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Protein

LIM domain-containing protein ajuba

Gene

Ajuba

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, mitosis, cell-cell adhesion, cell differentiation, proliferation and migration. Contributes to the linking and/or strengthening of epithelia cell-cell junctions in part by linking adhesive receptors to the actin cytoskeleton. May be involved in signal transduction from cell adhesion sites to the nucleus. Plays an important role in regulation of the kinase activity of AURKA for mitotic commitment. Also a component of the IL-1 signaling pathway modulating IL-1-induced NFKB1 activation by influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6 multiprotein signaling complex. Functions as an HDAC-dependent corepressor for a subset of GFI1 target genes. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1.5 Publications

GO - Molecular functioni

  • actin filament binding Source: MGI
  • alpha-catenin binding Source: MGI
  • chromatin binding Source: MGI
  • transcription corepressor activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  • cell cycle Source: UniProtKB-KW
  • cellular protein localization Source: MGI
  • focal adhesion assembly Source: MGI
  • gene silencing by miRNA Source: MGI
  • glycerophospholipid biosynthetic process Source: MGI
  • lamellipodium assembly Source: MGI
  • negative regulation of hippo signaling Source: UniProtKB
  • negative regulation of kinase activity Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of cellular biosynthetic process Source: MGI
  • positive regulation of gene silencing by miRNA Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of kinase activity Source: MGI
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of protein complex assembly Source: MGI
  • regulation of cell migration Source: MGI
  • regulation of cellular response to hypoxia Source: MGI
  • regulation of GTPase activity Source: MGI
  • response to hypoxia Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
  • wound healing, spreading of epidermal cells Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Cell adhesion, Cell cycle, RNA-mediated gene silencing, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
LIM domain-containing protein ajuba
Gene namesi
Name:Ajuba
Synonyms:Jub
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1341886. Ajuba.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: MGI
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: MGI
  • focal adhesion Source: MGI
  • lamellipodium Source: MGI
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547LIM domain-containing protein ajubaPRO_0000312626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891PhosphoserineBy similarity
Modified residuei129 – 1291PhosphoserineBy similarity
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei185 – 1851PhosphoserineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by LATS2 during mitosis. Phosphorylated by AURKA (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ91XC0.
PaxDbiQ91XC0.
PeptideAtlasiQ91XC0.
PRIDEiQ91XC0.

PTM databases

iPTMnetiQ91XC0.
PhosphoSiteiQ91XC0.

Expressioni

Tissue specificityi

Expressed in skin, brain and genitourinary organs.1 Publication

Developmental stagei

Detected in all embryonic germ layers, in the extraembryonic yolk sac blood islands and in the fetal components of the developing placenta. As development progressed, expression is dramatically restricted.1 Publication

Gene expression databases

BgeeiQ91XC0.
CleanExiMM_JUB.
GenevisibleiQ91XC0. MM.

Interactioni

Subunit structurei

Interacts with SLC1A2. Interacts with AURKA; the interaction occurs during mitosis and both proteins are phosphorylated as they form a complex. Interacts with CTNNA1 and with F-actin. Interacts with LATS2; the interaction occurs during mitosis and the complex regulates organization of the spindle apparatus through recruitment of TUBG to the centrosome. Forms a complex with SQSTM1, PRKCZ and TRAF6. Component of the GFI1-AJUBA-HDAC1 repressor complex. Interacts directly (via the LIM domains) with GFI1; the interaction results in the HDAC-dependent corepression of a subset of GFI1 target genes, and is independent of the GFI1 SNAG domain. Interacts with HDAC1, HDAC2 and HDAC3 (By similarity). Interacts with GRB2 and PIP5K1B. Interacts with HDAC1, HDAC2 and HDAC3. Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, SAV1, EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM domains) with VHL (By similarity). Interacts (via LIM domains) with SNAI1 (via SNAG domain), SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GFI1Q996844EBI-1565930,EBI-949368From a different organism.

GO - Molecular functioni

  • actin filament binding Source: MGI
  • alpha-catenin binding Source: MGI

Protein-protein interaction databases

BioGridi200870. 1 interaction.
DIPiDIP-38451N.
IntActiQ91XC0. 1 interaction.
STRINGi10090.ENSMUSP00000056977.

Structurei

3D structure databases

ProteinModelPortaliQ91XC0.
SMRiQ91XC0. Positions 347-513.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini345 – 40662LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini410 – 47061LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini471 – 53969LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 344344PreLIMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi289 – 2979Nuclear localization signalSequence analysis

Domaini

LIM region interacts with CTNNA1. The preLIM region binds directly actin filaments (By similarity).By similarity
LIM-2 and LIM-3 domains mediate the interaction with the N-terminal region of AURKA. The association between LATS2 and AJUBA required the second LIM domain of AJUBA (By similarity).By similarity

Sequence similaritiesi

Belongs to the zyxin/ajuba family.Curated
Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiKOG1701. Eukaryota.
ENOG410Y3GP. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000113139.
HOVERGENiHBG095660.
InParanoidiQ91XC0.
KOiK16682.
OMAiRQPPTNY.
OrthoDBiEOG793B7F.
PhylomeDBiQ91XC0.
TreeFamiTF320310.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 3 hits.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91XC0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERLGEKASR LLEKLRLSDS GSAKFGRRKG EASRSGSDGT PGAGKGRLSG
60 70 80 90 100
LGGPRKSGHR GANGGPGDEP LEPAREQGPL DAERNARGSF EAQRFEGSFP
110 120 130 140 150
GGPPPTRALP LPLSSPPDFR LETTAPALSP RSSFASSSAS DASKPSSPRG
160 170 180 190 200
SLLLDGAGAS GAGGSRPCSN RTSGISMGYD QRHGSPLPAG PCLFGLPLTT
210 220 230 240 250
APAGYPGGAP SAYPELHAAL DRLCAHRSVG FGCQESRHSY PPALGSPGAL
260 270 280 290 300
TGAVVGTAGP LERRGAQPGR HSVTGYGDCA AGARYQDELT ALLRLTVATG
310 320 330 340 350
GREAGARGEP SGIEPSGLEE SPGPFVPEAS RSRIREPEAR EDYFGTCIKC
360 370 380 390 400
NKGIYGQSNA CQALDSLYHT QCFVCCSCGR TLRCKAFYSV NGSVYCEEDY
410 420 430 440 450
LFSGFQEAAE KCCVCGHLIL EKILQAMGKS YHPGCFRCIV CNKCLDGVPF
460 470 480 490 500
TVDFSNQVYC VTDYHKNYAP KCAACGQPIL PSEGCEDIVR VISMDRDYHF
510 520 530 540
ECYHCEDCRM QLSDEEGCCC FPLDGHLLCH GCHMQRLSAR QPSTNYI
Length:547
Mass (Da):57,920
Last modified:December 1, 2001 - v1
Checksum:iC326772AC1C155B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti534 – 5341M → I in AAB38287 (PubMed:10330178).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79776 mRNA. Translation: AAB38287.1.
BC011035 mRNA. Translation: AAH11035.1.
CCDSiCCDS27093.1.
RefSeqiNP_034720.2. NM_010590.5.
UniGeneiMm.100253.

Genome annotation databases

EnsembliENSMUST00000054487; ENSMUSP00000056977; ENSMUSG00000022178.
GeneIDi16475.
KEGGimmu:16475.
UCSCiuc007twj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79776 mRNA. Translation: AAB38287.1.
BC011035 mRNA. Translation: AAH11035.1.
CCDSiCCDS27093.1.
RefSeqiNP_034720.2. NM_010590.5.
UniGeneiMm.100253.

3D structure databases

ProteinModelPortaliQ91XC0.
SMRiQ91XC0. Positions 347-513.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200870. 1 interaction.
DIPiDIP-38451N.
IntActiQ91XC0. 1 interaction.
STRINGi10090.ENSMUSP00000056977.

PTM databases

iPTMnetiQ91XC0.
PhosphoSiteiQ91XC0.

Proteomic databases

MaxQBiQ91XC0.
PaxDbiQ91XC0.
PeptideAtlasiQ91XC0.
PRIDEiQ91XC0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054487; ENSMUSP00000056977; ENSMUSG00000022178.
GeneIDi16475.
KEGGimmu:16475.
UCSCiuc007twj.2. mouse.

Organism-specific databases

CTDi84962.
MGIiMGI:1341886. Ajuba.

Phylogenomic databases

eggNOGiKOG1701. Eukaryota.
ENOG410Y3GP. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000113139.
HOVERGENiHBG095660.
InParanoidiQ91XC0.
KOiK16682.
OMAiRQPPTNY.
OrthoDBiEOG793B7F.
PhylomeDBiQ91XC0.
TreeFamiTF320310.

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Miscellaneous databases

PROiQ91XC0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91XC0.
CleanExiMM_JUB.
GenevisibleiQ91XC0. MM.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 3 hits.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ajuba, a novel LIM protein, interacts with Grb2, augments mitogen-activated protein kinase activity in fibroblasts, and promotes meiotic maturation of Xenopus oocytes in a Grb2- and Ras-dependent manner."
    Goyal R.K., Lin P., Kanungo J., Payne A.S., Muslin A.J., Longmore G.D.
    Mol. Cell. Biol. 19:4379-4389(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH GRB2.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Salivary gland.
  3. "Ajuba, a cytosolic LIM protein, shuttles into the nucleus and affects embryonal cell proliferation and fate decisions."
    Kanungo J., Pratt S.J., Marie H., Longmore G.D.
    Mol. Biol. Cell 11:3299-3313(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. "The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration."
    Pratt S.J., Epple H., Ward M., Feng Y., Braga V.M., Longmore G.D.
    J. Cell Biol. 168:813-824(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate levels in migrating cells through an interaction with and activation of PIPKI alpha."
    Kisseleva M., Feng Y., Ward M., Song C., Anderson R.A., Longmore G.D.
    Mol. Cell. Biol. 25:3956-3966(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIP5K1B.
  6. "The Ajuba LIM domain protein is a corepressor for SNAG domain mediated repression and participates in nucleocytoplasmic Shuttling."
    Ayyanathan K., Peng H., Hou Z., Fredericks W.J., Goyal R.K., Langer E.M., Longmore G.D., Rauscher F.J. III
    Cancer Res. 67:9097-9106(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Ajuba LIM proteins are snail/slug corepressors required for neural crest development in Xenopus."
    Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L., Longmore G.D.
    Dev. Cell 14:424-436(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNAI1; SNAI2/SLUG AND SCRT1.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Testis.

Entry informationi

Entry nameiAJUBA_MOUSE
AccessioniPrimary (citable) accession number: Q91XC0
Secondary accession number(s): P97472
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

'Ajuba' means 'curiosity' in Urdu, an Indian dialect.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.