ID K7CIZ4_PANTR Unreviewed; 1070 AA.
AC K7CIZ4; A0A2J8IRX2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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|EMBL:JAA32448.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA32448.1};
RN [1] {ECO:0000313|EMBL:JAA32448.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skin {ECO:0000313|EMBL:JAA32448.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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; GABD01000652; JAA32448.1; -; mRNA.
DR AlphaFoldDB; K7CIZ4; -.
DR STRING; 9598.ENSPTRP00000062721; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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; 4.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; 2.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00184; RING; 2.
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; 2.
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; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 2: Evidence at transcript level;
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 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 116..195
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 201..253
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 264..342
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 579..611
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 612..644
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 645..677
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 748..772
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 782..814
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 947..982
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1026..1059
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..122
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"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 115863 MW; 8FBDF790CD2FFD6A CRC64;
MAAALRRGRA LGSRPSGPTV SSRRSPQCPV AQEGLRARSR PRVAPRSLAR CGPSSRLMGW
KPSEARGQSQ SLQASGLQPR SLKAARRATG RPDRSRAARP TMDPSAHRSR AAPPNMDPDP
QAGVQVGMRV VRGVDWKWGQ QDGGEGGVGT VVELGRHGSP STPDRTVVVQ WDQGTRTNYR
AGYQGAHDLL LYDNAQIGVR HPNIICDCCK KHGLRGMRWK CRVCLDYDLC TQCYMHNKHE
LAHAFDRYET AHSRPVTLSP RQGLPRIPLR GIFQGAKVVR GPDWEWGSQD GGEGKPGRVV
DIRGWDVETG RSVASVTWAD GTTNVYRVGH KGKVDLKCVG EAAGGFYYKD HLPRLGKPAE
LQRRVSADSQ PFQHGDKVKC LLDTDVLREM QEGHGGWNPR MAEFIGQTGT VHRITDRGDV
RVQFNHETRW TFHPGALTKH HSFWVGDVVR VIGDLDTVKR LQAGHGEWTD DMAPALGRVG
KVVKVFGDGN LRVAVAGQRW TFSPSCLVAY RPEEDANLDV AERARENKSS LSVALDKLRA
QKSDPEHPGR LVVEVALGNA ARALDLLRRR PEQVDTKNQG RTALQVAAYL GQVELIRLLL
QARAGVDLPD DEGNTALHYA ALGNQPEAAR VLLSAGCRAD AINSTQSTAL HVAVQRGFLE
VVRALCERGC DVNLPDAHSD TPLHSAISAG TGASGIVEVL TEVPNIDVTA TNSQGFTLLH
HASLKGHALA VRKILARARQ LVDAKKEDGF TALHLAALNN HREVAQILIR EGRCDVNVRN
RKLQSPLHLA VQQAHVGLVP LLVDAGCSVN AEDEEGDTAL HVALQHHQLL PLVADGAGGD
PGPLQLLSRL QASGLPGSAE LTVGAAVACF LALEGADVSY TNHRGRSPLD LAAEGRVLKA
LQGCAQRFQE RQAGGGAAPG PRQTLGTPNT VTNLHVGAAP GPEAAECLVC SELALLVLFS
PCQHRTVCEE CARRMKKCIR CQVVVSKKLR PDGSEVASAA PAPGPPRQLV EELQSRYRQM
EERITCPICI DSHIRLVFQC GHGACAPCGS ALSACPICRQ PIRDRIQIFV
//
