Full text data of PHAX
PHAX
(RNUXA)
[Confidence: low (only semi-automatic identification from reviews)]
Phosphorylated adapter RNA export protein (RNA U small nuclear RNA export adapter protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphorylated adapter RNA export protein (RNA U small nuclear RNA export adapter protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H814
ID PHAX_HUMAN Reviewed; 394 AA.
AC Q9H814; Q9H8W1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 95.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retinoblastoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION IN U3 SNORNA TRANSPORT, RNA-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15574332; DOI=10.1016/j.molcel.2004.11.013;
RA Boulon S., Verheggen C., Jady B.E., Girard C., Pescia C., Paul C.,
RA Ospina J.K., Kiss T., Matera A.G., Bordonne R., Bertrand E.;
RT "PHAX and CRM1 are required sequentially to transport U3 snoRNA to
RT nucleoli.";
RL Mol. Cell 16:777-787(2004).
RN [5]
RP SUBCELLULAR LOCATION.
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
RT PHAX is a novel RNA-binding domain that is essential for U snRNA
RT export.";
RL RNA 7:351-360(2001).
RN [6]
RP FUNCTION IN SNORNA TRANSPORT, AND IDENTIFICATION IN A COMPLEX WITH U3
RP SNORNA.
RX PubMed=15574333; DOI=10.1016/j.molcel.2004.11.012;
RA Watkins N.J., Lemm I., Ingelfinger D., Schneider C., Hossbach M.,
RA Urlaub H., Luehrmann R.;
RT "Assembly and maturation of the U3 snoRNP in the nucleoplasm in a
RT large dynamic multiprotein complex.";
RL Mol. Cell 16:789-798(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASS
RP SPECTROMETRY.
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT THR-296, MASS SPECTROMETRY, AND CLEAVAGE OF
RP INITIATOR METHIONINE.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-14, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP STRUCTURE BY NMR OF 223-323, AND RNA-BINDING REGION.
RX PubMed=20430857; DOI=10.1261/rna.2009910;
RA Mourao A., Varrot A., Mackereth C.D., Cusack S., Sattler M.;
RT "Structure and RNA recognition by the snRNA and snoRNA transport
RT factor PHAX.";
RL RNA 16:1205-1216(2010).
CC -!- FUNCTION: A phosphoprotein adapter involved in the XPO1-mediated U
CC snRNA export from the nucleus. Bridge components required for U
CC snRNA export, the cap binding complex (CBC)-bound snRNA on the one
CC hand and the GTPase Ran in its active GTP-bound form together with
CC the export receptor XPO1 on the other. Its phosphorylation in the
CC nucleus is required for U snRNA export complex assembly and
CC export, while its dephosphorylation in the cytoplasm causes export
CC complex disassembly. It is recycled back to the nucleus via the
CC importin alpha/beta heterodimeric import receptor. The
CC directionality of nuclear export is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran
CC between the cytoplasm and nucleus. Its compartmentalized
CC phosphorylation cycle may also contribute to the directionality of
CC export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs
CC (snRNAs) in a sequence-unspecific manner and phosphorylation-
CC independent manner (By similarity). Plays also a role in the
CC biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3
CC snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly
CC to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to
CC trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to
CC telomerase RNA.
CC -!- SUBUNIT: Found in a U snRNA export complex with PHAX/RNUXA, NCBP1,
CC NCBP2, RAN, XPO1 and m7G-capped RNA. Part of a precomplex with
CC PHAX/RNUXA, NCBP1, NCBP2 and m7G-capped RNA. Interacts with NCBP1
CC (By similarity). Found in a complex with snoRNA.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, Cajal body.
CC Cytoplasm. Note=Located in the nucleoplasm and Cajal bodies.
CC Shuttles between the nucleus and the cytoplasm. Shuttles between
CC the nucleoplasm and Cajal bodies.
CC -!- PTM: Phosphorylated in the nucleus. Dephosphorylated in the
CC cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the PHAX family.
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DR EMBL; AK023255; BAB14489.1; -; mRNA.
DR EMBL; AK024065; BAB14809.1; -; mRNA.
DR EMBL; CR457305; CAG33586.1; -; mRNA.
DR EMBL; BC021161; AAH21161.1; -; mRNA.
DR RefSeq; NP_115553.2; NM_032177.3.
DR UniGene; Hs.555731; -.
DR UniGene; Hs.744042; -.
DR PDB; 2XC7; NMR; -; A=223-323.
DR PDBsum; 2XC7; -.
DR ProteinModelPortal; Q9H814; -.
DR SMR; Q9H814; 223-323.
DR IntAct; Q9H814; 14.
DR MINT; MINT-6781730; -.
DR STRING; 9606.ENSP00000297540; -.
DR TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
DR PhosphoSite; Q9H814; -.
DR DMDM; 74752718; -.
DR PaxDb; Q9H814; -.
DR PeptideAtlas; Q9H814; -.
DR PRIDE; Q9H814; -.
DR DNASU; 51808; -.
DR Ensembl; ENST00000297540; ENSP00000297540; ENSG00000164902.
DR GeneID; 51808; -.
DR KEGG; hsa:51808; -.
DR UCSC; uc003kua.2; human.
DR CTD; 51808; -.
DR GeneCards; GC05P125964; -.
DR HGNC; HGNC:10241; PHAX.
DR MIM; 604924; gene.
DR neXtProt; NX_Q9H814; -.
DR PharmGKB; PA164724444; -.
DR eggNOG; NOG326830; -.
DR HOGENOM; HOG000115525; -.
DR HOVERGEN; HBG058976; -.
DR InParanoid; Q9H814; -.
DR KO; K14291; -.
DR OMA; SQEHTKE; -.
DR OrthoDB; EOG7Q5HF9; -.
DR PhylomeDB; Q9H814; -.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RNUXA; -.
DR GenomeRNAi; 51808; -.
DR NextBio; 55936; -.
DR PMAP-CutDB; Q9H814; -.
DR PRO; PR:Q9H814; -.
DR Bgee; Q9H814; -.
DR CleanEx; HS_PHAX; -.
DR Genevestigator; Q9H814; -.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015643; F:toxic substance binding; IEA:Ensembl.
DR GO; GO:0034660; P:ncRNA metabolic process; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006408; P:snRNA export from nucleus; TAS:BHF-UCL.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; TAS:Reactome.
DR InterPro; IPR019385; PHAX_RNA-binding_domain.
DR Pfam; PF10258; RNA_GG_bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Nucleus;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW RNA-binding; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 394 Phosphorylated adapter RNA export
FT protein.
FT /FTId=PRO_0000239775.
FT REGION 2 329 Necessary for interaction with CBP80 (By
FT similarity).
FT REGION 228 328 Sufficient for poly U RNA-binding.
FT REGION 279 287 Necessary for poly U RNA-binding and
FT snRNA export (By similarity).
FT MOTIF 81 84 Nuclear localization signal (By
FT similarity).
FT MOTIF 130 139 Nuclear export signal (By similarity).
FT MOTIF 198 201 Nuclear localization signal (By
FT similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 296 296 Phosphothreonine.
FT MOD_RES 356 356 Phosphoserine.
FT VARIANT 82 82 R -> C (in dbSNP:rs3734173).
FT /FTId=VAR_051871.
FT CONFLICT 141 141 G -> A (in Ref. 1; BAB14489).
FT CONFLICT 346 346 D -> A (in Ref. 1; BAB14489).
FT HELIX 227 237
FT HELIX 243 253
FT HELIX 255 271
FT STRAND 277 281
FT HELIX 285 295
FT HELIX 301 308
SQ SEQUENCE 394 AA; 44403 MW; 3513FA5081C6F7CA CRC64;
MALEVGDMED GQLSDSDSDM TVAPSDRPLQ LPKVLGGDSA MRAFQNTATA CAPVSHYRAV
ESVDSSEESF SDSDDDSCLW KRKRQKCFNP PPKPEPFQFG QSSQKPPVAG GKKINNIWGA
VLQEQNQDAV ATELGILGME GTIDRSRQSE TYNYLLAKKL RKESQEHTKD LDKELDEYMH
GGKKMGSKEE ENGQGHLKRK RPVKDRLGNR PEMNYKGRYE ITAEDSQEKV ADEISFRLQE
PKKDLIARVV RIIGNKKAIE LLMETAEVEQ NGGLFIMNGS RRRTPGGVFL NLLKNTPSIS
EEQIKDIFYI ENQKEYENKK AARKRRTQVL GKKMKQAIKS LNFQEDDDTS RETFASDTNE
ALASLDESQE GHAEAKLEAE EAIEVDHSHD LDIF
//
ID PHAX_HUMAN Reviewed; 394 AA.
AC Q9H814; Q9H8W1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 95.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retinoblastoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION IN U3 SNORNA TRANSPORT, RNA-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15574332; DOI=10.1016/j.molcel.2004.11.013;
RA Boulon S., Verheggen C., Jady B.E., Girard C., Pescia C., Paul C.,
RA Ospina J.K., Kiss T., Matera A.G., Bordonne R., Bertrand E.;
RT "PHAX and CRM1 are required sequentially to transport U3 snoRNA to
RT nucleoli.";
RL Mol. Cell 16:777-787(2004).
RN [5]
RP SUBCELLULAR LOCATION.
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
RT PHAX is a novel RNA-binding domain that is essential for U snRNA
RT export.";
RL RNA 7:351-360(2001).
RN [6]
RP FUNCTION IN SNORNA TRANSPORT, AND IDENTIFICATION IN A COMPLEX WITH U3
RP SNORNA.
RX PubMed=15574333; DOI=10.1016/j.molcel.2004.11.012;
RA Watkins N.J., Lemm I., Ingelfinger D., Schneider C., Hossbach M.,
RA Urlaub H., Luehrmann R.;
RT "Assembly and maturation of the U3 snoRNP in the nucleoplasm in a
RT large dynamic multiprotein complex.";
RL Mol. Cell 16:789-798(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASS
RP SPECTROMETRY.
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT THR-296, MASS SPECTROMETRY, AND CLEAVAGE OF
RP INITIATOR METHIONINE.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-14, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP STRUCTURE BY NMR OF 223-323, AND RNA-BINDING REGION.
RX PubMed=20430857; DOI=10.1261/rna.2009910;
RA Mourao A., Varrot A., Mackereth C.D., Cusack S., Sattler M.;
RT "Structure and RNA recognition by the snRNA and snoRNA transport
RT factor PHAX.";
RL RNA 16:1205-1216(2010).
CC -!- FUNCTION: A phosphoprotein adapter involved in the XPO1-mediated U
CC snRNA export from the nucleus. Bridge components required for U
CC snRNA export, the cap binding complex (CBC)-bound snRNA on the one
CC hand and the GTPase Ran in its active GTP-bound form together with
CC the export receptor XPO1 on the other. Its phosphorylation in the
CC nucleus is required for U snRNA export complex assembly and
CC export, while its dephosphorylation in the cytoplasm causes export
CC complex disassembly. It is recycled back to the nucleus via the
CC importin alpha/beta heterodimeric import receptor. The
CC directionality of nuclear export is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran
CC between the cytoplasm and nucleus. Its compartmentalized
CC phosphorylation cycle may also contribute to the directionality of
CC export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs
CC (snRNAs) in a sequence-unspecific manner and phosphorylation-
CC independent manner (By similarity). Plays also a role in the
CC biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3
CC snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly
CC to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to
CC trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to
CC telomerase RNA.
CC -!- SUBUNIT: Found in a U snRNA export complex with PHAX/RNUXA, NCBP1,
CC NCBP2, RAN, XPO1 and m7G-capped RNA. Part of a precomplex with
CC PHAX/RNUXA, NCBP1, NCBP2 and m7G-capped RNA. Interacts with NCBP1
CC (By similarity). Found in a complex with snoRNA.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, Cajal body.
CC Cytoplasm. Note=Located in the nucleoplasm and Cajal bodies.
CC Shuttles between the nucleus and the cytoplasm. Shuttles between
CC the nucleoplasm and Cajal bodies.
CC -!- PTM: Phosphorylated in the nucleus. Dephosphorylated in the
CC cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the PHAX family.
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DR EMBL; AK023255; BAB14489.1; -; mRNA.
DR EMBL; AK024065; BAB14809.1; -; mRNA.
DR EMBL; CR457305; CAG33586.1; -; mRNA.
DR EMBL; BC021161; AAH21161.1; -; mRNA.
DR RefSeq; NP_115553.2; NM_032177.3.
DR UniGene; Hs.555731; -.
DR UniGene; Hs.744042; -.
DR PDB; 2XC7; NMR; -; A=223-323.
DR PDBsum; 2XC7; -.
DR ProteinModelPortal; Q9H814; -.
DR SMR; Q9H814; 223-323.
DR IntAct; Q9H814; 14.
DR MINT; MINT-6781730; -.
DR STRING; 9606.ENSP00000297540; -.
DR TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
DR PhosphoSite; Q9H814; -.
DR DMDM; 74752718; -.
DR PaxDb; Q9H814; -.
DR PeptideAtlas; Q9H814; -.
DR PRIDE; Q9H814; -.
DR DNASU; 51808; -.
DR Ensembl; ENST00000297540; ENSP00000297540; ENSG00000164902.
DR GeneID; 51808; -.
DR KEGG; hsa:51808; -.
DR UCSC; uc003kua.2; human.
DR CTD; 51808; -.
DR GeneCards; GC05P125964; -.
DR HGNC; HGNC:10241; PHAX.
DR MIM; 604924; gene.
DR neXtProt; NX_Q9H814; -.
DR PharmGKB; PA164724444; -.
DR eggNOG; NOG326830; -.
DR HOGENOM; HOG000115525; -.
DR HOVERGEN; HBG058976; -.
DR InParanoid; Q9H814; -.
DR KO; K14291; -.
DR OMA; SQEHTKE; -.
DR OrthoDB; EOG7Q5HF9; -.
DR PhylomeDB; Q9H814; -.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RNUXA; -.
DR GenomeRNAi; 51808; -.
DR NextBio; 55936; -.
DR PMAP-CutDB; Q9H814; -.
DR PRO; PR:Q9H814; -.
DR Bgee; Q9H814; -.
DR CleanEx; HS_PHAX; -.
DR Genevestigator; Q9H814; -.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015643; F:toxic substance binding; IEA:Ensembl.
DR GO; GO:0034660; P:ncRNA metabolic process; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006408; P:snRNA export from nucleus; TAS:BHF-UCL.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; TAS:Reactome.
DR InterPro; IPR019385; PHAX_RNA-binding_domain.
DR Pfam; PF10258; RNA_GG_bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Nucleus;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW RNA-binding; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 394 Phosphorylated adapter RNA export
FT protein.
FT /FTId=PRO_0000239775.
FT REGION 2 329 Necessary for interaction with CBP80 (By
FT similarity).
FT REGION 228 328 Sufficient for poly U RNA-binding.
FT REGION 279 287 Necessary for poly U RNA-binding and
FT snRNA export (By similarity).
FT MOTIF 81 84 Nuclear localization signal (By
FT similarity).
FT MOTIF 130 139 Nuclear export signal (By similarity).
FT MOTIF 198 201 Nuclear localization signal (By
FT similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 296 296 Phosphothreonine.
FT MOD_RES 356 356 Phosphoserine.
FT VARIANT 82 82 R -> C (in dbSNP:rs3734173).
FT /FTId=VAR_051871.
FT CONFLICT 141 141 G -> A (in Ref. 1; BAB14489).
FT CONFLICT 346 346 D -> A (in Ref. 1; BAB14489).
FT HELIX 227 237
FT HELIX 243 253
FT HELIX 255 271
FT STRAND 277 281
FT HELIX 285 295
FT HELIX 301 308
SQ SEQUENCE 394 AA; 44403 MW; 3513FA5081C6F7CA CRC64;
MALEVGDMED GQLSDSDSDM TVAPSDRPLQ LPKVLGGDSA MRAFQNTATA CAPVSHYRAV
ESVDSSEESF SDSDDDSCLW KRKRQKCFNP PPKPEPFQFG QSSQKPPVAG GKKINNIWGA
VLQEQNQDAV ATELGILGME GTIDRSRQSE TYNYLLAKKL RKESQEHTKD LDKELDEYMH
GGKKMGSKEE ENGQGHLKRK RPVKDRLGNR PEMNYKGRYE ITAEDSQEKV ADEISFRLQE
PKKDLIARVV RIIGNKKAIE LLMETAEVEQ NGGLFIMNGS RRRTPGGVFL NLLKNTPSIS
EEQIKDIFYI ENQKEYENKK AARKRRTQVL GKKMKQAIKS LNFQEDDDTS RETFASDTNE
ALASLDESQE GHAEAKLEAE EAIEVDHSHD LDIF
//
MIM
604924
*RECORD*
*FIELD* NO
604924
*FIELD* TI
*604924 RNA, U SMALL NUCLEAR, EXPORT ADAPTOR; RNUXA
;;PHOSPHORYLATED ADAPTOR FOR RNA EXPORT; PHAX
read more*FIELD* TX
In metazoa, assembly of spliceosomal U small nuclear ribonucleoprotein
particles (snRNPs) requires nuclear export of U snRNA precursors. Export
depends upon the RNA cap structure, nuclear cap-binding complex (see
NCBP1; 600469), the export receptor CRM1 (XPO1; 602559), and RanGTP (see
RANGAP1; 602362). These components are, however, insufficient to support
U snRNA export. In mouse, Ohno et al. (2000) identified Phax
(phosphorylated adaptor for RNA export) as the additional factor
required for U snRNA export complex assembly in vitro. In vivo, Phax is
required for U snRNA export but not for Crm1-mediated export in general.
Phax is phosphorylated in the nucleus and then exported with RNA to the
cytoplasm, where it is dephosphorylated. Phax phosphorylation is
essential for export complex assembly, while its dephosphorylation
causes export complex disassembly. The compartmentalized Phax
phosphorylation cycle can contribute to the directionality of export.
Several human ESTs share more than 90% homology with the mouse Phax
gene, indicating that a homologous PHAX gene exists in the human genome.
*FIELD* RF
1. Ohno, M.; Segref, A.; Bachi, A.; Wilm, M.; Mattaj, I. W.: PHAX,
a mediator of U snRNA nuclear export whose activity is regulated by
phosphorylation. Cell 101: 187-198, 2000.
*FIELD* CD
Stylianos E. Antonarakis: 5/5/2000
*FIELD* ED
mgross: 07/23/2001
mgross: 5/5/2000
*RECORD*
*FIELD* NO
604924
*FIELD* TI
*604924 RNA, U SMALL NUCLEAR, EXPORT ADAPTOR; RNUXA
;;PHOSPHORYLATED ADAPTOR FOR RNA EXPORT; PHAX
read more*FIELD* TX
In metazoa, assembly of spliceosomal U small nuclear ribonucleoprotein
particles (snRNPs) requires nuclear export of U snRNA precursors. Export
depends upon the RNA cap structure, nuclear cap-binding complex (see
NCBP1; 600469), the export receptor CRM1 (XPO1; 602559), and RanGTP (see
RANGAP1; 602362). These components are, however, insufficient to support
U snRNA export. In mouse, Ohno et al. (2000) identified Phax
(phosphorylated adaptor for RNA export) as the additional factor
required for U snRNA export complex assembly in vitro. In vivo, Phax is
required for U snRNA export but not for Crm1-mediated export in general.
Phax is phosphorylated in the nucleus and then exported with RNA to the
cytoplasm, where it is dephosphorylated. Phax phosphorylation is
essential for export complex assembly, while its dephosphorylation
causes export complex disassembly. The compartmentalized Phax
phosphorylation cycle can contribute to the directionality of export.
Several human ESTs share more than 90% homology with the mouse Phax
gene, indicating that a homologous PHAX gene exists in the human genome.
*FIELD* RF
1. Ohno, M.; Segref, A.; Bachi, A.; Wilm, M.; Mattaj, I. W.: PHAX,
a mediator of U snRNA nuclear export whose activity is regulated by
phosphorylation. Cell 101: 187-198, 2000.
*FIELD* CD
Stylianos E. Antonarakis: 5/5/2000
*FIELD* ED
mgross: 07/23/2001
mgross: 5/5/2000