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Q96IF1

- AJUBA_HUMAN

UniProt

Q96IF1 - AJUBA_HUMAN

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Protein

LIM domain-containing protein ajuba

Gene
AJUBA, JUB
Organism
Homo sapiens (Human)
Status
Reviewed - 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 YAP1.9 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
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

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.6 Publications

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
Complete GO annotation...

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.

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).10 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.

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi280 – 2889Nuclear localization signal Reviewed prediction

Domaini

LIM region interacts with CTNNA1. The preLIM region binds directly actin filaments.1 Publication
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.1 Publication

Sequence similaritiesi

Belongs to the zyxin/ajuba family.

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. VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 115 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

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