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Protein

Phosphorylated adapter RNA export protein

Gene

PHAX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Plays also a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA.By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-191859. snRNP Assembly.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.

Protein family/group databases

TCDBi9.A.60.1.1. the small nuclear rna exporter (snrna-e).

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphorylated adapter RNA export protein
Alternative name(s):
RNA U small nuclear RNA export adapter protein
Gene namesi
Name:PHAX
Synonyms:RNUXA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:10241. PHAX.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164724444.

Polymorphism and mutation databases

BioMutaiPHAX.
DMDMi74752718.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 394393Phosphorylated adapter RNA export proteinPRO_0000239775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei65 – 651PhosphoserineBy similarity
Modified residuei66 – 661PhosphoserineBy similarity
Modified residuei69 – 691PhosphoserineBy similarity
Modified residuei73 – 731PhosphoserineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei296 – 2961PhosphothreonineCombined sources
Modified residuei356 – 3561PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated in the nucleus. Dephosphorylated in the cytoplasm (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H814.
MaxQBiQ9H814.
PaxDbiQ9H814.
PeptideAtlasiQ9H814.
PRIDEiQ9H814.

PTM databases

iPTMnetiQ9H814.
PhosphoSiteiQ9H814.

Miscellaneous databases

PMAP-CutDBQ9H814.

Expressioni

Gene expression databases

BgeeiQ9H814.
CleanExiHS_PHAX.
GenevisibleiQ9H814. HS.

Interactioni

Subunit structurei

Found in a U snRNA export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Part of a precomplex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20 and m7G-capped RNA. Interacts with NCBP1/CBP80 (By similarity). Found in a complex with snoRNA. Interacts with NCBP2/CBP20 (PubMed:26382858).By similarity2 Publications

Protein-protein interaction databases

BioGridi119734. 50 interactions.
IntActiQ9H814. 31 interactions.
MINTiMINT-6781730.
STRINGi9606.ENSP00000297540.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi227 – 23711Combined sources
Helixi243 – 25311Combined sources
Helixi255 – 27117Combined sources
Beta strandi277 – 2815Combined sources
Helixi285 – 29511Combined sources
Helixi301 – 3088Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XC7NMR-A223-323[»]
ProteinModelPortaliQ9H814.
SMRiQ9H814. Positions 223-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 329328Necessary for interaction with CBP80By similarityAdd
BLAST
Regioni228 – 328101Sufficient for poly U RNA-bindingAdd
BLAST
Regioni279 – 2879Necessary for poly U RNA-binding and snRNA exportBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi81 – 844Nuclear localization signalBy similarity
Motifi130 – 13910Nuclear export signalBy similarity
Motifi198 – 2014Nuclear localization signalBy similarity

Sequence similaritiesi

Belongs to the PHAX family.Curated

Phylogenomic databases

eggNOGiKOG3948. Eukaryota.
ENOG4110D9C. LUCA.
GeneTreeiENSGT00390000011084.
HOGENOMiHOG000115525.
HOVERGENiHBG058976.
InParanoidiQ9H814.
KOiK14291.
OMAiDAGDMED.
OrthoDBiEOG7Q5HF9.
PhylomeDBiQ9H814.
TreeFamiTF321050.

Family and domain databases

InterProiIPR019385. PHAX_RNA-binding_domain.
[Graphical view]
PfamiPF10258. RNA_GG_bind. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9H814-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALEVGDMED GQLSDSDSDM TVAPSDRPLQ LPKVLGGDSA MRAFQNTATA
60 70 80 90 100
CAPVSHYRAV ESVDSSEESF SDSDDDSCLW KRKRQKCFNP PPKPEPFQFG
110 120 130 140 150
QSSQKPPVAG GKKINNIWGA VLQEQNQDAV ATELGILGME GTIDRSRQSE
160 170 180 190 200
TYNYLLAKKL RKESQEHTKD LDKELDEYMH GGKKMGSKEE ENGQGHLKRK
210 220 230 240 250
RPVKDRLGNR PEMNYKGRYE ITAEDSQEKV ADEISFRLQE PKKDLIARVV
260 270 280 290 300
RIIGNKKAIE LLMETAEVEQ NGGLFIMNGS RRRTPGGVFL NLLKNTPSIS
310 320 330 340 350
EEQIKDIFYI ENQKEYENKK AARKRRTQVL GKKMKQAIKS LNFQEDDDTS
360 370 380 390
RETFASDTNE ALASLDESQE GHAEAKLEAE EAIEVDHSHD LDIF
Length:394
Mass (Da):44,403
Last modified:March 1, 2001 - v1
Checksum:i3513FA5081C6F7CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411G → A in BAB14489 (PubMed:14702039).Curated
Sequence conflicti346 – 3461D → A in BAB14489 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821R → C.
Corresponds to variant rs3734173 [ dbSNP | Ensembl ].
VAR_051871

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023255 mRNA. Translation: BAB14489.1.
AK024065 mRNA. Translation: BAB14809.1.
CR457305 mRNA. Translation: CAG33586.1.
BC021161 mRNA. Translation: AAH21161.1.
CCDSiCCDS4138.1.
RefSeqiNP_115553.2. NM_032177.3.
UniGeneiHs.555731.
Hs.744042.

Genome annotation databases

EnsembliENST00000297540; ENSP00000297540; ENSG00000164902.
GeneIDi51808.
KEGGihsa:51808.
UCSCiuc003kua.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023255 mRNA. Translation: BAB14489.1.
AK024065 mRNA. Translation: BAB14809.1.
CR457305 mRNA. Translation: CAG33586.1.
BC021161 mRNA. Translation: AAH21161.1.
CCDSiCCDS4138.1.
RefSeqiNP_115553.2. NM_032177.3.
UniGeneiHs.555731.
Hs.744042.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XC7NMR-A223-323[»]
ProteinModelPortaliQ9H814.
SMRiQ9H814. Positions 223-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119734. 50 interactions.
IntActiQ9H814. 31 interactions.
MINTiMINT-6781730.
STRINGi9606.ENSP00000297540.

Protein family/group databases

TCDBi9.A.60.1.1. the small nuclear rna exporter (snrna-e).

PTM databases

iPTMnetiQ9H814.
PhosphoSiteiQ9H814.

Polymorphism and mutation databases

BioMutaiPHAX.
DMDMi74752718.

Proteomic databases

EPDiQ9H814.
MaxQBiQ9H814.
PaxDbiQ9H814.
PeptideAtlasiQ9H814.
PRIDEiQ9H814.

Protocols and materials databases

DNASUi51808.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297540; ENSP00000297540; ENSG00000164902.
GeneIDi51808.
KEGGihsa:51808.
UCSCiuc003kua.3. human.

Organism-specific databases

CTDi51808.
GeneCardsiPHAX.
HGNCiHGNC:10241. PHAX.
MIMi604924. gene.
neXtProtiNX_Q9H814.
PharmGKBiPA164724444.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3948. Eukaryota.
ENOG4110D9C. LUCA.
GeneTreeiENSGT00390000011084.
HOGENOMiHOG000115525.
HOVERGENiHBG058976.
InParanoidiQ9H814.
KOiK14291.
OMAiDAGDMED.
OrthoDBiEOG7Q5HF9.
PhylomeDBiQ9H814.
TreeFamiTF321050.

Enzyme and pathway databases

ReactomeiR-HSA-191859. snRNP Assembly.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.

Miscellaneous databases

ChiTaRSiPHAX. human.
GeneWikiiRNUXA.
GenomeRNAii51808.
PMAP-CutDBQ9H814.
PROiQ9H814.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H814.
CleanExiHS_PHAX.
GenevisibleiQ9H814. HS.

Family and domain databases

InterProiIPR019385. PHAX_RNA-binding_domain.
[Graphical view]
PfamiPF10258. RNA_GG_bind. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Retinoblastoma.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  4. "PHAX and CRM1 are required sequentially to transport U3 snoRNA to nucleoli."
    Boulon S., Verheggen C., Jady B.E., Girard C., Pescia C., Paul C., Ospina J.K., Kiss T., Matera A.G., Bordonne R., Bertrand E.
    Mol. Cell 16:777-787(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN U3 SNORNA TRANSPORT, RNA-BINDING, SUBCELLULAR LOCATION.
  5. "The evolutionarily conserved region of the U snRNA export mediator PHAX is a novel RNA-binding domain that is essential for U snRNA export."
    Segref A., Mattaj I.W., Ohno M.
    RNA 7:351-360(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex."
    Watkins N.J., Lemm I., Ingelfinger D., Schneider C., Hossbach M., Urlaub H., Luehrmann R.
    Mol. Cell 16:789-798(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SNORNA TRANSPORT, IDENTIFICATION IN A COMPLEX WITH U3 SNORNA.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-296, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "mRNA export through an additional cap-binding complex consisting of NCBP1 and NCBP3."
    Gebhardt A., Habjan M., Benda C., Meiler A., Haas D.A., Hein M.Y., Mann A., Mann M., Habermann B., Pichlmair A.
    Nat. Commun. 6:8192-8192(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCBP2.
  13. "Structure and RNA recognition by the snRNA and snoRNA transport factor PHAX."
    Mourao A., Varrot A., Mackereth C.D., Cusack S., Sattler M.
    RNA 16:1205-1216(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 223-323, RNA-BINDING REGION.

Entry informationi

Entry nameiPHAX_HUMAN
AccessioniPrimary (citable) accession number: Q9H814
Secondary accession number(s): Q9H8W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.