PHAX_MOUSE
ID PHAX_MOUSE Reviewed; 385 AA.
AC Q9JJT9; Q8BSR8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Phosphorylated adapter RNA export protein;
DE AltName: Full=RNA U small nuclear RNA export adapter protein;
GN Name=Phax; Synonyms=Rnuxa;
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 [MRNA], FUNCTION IN U SNRNA EXPORT, IDENTIFICATION IN A
RP U SNRNA EXPORT COMPLEX WITH NCBP1; NCBP2; RAN; XPO1 AND M7G-CAPPED RNA,
RP PHOSPHORYLATION, MUTAGENESIS OF 124-LEU--MET-129, RNA-BINDING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10786834; DOI=10.1016/s0092-8674(00)80829-6;
RA Ohno M., Segref A., Bachi A., Wilm M., Mattaj I.W.;
RT "PHAX, a mediator of U snRNA nuclear export whose activity is regulated by
RT phosphorylation.";
RL Cell 101:187-198(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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 [4]
RP FUNCTION IN U SNRNA EXPORT, INTERACTION WITH NCBP1, RNA-BINDING, AND
RP MUTAGENESIS OF 71-LYS--ARG-74; 190-ARG-LYS-191; 255-GLU--GLU-258;
RP 260-GLU--ASN-262; 263-GLY-GLY-264; 270-GLY-SER-271; 273-ARG-ARG-274;
RP 275-THR-PRO-276; 289-SER--GLU-293 AND 315-LYS-ARG-316.
RX PubMed=11333016; DOI=10.1017/s1355838201002278;
RA Segref A., Mattaj I.W., Ohno M.;
RT "The evolutionarily conserved region of the U snRNA export mediator PHAX is
RT a novel RNA-binding domain that is essential for U snRNA export.";
RL RNA 7:351-360(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
CC -!- FUNCTION: A phosphoprotein adapter involved in the XPO1-mediated U
CC snRNA export from the nucleus. Bridge components required for U snRNA
CC export, the cap binding complex (CBC)-bound snRNA on the one hand and
CC the GTPase Ran in its active GTP-bound form together with the export
CC receptor XPO1 on the other. Its phosphorylation in the nucleus is
CC required for U snRNA export complex assembly and export, while its
CC dephosphorylation in the cytoplasm causes export complex disassembly.
CC It is recycled back to the nucleus via the importin alpha/beta
CC heterodimeric import receptor. The directionality of nuclear export is
CC thought to be conferred by an asymmetric distribution of the GTP- and
CC GDP-bound forms of Ran between the cytoplasm and nucleus. Its
CC compartmentalized phosphorylation cycle may also contribute to the
CC directionality of export. Binds strongly to m7G-capped U1 and U5 small
CC nuclear RNAs (snRNAs) in a sequence-unspecific manner and
CC phosphorylation-independent manner. Also plays a role in the biogenesis
CC of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport
CC from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8
CC and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3,
CC U8 and U13 snoRNAs. Binds also to telomerase RNA (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10786834,
CC ECO:0000269|PubMed:11333016}.
CC -!- SUBUNIT: Found in a U snRNA export complex with PHAX/RNUXA,
CC NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Part of a
CC precomplex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20 and m7G-capped
CC RNA. Interacts with NCBP1/CBP80. Found in a complex with snoRNA.
CC Interacts with NCBP2/CBP20 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H814, ECO:0000269|PubMed:10786834,
CC ECO:0000269|PubMed:11333016}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H814}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q9H814}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:Q9H814}. Cytoplasm
CC {ECO:0000269|PubMed:10786834}. Note=Shuttles between the nucleus and
CC the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies.
CC {ECO:0000250|UniProtKB:Q9H814}.
CC -!- PTM: Phosphorylated in the nucleus. Dephosphorylated in the cytoplasm.
CC {ECO:0000269|PubMed:10786834}.
CC -!- SIMILARITY: Belongs to the PHAX family. {ECO:0000305}.
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DR EMBL; AJ276504; CAB87994.1; -; mRNA.
DR EMBL; AK030749; BAC27117.1; -; mRNA.
DR EMBL; BC049590; AAH49590.1; -; mRNA.
DR EMBL; BC061110; AAH61110.1; -; mRNA.
DR CCDS; CCDS29259.1; -.
DR RefSeq; NP_001156461.1; NM_001162989.1.
DR RefSeq; NP_064380.3; NM_019996.4.
DR AlphaFoldDB; Q9JJT9; -.
DR SMR; Q9JJT9; -.
DR BioGRID; 208128; 9.
DR STRING; 10090.ENSMUSP00000008445; -.
DR iPTMnet; Q9JJT9; -.
DR PhosphoSitePlus; Q9JJT9; -.
DR EPD; Q9JJT9; -.
DR jPOST; Q9JJT9; -.
DR MaxQB; Q9JJT9; -.
DR PaxDb; Q9JJT9; -.
DR PRIDE; Q9JJT9; -.
DR ProteomicsDB; 287696; -.
DR Antibodypedia; 45036; 202 antibodies from 27 providers.
DR DNASU; 56698; -.
DR Ensembl; ENSMUST00000008445; ENSMUSP00000008445; ENSMUSG00000008301.
DR GeneID; 56698; -.
DR KEGG; mmu:56698; -.
DR UCSC; uc008eyq.2; mouse.
DR CTD; 51808; -.
DR MGI; MGI:1891839; Phax.
DR VEuPathDB; HostDB:ENSMUSG00000008301; -.
DR eggNOG; KOG3948; Eukaryota.
DR GeneTree; ENSGT00390000011084; -.
DR HOGENOM; CLU_058840_1_0_1; -.
DR InParanoid; Q9JJT9; -.
DR OMA; EEGCIKK; -.
DR OrthoDB; 1223195at2759; -.
DR PhylomeDB; Q9JJT9; -.
DR TreeFam; TF321050; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 56698; 21 hits in 72 CRISPR screens.
DR PRO; PR:Q9JJT9; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9JJT9; protein.
DR Bgee; ENSMUSG00000008301; Expressed in otic placode and 253 other tissues.
DR ExpressionAtlas; Q9JJT9; baseline and differential.
DR Genevisible; Q9JJT9; MM.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0140262; F:mRNA cap binding complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043489; P:RNA stabilization; ISO:MGI.
DR GO; GO:0006408; P:snRNA export from nucleus; IDA:MGI.
DR Gene3D; 1.10.10.1440; -; 1.
DR InterPro; IPR039047; PHAX.
DR InterPro; IPR019385; PHAX_RNA-binding_domain.
DR InterPro; IPR038092; PHAX_RNA-binding_sf.
DR PANTHER; PTHR13135; PTHR13135; 1.
DR Pfam; PF10258; RNA_GG_bind; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; RNA-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CHAIN 2..385
FT /note="Phosphorylated adapter RNA export protein"
FT /id="PRO_0000239776"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..320
FT /note="Necessary for interaction with CBP80"
FT REGION 75..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..319
FT /note="Sufficient for poly U RNA-binding"
FT REGION 270..278
FT /note="Necessary for poly U RNA-binding and snRNA export"
FT REGION 335..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 71..74
FT /note="Nuclear localization signal"
FT MOTIF 120..129
FT /note="Nuclear export signal"
FT MOTIF 189..192
FT /note="Nuclear localization signal"
FT COMPBIAS 164..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63068"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63068"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63068"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63068"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MUTAGEN 71..74
FT /note="KRKR->ARAA: Strongly reduces its import in the
FT nucleus. Abolishes its import in the nucleus, does not
FT change its export to the cytoplasm and the export of U
FT snRNA complex; when associated with 190-AA-191."
FT /evidence="ECO:0000269|PubMed:11333016"
FT MUTAGEN 124..129
FT /note="LGILGM->AGIAGA: Reduces U snRNA export. Strongly
FT abolishes the U snRNA export complex formation. Does not
FT abolish the pre-complex formation."
FT /evidence="ECO:0000269|PubMed:10786834"
FT MUTAGEN 190..191
FT /note="RK->AA: Strongly reduces its import in the nucleus.
FT Abolishes its import in the nucleus, does not change its
FT export to the cytoplasm and the export of the U snRNA
FT complex; when associated with 71-ARAA-74."
FT /evidence="ECO:0000269|PubMed:11333016"
FT MUTAGEN 255..258
FT /note="ETAE->AAAA: Does not inhibit U RNA-binding."
FT /evidence="ECO:0000269|PubMed:11333016"
FT MUTAGEN 260..262
FT /note="EQN->AAA: Partially inhibits U RNA-binding."
FT /evidence="ECO:0000269|PubMed:11333016"
FT MUTAGEN 263..264
FT /note="GG->AA: Strongly inhibits U RNA-binding."
FT /evidence="ECO:0000269|PubMed:11333016"
FT MUTAGEN 270..271
FT /note="GS->AA: Partially inhibits U RNA-binding."
FT /evidence="ECO:0000269|PubMed:11333016"
FT MUTAGEN 273..274
FT /note="RR->AA: Partially reduces its import in the
FT nucleus."
FT /evidence="ECO:0000269|PubMed:11333016"
FT MUTAGEN 275..276
FT /note="TP->AA: Partially inhibits U RNA-binding."
FT /evidence="ECO:0000269|PubMed:11333016"
FT MUTAGEN 289..293
FT /note="SISEE->AIAEA: Does not inhibit U RNA-binding."
FT /evidence="ECO:0000269|PubMed:11333016"
FT MUTAGEN 315..316
FT /note="KR->AA: Partially reduces its import in the
FT nucleus."
FT /evidence="ECO:0000269|PubMed:11333016"
FT CONFLICT 236
FT /note="L -> Q (in Ref. 2; BAC27117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43247 MW; 90946BE46B7ABDCA CRC64;
MALEAGDMEE GQLSDSDSDM TVVPSDRPLQ MAKVLGGGSA ACAPVSHYRT VKHVDSSEES
LDSDDDCSLW KRKRQKCHNT PPKPEPFPFG PSGQKTALNG GKKVNNIWGA VLQEQNQDAV
ATELGILGME GSIDRSRQSE TYNYLLAKKL AKKESQEYTK ELDKDLDEYM HGDKKPGSKE
DENGQGHLKR KRPVRDRLGN RVEMNYKGRY EITEEDAPEK VADEIAFRLQ EPKKDLIARV
VRILGNKKAI ELLMETAEVE QNGGLFIMNG SRRRTPGGVF LNLLKNTPSI SEEQIKDIFY
VENQKEYENK KAARKRRTQL LGKKMKQAIK SLNFQEDDDT SRETFASDTN EALASLDEAQ
EGPGETKLDA EEAIEVDHPQ DLDIF
