Q96IF1 (AJUBA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
LIM domain-containing protein ajuba

Gene names

Name:	AJUBA
Synonyms:	JUB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	538 AA.
Sequence status	Complete.
Protein existence	Evidence 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, EIF2C1, EIF2C2, 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). Ref.1 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.19
Subcellular location	Cytoplasm › cytoskeleton. Cell membrane. Cell junction. Nucleus. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › P-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 process	Cell adhesion Cell cycle RNA-mediated gene silencing Transcription Transcription regulation
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	calcium-dependent cell-cell adhesion Inferred from electronic annotation. Source: Compara cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cellular protein localization Inferred from electronic annotation. Source: Compara focal adhesion assembly Inferred from electronic annotation. Source: Compara gene silencing by miRNA Inferred from mutant phenotype Ref.16. Source: MGI glycerophospholipid biosynthetic process Inferred from electronic annotation. Source: Compara lamellipodium assembly Inferred from electronic annotation. Source: Compara negative regulation of hippo signaling cascade Inferred from direct assay Ref.15. Source: UniProtKB negative regulation of kinase activity Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from electronic annotation. Source: Compara positive regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara positive regulation of cellular biosynthetic process Inferred from electronic annotation. Source: Compara 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: Compara regulation of cell migration Inferred from electronic annotation. Source: Compara 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW wound healing, spreading of epidermal cells Inferred from electronic annotation. Source: Compara
Cellular_component	cell-cell junction Inferred from direct assay Ref.6. Source: MGI cytoplasmic mRNA processing body Inferred from direct assay Ref.16. Source: MGI cytosol Inferred from electronic annotation. Source: Compara focal adhesion Inferred from electronic annotation. Source: Compara lamellipodium Inferred from electronic annotation. Source: Compara 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: Compara
Molecular_function	alpha-catenin binding Inferred from direct assay Ref.6. Source: MGI chromatin binding Inferred from electronic annotation. Source: Compara transcription corepressor activity Inferred from direct assay Ref.12. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 538	538	LIM domain-containing protein ajuba		PRO_0000312625
Regions
	Domain	336 – 397	62	LIM zinc-binding 1
	Domain	401 – 461	61	LIM zinc-binding 2
	Domain	462 – 530	69	LIM zinc-binding 3
	Region	1 – 335	335	PreLIM
	Motif	280 – 288	9	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	79	1	Phosphoserine Ref.18
	Modified residue	119	1	Phosphoserine Ref.13 Ref.14 Ref.17 Ref.18
	Modified residue	175	1	Phosphoserine Ref.17
Natural variations
	Alternative sequence	1 – 417	417	Missing in isoform 2.		VSP_044227

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 1E0DFA0336976A3C	FASTA	538	56,934
	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
	Isoform 2 [UniParc]. Checksum: 8799BD8A070CCCE5	FASTA	121	13,795
	10 20 30 40 50 60 MGKSYHPGCF RCIVCNKCLD GIPFTVDFSN QVYCVTDYHK NYAPKCAACG QPILPSEGCE 70 80 90 100 110 120 DIVRVISMDR DYHFECYHCE DCRMQLSDEE GCCCFPLDGH LLCHGCHMQR LNARQPPANY I

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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 WITH 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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; EIF2C1; EIF2C2; 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.
IPI	IPI00063605.
RefSeq	NP_116265.1. NM_032876.4. NP_932352.1. NM_198086.1.
UniGene	Hs.655832.
3D structure databases
HSSP	HSSP built from PDB template 1QLI based on UniProtKB Q05158.
ProteinModelPortal	Q96IF1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96IF1. 1 interaction.
MINT	MINT-1772035.
STRING	9606.ENSP00000262713.
PTM databases
PhosphoSite	Q96IF1.
Polymorphism databases
DMDM	74751933.
Proteomic databases
PaxDb	Q96IF1.
PRIDE	Q96IF1.
Protocols and materials databases
DNASU	84962.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262713; ENSP00000262713; ENSG00000129474. ENST00000361265; ENSP00000354491; ENSG00000129474. ENST00000397388; ENSP00000380543; ENSG00000129474.
GeneID	84962.
KEGG	hsa:84962.
UCSC	uc001whz.3. human.
Organism-specific databases
CTD	84962.
GeneCards	GC14M023441.
HGNC	HGNC:20250. AJUBA.
HPA	HPA006171.
MIM	609066. gene.
neXtProt	NX_Q96IF1.
PharmGKB	PA134978308.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG331290.
HOGENOM	HOG000113139.
HOVERGEN	HBG095660.
InParanoid	Q96IF1.
KO	K16682.
OMA	YEGSFPG.
OrthoDB	EOG4GMTX9.
PhylomeDB	Q96IF1.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_a_pathway. Aurora A signaling.
Gene expression databases
ArrayExpress	Q96IF1.
Bgee	Q96IF1.
CleanEx	HS_JUB.
Genevestigator	Q96IF1.
Family and domain databases
Gene3D	2.10.110.10. 3 hits.
InterPro	IPR001781. Znf_LIM. [Graphical view]
Pfam	PF00412. LIM. 3 hits. [Graphical view]
SMART	SM00132. LIM. 3 hits. [Graphical view]
PROSITE	PS00478. LIM_DOMAIN_1. 2 hits. PS50023. LIM_DOMAIN_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	AJUBA. human.
GenomeRNAi	84962.
NextBio	75479.
SOURCE	Search...

Entry information

Entry name

AJUBA_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.