UIF_HUMAN - dbPTM
UIF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UIF_HUMAN
UniProt AC Q96QD9
Protein Name UAP56-interacting factor
Gene Name FYTTD1
Organism Homo sapiens (Human).
Sequence Length 318
Subcellular Localization Nucleus, nucleoplasm . Nucleus speckle .
Protein Description Required for mRNA export from the nucleus to the cytoplasm. Acts as an adapter that uses the DDX39B/UAP56-NFX1 pathway to ensure efficient mRNA export and delivering to the nuclear pore. Associates with spliced and unspliced mRNAs simultaneously with ALYREF/THOC4..
Protein Sequence MNRFGTRLVGATATSSPPPKARSNENLDKIDMSLDDIIKLNRKEGKKQNFPRLNRRLLQQSGAQQFRMRVRWGIQQNSGFGKTSLNRRGRVMPGKRRPNGVITGLAARKTTGIRKGISPMNRPPLSDKNIEQYFPVLKRKANLLRQNEGQRKPVAVLKRPSQLSRKNNIPANFTRSGNKLNHQKDTRQATFLFRRGLKVQAQLNTEQLLDDVVAKRTRQWRTSTTNGGILTVSIDNPGAVQCPVTQKPRLTRTAVPSFLTKREQSDVKKVPKGVPLQFDINSVGKQTGMTLNERFGILKEQRATLTYNKGGSRFVTVG
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
1Acetylation-------MNRFGTRL
-------CCCCCCCC
7.9819413330
6Phosphorylation--MNRFGTRLVGATA
--CCCCCCCCCCCCC
20.3730576142
12PhosphorylationGTRLVGATATSSPPP
CCCCCCCCCCCCCCC
25.2530266825
14PhosphorylationRLVGATATSSPPPKA
CCCCCCCCCCCCCCC
25.9430266825
15PhosphorylationLVGATATSSPPPKAR
CCCCCCCCCCCCCCC
38.0829255136
16PhosphorylationVGATATSSPPPKARS
CCCCCCCCCCCCCCC
36.7529255136
20UbiquitinationATSSPPPKARSNENL
CCCCCCCCCCCCCCH
63.31-
23PhosphorylationSPPPKARSNENLDKI
CCCCCCCCCCCHHHH
54.0430266825
33PhosphorylationNLDKIDMSLDDIIKL
CHHHHCCCHHHHHHH
25.5423403867
39UbiquitinationMSLDDIIKLNRKEGK
CCHHHHHHHHHHCHH
39.79-
61PhosphorylationNRRLLQQSGAQQFRM
HHHHHHHHCCHHHHH
24.1222115753
118 (in isoform 4)Phosphorylation-27.1125056879
118PhosphorylationTGIRKGISPMNRPPL
CCCCCCCCCCCCCCC
27.1130266825
126PhosphorylationPMNRPPLSDKNIEQY
CCCCCCCCCCCHHHH
52.9230266825
138UbiquitinationEQYFPVLKRKANLLR
HHHHHHHHHHHHHHH
52.68-
140SumoylationYFPVLKRKANLLRQN
HHHHHHHHHHHHHHC
39.79-
140AcetylationYFPVLKRKANLLRQN
HHHHHHHHHHHHHHC
39.797677927
140SumoylationYFPVLKRKANLLRQN
HHHHHHHHHHHHHHC
39.7928112733
152AcetylationRQNEGQRKPVAVLKR
HHCCCCCCCEEEECC
35.647677937
161PhosphorylationVAVLKRPSQLSRKNN
EEEECCHHHHHHCCC
48.0330266825
166UbiquitinationRPSQLSRKNNIPANF
CHHHHHHCCCCCCCC
51.47-
179UbiquitinationNFTRSGNKLNHQKDT
CCCCCCCCCCCCCCH
54.94-
205PhosphorylationKVQAQLNTEQLLDDV
CEEEECCHHHHHHHH
33.43-
215UbiquitinationLLDDVVAKRTRQWRT
HHHHHHHHHCCCCCC
42.57-
235AcetylationGILTVSIDNPGAVQC
CEEEEEECCCCCEEC
48.0019413330
253PhosphorylationQKPRLTRTAVPSFLT
CCCCCCCCCCCCHHH
27.1128555341
257PhosphorylationLTRTAVPSFLTKREQ
CCCCCCCCHHHHHCH
26.7023898821
260PhosphorylationTAVPSFLTKREQSDV
CCCCCHHHHHCHHCC
26.5023898821
261UbiquitinationAVPSFLTKREQSDVK
CCCCHHHHHCHHCCC
56.9619413330
261AcetylationAVPSFLTKREQSDVK
CCCCHHHHHCHHCCC
56.9619413330
282PhosphorylationPLQFDINSVGKQTGM
CCEEEECCHHHHHCC
32.3621406692
290PhosphorylationVGKQTGMTLNERFGI
HHHHHCCCHHHHHCC
27.98-
299UbiquitinationNERFGILKEQRATLT
HHHHCCCHHCEEEEE
50.29-
304PhosphorylationILKEQRATLTYNKGG
CCHHCEEEEEEECCC
23.0924173317
309UbiquitinationRATLTYNKGGSRFVT
EEEEEEECCCCEEEE
54.99-

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
205TPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UIF_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 UIF_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DX39B_HUMANDDX39Bphysical
19836239
NXF1_HUMANNXF1physical
19836239
HTSF1_HUMANHTATSF1physical
19836239
NUCL_HUMANNCLphysical
19836239
SSRP1_HUMANSSRP1physical
19836239
UIF_HUMANFYTTD1physical
19836239
TBB5_HUMANTUBBphysical
19836239
PAIRB_HUMANSERBP1physical
19836239
STRAP_HUMANSTRAPphysical
19836239
C1QBP_HUMANC1QBPphysical
19836239
AN32E_HUMANANP32Ephysical
19836239
SET_HUMANSETphysical
19836239
SP16H_HUMANSUPT16Hphysical
19836239
PALM_HUMANPALMphysical
26186194
PLSI_HUMANPLS1physical
26186194
ERIC5_HUMANERICH5physical
26186194
GBG10_HUMANGNG10physical
26186194
PTPRG_HUMANPTPRGphysical
26186194
GNAZ_HUMANGNAZphysical
26186194
GNA11_HUMANGNA11physical
26186194
GNAQ_HUMANGNAQphysical
26186194
GNA13_HUMANGNA13physical
26186194
YES_HUMANYES1physical
26186194
SRC_HUMANSRCphysical
26186194
CHTOP_HUMANCHTOPphysical
26186194
LASP1_HUMANLASP1physical
26186194
UBA6_HUMANUBA6physical
26186194
EEPD1_HUMANEEPD1physical
26186194
CYB5_HUMANCYB5Aphysical
26186194
GBG5_HUMANGNG5physical
26186194
CCNY_HUMANCCNYphysical
26186194
CCYL1_HUMANCCNYL1physical
26186194
PRRC1_HUMANPRRC1physical
26186194
GBG7_HUMANGNG7physical
26186194
EPCR_HUMANPROCRphysical
26186194
TARA_HUMANTRIOBPphysical
26186194
CHTOP_HUMANCHTOPphysical
28514442
CCYL1_HUMANCCNYL1physical
28514442
ERIC5_HUMANERICH5physical
28514442
LASP1_HUMANLASP1physical
28514442
OCC1_HUMANC12orf75physical
28514442
PTPRG_HUMANPTPRGphysical
28514442
PLSI_HUMANPLS1physical
28514442
GNAQ_HUMANGNAQphysical
28514442
SRC_HUMANSRCphysical
28514442
UBA6_HUMANUBA6physical
28514442
EEPD1_HUMANEEPD1physical
28514442
PRRC1_HUMANPRRC1physical
28514442
XRCC4_HUMANXRCC4physical
28514442
GBG5_HUMANGNG5physical
28514442
PALM_HUMANPALMphysical
28514442
GBG10_HUMANGNG10physical
28514442
TARA_HUMANTRIOBPphysical
28514442
PMVK_HUMANPMVKphysical
28514442
GNAZ_HUMANGNAZphysical
28514442

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 UIF_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-15 AND SER-16, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-15 AND SER-16, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY.

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