ID A0A2K6A7D1_MANLE Unreviewed; 4524 AA.
AC A0A2K6A7D1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=MYC binding protein 2 {ECO:0000313|Ensembl:ENSMLEP00000035974.1};
GN Name=MYCBP2 {ECO:0000313|Ensembl:ENSMLEP00000035974.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000035974.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000035974.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR Ensembl; ENSMLET00000059574.1; ENSMLEP00000035974.1; ENSMLEG00000041844.1.
DR GeneTree; ENSGT00940000155756; -.
DR OMA; MAHPGCG; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd19799; Bbox2_MYCBP2; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.120.820; PHR domain; 2.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012983; PHR.
DR InterPro; IPR038648; PHR_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45943; E3 UBIQUITIN-PROTEIN LIGASE MYCBP2; 1.
DR PANTHER; PTHR45943:SF1; E3 UBIQUITIN-PROTEIN LIGASE MYCBP2; 1.
DR Pfam; PF08005; PHR; 2.
DR Pfam; PF00415; RCC1; 1.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM01337; APC10; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 3.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 4270..4288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 536..591
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 894..944
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 945..1002
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 2235..2328
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT DOMAIN 3612..3780
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT REGION 107..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2209..2236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2603..2825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2837..2857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2873..2914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3499..3525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3799..3820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2608..2629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2630..2651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2677..2709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2717..2750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2754..2784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2795..2817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3803..3817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4524 AA; 498781 MW; EA316B1665D7DE08 CRC64;
KFRTLPSSPG IFFLFFEMES HSVFQAGVQW CVILAHCSFY LLGSSNFPTS CEMEILCFVF
QSENLENTVI IPDIKLHSNP SAFNIYCNVR HCVLEWQKKE ISLAAASKNS VQSGESDSDE
EEESKEPPIK LPKIIEVGLC EVFELIKETR FSHPSLCLRS LQALLNVLQG QQPEGLQSEP
PEVLESLFQL LLEITVRSTG MNDSTGQSLT ALSCACLFSL VASWGETGRT LQAISAILTN
NGSHACQTIQ VPTILNSLQR SVQAVLVGKI QIQDWFSNGI KKAALMHKWP LKEISVDEDD
QCLLQNDGFF LYLLCKDGLY KIGSGYSGTV RGHIYNSTSR IRNRKEKKSW LGYAQGYLLY
RDVNNHSMTA IRISPETLEQ DGTVMLPDCH TESQNILFTD GEYINQIAAS RDDGFVVRIF
ATSTEPVLQQ ELQLKLARKC LHACGISLFD LEKDLHIIST GFDEESAILG AGREFALMKT
ANGKIYYTGK YQSLGIKQGG PSAGKWVELP ITKSPKIVHF SVGHDGSHAL LVAEDGSIFF
TGSASKGEDG ESTKSRRQSK PYKPKKIIKM EGKIVVYTAC NNGSSSVISK DGELYMFGKD
AIYSDSSSLV TDLKGHFVTQ VAMGKAHTCV LMKNGEVWTF GVNNKGQCGR DTGAMNQGGK
GFGVENMATA MDEDLEEELD EKDEKSMMCP PGMHKWKLEQ CMVCTVCGDC TGYGASCVSS
GRPDRVPGGI CGCGSGESGC AVCGCCKACA RELDGQEARQ RGILDAVKEM IPLDLLLAVP
VPGVNIEEHL QLRQEEKRQR VIRRHRLEEG RGPLVFAGPI FMNHREQALA RLRSHPAQLK
HKRDKHKDGS GERGEKDASK ITTYPPGSVR FDCELRAVQV SCGFHHSVVL MENGDVYTFG
YGQHGQLGHG DVNSRGCPTL VQALPGPSTQ VTAGSNHTAV LLMDGQVFTF GSFSKGQLGR
PILDVPYWNA KPAPMPNIGS KYGRKATWIG ASGDQTFLRI DEALINSHVL ATSEIFASKH
IIGLVPASIS EPPPFKCLLI NKVDGSCKTF NDSEQEDLQG FGVCLDPVYD VIWRFRPNTR
ELWCYNAVVA DARLPSAADM QSRCSILSPE LALPTGSRAL TTRSHAALHI LGCLDTLAAM
QDLKMGVAST EEETQAVMKV YSKEDYSVVN RFESHGGGWG YSAHSVEAIR FSADTDILLG
GLGLFGGRGE YTAKIKLFEL GPDGGDHETD GDLLAETDVL AYDCAAREKY AMMFDEPVLL
QAGWWYVAWA RVSGPSSDCG SHGQASITTD DGVVFQFKSS KKSNNGTDVN AGQIPQLLYR
LPTSDGSASK GKQQTSEPVH ILKRSFARTV SVECFESLLS ILHWSWTTLV LGVEELRGLK
GFQFTATLLD LERLRFVGTC CLRLLRVYTC EIYPVSATGK AVVEETSKLA ECIGKTRTLL
RKILSEGVDH CMVKLDNDPQ GYLSQPLSLL EAVLQECHNT FTACFHSFYP TPALQWACLC
DLLNCLDQDI QEANFKTSSS RLLAAVMSAL CHTSVKLTSI FPIAYDGEVL LRSIVKQVST
ENDSTLVHRF PLLVAHMEKL SQSEENISGM TSFREVLEKM LVIVVLPVRN SLRRENELFS
SHLVSNTCGL LASIVSELTA SALGSEVDGL NSLHSVKASA NRFTKTSQGR SWNTGNGSPD
AICFSVDKPG IVVVGFSVYG GGGIHEYELE VLVDDSEHAG DSTHSHRWTS LELVKGTYTT
DDSPSDIAEI RLDKVVPLKE NVKYAVRLRN YGSRTANGDG GMTTVQCPDG VTFTFSTCSL
SSNGTNQTRG QIPQILYYRS EFDGDLQSQL LSKANEEDKN CSRALSVVST VVRASKDLLH
RALAVDADDI PELLSSSSLF SMLLPLIIAY IGPVAAAIPK VAVEVFGLVQ QLLPSVAILN
QKYAPPAFNP NQSTDSTTGN QPEQGLSACT TSNHYAVIES EHPYKPACVM HYKVTFPECV
RWMTIEFDPQ CGTAQSEDVL RLLIPVRTFQ NSGYGPKLTS VHENLNSWIE LKKFSGSSGW
PTMVLVLPGN EALFSLETAS DYVKDDKASF YGFKCFAIGY EFSPGPDEGV IQLEKELANL
GGVCAAALMK KDLALPIGNE LEEDLEILEE AALQMLIGVW GFVYLFFIAI RWLQPDSYAD
PQKTSLILNK DDIRCGWPTT ITVQTKDQYG DVVHVPNMKV EVKAVPVSQK KTSLQQDQAK
KPQRIPGSPA VTTASSNTDM TFGGLASPKL DVSYEPMIVK EARYIAITMM KVYENYSFEE
LRFASPTPKR PSENMLIRVN NDGTYCANWT PGAIGLYTIH VTIDGIEIDA GLEVKVKDPP
KGMIPPGTQL VKPKTEPQPN KVRKFVAKDS AGLRIRSHPS LQSEQIGIVK VNGTITFIDE
IHNDDGVWLR LNDETIKKYV PNMNGYTEAW CLSFNQHLGK SLLVPVDESK TNTDDFFKDI
NSCCPQEATM QEQDMPFLRG GPGMYKVVKT GPSGHNIRSC PNLRGIPIGM LVLGNKVKAV
GEVTNSEGTW VQLDQNSMVE FCESDEGEAW SLARDRGGNQ YLRHEDEQVL LDQNSQTPPP
SPFSVQAFNK GASCSAQGFD YGLGNNKGDR GNISTSSRPA STSGKSELSS KHSRSLKPDG
HMSRTTADQK KPRGTDSLSA SESLILKSDA AKLRSDSHSR SLSPNHNTLQ TLKSDGRMPS
SSRAESPGPG SRLSSPKPKT LPANRSSPSG ASSPRSSSPH DKNLPQKSTA PVKTKLDPPR
ERSKSDSYTL DPDTLRKKKM PLTEPLRGRS TSPKPKSVPK DSTDSPGSEN RAPSPHVVQE
NLHSEVVEVC TSSTLKTNSL TDSTCDDSSE FKSVDEGSNK VHFSIGKAPL KDEQEMRASP
KISRKCANRH TRPKKEKSSF LFKGDGSKPL EPAKQAMSPS VAECARAVFA SFLWHEGIVH
DAMACSSFLK FHPELSKEHA PIRSSLNSQQ PAEEKETKLK NRHSLEISSA LNMFNIAPHG
PDISKMGSIN KNKVLSMLKE PPLHEKCEDG KTETTFEMSM HHTMKSKSPL PLTLQHLVAF
WEDISLATIK AASQNMIFPS PGSCAVLKKK ECEKENKKAK KEKKKKEKAE VRPRGNLFGE
MAQLAVGGPE KDTICELCGE SHPYPVTYHM RQAHPGCGRY AGGQGYNSIG HFCGGWAGNC
GDGGIGGSTW YLVCDRCREK YLREKQAAAR EKVKQSRRKP MQVKTPRALP TMEAHQVIKA
NALFLLSLSS AAEPSILCYH PAKPFQSQLP SVKEGISEDL PVKMPCLYLQ TLARHHHENF
VGYQDDNLFQ DEMRYLRSTS VPAPYISVTP DASPNVFEEP ESNMKSMPPS LETSPITDTD
LAKRTVFQRS YSVVASEYDK QHSILPARVK AIPRRRVNSG DTEVGSSLLR HPSPELSRLI
SAHSSLSKGE RNFQWPVLAF VIQHHDLEGL EIAMKQALRK SACRVFAMEA FNWLLCNVIQ
TTSLHDILWH FVASLTPAPV EPEEEEDEEN KTNKESSEQE KDTRVCEHPL SDIVIAGEAA
HPLPHTFHRL LQTISDLMMS LPSGSSLQQM ALRCWSLKFK QSDHQFLHQS NVFHHINNIL
SKSDDGDSEE SFSISIQSGF EAMSQELCIV MCLKDLTSIV DIKTSSRPAM IGSLTDGSTE
TFWESGDEDK NKTKNITINC VKGINARYVS VHVDNSRDLG LKQVPASFLL NQVDLDSRHI
GWVTSELPGG DNHIIKIELK GPENTLRVRQ VKVLGWKDGE STKIAGQISA SVAQQRNCEA
ETLRVFRLIT SQVFGKLISG DAEPTPEQEE KALLSSPEGE EKVYNATSDA DLKEHMVGII
FSRSKLTNLQ KQVCAHIVQA IRMEATRVRE EWEHAISSKE NANSQPNDED ASSDAYCFEL
LSMVLALSGS NVGRQYLAQQ LTLLQDLFSL LHTASPRVQR QVTSLLRRVL PEVTPNRLAS
IIGVKSLPPA DISDIIHSTE KGDWNKLGIL DMFLGCIAKA LTVQLKAKGT TITGTAGTTV
GKGVTTVTLP MIFNSSYLRR GESHWWMKGS TPTQISEIII KLIKDMAAVN QPEKDKICNS
FPFQQLWLAL ASLCVLDQDH VDRLSSGRWM GKDGQQKQMP MCDNHDDGET AAIILCNVCG
NLCTDCDRFL HLHRRTKTHQ RQVFKEEEEA IKVDLHEGCG RTKLFWLMAL ADSKTMKAMV
EFREHTGKPT TSSSEACRFC GSRSGTELSA VGSVCSDADC QAIPLSNGPC SPVTPLLHMD
KSYSSASLQL TQLFIIIIFA YVLFFSLFKL DCSHVFHLQC CRRVLENRWL GPRITFGFIS
CPICKNKINH IVLKDLLDPI KELYEDVRRK ALMRLEYEGL HKSEAITTPG VRFYNDPAGY
AMNRYAYYVC YKCRKAYFGG EARCDAEAGQ GDDYDPRELI CGACSDVSRA QMCPKHGTDF
LEYKCRYCCS VAVFFCFGTT HFCNACHDDF QRMTSIPKEE LPHCPAGPKG KQLEGTECPL
HVVHPPTGEE FALGCGVCRN AHTF
//
