RAE1L_HUMAN
ID RAE1L_HUMAN Reviewed; 368 AA.
AC P78406; A8K882; O15306; Q3SYL7; Q5TCH8; Q6V708; Q9H100; Q9NQM6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=mRNA export factor RAE1 {ECO:0000305};
DE AltName: Full=Rae1 protein homolog;
DE AltName: Full=mRNA-associated protein mrnp 41;
GN Name=RAE1; Synonyms=MRNP41;
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 [MRNA].
RC TISSUE=Mammary carcinoma;
RX PubMed=9370289; DOI=10.1016/s0378-1119(97)00322-3;
RA Bharathi A., Ghosh A., Whalen W.A., Yoon J.H., Pu R., Dasso M., Dhar R.;
RT "The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe
RT rae1 gene involved in nuclear export of poly(A)+ RNA.";
RL Gene 198:251-258(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=9256445; DOI=10.1073/pnas.94.17.9119;
RA Kraemer D.M., Blobel G.;
RT "mRNA binding protein mrnp 41 localizes to both nucleus and cytoplasm.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9119-9124(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Lu L., Huang X.Y., Xu M., Yin L.L., Li J.M., Zhou Z.M., Sha J.H.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [8]
RP FUNCTION, INTERACTION WITH NUMA1, AND SUBCELLULAR LOCATION.
RX PubMed=17172455; DOI=10.1073/pnas.0609582104;
RA Wong R.W., Blobel G., Coutavas E.;
RT "Rae1 interaction with NuMA is required for bipolar spindle formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19783-19787(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-229, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
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 [12]
RP INTERACTION WITH USP11.
RX PubMed=29293652; DOI=10.1371/journal.pone.0190513;
RA Stockum A., Snijders A.P., Maertens G.N.;
RT "USP11 deubiquitinates RAE1 and plays a key role in bipolar spindle
RT formation.";
RL PLoS ONE 13:e0190513-e0190513(2018).
RN [13]
RP INTERACTION WITH MYCBP2.
RX PubMed=22357847; DOI=10.1523/jneurosci.2901-11.2012;
RA Grill B., Chen L., Tulgren E.D., Baker S.T., Bienvenut W., Anderson M.,
RA Quadroni M., Jin Y., Garner C.C.;
RT "RAE-1, a novel PHR binding protein, is required for axon termination and
RT synapse formation in Caenorhabditis elegans.";
RL J. Neurosci. 32:2628-2636(2012).
RN [14]
RP INTERACTION WITH SARS-COV-2 ORF6 PROTEIN (MICROBIAL INFECTION).
RX PubMed=33097660; DOI=10.1073/pnas.2016650117;
RA Miorin L., Kehrer T., Sanchez-Aparicio M.T., Zhang K., Cohen P.,
RA Patel R.S., Cupic A., Makio T., Mei M., Moreno E., Danziger O., White K.M.,
RA Rathnasinghe R., Uccellini M., Gao S., Aydillo T., Mena I., Yin X.,
RA Martin-Sancho L., Krogan N.J., Chanda S.K., Schotsaert M., Wozniak R.W.,
RA Ren Y., Rosenberg B.R., Fontoura B.M.A., Garcia-Sastre A.;
RT "SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize
RT interferon signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:28344-28354(2020).
RN [15]
RP INTERACTION WITH SARS-COV-2 ORF6 PROTEIN (MICROBIAL INFECTION), AND
RP SUBCELLULAR LOCATION.
RX PubMed=33360543; DOI=10.1016/j.bbrc.2020.11.115;
RA Kato K., Ikliptikawati D.K., Kobayashi A., Kondo H., Lim K., Hazawa M.,
RA Wong R.W.;
RT "Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from
RT the nuclear pore complex.";
RL Biochem. Biophys. Res. Commun. 536:59-66(2021).
RN [16]
RP FUNCTION, AND INTERACTION WITH SARS-COV-2 ORF6 PROTEIN (MICROBIAL
RP INFECTION) AND SARS-COV ORF6 PROTEIN (MICROBIAL INFECTION).
RX PubMed=33849972; DOI=10.1128/mbio.00065-21;
RA Addetia A., Lieberman N.A.P., Phung Q., Hsiang T.Y., Xie H.,
RA Roychoudhury P., Shrestha L., Loprieno M.A., Huang M.L., Gale M. Jr.,
RA Jerome K.R., Greninger A.L.;
RT "SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through
RT Interactions with Rae1 and Nup98.";
RL MBio 12:0-0(2021).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NUP98, FUNCTION, AND
RP WD REPEATS.
RX PubMed=20498086; DOI=10.1073/pnas.1005389107;
RA Ren Y., Seo H.S., Blobel G., Hoelz A.;
RT "Structural and functional analysis of the interaction between the
RT nucleoporin Nup98 and the mRNA export factor Rae1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10406-10411(2010).
CC -!- FUNCTION: Acts as mRNA export factor involved in nucleocytoplasmic
CC transport (PubMed:33849972, PubMed:20498086). Plays a role in mitotic
CC bipolar spindle formation (PubMed:17172455). May function in attaching
CC cytoplasmic mRNPs to the cytoskeleton both directly or indirectly
CC (PubMed:17172455). {ECO:0000269|PubMed:17172455,
CC ECO:0000269|PubMed:20498086, ECO:0000269|PubMed:33849972}.
CC -!- SUBUNIT: Interacts with NUMA1 (via N-terminal end of the coiled-coil
CC domain); this interaction promotes spindle formation in mitosis
CC (PubMed:17172455). Interacts with NUP98 (PubMed:20498086). Interacts
CC with MYCBP2 (PubMed:22357847). Interacts with USP11 (PubMed:29293652).
CC {ECO:0000269|PubMed:17172455, ECO:0000269|PubMed:20498086,
CC ECO:0000269|PubMed:22357847, ECO:0000269|PubMed:29293652}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS-
CC CoV-2 ORF6 protein; the interaction displaces RAE1 from the nuclear
CC envelope and impairs its role in nucleocytoplasmic transport.
CC {ECO:0000269|PubMed:33097660, ECO:0000269|PubMed:33360543,
CC ECO:0000269|PubMed:33849972}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus/SARS-CoV
CC ORF6 protein. {ECO:0000269|PubMed:33849972}.
CC -!- INTERACTION:
CC P78406; P42858: HTT; NbExp=4; IntAct=EBI-724495, EBI-466029;
CC P78406; Q14980: NUMA1; NbExp=6; IntAct=EBI-724495, EBI-521611;
CC P78406; P52948: NUP98; NbExp=9; IntAct=EBI-724495, EBI-295727;
CC P78406; Q14683: SMC1A; NbExp=5; IntAct=EBI-724495, EBI-80690;
CC P78406; E5LBS6: ORF10; Xeno; NbExp=2; IntAct=EBI-724495, EBI-14033439;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9256445}. Nucleus
CC {ECO:0000269|PubMed:9256445}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:17172455}. Nucleus envelope
CC {ECO:0000269|PubMed:33360543}. Note=Recruited from interphase nuclei to
CC spindle MTs during mitosis. {ECO:0000269|PubMed:17172455}.
CC -!- SIMILARITY: Belongs to the WD repeat rae1 family. {ECO:0000305}.
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DR EMBL; U84720; AAC28126.1; -; mRNA.
DR EMBL; U85943; AAC28127.1; -; mRNA.
DR EMBL; AY349350; AAR04856.1; -; mRNA.
DR EMBL; AK292247; BAF84936.1; -; mRNA.
DR EMBL; AL135939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75523.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75524.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75525.1; -; Genomic_DNA.
DR EMBL; BC103754; AAI03755.1; -; mRNA.
DR EMBL; BC106924; AAI06925.1; -; mRNA.
DR EMBL; BC106923; AAI06924.1; -; mRNA.
DR CCDS; CCDS13458.1; -.
DR RefSeq; NP_001015885.1; NM_001015885.1.
DR RefSeq; NP_003601.1; NM_003610.3.
DR RefSeq; XP_005260639.2; XM_005260582.2.
DR RefSeq; XP_011527390.1; XM_011529088.2.
DR RefSeq; XP_011527391.1; XM_011529089.1.
DR PDB; 3MMY; X-ray; 1.65 A; A/C/E/G=1-368.
DR PDB; 4OWR; X-ray; 3.15 A; A=31-368.
DR PDB; 7VPG; X-ray; 2.49 A; A/C/E/G=1-368.
DR PDB; 7VPH; X-ray; 2.80 A; A/C/E/G=1-368.
DR PDBsum; 3MMY; -.
DR PDBsum; 4OWR; -.
DR PDBsum; 7VPG; -.
DR PDBsum; 7VPH; -.
DR AlphaFoldDB; P78406; -.
DR SMR; P78406; -.
DR BioGRID; 114054; 204.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR DIP; DIP-41063N; -.
DR IntAct; P78406; 72.
DR MINT; P78406; -.
DR STRING; 9606.ENSP00000379182; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; P78406; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P78406; -.
DR PhosphoSitePlus; P78406; -.
DR SwissPalm; P78406; -.
DR BioMuta; RAE1; -.
DR DMDM; 3122666; -.
DR EPD; P78406; -.
DR jPOST; P78406; -.
DR MassIVE; P78406; -.
DR MaxQB; P78406; -.
DR PaxDb; P78406; -.
DR PeptideAtlas; P78406; -.
DR PRIDE; P78406; -.
DR ProteomicsDB; 57614; -.
DR TopDownProteomics; P78406; -.
DR Antibodypedia; 14158; 289 antibodies from 39 providers.
DR DNASU; 8480; -.
DR Ensembl; ENST00000371242.6; ENSP00000360286.2; ENSG00000101146.13.
DR Ensembl; ENST00000395840.6; ENSP00000379181.2; ENSG00000101146.13.
DR Ensembl; ENST00000395841.7; ENSP00000379182.2; ENSG00000101146.13.
DR GeneID; 8480; -.
DR KEGG; hsa:8480; -.
DR MANE-Select; ENST00000395841.7; ENSP00000379182.2; NM_003610.4; NP_003601.1.
DR UCSC; uc002xyg.4; human.
DR CTD; 8480; -.
DR DisGeNET; 8480; -.
DR GeneCards; RAE1; -.
DR HGNC; HGNC:9828; RAE1.
DR HPA; ENSG00000101146; Tissue enhanced (testis).
DR MIM; 603343; gene.
DR neXtProt; NX_P78406; -.
DR OpenTargets; ENSG00000101146; -.
DR PharmGKB; PA34182; -.
DR VEuPathDB; HostDB:ENSG00000101146; -.
DR eggNOG; KOG0647; Eukaryota.
DR GeneTree; ENSGT00950000183091; -.
DR HOGENOM; CLU_038526_1_0_1; -.
DR InParanoid; P78406; -.
DR OMA; EAMDQSI; -.
DR OrthoDB; 1048963at2759; -.
DR PhylomeDB; P78406; -.
DR TreeFam; TF105481; -.
DR PathwayCommons; P78406; -.
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-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; P78406; -.
DR SIGNOR; P78406; -.
DR BioGRID-ORCS; 8480; 762 hits in 1069 CRISPR screens.
DR ChiTaRS; RAE1; human.
DR EvolutionaryTrace; P78406; -.
DR GeneWiki; RAE1; -.
DR GenomeRNAi; 8480; -.
DR Pharos; P78406; Tbio.
DR PRO; PR:P78406; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P78406; protein.
DR Bgee; ENSG00000101146; Expressed in secondary oocyte and 201 other tissues.
DR ExpressionAtlas; P78406; baseline and differential.
DR Genevisible; P78406; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0097431; C:mitotic spindle pole; IMP:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:GO_Central.
DR GO; GO:0005643; C:nuclear pore; IDA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; TAS:ProtInc.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037631; Gle2/RAE1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10971:SF11; PTHR10971:SF11; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Host-virus interaction; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..368
FT /note="mRNA export factor RAE1"
FT /id="PRO_0000051181"
FT REPEAT 37..79
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:20498086"
FT REPEAT 84..114
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:20498086"
FT REPEAT 125..157
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:20498086"
FT REPEAT 168..206
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:20498086"
FT REPEAT 215..255
FT /note="WD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:20498086"
FT REPEAT 271..301
FT /note="WD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:20498086"
FT REPEAT 310..346
FT /note="WD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:20498086"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CONFLICT 10
FT /note="F -> L (in Ref. 2; AAC28127)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="D -> G (in Ref. 2; AAC28127)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="F -> S (in Ref. 2; AAC28127)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="A -> V (in Ref. 3; AAR04856)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="T -> N (in Ref. 2; AAC28127)"
FT /evidence="ECO:0000305"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3MMY"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:3MMY"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:3MMY"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:3MMY"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:3MMY"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:3MMY"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:3MMY"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:3MMY"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:3MMY"
SQ SEQUENCE 368 AA; 40968 MW; 89A99C34BA668A97 CRC64;
MSLFGTTSGF GTSGTSMFGS ATTDNHNPMK DIEVTSSPDD SIGCLSFSPP TLPGNFLIAG
SWANDVRCWE VQDSGQTIPK AQQMHTGPVL DVCWSDDGSK VFTASCDKTA KMWDLSSNQA
IQIAQHDAPV KTIHWIKAPN YSCVMTGSWD KTLKFWDTRS SNPMMVLQLP ERCYCADVIY
PMAVVATAER GLIVYQLENQ PSEFRRIESP LKHQHRCVAI FKDKQNKPTG FALGSIEGRV
AIHYINPPNP AKDNFTFKCH RSNGTNTSAP QDIYAVNGIA FHPVHGTLAT VGSDGRFSFW
DKDARTKLKT SEQLDQPISA CCFNHNGNIF AYASSYDWSK GHEFYNPQKK NYIFLRNAAE
ELKPRNKK
