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Q96IF1

- AJUBA_HUMAN

UniProt

Q96IF1 - AJUBA_HUMAN

Protein

LIM domain-containing protein ajuba

Gene

AJUBA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 YAP1.9 Publications

    GO - Molecular functioni

    1. alpha-catenin binding Source: MGI
    2. chromatin binding Source: Ensembl
    3. protein binding Source: UniProtKB
    4. transcription corepressor activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. calcium-dependent cell-cell adhesion Source: Ensembl
    2. cellular protein localization Source: Ensembl
    3. focal adhesion assembly Source: Ensembl
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. gene silencing by miRNA Source: MGI
    6. glycerophospholipid biosynthetic process Source: Ensembl
    7. lamellipodium assembly Source: Ensembl
    8. mitotic cell cycle Source: Reactome
    9. negative regulation of hippo signaling Source: UniProtKB
    10. negative regulation of kinase activity Source: Ensembl
    11. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    12. positive regulation of cellular biosynthetic process Source: Ensembl
    13. positive regulation of gene silencing by miRNA Source: UniProtKB
    14. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    15. positive regulation of MAP kinase activity Source: Ensembl
    16. positive regulation of protein complex assembly Source: MGI
    17. regulation of cell migration Source: Ensembl
    18. regulation of cellular response to hypoxia Source: UniProtKB
    19. regulation of GTPase activity Source: Ensembl
    20. response to hypoxia Source: UniProtKB
    21. transcription, DNA-templated Source: UniProtKB-KW
    22. wound healing, spreading of epidermal cells Source: Ensembl

    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

    ReactomeiREACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LIM domain-containing protein ajuba
    Gene namesi
    Name:AJUBA
    Synonyms:JUB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:20250. AJUBA.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell membrane. Cell junction. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. CytoplasmP-body
    Note: Shuttles between the cytoplasm and the nucleus. Localizes on centrosomes during G2-M phase. Preferentially co- localizes with cadherin-adhesive complexes at sites of cell-cell contacts. Colocalizes with GFI1 in the nucleus.

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cytoplasmic mRNA processing body Source: MGI
    3. cytosol Source: Reactome
    4. focal adhesion Source: Ensembl
    5. lamellipodium Source: Ensembl
    6. microtubule organizing center Source: UniProtKB-SubCell
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: UniProtKB-SubCell
    9. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134978308.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 538538LIM domain-containing protein ajubaPRO_0000312625Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791Phosphoserine1 Publication
    Modified residuei119 – 1191Phosphoserine4 Publications
    Modified residuei175 – 1751Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by LATS2 during mitosis. Phosphorylated by AURKA.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96IF1.
    PaxDbiQ96IF1.
    PRIDEiQ96IF1.

    PTM databases

    PhosphoSiteiQ96IF1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96IF1.
    BgeeiQ96IF1.
    CleanExiHS_JUB.
    GenevestigatoriQ96IF1.

    Organism-specific databases

    HPAiHPA006171.

    Interactioni

    Subunit structurei

    Interacts with GRB2, PIP5K1B and SLC1A2 By similarity. 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. Interacts with SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain) By similarity. Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, SAV1, EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM domains) with isoform 1 and isoform 3 of VHL. Interacts (via LIM domains) with SNAI1 (via SNAG domain).By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LATS2Q9NRM76EBI-949782,EBI-3506895
    SFNP319472EBI-949782,EBI-476295

    Protein-protein interaction databases

    BioGridi124393. 20 interactions.
    IntActiQ96IF1. 3 interactions.
    MINTiMINT-1772035.
    STRINGi9606.ENSP00000262713.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96IF1.
    SMRiQ96IF1. Positions 338-520.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini336 – 39762LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini401 – 46161LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini462 – 53069LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 335335PreLIMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi280 – 2889Nuclear localization signalSequence Analysis

    Domaini

    LIM region interacts with CTNNA1. The preLIM region binds directly actin filaments.
    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.

    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

    eggNOGiNOG331290.
    HOGENOMiHOG000113139.
    HOVERGENiHBG095660.
    InParanoidiQ96IF1.
    KOiK16682.
    OMAiRQPPTNY.
    OrthoDBiEOG793B7F.
    PhylomeDBiQ96IF1.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96IF1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MERLGEKASR LLEKFGRRKG ESSRSGSDGT PGPGKGRLSG LGGPRKSGPR    50
    GATGGPGDEP LEPAREQGSL DAERNQRGSF EAPRYEGSFP AGPPPTRALP 100
    LPQSLPPDFR LEPTAPALSP RSSFASSSAS DASKPSSPRG SLLLDGAGAG 150
    GAGGSRPCSN RTSGISMGYD QRHGSPLPAG PCLFGPPLAG APAGYSPGGV 200
    PSAYPELHAA LDRLYAQRPA GFGCQESRHS YPPALGSPGA LAGAGVGAAG 250
    PLERRGAQPG RHSVTGYGDC AVGARYQDEL TALLRLTVGT GGREAGARGE 300
    PSGIEPSGLE EPPGPFVPEA ARARMREPEA REDYFGTCIK CNKGIYGQSN 350
    ACQALDSLYH TQCFVCCSCG RTLRCKAFYS VNGSVYCEED YLFSGFQEAA 400
    EKCCVCGHLI LEKILQAMGK SYHPGCFRCI VCNKCLDGIP FTVDFSNQVY 450
    CVTDYHKNYA PKCAACGQPI LPSEGCEDIV RVISMDRDYH FECYHCEDCR 500
    MQLSDEEGCC CFPLDGHLLC HGCHMQRLNA RQPPANYI 538
    Length:538
    Mass (Da):56,934
    Last modified:December 1, 2001 - v1
    Checksum:i1E0DFA0336976A3C
    GO
    Isoform 2 (identifier: Q96IF1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-417: Missing.

    Show »
    Length:121
    Mass (Da):13,795
    Checksum:i8799BD8A070CCCE5
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 417417Missing in isoform 2. 1 PublicationVSP_044227Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY169959 mRNA. Translation: AAO37641.1.
    AK096128 mRNA. Translation: BAG53217.1.
    AL132780 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW66204.1.
    CH471078 Genomic DNA. Translation: EAW66205.1.
    BC007580 mRNA. Translation: AAH07580.1.
    BC034968 mRNA. Translation: AAH34968.1.
    CCDSiCCDS9581.1. [Q96IF1-1]
    CCDS9582.1. [Q96IF1-2]
    RefSeqiNP_001276026.1. NM_001289097.1.
    NP_116265.1. NM_032876.5. [Q96IF1-1]
    NP_932352.1. NM_198086.2. [Q96IF1-2]
    UniGeneiHs.655832.

    Genome annotation databases

    EnsembliENST00000262713; ENSP00000262713; ENSG00000129474. [Q96IF1-1]
    ENST00000361265; ENSP00000354491; ENSG00000129474. [Q96IF1-1]
    ENST00000397388; ENSP00000380543; ENSG00000129474. [Q96IF1-2]
    GeneIDi84962.
    KEGGihsa:84962.
    UCSCiuc001why.3. human. [Q96IF1-2]
    uc001whz.3. human. [Q96IF1-1]

    Polymorphism databases

    DMDMi74751933.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY169959 mRNA. Translation: AAO37641.1 .
    AK096128 mRNA. Translation: BAG53217.1 .
    AL132780 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW66204.1 .
    CH471078 Genomic DNA. Translation: EAW66205.1 .
    BC007580 mRNA. Translation: AAH07580.1 .
    BC034968 mRNA. Translation: AAH34968.1 .
    CCDSi CCDS9581.1. [Q96IF1-1 ]
    CCDS9582.1. [Q96IF1-2 ]
    RefSeqi NP_001276026.1. NM_001289097.1.
    NP_116265.1. NM_032876.5. [Q96IF1-1 ]
    NP_932352.1. NM_198086.2. [Q96IF1-2 ]
    UniGenei Hs.655832.

    3D structure databases

    ProteinModelPortali Q96IF1.
    SMRi Q96IF1. Positions 338-520.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124393. 20 interactions.
    IntActi Q96IF1. 3 interactions.
    MINTi MINT-1772035.
    STRINGi 9606.ENSP00000262713.

    PTM databases

    PhosphoSitei Q96IF1.

    Polymorphism databases

    DMDMi 74751933.

    Proteomic databases

    MaxQBi Q96IF1.
    PaxDbi Q96IF1.
    PRIDEi Q96IF1.

    Protocols and materials databases

    DNASUi 84962.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262713 ; ENSP00000262713 ; ENSG00000129474 . [Q96IF1-1 ]
    ENST00000361265 ; ENSP00000354491 ; ENSG00000129474 . [Q96IF1-1 ]
    ENST00000397388 ; ENSP00000380543 ; ENSG00000129474 . [Q96IF1-2 ]
    GeneIDi 84962.
    KEGGi hsa:84962.
    UCSCi uc001why.3. human. [Q96IF1-2 ]
    uc001whz.3. human. [Q96IF1-1 ]

    Organism-specific databases

    CTDi 84962.
    GeneCardsi GC14M023441.
    HGNCi HGNC:20250. AJUBA.
    HPAi HPA006171.
    MIMi 609066. gene.
    neXtProti NX_Q96IF1.
    PharmGKBi PA134978308.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG331290.
    HOGENOMi HOG000113139.
    HOVERGENi HBG095660.
    InParanoidi Q96IF1.
    KOi K16682.
    OMAi RQPPTNY.
    OrthoDBi EOG793B7F.
    PhylomeDBi Q96IF1.
    TreeFami TF320310.

    Enzyme and pathway databases

    Reactomei REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    ChiTaRSi AJUBA. human.
    GeneWikii JUB_(gene).
    GenomeRNAii 84962.
    NextBioi 75479.
    PROi Q96IF1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96IF1.
    Bgeei Q96IF1.
    CleanExi HS_JUB.
    Genevestigatori Q96IF1.

    Family and domain databases

    Gene3Di 2.10.110.10. 3 hits.
    InterProi IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 3 hits.
    [Graphical view ]
    SMARTi SM00132. LIM. 3 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells."
      Hirota T., Kunitoku N., Sasayama T., Marumoto T., Zhang D., Nitta M., Hatakeyama K., Saya H.
      Cell 114:585-598(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AURKA.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Liver.
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Placenta and Testis.
    6. "The LIM protein Ajuba is recruited to cadherin-dependent cell junctions through an association with alpha-catenin."
      Marie H., Pratt S.J., Betson M., Epple H., Kittler J.T., Meek L., Moss S.J., Troyanovsky S., Attwell D., Longmore G.D., Braga V.M.
      J. Biol. Chem. 278:1220-1228(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNA1 AND F-ACTIN.
    7. "The LIM protein Ajuba influences interleukin-1-induced NF-kappaB activation by affecting the assembly and activity of the protein kinase Czeta/p62/TRAF6 signaling complex."
      Feng Y., Longmore G.D.
      Mol. Cell. Biol. 25:4010-4022(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TRAF6; PRKCZ AND SQSTM1.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and spindle organization during mitosis."
      Abe Y., Ohsugi M., Haraguchi K., Fujimoto J., Yamamoto T.
      FEBS Lett. 580:782-788(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH LATS2.
    10. "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: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH SNAG-DOMAIN.
    11. "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: INTERACTION WITH SNAI1.
    12. "Ajuba functions as a histone deacetylase-dependent co-repressor for autoregulation of the growth factor-independent-1 transcription factor."
      Montoya-Durango D.E., Velu C.S., Kazanjian A., Rojas M.E., Jay C.M., Longmore G.D., Grimes H.L.
      J. Biol. Chem. 283:32056-32065(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE GFI1-AJUBA-HDAC1 COMPLEX, INTERACTION WITH GFI1; HDAC1; HDAC2 AND HDAC3, SUBCELLULAR LOCATION, FUNCTION.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Ajuba LIM proteins are negative regulators of the Hippo signaling pathway."
      Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B., Longmore G.D.
      Curr. Biol. 20:657-662(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LATS1; LATS2 AND SAV1.
    16. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4E; AGO1; AGO2; DCP2 AND DDX6.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: FUNCTION, INTERACTION WITH EGLN1/PHD2; EGLN3/PHD3 AND VHL.

    Entry informationi

    Entry nameiAJUBA_HUMAN
    AccessioniPrimary (citable) accession number: Q96IF1
    Secondary accession number(s): A8MX18, D3DS37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 4, 2007
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3