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Protein

LIM domain-containing protein ajuba

Gene

AJUBA

Organism
Homo sapiens (Human)
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 YAP1.9 Publications

GO - Molecular functioni

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

GO - Biological processi

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 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20250. AJUBA.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: MGI
  • cytoplasmic mRNA processing body Source: MGI
  • cytosol Source: Reactome
  • focal adhesion Source: Ensembl
  • lamellipodium Source: Ensembl
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • 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.

Polymorphism and mutation databases

BioMutaiAJUBA.
DMDMi74751933.

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
Modified residuei263 – 2631Phosphoserine1 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

BgeeiQ96IF1.
CleanExiHS_JUB.
ExpressionAtlasiQ96IF1. baseline and differential.
GenevisibleiQ96IF1. HS.

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 338-504.
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.
GeneTreeiENSGT00760000119039.
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. AlignAdd to basket

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

        10         20         30         40         50
MERLGEKASR LLEKFGRRKG ESSRSGSDGT PGPGKGRLSG LGGPRKSGPR
60 70 80 90 100
GATGGPGDEP LEPAREQGSL DAERNQRGSF EAPRYEGSFP AGPPPTRALP
110 120 130 140 150
LPQSLPPDFR LEPTAPALSP RSSFASSSAS DASKPSSPRG SLLLDGAGAG
160 170 180 190 200
GAGGSRPCSN RTSGISMGYD QRHGSPLPAG PCLFGPPLAG APAGYSPGGV
210 220 230 240 250
PSAYPELHAA LDRLYAQRPA GFGCQESRHS YPPALGSPGA LAGAGVGAAG
260 270 280 290 300
PLERRGAQPG RHSVTGYGDC AVGARYQDEL TALLRLTVGT GGREAGARGE
310 320 330 340 350
PSGIEPSGLE EPPGPFVPEA ARARMREPEA REDYFGTCIK CNKGIYGQSN
360 370 380 390 400
ACQALDSLYH TQCFVCCSCG RTLRCKAFYS VNGSVYCEED YLFSGFQEAA
410 420 430 440 450
EKCCVCGHLI LEKILQAMGK SYHPGCFRCI VCNKCLDGIP FTVDFSNQVY
460 470 480 490 500
CVTDYHKNYA PKCAACGQPI LPSEGCEDIV RVISMDRDYH FECYHCEDCR
510 520 530
MQLSDEEGCC CFPLDGHLLC HGCHMQRLNA RQPPANYI
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000361265; ENSP00000354491; ENSG00000129474.
ENST00000397388; ENSP00000380543; ENSG00000129474. [Q96IF1-2]
GeneIDi84962.
KEGGihsa:84962.
UCSCiuc001why.3. human. [Q96IF1-2]
uc001whz.3. human. [Q96IF1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ96IF1.
SMRiQ96IF1. Positions 338-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ96IF1.

Polymorphism and mutation databases

BioMutaiAJUBA.
DMDMi74751933.

Proteomic databases

MaxQBiQ96IF1.
PaxDbiQ96IF1.
PRIDEiQ96IF1.

Protocols and materials databases

DNASUi84962.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi84962.
GeneCardsiGC14M023441.
HGNCiHGNC:20250. AJUBA.
HPAiHPA006171.
MIMi609066. gene.
neXtProtiNX_Q96IF1.
PharmGKBiPA134978308.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG331290.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000113139.
HOVERGENiHBG095660.
InParanoidiQ96IF1.
KOiK16682.
OMAiRQPPTNY.
OrthoDBiEOG793B7F.
PhylomeDBiQ96IF1.
TreeFamiTF320310.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikiiJUB_(gene).
GenomeRNAii84962.
NextBioi75479.
PROiQ96IF1.
SOURCEiSearch...

Gene expression databases

BgeeiQ96IF1.
CleanExiHS_JUB.
ExpressionAtlasiQ96IF1. baseline and differential.
GenevisibleiQ96IF1. HS.

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. "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.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: July 22, 2015
This is version 125 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

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 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.