AAAS_MOUSE
ID AAAS_MOUSE Reviewed; 546 AA.
AC P58742; Q544M6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Aladin;
DE AltName: Full=Adracalin;
GN Name=Aaas;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Lung, Spleen, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; SER-511; SER-522;
RP SER-525 AND SER-541, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DISRUPTION PHENOTYPE.
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. 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.
CC {ECO:0000250|UniProtKB:Q9NRG9}.
CC -!- SUBUNIT: Interacts with NDC1, the interaction is required for nuclear
CC pore localization. Interacts with the inactive form aurora kinase
CC AURKA. Interacts with PGRMC2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRG9}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q9NRG9}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q9NRG9}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q9NRG9}. Note=In metaphase cells localizes
CC within the spindle with some accumulation around spindle poles, with
CC the highest concentration between the centrosome and metaphase plate.
CC The localization to the spindle is microtubule-mediated.
CC {ECO:0000250|UniProtKB:Q9NRG9}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Particularly abundant in
CC cerebellum, corpus callosum, adrenal gland, pituitary gland,
CC gastrointestinal structures and fetal lung.
CC {ECO:0000250|UniProtKB:Q9NRG9}.
CC -!- DISRUPTION PHENOTYPE: Female mutants are sterile due to delayed oocyte
CC maturation and meiotic spindle assembly. {ECO:0000269|PubMed:27754849}.
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DR EMBL; AK034591; BAC28764.1; -; mRNA.
DR EMBL; AK083537; BAC38945.1; -; mRNA.
DR EMBL; AK134406; BAE22131.1; -; mRNA.
DR EMBL; AK165243; BAE38099.1; -; mRNA.
DR EMBL; AK166118; BAE38581.1; -; mRNA.
DR EMBL; BC018191; AAH18191.1; -; mRNA.
DR CCDS; CCDS27880.1; -.
DR RefSeq; NP_700465.2; NM_153416.2.
DR AlphaFoldDB; P58742; -.
DR SMR; P58742; -.
DR BioGRID; 230214; 9.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; P58742; 1.
DR STRING; 10090.ENSMUSP00000044604; -.
DR iPTMnet; P58742; -.
DR PhosphoSitePlus; P58742; -.
DR EPD; P58742; -.
DR jPOST; P58742; -.
DR MaxQB; P58742; -.
DR PaxDb; P58742; -.
DR PeptideAtlas; P58742; -.
DR PRIDE; P58742; -.
DR ProteomicsDB; 285624; -.
DR Antibodypedia; 27006; 261 antibodies from 32 providers.
DR Ensembl; ENSMUST00000041208; ENSMUSP00000044604; ENSMUSG00000036678.
DR GeneID; 223921; -.
DR KEGG; mmu:223921; -.
DR UCSC; uc007xvk.2; mouse.
DR CTD; 8086; -.
DR MGI; MGI:2443767; Aaas.
DR VEuPathDB; HostDB:ENSMUSG00000036678; -.
DR eggNOG; KOG2139; Eukaryota.
DR GeneTree; ENSGT00390000009446; -.
DR HOGENOM; CLU_027691_0_1_1; -.
DR InParanoid; P58742; -.
DR OMA; RGGICIW; -.
DR OrthoDB; 628517at2759; -.
DR PhylomeDB; P58742; -.
DR TreeFam; TF324412; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR BioGRID-ORCS; 223921; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Aaas; mouse.
DR PRO; PR:P58742; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P58742; protein.
DR Bgee; ENSMUSG00000036678; Expressed in embryonic post-anal tail and 185 other tissues.
DR ExpressionAtlas; P58742; baseline and differential.
DR Genevisible; P58742; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045139; Aladin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR14494; PTHR14494; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG9"
FT CHAIN 2..546
FT /note="Aladin"
FT /id="PRO_0000050829"
FT REPEAT 149..188
FT /note="WD 1"
FT REPEAT 191..230
FT /note="WD 2"
FT REPEAT 243..282
FT /note="WD 3"
FT REPEAT 285..324
FT /note="WD 4"
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 517..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylcysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG9"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG9"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 546 AA; 59431 MW; 5F483AEB8C2E969B CRC64;
MCSLGLFPPP PPRGQVTLYE HNNELVTGNS YESPPPDFRG QWINLPVLHL TKDPLKAPGR
LDHGTRTAFI HHREQVWKRC INVWHDVGLF GVLNEIANSE EEVFEWVKTA CSWALALCGR
ASSLHGSLFP HLSLRSEDLI AEFAQVTNWS SCCLRVFAWH PHTNKFAVAL LDDSIRVYNA
NSTIVPSLKH RLQRNVAALA WKPLSASVLA VACQSCILIW TLDPTSLSTR PSSGCAQVLS
HPGHTPVTSL AWAPNGGWLL SASPVDAVIL VWDVSTETCV PLPWFRGGGV TNLLWSPDGS
KVLATTPSAV FRVWEAQMWT CEAWPTLSGR CQTGCWSPDG NRLLFTVLGE ALIYSLSFPE
RCGTGKGHVG GAKSATIVAD LSETTIQTPD GEERLGGEAH SMVWDPSGER LAVLMKGNPQ
VQDGNPVILL FRTRNSPVFE LLPCGIIQGE PGAQAQLITF HPSFNKGALL SVCWSTGRIT
HIPLYFVNAQ FPRFSPVLGR AQEPPAGGGG SIHEVPLFTE TSPTSAPWDP LPGQSSAQPH
SPHSHL
