Full text data of AIDA
AIDA
(C1orf80)
[Confidence: low (only semi-automatic identification from reviews)]
Axin interactor, dorsalization-associated protein (Axin interaction partner and dorsalization antagonist)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Axin interactor, dorsalization-associated protein (Axin interaction partner and dorsalization antagonist)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96BJ3
ID AIDA_HUMAN Reviewed; 306 AA.
AC Q96BJ3; A8K1F0; Q49A81; Q5JRA4; Q658P1; Q9H9E8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 98.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RT Axin/JNK 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 MASS
RP SPECTROMETRY.
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.,
RA Buerckstuemmer T., 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.
CC Inhibits axin-mediated JNK activation by binding axin and
CC disrupting axin homodimerization. This in turn antagonizes a
CC Wnt/beta-catenin-independent dorsalization pathway activated by
CC AXIN/JNK-signaling (By similarity).
CC -!- SUBUNIT: Interacts with AXIN1 (By similarity).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q96BJ3-3; Sequence=VSP_034661;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues, with
CC highest expression in the heart and skeletal muscle.
CC -!- SIMILARITY: Belongs to the AIDA family.
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DR EMBL; AK022868; BAB14281.1; -; mRNA.
DR EMBL; AK289865; BAF82554.1; -; mRNA.
DR EMBL; AL392172; CAH73929.1; -; Genomic_DNA.
DR EMBL; AL592148; CAH73929.1; JOINED; Genomic_DNA.
DR EMBL; AL392172; CAH73930.1; -; Genomic_DNA.
DR EMBL; AL592148; CAH73930.1; JOINED; Genomic_DNA.
DR EMBL; AL592148; CAI40463.1; -; Genomic_DNA.
DR EMBL; AL392172; CAI40463.1; JOINED; Genomic_DNA.
DR EMBL; AL592148; CAI40464.1; -; Genomic_DNA.
DR EMBL; AL392172; CAI40464.1; JOINED; 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 RefSeq; NP_073742.2; NM_022831.2.
DR UniGene; Hs.156625; -.
DR UniGene; Hs.534965; -.
DR ProteinModelPortal; Q96BJ3; -.
DR SMR; Q96BJ3; 3-115, 152-305.
DR IntAct; Q96BJ3; 2.
DR MINT; MINT-8247588; -.
DR STRING; 9606.ENSP00000339161; -.
DR PhosphoSite; Q96BJ3; -.
DR DMDM; 74751770; -.
DR PaxDb; Q96BJ3; -.
DR PRIDE; Q96BJ3; -.
DR Ensembl; ENST00000340020; ENSP00000339161; ENSG00000186063.
DR Ensembl; ENST00000355727; ENSP00000347964; ENSG00000186063.
DR GeneID; 64853; -.
DR KEGG; hsa:64853; -.
DR UCSC; uc001hnn.3; human.
DR CTD; 64853; -.
DR GeneCards; GC01M222841; -.
DR H-InvDB; HIX0001616; -.
DR H-InvDB; HIX0028617; -.
DR HGNC; HGNC:25761; AIDA.
DR HPA; HPA027935; -.
DR MIM; 612375; gene.
DR neXtProt; NX_Q96BJ3; -.
DR PharmGKB; PA162376104; -.
DR eggNOG; NOG48105; -.
DR HOGENOM; HOG000006666; -.
DR HOVERGEN; HBG057354; -.
DR InParanoid; Q96BJ3; -.
DR OMA; ATCLEMR; -.
DR OrthoDB; EOG7XPZ6D; -.
DR PhylomeDB; Q96BJ3; -.
DR GenomeRNAi; 64853; -.
DR NextBio; 66981; -.
DR PRO; PR:Q96BJ3; -.
DR ArrayExpress; Q96BJ3; -.
DR Bgee; Q96BJ3; -.
DR CleanEx; HS_AIDA; -.
DR Genevestigator; Q96BJ3; -.
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:0043496; P:regulation of protein homodimerization activity; ISS:UniProtKB.
DR Gene3D; 1.20.120.360; -; 1.
DR InterPro; IPR025939; Aida_C.
DR InterPro; IPR023421; AIDA_N.
DR Pfam; PF14186; Aida_C2; 1.
DR Pfam; PF08910; Aida_N; 1.
DR SUPFAM; SSF109779; SSF109779; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Developmental protein; Phosphoprotein; Reference proteome.
FT CHAIN 1 306 Axin interactor, dorsalization-associated
FT protein.
FT /FTId=PRO_0000305277.
FT REGION 154 221 Axin-binding (By similarity).
FT COILED 27 62 Potential.
FT MOD_RES 144 144 Phosphoserine.
FT VAR_SEQ 1 165 Missing (in isoform 2).
FT /FTId=VSP_028322.
FT VAR_SEQ 155 236 Missing (in isoform 3).
FT /FTId=VSP_034661.
FT CONFLICT 130 130 E -> G (in Ref. 1; BAB14281).
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
//
ID AIDA_HUMAN Reviewed; 306 AA.
AC Q96BJ3; A8K1F0; Q49A81; Q5JRA4; Q658P1; Q9H9E8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 98.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RT Axin/JNK 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 MASS
RP SPECTROMETRY.
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.,
RA Buerckstuemmer T., 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.
CC Inhibits axin-mediated JNK activation by binding axin and
CC disrupting axin homodimerization. This in turn antagonizes a
CC Wnt/beta-catenin-independent dorsalization pathway activated by
CC AXIN/JNK-signaling (By similarity).
CC -!- SUBUNIT: Interacts with AXIN1 (By similarity).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q96BJ3-3; Sequence=VSP_034661;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues, with
CC highest expression in the heart and skeletal muscle.
CC -!- SIMILARITY: Belongs to the AIDA family.
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DR EMBL; AK022868; BAB14281.1; -; mRNA.
DR EMBL; AK289865; BAF82554.1; -; mRNA.
DR EMBL; AL392172; CAH73929.1; -; Genomic_DNA.
DR EMBL; AL592148; CAH73929.1; JOINED; Genomic_DNA.
DR EMBL; AL392172; CAH73930.1; -; Genomic_DNA.
DR EMBL; AL592148; CAH73930.1; JOINED; Genomic_DNA.
DR EMBL; AL592148; CAI40463.1; -; Genomic_DNA.
DR EMBL; AL392172; CAI40463.1; JOINED; Genomic_DNA.
DR EMBL; AL592148; CAI40464.1; -; Genomic_DNA.
DR EMBL; AL392172; CAI40464.1; JOINED; 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 RefSeq; NP_073742.2; NM_022831.2.
DR UniGene; Hs.156625; -.
DR UniGene; Hs.534965; -.
DR ProteinModelPortal; Q96BJ3; -.
DR SMR; Q96BJ3; 3-115, 152-305.
DR IntAct; Q96BJ3; 2.
DR MINT; MINT-8247588; -.
DR STRING; 9606.ENSP00000339161; -.
DR PhosphoSite; Q96BJ3; -.
DR DMDM; 74751770; -.
DR PaxDb; Q96BJ3; -.
DR PRIDE; Q96BJ3; -.
DR Ensembl; ENST00000340020; ENSP00000339161; ENSG00000186063.
DR Ensembl; ENST00000355727; ENSP00000347964; ENSG00000186063.
DR GeneID; 64853; -.
DR KEGG; hsa:64853; -.
DR UCSC; uc001hnn.3; human.
DR CTD; 64853; -.
DR GeneCards; GC01M222841; -.
DR H-InvDB; HIX0001616; -.
DR H-InvDB; HIX0028617; -.
DR HGNC; HGNC:25761; AIDA.
DR HPA; HPA027935; -.
DR MIM; 612375; gene.
DR neXtProt; NX_Q96BJ3; -.
DR PharmGKB; PA162376104; -.
DR eggNOG; NOG48105; -.
DR HOGENOM; HOG000006666; -.
DR HOVERGEN; HBG057354; -.
DR InParanoid; Q96BJ3; -.
DR OMA; ATCLEMR; -.
DR OrthoDB; EOG7XPZ6D; -.
DR PhylomeDB; Q96BJ3; -.
DR GenomeRNAi; 64853; -.
DR NextBio; 66981; -.
DR PRO; PR:Q96BJ3; -.
DR ArrayExpress; Q96BJ3; -.
DR Bgee; Q96BJ3; -.
DR CleanEx; HS_AIDA; -.
DR Genevestigator; Q96BJ3; -.
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:0043496; P:regulation of protein homodimerization activity; ISS:UniProtKB.
DR Gene3D; 1.20.120.360; -; 1.
DR InterPro; IPR025939; Aida_C.
DR InterPro; IPR023421; AIDA_N.
DR Pfam; PF14186; Aida_C2; 1.
DR Pfam; PF08910; Aida_N; 1.
DR SUPFAM; SSF109779; SSF109779; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Developmental protein; Phosphoprotein; Reference proteome.
FT CHAIN 1 306 Axin interactor, dorsalization-associated
FT protein.
FT /FTId=PRO_0000305277.
FT REGION 154 221 Axin-binding (By similarity).
FT COILED 27 62 Potential.
FT MOD_RES 144 144 Phosphoserine.
FT VAR_SEQ 1 165 Missing (in isoform 2).
FT /FTId=VSP_028322.
FT VAR_SEQ 155 236 Missing (in isoform 3).
FT /FTId=VSP_034661.
FT CONFLICT 130 130 E -> G (in Ref. 1; BAB14281).
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
//
MIM
612375
*RECORD*
*FIELD* NO
612375
*FIELD* TI
*612375 AXIN INTERACTOR, DORSALIZATION-ASSOCIATED; AIDA
;;AXIN-INTERACTING PROTEIN AND DORSALIZATION ANTAGONIST
read more*FIELD* TX
CLONING
Rui et al. (2007) cloned mouse and zebrafish Aida and identified the
Xenopus and human orthologs by database analysis. The deduced human and
mouse proteins contain 306 and 305 amino acids, respectively, and all
orthologs share a high degree of identity. Northern blot analysis
detected a 2.5-kb AIDA transcript in all human tissues examined.
GENE FUNCTION
Using yeast 2-hybrid analysis, immunoprecipitation analysis, and protein
pull-down assays, Rui et al. (2007) showed that vertebrate Aida
interacted with Axin (AXIN1; 603816). Aida inhibited Axin-mediated JNK
(see MAPK8; 601158) activation by disrupting Axin homodimerization. In
zebrafish embryos, Aida overexpression induced ventralization and
inhibited axin-induced dorsalization.
MAPPING
Hartz (2008) mapped the AIDA gene to chromosome 1q41 based on an
alignment of the AIDA sequence (GenBank GENBANK AL833718) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/29/2008.
2. Rui, Y.; Xu, Z.; Xiong, B.; Cao, Y.; Lin, S.; Zhang, M.; Chan,
S.-C.; Luo, W.; Han, Y.; Lu, Z.; Ye, Z.; Zhou, H.-M.; Han, J.; Meng,
A.; Lin, S.-C.: A beta-catenin-independent dorsalization pathway
activated by Axin/JNK signaling and antagonized by Aida. Dev. Cell 13:
268-282, 2007.
*FIELD* CD
Patricia A. Hartz: 10/28/2008
*FIELD* ED
mgross: 10/29/2008
*RECORD*
*FIELD* NO
612375
*FIELD* TI
*612375 AXIN INTERACTOR, DORSALIZATION-ASSOCIATED; AIDA
;;AXIN-INTERACTING PROTEIN AND DORSALIZATION ANTAGONIST
read more*FIELD* TX
CLONING
Rui et al. (2007) cloned mouse and zebrafish Aida and identified the
Xenopus and human orthologs by database analysis. The deduced human and
mouse proteins contain 306 and 305 amino acids, respectively, and all
orthologs share a high degree of identity. Northern blot analysis
detected a 2.5-kb AIDA transcript in all human tissues examined.
GENE FUNCTION
Using yeast 2-hybrid analysis, immunoprecipitation analysis, and protein
pull-down assays, Rui et al. (2007) showed that vertebrate Aida
interacted with Axin (AXIN1; 603816). Aida inhibited Axin-mediated JNK
(see MAPK8; 601158) activation by disrupting Axin homodimerization. In
zebrafish embryos, Aida overexpression induced ventralization and
inhibited axin-induced dorsalization.
MAPPING
Hartz (2008) mapped the AIDA gene to chromosome 1q41 based on an
alignment of the AIDA sequence (GenBank GENBANK AL833718) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/29/2008.
2. Rui, Y.; Xu, Z.; Xiong, B.; Cao, Y.; Lin, S.; Zhang, M.; Chan,
S.-C.; Luo, W.; Han, Y.; Lu, Z.; Ye, Z.; Zhou, H.-M.; Han, J.; Meng,
A.; Lin, S.-C.: A beta-catenin-independent dorsalization pathway
activated by Axin/JNK signaling and antagonized by Aida. Dev. Cell 13:
268-282, 2007.
*FIELD* CD
Patricia A. Hartz: 10/28/2008
*FIELD* ED
mgross: 10/29/2008