MIB2_RAT
ID MIB2_RAT Reviewed; 971 AA.
AC Q68LP1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=E3 ubiquitin-protein ligase MIB2;
DE EC=2.3.2.27;
DE AltName: Full=Mind bomb homolog 2;
DE AltName: Full=RBSC-skeletrophin/dystrophin-like polypeptide;
DE AltName: Full=RING-type E3 ubiquitin transferase MIB2 {ECO:0000305};
GN Name=Mib2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-85.
RC STRAIN=Sprague-Dawley; TISSUE=Brain stem;
RA Leff P., Matus M., Gonzaga R., Arreola R., Salazar A., Calva J.C.,
RA Acevedo R., Flores A., Martinez C., Cervantes R., Retana I., Arias A.,
RA Parra L., Barbosa S., Pavon L., Gonzalez R., Alagon A., Anton B.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC Delta receptors, which act as ligands of Notch proteins. Positively
CC regulates the Delta-mediated Notch signaling by ubiquitinating the
CC intracellular domain of Delta, leading to endocytosis of Delta
CC receptors. {ECO:0000250|UniProtKB:Q8R516}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with actin monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}.
CC Note=Colocalizes with endosomal compartments. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Possibly via autoubiquitination (By similarity).
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT94937.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; AABR03042923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03045598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY675183; AAT94937.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q68LP1; -.
DR SMR; Q68LP1; -.
DR STRING; 10116.ENSRNOP00000023696; -.
DR iPTMnet; Q68LP1; -.
DR PhosphoSitePlus; Q68LP1; -.
DR PaxDb; Q68LP1; -.
DR PRIDE; Q68LP1; -.
DR RGD; 1359469; Mib2.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR HOGENOM; CLU_007287_2_0_1; -.
DR InParanoid; Q68LP1; -.
DR PhylomeDB; Q68LP1; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q68LP1; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q68LP1; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase 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; ISO:RGD.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.30.60.90; -; 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 Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00184; RING; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF159034; SSF159034; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
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 1: Evidence at protein level;
KW Actin-binding; ANK repeat; Cytoplasm; Endosome; Metal-binding;
KW Notch signaling pathway; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..971
FT /note="E3 ubiquitin-protein ligase MIB2"
FT /id="PRO_0000055949"
FT DOMAIN 1..80
FT /note="MIB/HERC2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT DOMAIN 149..227
FT /note="MIB/HERC2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT REPEAT 478..507
FT /note="ANK 1"
FT REPEAT 511..540
FT /note="ANK 2"
FT REPEAT 544..573
FT /note="ANK 3"
FT REPEAT 577..609
FT /note="ANK 4"
FT REPEAT 613..642
FT /note="ANK 5"
FT REPEAT 647..677
FT /note="ANK 6"
FT REPEAT 681..710
FT /note="ANK 7"
FT REPEAT 714..742
FT /note="ANK 8"
FT REPEAT 783..812
FT /note="ANK 9"
FT ZN_FING 86..138
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 848..883
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 927..960
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 971 AA; 105542 MW; 684526E518A9E505 CRC64;
MDLDPHAGVQ VGMRVVRGMD WKWGQQDGGE GGVGTVVELG RHGSPSTPDR TVVVQWDQGT
RTNYRAGYQG AHDLLLYDNA QIGIRHPNII CDCCKKHGLR GMRWKCRVCF DYDLCTQCYM
HNKHDLTHAF ERYETSHSRP VTLSPRQGLP RIPLRGIFQG AKVVRGPDWE WGSQDGGEGK
TGRVVDIRGW DVETGRSVAS VTWADGTTNV YRVGHKGKVD LKCVGEAAGG FYYKEHLPKL
GKPAELQRRV SADGQPFQRG DKVKCLLDTD VLRDMQEGHG GWNPRMAEFI GQMGTVHRIT
DRGDVRVQFN HETRWTFHPG ALTKHNSFWV GDVVRVIDDL DTVKRLQAGH GEWTDDMAPA
LGRVGKVVKV FGDGNLRVAV GGQRWTFSPA CLVACRPEED ANLGVAERAR ENKSAASVPV
AGSLSVALDK LRTQKSDPEH PGRLVVEAAL GNVARALDLL RRHPEQAGFH PAVDTKNQGR
TALQVAAYLG QVELVRLLLQ ARASVDLLDE EGNTALHYTA MGNQPEATRL LLSAGCGVDA
QNGTRSTALH VAVQRGFLEV VKILCEHGCD VNLPDAHADT PLHSAISAGA GASSIVEVLT
EVPGIDVTAT NSQGFTLLHH ASLKGHVLAV RKILARARQL VDAKKEDGFT ALHLAALNNH
REVAQVLIRE GRCDVNVRNR KLQSPLHLAV QQAHLGLVPL LVDAGCNVNT EDEEGDTALH
VALQRHQLLP LVADRAGGDP GPLQLLSRLQ ASGLPGSTEL TVGAAVACFL ALEGADVSYA
NHRGRSPLDL ATEGRVLKAL QGCAQRFRER QAGGGGGVPP GPRHVLSTPN TVTNLHVSGT
AGPEAAECLV CSELALLVLF SPCQHRTVCE ECARRMKKCI RCQVIISKKL RPDGSEVVNA
IQVPGPPRQL VEELQSRYRQ MEERITCPIC IDSHIRLVFQ CGHGACAPCG AALNACPICR
QPIRDRIQIF V
