PHAX_HUMAN - dbPTM
PHAX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHAX_HUMAN
UniProt AC Q9H814
Protein Name Phosphorylated adapter RNA export protein
Gene Name PHAX
Organism Homo sapiens (Human).
Sequence Length 394
Subcellular Localization Nucleus, nucleoplasm . Nucleus, Cajal body . Cytoplasm . Located in the nucleoplasm and Cajal bodies. Shuttles between the nucleus and the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies.
Protein Description 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 MALEVGDMEDGQLSDSDSDMTVAPSDRPLQLPKVLGGDSAMRAFQNTATACAPVSHYRAVESVDSSEESFSDSDDDSCLWKRKRQKCFNPPPKPEPFQFGQSSQKPPVAGGKKINNIWGAVLQEQNQDAVATELGILGMEGTIDRSRQSETYNYLLAKKLRKESQEHTKDLDKELDEYMHGGKKMGSKEEENGQGHLKRKRPVKDRLGNRPEMNYKGRYEITAEDSQEKVADEISFRLQEPKKDLIARVVRIIGNKKAIELLMETAEVEQNGGLFIMNGSRRRTPGGVFLNLLKNTPSISEEQIKDIFYIENQKEYENKKAARKRRTQVLGKKMKQAIKSLNFQEDDDTSRETFASDTNEALASLDESQEGHAEAKLEAEEAIEVDHSHDLDIF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MALEVGDME
------CCCEECCCC		16.6621406692
14PhosphorylationDMEDGQLSDSDSDMT
CCCCCCCCCCCCCCC		27.4725159151
16PhosphorylationEDGQLSDSDSDMTVA
CCCCCCCCCCCCCCC		35.3225159151
18PhosphorylationGQLSDSDSDMTVAPS
CCCCCCCCCCCCCCC		32.9825159151
21PhosphorylationSDSDSDMTVAPSDRP
CCCCCCCCCCCCCCC		20.6422617229
25PhosphorylationSDMTVAPSDRPLQLP
CCCCCCCCCCCCCCC		36.1923663014
39PhosphorylationPKVLGGDSAMRAFQN
CCCCCCHHHHHHHHH		27.5221815630
47PhosphorylationAMRAFQNTATACAPV
HHHHHHHHHCCCCCC		18.0128555341
55PhosphorylationATACAPVSHYRAVES
HCCCCCCCHHEEEEC		17.4729978859
57PhosphorylationACAPVSHYRAVESVD
CCCCCCHHEEEECCC		7.8629978859
62PhosphorylationSHYRAVESVDSSEES
CHHEEEECCCCCCCC		25.3227251275
65PhosphorylationRAVESVDSSEESFSD
EEEECCCCCCCCCCC		37.1825137130
66PhosphorylationAVESVDSSEESFSDS
EEECCCCCCCCCCCC		40.7025137130
69PhosphorylationSVDSSEESFSDSDDD
CCCCCCCCCCCCCCC		26.4625137130
71PhosphorylationDSSEESFSDSDDDSC
CCCCCCCCCCCCCCC		45.5525137130
73PhosphorylationSEESFSDSDDDSCLW
CCCCCCCCCCCCCHH		41.5625137130
77PhosphorylationFSDSDDDSCLWKRKR
CCCCCCCCCHHHHHH		20.3627251275
102PhosphorylationEPFQFGQSSQKPPVA
CCCCCCCCCCCCCCC		34.8125159151
103PhosphorylationPFQFGQSSQKPPVAG
CCCCCCCCCCCCCCC		34.0425627689
105AcetylationQFGQSSQKPPVAGGK
CCCCCCCCCCCCCCC		53.9225953088
112AcetylationKPPVAGGKKINNIWG
CCCCCCCCEECCHHH		49.9526051181
146PhosphorylationMEGTIDRSRQSETYN
CCCCCCCHHHHHHHH		30.8121712546
149PhosphorylationTIDRSRQSETYNYLL
CCCCHHHHHHHHHHH		30.6928796482
151PhosphorylationDRSRQSETYNYLLAK
CCHHHHHHHHHHHHH		23.4728796482
152PhosphorylationRSRQSETYNYLLAKK
CHHHHHHHHHHHHHH		9.5828796482
154PhosphorylationRQSETYNYLLAKKLR
HHHHHHHHHHHHHHH		7.8428796482
164PhosphorylationAKKLRKESQEHTKDL
HHHHHHHHHHHHHHH		43.8530108239
168PhosphorylationRKESQEHTKDLDKEL
HHHHHHHHHHHHHHH		26.0430108239
169"N6,N6-dimethyllysine"KESQEHTKDLDKELD
HHHHHHHHHHHHHHH		59.19-
169MethylationKESQEHTKDLDKELD
HHHHHHHHHHHHHHH		59.19-
178PhosphorylationLDKELDEYMHGGKKM
HHHHHHHHHCCCCCC		8.2829978859
183AcetylationDEYMHGGKKMGSKEE
HHHHCCCCCCCCCCC		44.1525953088
184AcetylationEYMHGGKKMGSKEEE
HHHCCCCCCCCCCCC		52.3330583977
187PhosphorylationHGGKKMGSKEEENGQ
CCCCCCCCCCCCCCC		33.1429214152
216UbiquitinationNRPEMNYKGRYEITA
CCCCCCCCCCEEEEC		31.7224816145
222PhosphorylationYKGRYEITAEDSQEK
CCCCEEEECCCHHHH		16.4427251275
226PhosphorylationYEITAEDSQEKVADE
EEEECCCHHHHHHHH		31.5717525332
242UbiquitinationSFRLQEPKKDLIARV
HHHCCCCCHHHHHHH		59.1624816145
284PhosphorylationMNGSRRRTPGGVFLN
ECCCCCCCCCCHHHH		25.1928555341
296PhosphorylationFLNLLKNTPSISEEQ
HHHHHHCCCCCCHHH		19.4725159151
316PhosphorylationYIENQKEYENKKAAR
EECCHHHHCCHHHHH		31.6627251275
327PhosphorylationKAARKRRTQVLGKKM
HHHHHHHHHHHHHHH		27.36-
332AcetylationRRTQVLGKKMKQAIK
HHHHHHHHHHHHHHH		45.6025953088
339UbiquitinationKKMKQAIKSLNFQED
HHHHHHHHHCCCCCC		52.4829967540
340PhosphorylationKMKQAIKSLNFQEDD
HHHHHHHHCCCCCCC		23.5628450419
349PhosphorylationNFQEDDDTSRETFAS
CCCCCCCCCCHHHHH		36.3623927012
350PhosphorylationFQEDDDTSRETFASD
CCCCCCCCCHHHHHH		34.8025159151
353PhosphorylationDDDTSRETFASDTNE
CCCCCCHHHHHHHHH		24.3230266825
356PhosphorylationTSRETFASDTNEALA
CCCHHHHHHHHHHHH		40.5530266825
358PhosphorylationRETFASDTNEALASL
CHHHHHHHHHHHHCC		32.2530266825
364PhosphorylationDTNEALASLDESQEG
HHHHHHHCCCHHHCC		36.8830266825
368PhosphorylationALASLDESQEGHAEA
HHHCCCHHHCCCHHH		32.9530266825
388PhosphorylationEAIEVDHSHDLDIF-
HHHCCCCCCCCCCC-		17.7730266825
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PHAX_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHAX_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PHAX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CALD1_HUMANCALD1physical
22863883
ENPL_HUMANHSP90B1physical
22863883
IMA5_HUMANKPNA1physical
26496610
NCBP1_HUMANNCBP1physical
26496610
RL10_HUMANRPL10physical
26496610
SSRP1_HUMANSSRP1physical
26496610
TNR1A_HUMANTNFRSF1Aphysical
26496610
XYLK_HUMANFAM20Bphysical
26496610
SPAS2_HUMANSPATS2physical
26496610
REEP4_HUMANREEP4physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHAX_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.

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