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 28-JAN-2026, entry version 214. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001173466.2. [Q9NRG9-2] DR RefSeq; NP_056480.1; NM_015665.6. [Q9NRG9-1] DR PDB; 7R5J; EM; 50.00 A; 40/41=1-546. DR PDB; 7R5K; EM; 12.00 A; 40/41=1-546. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR AlphaFoldDB; Q9NRG9; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR SMR; Q9NRG9; -. DR BioGRID; 113759; 200. DR ComplexPortal; CPX-873; Nuclear pore complex. DR CORUM; Q9NRG9; -. DR FunCoup; Q9NRG9; 3767. DR IntAct; Q9NRG9; 87. DR MINT; Q9NRG9; -. DR STRING; 9606.ENSP00000209873; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; Q9NRG9; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9NRG9; -. DR PhosphoSitePlus; Q9NRG9; -. DR SwissPalm; Q9NRG9; -. DR BioMuta; AAAS; -. DR DMDM; 20137527; -. DR jPOST; Q9NRG9; -. DR MassIVE; Q9NRG9; -. DR PaxDb; 9606-ENSP00000209873; -. DR PeptideAtlas; Q9NRG9; -. DR ProteomicsDB; 82359; -. [Q9NRG9-1] DR ProteomicsDB; 82360; -. [Q9NRG9-2] DR Pumba; Q9NRG9; -. DR Antibodypedia; 27006; 262 antibodies from 32 providers. DR DNASU; 8086; -. DR Ensembl; ENST00000209873.9; ENSP00000209873.4; ENSG00000094914.15. [Q9NRG9-1] DR Ensembl; ENST00000394384.7; ENSP00000377908.3; ENSG00000094914.15. [Q9NRG9-2] DR Ensembl; ENST00000708962.1; ENSP00000517437.1; ENSG00000291836.1. [Q9NRG9-2] DR Ensembl; ENST00000708963.1; ENSP00000517438.1; ENSG00000291836.1. [Q9NRG9-1] 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 AGR; HGNC:13666; -. DR ClinPGx; PA24361; -. 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 OpenTargets; ENSG00000094914; -. DR Orphanet; 869; Triple A syndrome. DR VEuPathDB; HostDB:ENSG00000094914; -. DR eggNOG; KOG2139; Eukaryota. DR GeneTree; ENSGT00390000009446; -. DR HOGENOM; CLU_027691_0_1_1; -. DR InParanoid; Q9NRG9; -. DR OMA; FQPLYKD; -. DR OrthoDB; 411991at2759; -. DR PAN-GO; Q9NRG9; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9NRG9; -. 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 Agora; ENSG00000094914; -. DR BioGRID-ORCS; 8086; 177 hits in 1161 CRISPR screens. DR CD-CODE; D6A53B8E; Nuclear pore complex. 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 175 other cell types or tissues. DR ExpressionAtlas; Q9NRG9; baseline and differential. 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:0097229; C:sperm end piece; IDA:HPA. DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB. DR GO; GO:0009566; P:fertilization; IEA:Ensembl. DR GO; GO:0006749; P:glutathione metabolic process; 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:0035264; P:multicellular organism growth; IEA:Ensembl. 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 GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl. DR FunFam; 2.130.10.10:FF:000456; aladin isoform X3; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR045139; Aladin. DR InterPro; IPR057403; Beta-prop_Aladin. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR14494:SF0; ALADIN; 1. DR PANTHER; PTHR14494; ALADIN/ADRACALIN/AAAS; 1. DR Pfam; PF25460; Beta-prop_Aladin; 1. DR SMART; SM00320; WD40; 4. DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1. 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 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; KW Disease variant; mRNA transport; Nuclear pore complex; Nucleus; KW Phosphoprotein; Protein transport; Proteomics identification; KW Reference proteome; Repeat; 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 529..539 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:11159947" FT /id="VAR_080415" FT VARIANT 342..546 FT /note="Missing (in AAAS; uncertain 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 //