AAAS_HUMAN
ID AAAS_HUMAN Reviewed; 546 AA.
AC Q9NRG9; Q5JB47; Q9NWI6; Q9UG19;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Aladin;
DE AltName: Full=Adracalin;
GN Name=AAAS; Synonyms=ADRACALA; ORFNames=GL003;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=11062474; DOI=10.1038/81642;
RA Tullio-Pelet A., Salomon R., Hadj-Rabia S., Mugnier C., de Laet M.-H.,
RA Chaouachi B., Bakiri F., Brottier P., Cattolico L., Penet C., Begeot M.,
RA Naville D., Nicolino M., Chaussain J.-L., Weissenbach J., Munnich A.,
RA Lyonnet S.;
RT "Mutant WD-repeat protein in triple-A syndrome.";
RL Nat. Genet. 26:332-335(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS AAAS LYS-15; 84-TRP--LEU-546
RP DEL; ARG-160; PRO-263; 286-ARG--LEU-546 DEL AND 342-ARG--LEU-546 DEL,
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11159947; DOI=10.1093/hmg/10.3.283;
RA Handschug K., Sperling S., Yoon S.-J.K., Hennig S., Clark A.J.L.,
RA Huebner A.;
RT "Triple A syndrome is caused by mutations in AAAS, a new WD-repeat protein
RT gene.";
RL Hum. Mol. Genet. 10:283-290(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16022285; DOI=10.1007/s11033-004-6939-9;
RA Li X., Ji C., Gu J., Xu J., Jin Z., Sun L., Zou X., Lin Y., Sun R.,
RA Wang P., Gu S., Mao Y.;
RT "Molecular cloning and characterization of AAAS-V2, a novel splice variant
RT of human AAAS.";
RL Mol. Biol. Rep. 32:127-131(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human liver non-tumor tissues.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 210-546 (ISOFORM 1).
RC TISSUE=Uterus;
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, 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 [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NDC1.
RX PubMed=19782045; DOI=10.1016/j.bbrc.2009.09.080;
RA Kind B., Koehler K., Lorenz M., Huebner A.;
RT "The nuclear pore complex protein ALADIN is anchored via NDC1 but not via
RT POM121 and GP210 in the nuclear envelope.";
RL Biochem. Biophys. Res. Commun. 390:205-210(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-495, 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 [13]
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).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; SER-511 AND SER-541, AND
RP IDENTIFICATION BY 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).
RN [17]
RP FUNCTION, INTERACTION WITH AURKA, AND SUBCELLULAR LOCATION.
RX PubMed=26246606; DOI=10.1091/mbc.e15-02-0113;
RA Carvalhal S., Ribeiro S.A., Arocena M., Kasciukovic T., Temme A.,
RA Koehler K., Huebner A., Griffis E.R.;
RT "The nucleoporin ALADIN regulates Aurora A localization to ensure robust
RT mitotic spindle formation.";
RL Mol. Biol. Cell 26:3424-3438(2015).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP INTERACTION WITH PGRMC2, AND SUBCELLULAR LOCATION.
RX PubMed=27754849; DOI=10.1242/bio.021162;
RA Juehlen R., Landgraf D., Huebner A., Koehler K.;
RT "Identification of a novel putative interaction partner of the nucleoporin
RT ALADIN.";
RL Biol. Open 5:1697-1705(2016).
CC -!- FUNCTION: Plays a role in the normal development of the peripheral and
CC central nervous system (PubMed:11062474, PubMed:11159947,
CC PubMed:16022285). Required for the correct localization of aurora
CC kinase AURKA and the microtubule minus end-binding protein NUMA1 as
CC well as a subset of AURKA targets which ensures proper spindle
CC formation and timely chromosome alignment (PubMed:26246606).
CC {ECO:0000269|PubMed:11062474, ECO:0000269|PubMed:11159947,
CC ECO:0000269|PubMed:16022285, ECO:0000269|PubMed:26246606}.
CC -!- SUBUNIT: Interacts with NDC1, the interaction is required for nuclear
CC pore localization (PubMed:19782045). Interacts with the inactive form
CC aurora kinase AURKA (PubMed:26246606). Interacts with PGRMC2
CC (PubMed:27754849). {ECO:0000269|PubMed:19782045,
CC ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:27754849}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:19782045}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:26246606}. Nucleus envelope
CC {ECO:0000269|PubMed:27754849}. Note=In metaphase cells localizes within
CC the spindle with some accumulation around spindle poles, with the
CC highest concentration between the centrosome and metaphase plate
CC (PubMed:26246606). The localization to the spindle is microtubule-
CC mediated (PubMed:26246606). {ECO:0000269|PubMed:26246606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AAAS-v1;
CC IsoId=Q9NRG9-1; Sequence=Displayed;
CC Name=2; Synonyms=AAAS-v2;
CC IsoId=Q9NRG9-2; Sequence=VSP_043014;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:11159947,
CC PubMed:16022285). Particularly abundant in cerebellum, corpus callosum,
CC adrenal gland, pituitary gland, gastrointestinal structures and fetal
CC lung (PubMed:11159947). {ECO:0000269|PubMed:11159947,
CC ECO:0000269|PubMed:16022285}.
CC -!- DISEASE: Achalasia-addisonianism-alacrima syndrome (AAAS) [MIM:231550]:
CC An autosomal recessive disorder characterized by adreno-corticotropic
CC hormone (ACTH)-resistant adrenal failure, achalasia of the esophageal
CC cardia and alacrima. The syndrome is associated with variable and
CC progressive neurological impairment involving the central, peripheral,
CC and autonomic nervous system. Other features such as palmoplantar
CC hyperkeratosis, short stature, facial dysmorphy and osteoporosis may
CC also be present. {ECO:0000269|PubMed:11159947}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Ubiquitously expressed. {ECO:0000305}.
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DR EMBL; AJ289857; CAC19017.1; -; mRNA.
DR EMBL; AJ289841; CAC19038.1; -; Genomic_DNA.
DR EMBL; AJ289842; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289843; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289844; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289845; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289846; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289847; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289848; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289849; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289850; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289851; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289852; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289853; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289854; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289855; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ289856; CAC19038.1; JOINED; Genomic_DNA.
DR EMBL; AJ297977; CAC17465.1; -; Genomic_DNA.
DR EMBL; AY237818; AAP69911.1; -; mRNA.
DR EMBL; AF226048; AAF86948.1; -; mRNA.
DR EMBL; AK000833; BAA91394.1; -; mRNA.
DR EMBL; BT006912; AAP35558.1; -; mRNA.
DR EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000659; AAH00659.1; -; mRNA.
DR EMBL; AL110160; CAB53665.2; -; mRNA.
DR CCDS; CCDS53797.1; -. [Q9NRG9-2]
DR CCDS; CCDS8856.1; -. [Q9NRG9-1]
DR RefSeq; NP_001166937.1; NM_001173466.1. [Q9NRG9-2]
DR RefSeq; NP_056480.1; NM_015665.5. [Q9NRG9-1]
DR AlphaFoldDB; Q9NRG9; -.
DR SMR; Q9NRG9; -.
DR BioGRID; 113759; 155.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR IntAct; Q9NRG9; 30.
DR MINT; Q9NRG9; -.
DR STRING; 9606.ENSP00000209873; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9NRG9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NRG9; -.
DR PhosphoSitePlus; Q9NRG9; -.
DR SwissPalm; Q9NRG9; -.
DR BioMuta; AAAS; -.
DR DMDM; 20137527; -.
DR EPD; Q9NRG9; -.
DR jPOST; Q9NRG9; -.
DR MassIVE; Q9NRG9; -.
DR MaxQB; Q9NRG9; -.
DR PaxDb; Q9NRG9; -.
DR PeptideAtlas; Q9NRG9; -.
DR PRIDE; Q9NRG9; -.
DR ProteomicsDB; 82359; -. [Q9NRG9-1]
DR ProteomicsDB; 82360; -. [Q9NRG9-2]
DR Antibodypedia; 27006; 261 antibodies from 32 providers.
DR DNASU; 8086; -.
DR Ensembl; ENST00000209873.9; ENSP00000209873.4; ENSG00000094914.14. [Q9NRG9-1]
DR Ensembl; ENST00000394384.7; ENSP00000377908.3; ENSG00000094914.14. [Q9NRG9-2]
DR GeneID; 8086; -.
DR KEGG; hsa:8086; -.
DR MANE-Select; ENST00000209873.9; ENSP00000209873.4; NM_015665.6; NP_056480.1.
DR UCSC; uc001scr.5; human. [Q9NRG9-1]
DR CTD; 8086; -.
DR DisGeNET; 8086; -.
DR GeneCards; AAAS; -.
DR HGNC; HGNC:13666; AAAS.
DR HPA; ENSG00000094914; Low tissue specificity.
DR MalaCards; AAAS; -.
DR MIM; 231550; phenotype.
DR MIM; 605378; gene.
DR neXtProt; NX_Q9NRG9; -.
DR OpenTargets; ENSG00000094914; -.
DR Orphanet; 869; Triple A syndrome.
DR PharmGKB; PA24361; -.
DR VEuPathDB; HostDB:ENSG00000094914; -.
DR eggNOG; KOG2139; Eukaryota.
DR GeneTree; ENSGT00390000009446; -.
DR HOGENOM; CLU_027691_0_1_1; -.
DR InParanoid; Q9NRG9; -.
DR OMA; RGGICIW; -.
DR OrthoDB; 628517at2759; -.
DR PhylomeDB; Q9NRG9; -.
DR TreeFam; TF324412; -.
DR PathwayCommons; Q9NRG9; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q9NRG9; -.
DR SIGNOR; Q9NRG9; -.
DR BioGRID-ORCS; 8086; 173 hits in 1080 CRISPR screens.
DR ChiTaRS; AAAS; human.
DR GeneWiki; AAAS_(gene); -.
DR GenomeRNAi; 8086; -.
DR Pharos; Q9NRG9; Tbio.
DR PRO; PR:Q9NRG9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NRG9; protein.
DR Bgee; ENSG00000094914; Expressed in right adrenal gland cortex and 173 other tissues.
DR ExpressionAtlas; Q9NRG9; baseline and differential.
DR Genevisible; Q9NRG9; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; NAS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR045139; Aladin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR PANTHER; PTHR14494; PTHR14494; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Disease variant; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..546
FT /note="Aladin"
FT /id="PRO_0000050828"
FT REPEAT 142..180
FT /note="WD 1"
FT REPEAT 183..222
FT /note="WD 2"
FT REPEAT 234..274
FT /note="WD 3"
FT REPEAT 280..316
FT /note="WD 4"
FT REPEAT 324..380
FT /note="WD 5"
FT REPEAT 386..433
FT /note="WD 6"
FT REPEAT 442..482
FT /note="WD 7"
FT REGION 500..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 544..546
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 527..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylcysteine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58742"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58742"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 149..182
FT /note="WSSCCLRVFAWHPHTNKFAVALLDDSVRVYNASS -> C (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16022285"
FT /id="VSP_043014"
FT VARIANT 15
FT /note="Q -> K (in AAAS; dbSNP:rs121918549)"
FT /evidence="ECO:0000269|PubMed:11159947"
FT /id="VAR_012804"
FT VARIANT 84..546
FT /note="Missing (in AAAS)"
FT /evidence="ECO:0000269|PubMed:11159947"
FT /id="VAR_080414"
FT VARIANT 108
FT /note="K -> M (in dbSNP:rs13330)"
FT /id="VAR_037060"
FT VARIANT 160
FT /note="H -> R (in AAAS; dbSNP:rs1297831120)"
FT /evidence="ECO:0000269|PubMed:11159947"
FT /id="VAR_012805"
FT VARIANT 263
FT /note="S -> P (in AAAS; dbSNP:rs121918550)"
FT /evidence="ECO:0000269|PubMed:11159947"
FT /id="VAR_012806"
FT VARIANT 286..546
FT /note="Missing (in AAAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:11159947"
FT /id="VAR_080415"
FT VARIANT 342..546
FT /note="Missing (in AAAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:11159947"
FT /id="VAR_080416"
FT CONFLICT 122
FT /note="S -> P (in Ref. 5; BAA91394)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="R -> K (in Ref. 5; BAA91394)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="I -> V (in Ref. 5; BAA91394)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 59574 MW; E0F4E7145D8C192E CRC64;
MCSLGLFPPP PPRGQVTLYE HNNELVTGSS YESPPPDFRG QWINLPVLQL TKDPLKTPGR
LDHGTRTAFI HHREQVWKRC INIWRDVGLF GVLNEIANSE EEVFEWVKTA SGWALALCRW
ASSLHGSLFP HLSLRSEDLI AEFAQVTNWS SCCLRVFAWH PHTNKFAVAL LDDSVRVYNA
SSTIVPSLKH RLQRNVASLA WKPLSASVLA VACQSCILIW TLDPTSLSTR PSSGCAQVLS
HPGHTPVTSL AWAPSGGRLL SASPVDAAIR VWDVSTETCV PLPWFRGGGV TNLLWSPDGS
KILATTPSAV FRVWEAQMWT CERWPTLSGR CQTGCWSPDG SRLLFTVLGE PLIYSLSFPE
RCGEGKGCVG GAKSATIVAD LSETTIQTPD GEERLGGEAH SMVWDPSGER LAVLMKGKPR
VQDGKPVILL FRTRNSPVFE LLPCGIIQGE PGAQPQLITF HPSFNKGALL SVGWSTGRIA
HIPLYFVNAQ FPRFSPVLGR AQEPPAGGGG SIHDLPLFTE TSPTSAPWDP LPGPPPVLPH
SPHSHL
