Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Phosphorylated adapter RNA export protein  

UniProtKB / Swiss-Prot ID :  PHAX_HUMAN

Gene Name (Synonyms) : 
PHAX, RNUXA  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus, nucleoplasm. Nucleus, Cajal body. Cytoplasm. Note=Located in the nucleoplasm and Cajal bodies. Shuttles between the nucleus and the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies. 

Protein Function :  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. 

Protein Sequence MALEVGDMEDGQLSDSDSDMTVAPSDRPLQLPKVLGGDSAMRAFQNTATACAPVSHYRAVESVDSSEESF...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
82R -> C (in dbSNP:rs3734173). VAR_051871
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
14PhosphoserineDGQLSDSDS
27.47HPRD
Link-
14PhosphoserineDGQLSDSDS
27.47PhosphoELM
Link-
14PhosphoserineDGQLSDSDS
27.47Phosphositeplus
Link-
14PhosphoserineDGQLSDSDS
27.47SysPTM
Link-
16PhosphoserineQLSDSDSDM
35.32HPRD
Link-
16PhosphoserineQLSDSDSDM
35.32PhosphoELM
Link-
16PhosphoserineQLSDSDSDM
35.32Phosphositeplus
Link-
16PhosphoserineQLSDSDSDM
35.32SysPTM
Link-
18PhosphoserineSDSDSDMTV
32.98HPRD
Link-
18PhosphoserineSDSDSDMTV
32.98SysPTM
Link-
21PhosphothreonineDSDMTVAPS
20.64HPRD
Link-
21PhosphothreonineDSDMTVAPS
20.64SysPTM
Link-
57PhosphotyrosinePVSHYRAVE
7.86Phosphositeplus
Link-
62PhosphoserineRAVESVDSS
25.32SysPTM
Link-
65PhosphoserineESVDSSEES
37.18PhosphoELM
Link-
65PhosphoserineESVDSSEES
37.18SysPTM
Link-
66PhosphoserineSVDSSEESF
40.70PhosphoELM
Link-
66PhosphoserineSVDSSEESF
40.70SysPTM
Link-
69PhosphoserineSSEESFSDS
26.46PhosphoELM
Link-
69PhosphoserineSSEESFSDS
26.46SysPTM
Link-
71PhosphoserineEESFSDSDD
45.55PhosphoELM
Link-
71PhosphoserineEESFSDSDD
45.55SysPTM
Link-
73PhosphoserineSFSDSDDDS
41.56PhosphoELM
Link-
73PhosphoserineSFSDSDDDS
41.56SysPTM
Link-
77PhosphoserineSDDDSCLWK
20.36SysPTM
Link-
164PhosphoserineLRKESQEHT
43.85HPRD
Link-
226PhosphoserineTAEDSQEKV
31.57HPRD
Link
226PhosphoserineTAEDSQEKV
31.57Phosphositeplus
Link
226Phosphoserine.TAEDSQEKV
31.57UniProtKB
Link
296PhosphothreonineLLKNTPSIS
19.47HPRD
Link
296PhosphothreonineLLKNTPSIS
19.47Phosphositeplus
Link
349PhosphothreonineEDDDTSRET
36.36HPRD
Link-
349PhosphothreonineEDDDTSRET
36.36PhosphoELM
Link-
349PhosphothreonineEDDDTSRET
36.36SysPTM
Link-
350PhosphoserineDDDTSRETF
34.80HPRD
Link-
350PhosphoserineDDDTSRETF
34.80PhosphoELM
Link-
350PhosphoserineDDDTSRETF
34.80SysPTM
Link-
353PhosphothreonineTSRETFASD
24.32SysPTM
Link-
356PhosphoserineETFASDTNE
40.55HPRD
Link-
356PhosphoserineETFASDTNE
40.55PhosphoELM
Link-
356PhosphoserineETFASDTNE
40.55Phosphositeplus
Link-
356PhosphoserineETFASDTNE
40.55SysPTM
Link-
356Phosphoserine.ETFASDTNE
40.55UniProtKB
Link-
358PhosphothreonineFASDTNEAL
32.25SysPTM
Link-
364PhosphoserineEALASLDES
36.88SysPTM
Link-
368PhosphoserineSLDESQEGH
32.95SysPTM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures