AJUBA_HUMAN
ID AJUBA_HUMAN Reviewed; 538 AA.
AC Q96IF1; A8MX18; D3DS37;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=LIM domain-containing protein ajuba;
GN Name=AJUBA; Synonyms=JUB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH AURKA.
RX PubMed=13678582; DOI=10.1016/s0092-8674(03)00642-1;
RA Hirota T., Kunitoku N., Sasayama T., Marumoto T., Zhang D., Nitta M.,
RA Hatakeyama K., Saya H.;
RT "Aurora-A and an interacting activator, the LIM protein Ajuba, are required
RT for mitotic commitment in human cells.";
RL Cell 114:585-598(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNA1 AND F-ACTIN.
RX PubMed=12417594; DOI=10.1074/jbc.m205391200;
RA Marie H., Pratt S.J., Betson M., Epple H., Kittler J.T., Meek L.,
RA Moss S.J., Troyanovsky S., Attwell D., Longmore G.D., Braga V.M.;
RT "The LIM protein Ajuba is recruited to cadherin-dependent cell junctions
RT through an association with alpha-catenin.";
RL J. Biol. Chem. 278:1220-1228(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH TRAF6; PRKCZ AND SQSTM1.
RX PubMed=15870274; DOI=10.1128/mcb.25.10.4010-4022.2005;
RA Feng Y., Longmore G.D.;
RT "The LIM protein Ajuba influences interleukin-1-induced NF-kappaB
RT activation by affecting the assembly and activity of the protein kinase
RT Czeta/p62/TRAF6 signaling complex.";
RL Mol. Cell. Biol. 25:4010-4022(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH LATS2.
RX PubMed=16413547; DOI=10.1016/j.febslet.2005.12.096;
RA Abe Y., Ohsugi M., Haraguchi K., Fujimoto J., Yamamoto T.;
RT "LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and
RT spindle organization during mitosis.";
RL FEBS Lett. 580:782-788(2006).
RN [10]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH SNAG-DOMAIN.
RX PubMed=17909014; DOI=10.1158/0008-5472.can-07-2987;
RA Ayyanathan K., Peng H., Hou Z., Fredericks W.J., Goyal R.K., Langer E.M.,
RA Longmore G.D., Rauscher F.J. III;
RT "The Ajuba LIM domain protein is a corepressor for SNAG domain mediated
RT repression and participates in nucleocytoplasmic Shuttling.";
RL Cancer Res. 67:9097-9106(2007).
RN [11]
RP INTERACTION WITH SNAI1.
RX PubMed=18331720; DOI=10.1016/j.devcel.2008.01.005;
RA Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L.,
RA Longmore G.D.;
RT "Ajuba LIM proteins are snail/slug corepressors required for neural crest
RT development in Xenopus.";
RL Dev. Cell 14:424-436(2008).
RN [12]
RP IDENTIFICATION IN THE GFI1-AJUBA-HDAC1 COMPLEX, INTERACTION WITH GFI1;
RP HDAC1; HDAC2 AND HDAC3, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18805794; DOI=10.1074/jbc.m802320200;
RA Montoya-Durango D.E., Velu C.S., Kazanjian A., Rojas M.E., Jay C.M.,
RA Longmore G.D., Grimes H.L.;
RT "Ajuba functions as a histone deacetylase-dependent co-repressor for
RT autoregulation of the growth factor-independent-1 transcription factor.";
RL J. Biol. Chem. 283:32056-32065(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP FUNCTION, AND INTERACTION WITH LATS1; LATS2 AND SAV1.
RX PubMed=20303269; DOI=10.1016/j.cub.2010.02.035;
RA Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B.,
RA Longmore G.D.;
RT "Ajuba LIM proteins are negative regulators of the Hippo signaling
RT pathway.";
RL Curr. Biol. 20:657-662(2010).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4E; AGO1; AGO2;
RP DCP2 AND DDX6.
RX PubMed=20616046; DOI=10.1073/pnas.0914987107;
RA James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M.,
RA Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J.,
RA Longmore G.D., Bushell M., Sharp T.V.;
RT "LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-
RT mediated gene silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-175, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP FUNCTION, AND INTERACTION WITH EGLN1/PHD2; EGLN3/PHD3 AND VHL.
RX PubMed=22286099; DOI=10.1038/ncb2424;
RA Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C., Feng Y.,
RA Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J., Ingvarsson S.,
RA Ratcliffe P.J., Longmore G.D., Sharp T.V.;
RT "The LIMD1 protein bridges an association between the prolyl hydroxylases
RT and VHL to repress HIF-1 activity.";
RL Nat. Cell Biol. 14:201-208(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-119 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Adapter or scaffold protein which participates in the
CC assembly of numerous protein complexes and is involved in several
CC cellular processes such as cell fate determination, cytoskeletal
CC organization, repression of gene transcription, mitosis, cell-cell
CC adhesion, cell differentiation, proliferation and migration.
CC Contributes to the linking and/or strengthening of epithelia cell-cell
CC junctions in part by linking adhesive receptors to the actin
CC cytoskeleton. May be involved in signal transduction from cell adhesion
CC sites to the nucleus. Plays an important role in regulation of the
CC kinase activity of AURKA for mitotic commitment. Also a component of
CC the IL-1 signaling pathway modulating IL-1-induced NFKB1 activation by
CC influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6
CC multiprotein signaling complex. Functions as an HDAC-dependent
CC corepressor for a subset of GFI1 target genes. Acts as a
CC transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent
CC repression of E-cadherin transcription. Acts as a hypoxic regulator by
CC bridging an association between the prolyl hydroxylases and VHL
CC enabling efficient degradation of HIF1A. Positively regulates microRNA
CC (miRNA)-mediated gene silencing. Negatively regulates the Hippo
CC signaling pathway and antagonizes phosphorylation of YAP1.
CC {ECO:0000269|PubMed:12417594, ECO:0000269|PubMed:13678582,
CC ECO:0000269|PubMed:15870274, ECO:0000269|PubMed:16413547,
CC ECO:0000269|PubMed:17909014, ECO:0000269|PubMed:18805794,
CC ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046,
CC ECO:0000269|PubMed:22286099}.
CC -!- SUBUNIT: Interacts with GRB2, PIP5K1B and SLC1A2 (By similarity).
CC Interacts with AURKA; the interaction occurs during mitosis and both
CC proteins are phosphorylated as they form a complex. Interacts with
CC CTNNA1 and with F-actin. Interacts with LATS2; the interaction occurs
CC during mitosis and the complex regulates organization of the spindle
CC apparatus through recruitment of TUBG to the centrosome. Forms a
CC complex with SQSTM1, PRKCZ and TRAF6. Component of the GFI1-AJUBA-HDAC1
CC repressor complex. Interacts directly (via the LIM domains) with GFI1;
CC the interaction results in the HDAC-dependent corepression of a subset
CC of GFI1 target genes, and is independent of the GFI1 SNAG domain.
CC Interacts with HDAC1, HDAC2 and HDAC3. Interacts with SNAI2/SLUG (via
CC SNAG domain) and SCRT1 (via SNAG domain) (By similarity). Interacts
CC with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, SAV1, EGLN2/PHD1 and
CC EGLN3/PHD3. Interacts (via LIM domains) with isoform 1 and isoform 3 of
CC VHL. Interacts (via LIM domains) with SNAI1 (via SNAG domain).
CC {ECO:0000250, ECO:0000269|PubMed:12417594, ECO:0000269|PubMed:13678582,
CC ECO:0000269|PubMed:15870274, ECO:0000269|PubMed:16413547,
CC ECO:0000269|PubMed:17909014, ECO:0000269|PubMed:18331720,
CC ECO:0000269|PubMed:18805794, ECO:0000269|PubMed:20303269,
CC ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:22286099}.
CC -!- INTERACTION:
CC Q96IF1; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-949782, EBI-744545;
CC Q96IF1; Q02930-3: CREB5; NbExp=3; IntAct=EBI-949782, EBI-10192698;
CC Q96IF1; O95363: FARS2; NbExp=3; IntAct=EBI-949782, EBI-2513774;
CC Q96IF1; Q9NRM7: LATS2; NbExp=6; IntAct=EBI-949782, EBI-3506895;
CC Q96IF1; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-949782, EBI-10274069;
CC Q96IF1; Q13526: PIN1; NbExp=3; IntAct=EBI-949782, EBI-714158;
CC Q96IF1; P31947: SFN; NbExp=2; IntAct=EBI-949782, EBI-476295;
CC Q96IF1; O95863: SNAI1; NbExp=3; IntAct=EBI-949782, EBI-1045459;
CC Q96IF1; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-949782, EBI-8644516;
CC Q96IF1; Q01664: TFAP4; NbExp=3; IntAct=EBI-949782, EBI-2514218;
CC Q96IF1; Q99816: TSG101; NbExp=4; IntAct=EBI-949782, EBI-346882;
CC Q96IF1; Q96KM6: ZNF512B; NbExp=3; IntAct=EBI-949782, EBI-1049952;
CC Q96IF1; Q9H0D2: ZNF541; NbExp=3; IntAct=EBI-949782, EBI-3957075;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane. Cell
CC junction. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome. Cytoplasm, P-body. Note=Shuttles between the
CC cytoplasm and the nucleus. Localizes on centrosomes during G2-M phase.
CC Preferentially co- localizes with cadherin-adhesive complexes at sites
CC of cell-cell contacts. Colocalizes with GFI1 in the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96IF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96IF1-2; Sequence=VSP_044227;
CC -!- DOMAIN: LIM region interacts with CTNNA1. The preLIM region binds
CC directly actin filaments.
CC -!- DOMAIN: LIM-2 and LIM-3 domains mediate the interaction with the N-
CC terminal region of AURKA. The association between LATS2 and AJUBA
CC required the second LIM domain of AJUBA.
CC -!- PTM: Phosphorylated by LATS2 during mitosis. Phosphorylated by AURKA.
CC -!- MISCELLANEOUS: 'Ajuba' means 'curiosity' in Urdu, an Indian dialect.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; AY169959; AAO37641.1; -; mRNA.
DR EMBL; AK096128; BAG53217.1; -; mRNA.
DR EMBL; AL132780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66204.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66205.1; -; Genomic_DNA.
DR EMBL; BC007580; AAH07580.1; -; mRNA.
DR EMBL; BC034968; AAH34968.1; -; mRNA.
DR CCDS; CCDS9581.1; -. [Q96IF1-1]
DR CCDS; CCDS9582.1; -. [Q96IF1-2]
DR RefSeq; NP_001276026.1; NM_001289097.1.
DR RefSeq; NP_116265.1; NM_032876.5. [Q96IF1-1]
DR RefSeq; NP_932352.1; NM_198086.2. [Q96IF1-2]
DR AlphaFoldDB; Q96IF1; -.
DR BioGRID; 124393; 82.
DR CORUM; Q96IF1; -.
DR IntAct; Q96IF1; 20.
DR MINT; Q96IF1; -.
DR STRING; 9606.ENSP00000262713; -.
DR iPTMnet; Q96IF1; -.
DR PhosphoSitePlus; Q96IF1; -.
DR BioMuta; AJUBA; -.
DR DMDM; 74751933; -.
DR EPD; Q96IF1; -.
DR jPOST; Q96IF1; -.
DR MassIVE; Q96IF1; -.
DR MaxQB; Q96IF1; -.
DR PaxDb; Q96IF1; -.
DR PeptideAtlas; Q96IF1; -.
DR PRIDE; Q96IF1; -.
DR ProteomicsDB; 2289; -.
DR ProteomicsDB; 76825; -. [Q96IF1-1]
DR Antibodypedia; 8154; 94 antibodies from 28 providers.
DR DNASU; 84962; -.
DR Ensembl; ENST00000262713.7; ENSP00000262713.2; ENSG00000129474.16. [Q96IF1-1]
DR Ensembl; ENST00000361265.8; ENSP00000354491.4; ENSG00000129474.16. [Q96IF1-1]
DR Ensembl; ENST00000397388.7; ENSP00000380543.3; ENSG00000129474.16. [Q96IF1-2]
DR GeneID; 84962; -.
DR KEGG; hsa:84962; -.
DR MANE-Select; ENST00000262713.7; ENSP00000262713.2; NM_032876.6; NP_116265.1.
DR UCSC; uc001why.5; human. [Q96IF1-1]
DR CTD; 84962; -.
DR DisGeNET; 84962; -.
DR GeneCards; AJUBA; -.
DR HGNC; HGNC:20250; AJUBA.
DR HPA; ENSG00000129474; Tissue enhanced (skin).
DR MIM; 609066; gene.
DR neXtProt; NX_Q96IF1; -.
DR OpenTargets; ENSG00000129474; -.
DR PharmGKB; PA134978308; -.
DR VEuPathDB; HostDB:ENSG00000129474; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000160978; -.
DR HOGENOM; CLU_001357_11_2_1; -.
DR InParanoid; Q96IF1; -.
DR OMA; HQGTANY; -.
DR OrthoDB; 326249at2759; -.
DR PhylomeDB; Q96IF1; -.
DR TreeFam; TF320310; -.
DR PathwayCommons; Q96IF1; -.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR SignaLink; Q96IF1; -.
DR BioGRID-ORCS; 84962; 15 hits in 1082 CRISPR screens.
DR ChiTaRS; AJUBA; human.
DR GeneWiki; JUB_(gene); -.
DR GenomeRNAi; 84962; -.
DR Pharos; Q96IF1; Tbio.
DR PRO; PR:Q96IF1; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96IF1; protein.
DR Bgee; ENSG00000129474; Expressed in germinal epithelium of ovary and 156 other tissues.
DR ExpressionAtlas; Q96IF1; baseline and differential.
DR Genevisible; Q96IF1; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0045294; F:alpha-catenin binding; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048041; P:focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IMP:MGI.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IDA:UniProtKB.
DR GO; GO:0033673; P:negative regulation of kinase activity; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0031328; P:positive regulation of cellular biosynthetic process; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IMP:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:MGI.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:1900037; P:regulation of cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEA:Ensembl.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell cycle; Cell junction;
KW Cell membrane; Cytoplasm; Cytoskeleton; LIM domain; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..538
FT /note="LIM domain-containing protein ajuba"
FT /id="PRO_0000312625"
FT DOMAIN 336..397
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 401..461
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 462..530
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..335
FT /note="PreLIM"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 280..288
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..417
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044227"
SQ SEQUENCE 538 AA; 56934 MW; 1E0DFA0336976A3C CRC64;
MERLGEKASR LLEKFGRRKG ESSRSGSDGT PGPGKGRLSG LGGPRKSGPR GATGGPGDEP
LEPAREQGSL DAERNQRGSF EAPRYEGSFP AGPPPTRALP LPQSLPPDFR LEPTAPALSP
RSSFASSSAS DASKPSSPRG SLLLDGAGAG GAGGSRPCSN RTSGISMGYD QRHGSPLPAG
PCLFGPPLAG APAGYSPGGV PSAYPELHAA LDRLYAQRPA GFGCQESRHS YPPALGSPGA
LAGAGVGAAG PLERRGAQPG RHSVTGYGDC AVGARYQDEL TALLRLTVGT GGREAGARGE
PSGIEPSGLE EPPGPFVPEA ARARMREPEA REDYFGTCIK CNKGIYGQSN ACQALDSLYH
TQCFVCCSCG RTLRCKAFYS VNGSVYCEED YLFSGFQEAA EKCCVCGHLI LEKILQAMGK
SYHPGCFRCI VCNKCLDGIP FTVDFSNQVY CVTDYHKNYA PKCAACGQPI LPSEGCEDIV
RVISMDRDYH FECYHCEDCR MQLSDEEGCC CFPLDGHLLC HGCHMQRLNA RQPPANYI
