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Database: UniProt
Entry: A0A2I2ZD20_GORGO
LinkDB: A0A2I2ZD20_GORGO
Original site: A0A2I2ZD20_GORGO 
ID   A0A2I2ZD20_GORGO        Unreviewed;       979 AA.
AC   A0A2I2ZD20;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=MIB2 {ECO:0000313|Ensembl:ENSGGOP00000045153.1};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000045153.1, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000045153.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000045153.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000045153.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; CABD030000205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030000206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030000207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030000208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_018865393.1; XM_019009848.1.
DR   AlphaFoldDB; A0A2I2ZD20; -.
DR   STRING; 9593.ENSGGOP00000045153; -.
DR   Ensembl; ENSGGOT00000064466.1; ENSGGOP00000045153.1; ENSGGOG00000006337.3.
DR   GeneTree; ENSGT00940000158097; -.
DR   InParanoid; A0A2I2ZD20; -.
DR   OMA; HDAIGKD; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001519; Chromosome 1.
DR   Bgee; ENSGGOG00000006337; Expressed in heart and 5 other cell types or tissues.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16726; RING-HC_MIB2_rpt1; 1.
DR   CDD; cd02339; ZZ_Mind_bomb; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR042056; MIB1/2_ZZ.
DR   InterPro; IPR010606; Mib_Herc2.
DR   InterPro; IPR037252; Mib_Herc2_sf.
DR   InterPro; IPR040847; SH3_15.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR   PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13857; Ank_5; 1.
DR   Pfam; PF06701; MIB_HERC2; 2.
DR   Pfam; PF18346; SH3_15; 2.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF159034; Mib/herc2 domain-like; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 5.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS51416; MIB_HERC2; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          102..181
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000259|PROSITE:PS51416"
FT   DOMAIN          187..239
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          250..328
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000259|PROSITE:PS51416"
FT   REPEAT          565..597
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          598..630
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          631..663
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          734..758
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          768..800
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          933..968
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  105882 MW;  41520A8CAFD24785 CRC64;
     MAAALWQGRA LGSRPWGPTV SSRRSPQCPV AQEGLGARSR PRVAPRSLAR CGPSSRLMGW
     KPSEARGQSQ SLQASGLQPR SLKAARRATG QPDRSRAAPP NMDPDPQAGV QVGMRVVRGV
     DWKWGQQDGG EGGVGTVVEL GRHGSPSTPD RTVVVQWDQG TRTNYRAGYQ GAHDLLLYDN
     AQIGVRHPNI ICDCCKKHGL RGMRWKCRVC LDYDLCTQCY MHNKHELAHA FDRYETAHSR
     PVTLSPRQGL PRIPLRGIFQ GAKVVRGPDW EWGSQDGGEG KPGRVVDIRG WDVETGRSVA
     SVTWADGTTN VYRVGHKGKV DLKCVGEAAG GFYYKDHLPR LGKPAELQRR VSADSQPFQH
     GDKVKCLLDT DVLREMQEGH GGWNPRMAEF IGQTGTVHRI TDRGDVRVQF NHETRWTFHP
     GALTKHHSFW VGDVVRVIGD LDTVKRLQAG HGEWTDDMAP ALGRVGKVVK VFGDGNLRVA
     VAGQRWTFSP SCLVAYRPEE DANLDVAERA RENKSSLSVA LDKLRAQKSD PEHPGRLVVE
     VALGNAARAL DLLRRRPEQV DTKNQGRTAL QVAAYLGQVE SIRLLLQARA GVDLPDDEGN
     TALHYAALGN QPEAARVLMS AGCRADAINS TQSTALHVAV QRGFLEVVRA LCERGCDVNL
     PDAHSDTPLH SAISAGTGAS GIVEVLTEVP NIDVTATNSQ GFTLLHHASL KGHVLAVRKI
     LARARQLVDA KKEDGFTALH LAALNNHREV AQILIREGRC DVNVRNRKLQ SPLHLAVQQA
     HVGLVPLLVD AGCSVNAEDE EGDTALHVAL QRHQLLPLVA DGAGGDPGPL QLLSRLQASG
     LPGSAELTVG AAVACFLALE GADVSYSNHR GRSPLDLAAE GRVLKALQGC AQRFRERQAG
     GGAAPGPRQT LGTPNTVTNL HVGAALGPEA AECLVCSELA LLVLFSPCQH RTVCEECARR
     MKKCIRCQVV VSKKLRPGG
//
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