AIDA_HUMAN
ID AIDA_HUMAN Reviewed; 306 AA.
AC Q96BJ3; A8K1F0; Q49A81; Q5JRA4; Q658P1; Q9H9E8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Axin interactor, dorsalization-associated protein;
DE AltName: Full=Axin interaction partner and dorsalization antagonist;
GN Name=AIDA; Synonyms=C1orf80;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Caudate nucleus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pancreas, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-306 (ISOFORM 1).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17681137; DOI=10.1016/j.devcel.2007.07.006;
RA Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W.,
RA Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.;
RT "A beta-catenin-independent dorsalization pathway activated by Axin/JNK
RT signaling and antagonized by aida.";
RL Dev. Cell 13:268-282(2007).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acts as a ventralizing factor during embryogenesis. Inhibits
CC axin-mediated JNK activation by binding axin and disrupting axin
CC homodimerization. This in turn antagonizes a Wnt/beta-catenin-
CC independent dorsalization pathway activated by AXIN/JNK-signaling (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AXIN1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96BJ3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-4401674, EBI-742054;
CC Q96BJ3; Q9UJV9: DDX41; NbExp=3; IntAct=EBI-4401674, EBI-1046350;
CC Q96BJ3; Q7Z589-5: EMSY; NbExp=3; IntAct=EBI-4401674, EBI-11989522;
CC Q96BJ3; Q9NWS6: FAM118A; NbExp=6; IntAct=EBI-4401674, EBI-8638992;
CC Q96BJ3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-4401674, EBI-739832;
CC Q96BJ3; Q96BK5: PINX1; NbExp=4; IntAct=EBI-4401674, EBI-721782;
CC Q96BJ3; P83881: RPL36A; NbExp=3; IntAct=EBI-4401674, EBI-1054835;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96BJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96BJ3-2; Sequence=VSP_028322;
CC Name=3;
CC IsoId=Q96BJ3-3; Sequence=VSP_034661;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues, with highest
CC expression in the heart and skeletal muscle.
CC {ECO:0000269|PubMed:17681137}.
CC -!- SIMILARITY: Belongs to the AIDA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01259, ECO:0000305}.
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DR EMBL; AK022868; BAB14281.1; -; mRNA.
DR EMBL; AK289865; BAF82554.1; -; mRNA.
DR EMBL; AL392172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015535; AAH15535.1; -; mRNA.
DR EMBL; BC043142; AAH43142.1; -; mRNA.
DR EMBL; BC067805; AAH67805.1; -; mRNA.
DR EMBL; AL833718; CAH56257.1; -; mRNA.
DR CCDS; CCDS1533.1; -. [Q96BJ3-1]
DR RefSeq; NP_073742.2; NM_022831.2. [Q96BJ3-1]
DR AlphaFoldDB; Q96BJ3; -.
DR BMRB; Q96BJ3; -.
DR SMR; Q96BJ3; -.
DR BioGRID; 122326; 25.
DR IntAct; Q96BJ3; 20.
DR MINT; Q96BJ3; -.
DR STRING; 9606.ENSP00000339161; -.
DR iPTMnet; Q96BJ3; -.
DR PhosphoSitePlus; Q96BJ3; -.
DR SwissPalm; Q96BJ3; -.
DR BioMuta; AIDA; -.
DR DMDM; 74751770; -.
DR EPD; Q96BJ3; -.
DR jPOST; Q96BJ3; -.
DR MassIVE; Q96BJ3; -.
DR MaxQB; Q96BJ3; -.
DR PaxDb; Q96BJ3; -.
DR PeptideAtlas; Q96BJ3; -.
DR PRIDE; Q96BJ3; -.
DR ProteomicsDB; 76080; -. [Q96BJ3-1]
DR ProteomicsDB; 76081; -. [Q96BJ3-2]
DR ProteomicsDB; 76082; -. [Q96BJ3-3]
DR Antibodypedia; 34630; 136 antibodies from 23 providers.
DR DNASU; 64853; -.
DR Ensembl; ENST00000340020.11; ENSP00000339161.6; ENSG00000186063.13. [Q96BJ3-1]
DR Ensembl; ENST00000355727.3; ENSP00000347964.2; ENSG00000186063.13. [Q96BJ3-3]
DR GeneID; 64853; -.
DR KEGG; hsa:64853; -.
DR MANE-Select; ENST00000340020.11; ENSP00000339161.6; NM_022831.4; NP_073742.2.
DR UCSC; uc001hnn.4; human. [Q96BJ3-1]
DR CTD; 64853; -.
DR DisGeNET; 64853; -.
DR GeneCards; AIDA; -.
DR HGNC; HGNC:25761; AIDA.
DR HPA; ENSG00000186063; Low tissue specificity.
DR MIM; 612375; gene.
DR neXtProt; NX_Q96BJ3; -.
DR OpenTargets; ENSG00000186063; -.
DR PharmGKB; PA162376104; -.
DR VEuPathDB; HostDB:ENSG00000186063; -.
DR eggNOG; ENOG502QSD5; Eukaryota.
DR GeneTree; ENSGT00390000016465; -.
DR HOGENOM; CLU_064322_0_0_1; -.
DR InParanoid; Q96BJ3; -.
DR OMA; KLHAAWC; -.
DR OrthoDB; 1196787at2759; -.
DR PhylomeDB; Q96BJ3; -.
DR TreeFam; TF328541; -.
DR PathwayCommons; Q96BJ3; -.
DR SignaLink; Q96BJ3; -.
DR BioGRID-ORCS; 64853; 38 hits in 1038 CRISPR screens.
DR ChiTaRS; AIDA; human.
DR GenomeRNAi; 64853; -.
DR Pharos; Q96BJ3; Tbio.
DR PRO; PR:Q96BJ3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96BJ3; protein.
DR Bgee; ENSG00000186063; Expressed in parietal pleura and 191 other tissues.
DR Genevisible; Q96BJ3; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0048264; P:determination of ventral identity; IBA:GO_Central.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; ISS:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISS:UniProtKB.
DR Gene3D; 1.20.120.360; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR025939; Aida_C.
DR InterPro; IPR023421; AIDA_N.
DR InterPro; IPR036818; AIDA_N_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR Pfam; PF14186; Aida_C2; 1.
DR Pfam; PF08910; Aida_N; 1.
DR SUPFAM; SSF109779; SSF109779; 1.
DR PROSITE; PS51911; C2_AIDA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Developmental protein; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..306
FT /note="Axin interactor, dorsalization-associated protein"
FT /id="PRO_0000305277"
FT DOMAIN 157..304
FT /note="C2 Aida-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01259"
FT REGION 128..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..221
FT /note="Axin-binding"
FT /evidence="ECO:0000250"
FT COILED 27..62
FT /evidence="ECO:0000255"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..165
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028322"
FT VAR_SEQ 155..236
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034661"
FT CONFLICT 130
FT /note="E -> G (in Ref. 1; BAB14281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 35023 MW; 48E563CEEC398ECC CRC64;
MSEVTRSLLQ RWGASFRRGA DFDSWGQLVE AIDEYQILAR HLQKEAQAQH NNSEFTEEQK
KTIGKIATCL ELRSAALQST QSQEEFKLED LKKLEPILKN ILTYNKEFPF DVQPVPLRRI
LAPGEEENLE FEEDEEEGGA GAGSPDSFPA RVPGTLLPRL PSEPGMTLLT IRIEKIGLKD
AGQCIDPYIT VSVKDLNGID LTPVQDTPVA SRKEDTYVHF NVDIELQKHV EKLTKGAAIF
FEFKHYKPKK RFTSTKCFAF MEMDEIKPGP IVIELYKKPT DFKRKKLQLL TKKPLYLHLH
QTLHKE
