ASPDAGFPFV
SRTGKTNDFT KIKGWRGKFH SASASRNEGG NSEGSLKNRS AFCSDKLDEY LENEGKLMET
SMGFSSNAPT SPVVYQLPTK STSYVRTLDS VLKKQSTISP STSYSLKPHS VPSVSRKAKS
QNKQAPFSGR TKSSYKSILP YPVSPKQKHS HTIPGDKVTK NSSTTISENR VNNLVVPTLD
ENTFPKQISL RQAHQQQQQQ QQGTRPPGLS KSQVKLMDLE DCALWEGKPR TYITEERADV
SLTTLLTAQA SLKTKPIHTI IRKRAPPCNN DFCRLGCVCS SLALEKRQPA HCRRPDCMFG
CTCLKRKVVL VKGGSKTKHF QRKTAHRDPV FYDNLGEEQR EEEEGVREEE EQLKEKKKRK
KLEYTICETE PEQPVRHYPL WVKVEGEVDP EPVYIPTPSV IEPMKPLLLP QPEVLSTTVK
GKLLTGIKPA RAYTPKPNPV IREEDKDPVY LYFESMMTCA RVRVYERKQE EQRQPSPSPS
PSFQQQGSCH SSPENCSVKE PDSEQQPLKP ITCDLEDDSD KSQEKSWKSS CNEGESSSTS
YVHQRSPGGP TKLIEIISDC NWEEDRNKIL SILSQHINSN MPQSLKVGSF IIELASQRKS
RGEKNPPVYS SRVKISMPSC QDQDDMAEKS GSETPDGPLS PGKMDDISPV QTDALDSVRE
RLHGGKGLPF YAGLSPAGKL VAYKRKPSSS TSGLIQVNGK SYPQAKLLLG QMGALHPANR
LAAYITGRLR PSVLDLSTLS TVISKVASNA KVAASRKPRT LLPSTSNSKT ASSSSATTNR
PGKNLKAFVP AKRPIAARPS PGGVFTQFVM SKVGALQQKI PGVSTPQPLT GPQKFSIRPS
PVMVVTPVVS SEPVQVCSPV TAAVTTTTPQ VFLENVTAVT PVTAISDVGT KETTYSSGAP
TAGVVEVSET NTSTLVTPTQ STATVNLIKT TGITTPVASV AFPKSLVASP PTITLPVAST
ASTSIVVVTT AASSSMVTTP TSSLSSVPII LSGIDGSPPV SQRPENAPQI PVATPQVSPN
TVKRAGPRLL LIPVQQGSPT LRPVPNTQLQ GHRMVLQPVR SPSGMNLFRH PNGQIVQLLP
LHQLRGSNTQ PNLQPVMFRN PGSVMGIRLP TPSKPSETPP SSASSSSFSV MNPVIQAVGS
SPAMNVITQA PSLLSSGPSF VSQSGTLTLR ISPPEPQSFA SKTGSETKIT YSSGGQPVGT
ASLIPLQSGS FALLQLPGQK PVPSSILQHV ASLQMKRESQ NADQKDETSF LKREQETKKA
LQSGGEAIDP EANIIKQNSG ATVSEETLND SLEDGGDHLD EESLTEEGPA TVKPSQHAYI
TGSHTGEDYK NVDEEYGIRN HNNSKEKLTV LEVKTISGRA SNMTVQSVSN VQLKKLDVKV
EQQKGLDNPG EKSNEFPIIS KEESKLEFSG SRVVEQQSNP KPETKEKGCG DSLEKDSIRE
RWRKHLKGPL TQKCVRTSQE CKKETDEQLI KETETCQENS DVFQQEHGIS DLLGKSGTTE
NARILKTECD SWSRISSPAA FSIFPRRATK GSRGEGHFQG HLLLSGEQIK PKQEKKGGRS
SADFTVLDLE EDDEEDENEK TDDSIDEIVD VVSDYQSEEV DDVEKVNNCV EYIEDDEEQV
DIETVEEPPE EVNVVHMKTT AAHTQTFKQL CRTHITTDEK AAEKSRKATP VPLKLKPDYW
SEKLQKEAEA FAYYRRTHTA NERRRRGEMR DLFEKLKITL GLLHSSKVSK SLILTRAFSE
IQGLTDQADK LIGQKNLLTR KRNILIRKVS SLSGKTEEVV LKKLEYIYAK QQALEAQKRK
KKMGSDEFDV SPRTSKQQEG SSASSVDLGQ MFINNRKGKP LILSRKKDQA TENTSSSNTP
HTSANIVMTP QGQLLTLKGP LFSGPVVTVS PALLEADLKP QVASSAVAQS ENDDLFMMPR
IVNVTSLATE GGLVDMGGSK YPHEVPDGKP PDHLKNTVRN EDNSCEDLGR ISSRGNHRDV
RMALGTTQVY LSNKDSGFPQ IVDVSSMQEA QEFLPKKISS DMRGIQHKWK ESESRRERLK
TKESPFHKLK MKDLKDSSIE MELRKVASAI EEAALDPSEL LTNMEDEDDT DETLTSLLNE
IAFLNQQLND DSVNLAELPS SMDTEFPGDA RQAFISKLPP GNRATFQVGH LGTGLKELPD
VQGESDSVSP LLLHLEDDDF SENEKQLAEP ASEPDVLKIV IDSEIKDSVV SHRKAGDEGK
STGIPAEPES VSSPPILHMK AGLENSSTDT LWRPMPKLAP LGLKVANPSS DVDGQSLKVM
PCLAPVAAKA GSVGHKMNLT GNDQECRDSK MMPTLAPVVA KLGNSGASPS SAGK
//
