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Q96IF1 (AJUBA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LIM domain-containing protein ajuba
Gene names
Name:AJUBA
Synonyms:JUB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.15 Ref.16 Ref.19

Subunit structure

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 3of VHL. Interacts (via LIM domains) with SNAI1 (via SNAG domain). Ref.1 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.19

Subcellular location

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. Ref.1 Ref.6 Ref.9 Ref.10 Ref.12 Ref.16

Domain

LIM region interacts with CTNNA1. The preLIM region binds directly actin filaments. Ref.10

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. Ref.10

Post-translational modification

Phosphorylated by LATS2 during mitosis. Phosphorylated by AURKA.

Miscellaneous

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

Sequence similarities

Belongs to the zyxin/ajuba family.

Contains 3 LIM zinc-binding domains.

Ontologies

Keywords
   Biological processCell adhesion
Cell cycle
RNA-mediated gene silencing
Transcription
Transcription regulation
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

calcium-dependent cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

cellular protein localization

Inferred from electronic annotation. Source: Ensembl

focal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

gene silencing by miRNA

Inferred from mutant phenotype Ref.16. Source: MGI

glycerophospholipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of hippo signaling

Inferred from direct assay Ref.15. Source: UniProtKB

negative regulation of kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cellular biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene silencing by miRNA

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of protein complex assembly

Inferred from direct assay Ref.7. Source: MGI

regulation of GTPase activity

Inferred from electronic annotation. Source: Ensembl

regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of cellular response to hypoxia

Inferred from direct assay Ref.19. Source: UniProtKB

response to hypoxia

Inferred from direct assay Ref.19. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

wound healing, spreading of epidermal cells

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell-cell junction

Inferred from direct assay Ref.6. Source: MGI

cytoplasmic mRNA processing body

Inferred from direct assay Ref.16. Source: MGI

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: Ensembl

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionalpha-catenin binding

Inferred from direct assay Ref.6. Source: MGI

chromatin binding

Inferred from electronic annotation. Source: Ensembl

transcription corepressor activity

Inferred from direct assay Ref.12. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96IF1-1)

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.
Isoform 2 (identifier: Q96IF1-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 538538LIM domain-containing protein ajuba
PRO_0000312625

Regions

Domain336 – 39762LIM zinc-binding 1
Domain401 – 46161LIM zinc-binding 2
Domain462 – 53069LIM zinc-binding 3
Region1 – 335335PreLIM
Motif280 – 2889Nuclear localization signal Potential

Amino acid modifications

Modified residue791Phosphoserine Ref.18
Modified residue1191Phosphoserine Ref.13 Ref.14 Ref.17 Ref.18
Modified residue1751Phosphoserine Ref.17

Natural variations

Alternative sequence1 – 417417Missing in isoform 2.
VSP_044227

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1E0DFA0336976A3C

FASTA53856,934
        10         20         30         40         50         60 
MERLGEKASR LLEKFGRRKG ESSRSGSDGT PGPGKGRLSG LGGPRKSGPR GATGGPGDEP 

        70         80         90        100        110        120 
LEPAREQGSL DAERNQRGSF EAPRYEGSFP AGPPPTRALP LPQSLPPDFR LEPTAPALSP 

       130        140        150        160        170        180 
RSSFASSSAS DASKPSSPRG SLLLDGAGAG GAGGSRPCSN RTSGISMGYD QRHGSPLPAG 

       190        200        210        220        230        240 
PCLFGPPLAG APAGYSPGGV PSAYPELHAA LDRLYAQRPA GFGCQESRHS YPPALGSPGA 

       250        260        270        280        290        300 
LAGAGVGAAG PLERRGAQPG RHSVTGYGDC AVGARYQDEL TALLRLTVGT GGREAGARGE 

       310        320        330        340        350        360 
PSGIEPSGLE EPPGPFVPEA ARARMREPEA REDYFGTCIK CNKGIYGQSN ACQALDSLYH 

       370        380        390        400        410        420 
TQCFVCCSCG RTLRCKAFYS VNGSVYCEED YLFSGFQEAA EKCCVCGHLI LEKILQAMGK 

       430        440        450        460        470        480 
SYHPGCFRCI VCNKCLDGIP FTVDFSNQVY CVTDYHKNYA PKCAACGQPI LPSEGCEDIV 

       490        500        510        520        530 
RVISMDRDYH FECYHCEDCR MQLSDEEGCC CFPLDGHLLC HGCHMQRLNA RQPPANYI 

« Hide

Isoform 2 [UniParc].

Checksum: 8799BD8A070CCCE5
Show »

FASTA12113,795

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing."
James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M., Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J., Longmore G.D., Bushell M., Sharp T.V.
Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010) [PubMed] [Europe PMC] [Abstract]
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]"The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity."
Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C., Feng Y., Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J., Ingvarsson S., Ratcliffe P.J., Longmore G.D., Sharp T.V.
Nat. Cell Biol. 14:201-208(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EGLN1/PHD2; EGLN3/PHD3 AND VHL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_116265.1. NM_032876.5.
NP_932352.1. NM_198086.2.
UniGeneHs.655832.

3D structure databases

ProteinModelPortalQ96IF1.
SMRQ96IF1. Positions 336-528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124393. 20 interactions.
IntActQ96IF1. 3 interactions.
MINTMINT-1772035.
STRING9606.ENSP00000262713.

PTM databases

PhosphoSiteQ96IF1.

Polymorphism databases

DMDM74751933.

Proteomic databases

PaxDbQ96IF1.
PRIDEQ96IF1.

Protocols and materials databases

DNASU84962.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262713; ENSP00000262713; ENSG00000129474. [Q96IF1-1]
ENST00000361265; ENSP00000354491; ENSG00000129474. [Q96IF1-1]
ENST00000397388; ENSP00000380543; ENSG00000129474. [Q96IF1-2]
GeneID84962.
KEGGhsa:84962.
UCSCuc001why.3. human. [Q96IF1-2]
uc001whz.3. human. [Q96IF1-1]

Organism-specific databases

CTD84962.
GeneCardsGC14M023441.
HGNCHGNC:20250. AJUBA.
HPAHPA006171.
MIM609066. gene.
neXtProtNX_Q96IF1.
PharmGKBPA134978308.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331290.
HOGENOMHOG000113139.
HOVERGENHBG095660.
InParanoidQ96IF1.
KOK16682.
OMARQPPTNY.
OrthoDBEOG793B7F.
PhylomeDBQ96IF1.
TreeFamTF320310.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ96IF1.
BgeeQ96IF1.
CleanExHS_JUB.
GenevestigatorQ96IF1.

Family and domain databases

Gene3D2.10.110.10. 3 hits.
InterProIPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 3 hits.
[Graphical view]
SMARTSM00132. LIM. 3 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAJUBA. human.
GeneWikiJUB_(gene).
GenomeRNAi84962.
NextBio75479.
PROQ96IF1.
SOURCESearch...

Entry information

Entry nameAJUBA_HUMAN
AccessionPrimary (citable) accession number: Q96IF1
Secondary accession number(s): A8MX18, D3DS37
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM