AJUBA_BOVIN
ID AJUBA_BOVIN Reviewed; 548 AA.
AC E1BKA3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=LIM domain-containing protein ajuba;
GN Name=AJUBA; Synonyms=JUB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GRB2 and PIP5K1B. Interacts with AURKA; the
CC interaction occurs during mitosis and both proteins are phosphorylated
CC as they form a complex. Interacts with CTNNA1 and with F-actin.
CC Interacts with LATS2; the interaction occurs during mitosis and the
CC complex regulates organization of the spindle apparatus through
CC recruitment of TUBG to the centrosome. Forms a complex with SQSTM1,
CC PRKCZ and TRAF6. Component of the GFI1-AJUBA-HDAC1 repressor complex.
CC Interacts directly (via the LIM domains) with GFI1; the interaction
CC results in the HDAC-dependent corepression of a subset of GFI1 target
CC genes, and is independent of the GFI1 SNAG domain. Interacts with
CC HDAC1, HDAC2 and HDAC3 (By similarity). Interacts with SLC1A2.
CC Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, SAV1,
CC EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM domains) with VHL (By
CC similarity). Interacts (via LIM domains) with SNAI1 (via SNAG domain),
CC SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC membrane {ECO:0000250}. Cell junction {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}.
CC Note=Shuttles between the cytoplasm and the nucleus. Localizes on
CC centrosomes during G2-M phase. Colocalizes with GFI1 in the nucleus.
CC Preferentially colocalizes with cadherin-adhesive complexes at sites of
CC cell-cell contacts. {ECO:0000250}.
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.
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DR EMBL; DAAA02028044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02028045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001179446.1; NM_001192517.1.
DR AlphaFoldDB; E1BKA3; -.
DR STRING; 9913.ENSBTAP00000016915; -.
DR PaxDb; E1BKA3; -.
DR PRIDE; E1BKA3; -.
DR Ensembl; ENSBTAT00000016915; ENSBTAP00000016915; ENSBTAG00000012724.
DR GeneID; 519937; -.
DR KEGG; bta:519937; -.
DR CTD; 84962; -.
DR VEuPathDB; HostDB:ENSBTAG00000012724; -.
DR VGNC; VGNC:25769; AJUBA.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000160978; -.
DR HOGENOM; CLU_001357_11_2_1; -.
DR InParanoid; E1BKA3; -.
DR OMA; HQGTANY; -.
DR OrthoDB; 326249at2759; -.
DR TreeFam; TF320310; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000012724; Expressed in surface of tongue and 105 other tissues.
DR ExpressionAtlas; E1BKA3; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0035331; P:negative regulation of hippo signaling; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; LIM domain;
KW Membrane; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..548
FT /note="LIM domain-containing protein ajuba"
FT /id="PRO_0000416966"
FT DOMAIN 346..407
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 411..470
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 471..540
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 98..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
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 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IF1"
SQ SEQUENCE 548 AA; 57765 MW; 7B29799B3B02CA21 CRC64;
MERLGEKASR LLEKLRLSDS GSAKFGRRKG ESSRSGSDGT PGPGKGRLSG LGGPRKSGPR
GAAGGPGDEP LEPAREQGPL DAERNPRGSF EVPRYEGSFP GGPPPSRALP LPQSLPPDFR
LETTAPALSP RSSFASSSAS DASKPSSPRG SLLLDGAGAG GAGGSRPCSN RTSGISMGYD
QRHGSPLPAG PCLFGPPLAG VPAGYSSGGV PSAYPELHAA LDRLCAHRPA GFGCQESRHS
YPPALGSPGA LAGAGVGATG PLERRGAQPG RHSVTGYGDC AAGARYQDEL TALLRLTVGT
GGREAGVRGE SAGIEASGLE EPPGAFVPEA ARARIREPES REDYFGTCIK CNKGIYGQSN
ACQALDSLYH TQCFVCCSCG RTLRCKAFYS VNGSVYCEED YLFSGFQEAA EKCCVCGHLI
LEKILQAMGK SYHPGCFRCI VCNKCLDGIP FTVDFSNQVY CVTDYHKSYA PKCAACGQPI
LPSEGCEDIV RVISMDRDYH FECYHCEDCR MQLSDEEGCC CFPLDGHLLC HGCHMQRLSA
RQPPANYI
