AJUBA_MOUSE
ID AJUBA_MOUSE Reviewed; 547 AA.
AC Q91XC0; P97472;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=LIM domain-containing protein ajuba;
GN Name=Ajuba; Synonyms=Jub;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP TISSUE SPECIFICITY, FUNCTION, AND INTERACTION WITH GRB2.
RX PubMed=10330178; DOI=10.1128/mcb.19.6.4379;
RA Goyal R.K., Lin P., Kanungo J., Payne A.S., Muslin A.J., Longmore G.D.;
RT "Ajuba, a novel LIM protein, interacts with Grb2, augments mitogen-
RT activated protein kinase activity in fibroblasts, and promotes meiotic
RT maturation of Xenopus oocytes in a Grb2- and Ras-dependent manner.";
RL Mol. Cell. Biol. 19:4379-4389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11029037; DOI=10.1091/mbc.11.10.3299;
RA Kanungo J., Pratt S.J., Marie H., Longmore G.D.;
RT "Ajuba, a cytosolic LIM protein, shuttles into the nucleus and affects
RT embryonal cell proliferation and fate decisions.";
RL Mol. Biol. Cell 11:3299-3313(2000).
RN [4]
RP FUNCTION.
RX PubMed=15728191; DOI=10.1083/jcb.200406083;
RA Pratt S.J., Epple H., Ward M., Feng Y., Braga V.M., Longmore G.D.;
RT "The LIM protein Ajuba influences p130Cas localization and Rac1 activity
RT during cell migration.";
RL J. Cell Biol. 168:813-824(2005).
RN [5]
RP INTERACTION WITH PIP5K1B.
RX PubMed=15870270; DOI=10.1128/mcb.25.10.3956-3966.2005;
RA Kisseleva M., Feng Y., Ward M., Song C., Anderson R.A., Longmore G.D.;
RT "The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate
RT levels in migrating cells through an interaction with and activation of
RT PIPKI alpha.";
RL Mol. Cell. Biol. 25:3956-3966(2005).
RN [6]
RP FUNCTION.
RX PubMed=17909014; DOI=10.1158/0008-5472.can-07-2987;
RA Ayyanathan K., Peng H., Hou Z., Fredericks W.J., Goyal R.K., Langer E.M.,
RA Longmore G.D., Rauscher F.J. III;
RT "The Ajuba LIM domain protein is a corepressor for SNAG domain mediated
RT repression and participates in nucleocytoplasmic Shuttling.";
RL Cancer Res. 67:9097-9106(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH SNAI1; SNAI2/SLUG AND SCRT1.
RX PubMed=18331720; DOI=10.1016/j.devcel.2008.01.005;
RA Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L.,
RA Longmore G.D.;
RT "Ajuba LIM proteins are snail/slug corepressors required for neural crest
RT development in Xenopus.";
RL Dev. Cell 14:424-436(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Adapter or scaffold protein which participates in the
CC assembly of numerous protein complexes and is involved in several
CC cellular processes such as cell fate determination, cytoskeletal
CC organization, repression of gene transcription, mitosis, cell-cell
CC adhesion, cell differentiation, proliferation and migration.
CC Contributes to the linking and/or strengthening of epithelia cell-cell
CC junctions in part by linking adhesive receptors to the actin
CC cytoskeleton. May be involved in signal transduction from cell adhesion
CC sites to the nucleus. Plays an important role in regulation of the
CC kinase activity of AURKA for mitotic commitment. Also a component of
CC the IL-1 signaling pathway modulating IL-1-induced NFKB1 activation by
CC influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6
CC multiprotein signaling complex. Functions as an HDAC-dependent
CC corepressor for a subset of GFI1 target genes. Acts as a
CC transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent
CC repression of E-cadherin transcription. Acts as a hypoxic regulator by
CC bridging an association between the prolyl hydroxylases and VHL
CC enabling efficient degradation of HIF1A. Positively regulates microRNA
CC (miRNA)-mediated gene silencing. Negatively regulates the Hippo
CC signaling pathway and antagonizes phosphorylation of YAP1.
CC {ECO:0000269|PubMed:10330178, ECO:0000269|PubMed:11029037,
CC ECO:0000269|PubMed:15728191, ECO:0000269|PubMed:17909014,
CC ECO:0000269|PubMed:18331720}.
CC -!- SUBUNIT: Interacts with SLC1A2. Interacts with AURKA; the interaction
CC occurs during mitosis and both proteins are phosphorylated as they form
CC a complex. Interacts with CTNNA1 and with F-actin. Interacts with
CC LATS2; the interaction occurs during mitosis and the complex regulates
CC organization of the spindle apparatus through recruitment of TUBG to
CC the centrosome. Forms a complex with SQSTM1, PRKCZ and TRAF6. Component
CC of the GFI1-AJUBA-HDAC1 repressor complex. Interacts directly (via the
CC LIM domains) with GFI1; the interaction results in the HDAC-dependent
CC corepression of a subset of GFI1 target genes, and is independent of
CC the GFI1 SNAG domain. Interacts with HDAC1, HDAC2 and HDAC3 (By
CC similarity). Interacts with GRB2 and PIP5K1B. Interacts with HDAC1,
CC HDAC2 and HDAC3. Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1,
CC LATS2, SAV1, EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM domains)
CC with VHL (By similarity). Interacts (via LIM domains) with SNAI1 (via
CC SNAG domain), SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain).
CC {ECO:0000250, ECO:0000269|PubMed:10330178, ECO:0000269|PubMed:15870270,
CC ECO:0000269|PubMed:18331720}.
CC -!- INTERACTION:
CC Q91XC0; P18911: Rarg; NbExp=2; IntAct=EBI-1565930, EBI-8053650;
CC Q91XC0; Q99684: GFI1; Xeno; NbExp=4; IntAct=EBI-1565930, EBI-949368;
CC Q91XC0; O14744: PRMT5; Xeno; NbExp=4; IntAct=EBI-1565930, EBI-351098;
CC Q91XC0; P10276: RARA; Xeno; NbExp=7; IntAct=EBI-1565930, EBI-413374;
CC Q91XC0; P48443: RXRG; Xeno; NbExp=2; IntAct=EBI-1565930, EBI-712405;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane
CC {ECO:0000250}. Cell junction {ECO:0000250}. Nucleus. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Cytoplasm, P-body {ECO:0000250}. Note=Shuttles between the cytoplasm
CC and the nucleus. Localizes on centrosomes during G2-M phase (By
CC similarity). Preferentially colocalizes with cadherin-adhesive
CC complexes at sites of cell-cell contacts (By similarity). Colocalizes
CC with GFI1 in the nucleus (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in skin, brain and genitourinary organs.
CC {ECO:0000269|PubMed:10330178}.
CC -!- DEVELOPMENTAL STAGE: Detected in all embryonic germ layers, in the
CC extraembryonic yolk sac blood islands and in the fetal components of
CC the developing placenta. As development progressed, expression is
CC dramatically restricted. {ECO:0000269|PubMed:10330178}.
CC -!- DOMAIN: LIM region interacts with CTNNA1. The preLIM region binds
CC directly actin filaments (By similarity). {ECO:0000250}.
CC -!- DOMAIN: LIM-2 and LIM-3 domains mediate the interaction with the N-
CC terminal region of AURKA. The association between LATS2 and AJUBA
CC required the second LIM domain of AJUBA (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by LATS2 during mitosis. Phosphorylated by AURKA
CC (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: 'Ajuba' means 'curiosity' in Urdu, an Indian dialect.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; U79776; AAB38287.1; -; mRNA.
DR EMBL; BC011035; AAH11035.1; -; mRNA.
DR CCDS; CCDS27093.1; -.
DR RefSeq; NP_034720.2; NM_010590.5.
DR AlphaFoldDB; Q91XC0; -.
DR BioGRID; 200870; 17.
DR DIP; DIP-38451N; -.
DR IntAct; Q91XC0; 8.
DR STRING; 10090.ENSMUSP00000056977; -.
DR iPTMnet; Q91XC0; -.
DR PhosphoSitePlus; Q91XC0; -.
DR MaxQB; Q91XC0; -.
DR PaxDb; Q91XC0; -.
DR PeptideAtlas; Q91XC0; -.
DR PRIDE; Q91XC0; -.
DR ProteomicsDB; 285789; -.
DR Antibodypedia; 8154; 94 antibodies from 28 providers.
DR DNASU; 16475; -.
DR Ensembl; ENSMUST00000054487; ENSMUSP00000056977; ENSMUSG00000022178.
DR GeneID; 16475; -.
DR KEGG; mmu:16475; -.
DR UCSC; uc007twj.2; mouse.
DR CTD; 84962; -.
DR MGI; MGI:1341886; Ajuba.
DR VEuPathDB; HostDB:ENSMUSG00000022178; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000160978; -.
DR HOGENOM; CLU_001357_11_2_1; -.
DR InParanoid; Q91XC0; -.
DR OMA; HQGTANY; -.
DR OrthoDB; 326249at2759; -.
DR PhylomeDB; Q91XC0; -.
DR TreeFam; TF320310; -.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR BioGRID-ORCS; 16475; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Ajuba; mouse.
DR PRO; PR:Q91XC0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91XC0; protein.
DR Bgee; ENSMUSG00000022178; Expressed in molar tooth and 185 other tissues.
DR Genevisible; Q91XC0; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0045294; F:alpha-catenin binding; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048041; P:focal adhesion assembly; IMP:MGI.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:MGI.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; ISO:MGI.
DR GO; GO:0035331; P:negative regulation of hippo signaling; ISS:UniProtKB.
DR GO; GO:0033673; P:negative regulation of kinase activity; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0031328; P:positive regulation of cellular biosynthetic process; IMP:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IDA:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:MGI.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR GO; GO:1900037; P:regulation of cellular response to hypoxia; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IMP:MGI.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell cycle; Cell junction; Cell membrane; Cytoplasm;
KW Cytoskeleton; LIM domain; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-mediated gene silencing;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..547
FT /note="LIM domain-containing protein ajuba"
FT /id="PRO_0000312626"
FT DOMAIN 345..406
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 410..470
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 471..539
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..344
FT /note="PreLIM"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 289..297
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 20..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
FT CONFLICT 534
FT /note="M -> I (in Ref. 1; AAB38287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 57920 MW; C326772AC1C155B2 CRC64;
MERLGEKASR LLEKLRLSDS GSAKFGRRKG EASRSGSDGT PGAGKGRLSG LGGPRKSGHR
GANGGPGDEP LEPAREQGPL DAERNARGSF EAQRFEGSFP GGPPPTRALP LPLSSPPDFR
LETTAPALSP RSSFASSSAS DASKPSSPRG SLLLDGAGAS GAGGSRPCSN RTSGISMGYD
QRHGSPLPAG PCLFGLPLTT APAGYPGGAP SAYPELHAAL DRLCAHRSVG FGCQESRHSY
PPALGSPGAL TGAVVGTAGP LERRGAQPGR HSVTGYGDCA AGARYQDELT ALLRLTVATG
GREAGARGEP SGIEPSGLEE SPGPFVPEAS RSRIREPEAR EDYFGTCIKC NKGIYGQSNA
CQALDSLYHT QCFVCCSCGR TLRCKAFYSV NGSVYCEEDY LFSGFQEAAE KCCVCGHLIL
EKILQAMGKS YHPGCFRCIV CNKCLDGVPF TVDFSNQVYC VTDYHKNYAP KCAACGQPIL
PSEGCEDIVR VISMDRDYHF ECYHCEDCRM QLSDEEGCCC FPLDGHLLCH GCHMQRLSAR
QPSTNYI
