TIA1_HUMAN - dbPTM
TIA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIA1_HUMAN
UniProt AC P31483
Protein Name Nucleolysin TIA-1 isoform p40
Gene Name TIA1
Organism Homo sapiens (Human).
Sequence Length 386
Subcellular Localization Cytoplasm, Stress granule . Nucleus . Accumulates in cytoplasmic stress granules (SG) following cellular damage.
Protein Description Involved in alternative pre-RNA splicing and regulation of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs). Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis..
Protein Sequence MEDEMPKTLYVGNLSRDVTEALILQLFSQIGPCKNCKMIMDTAGNDPYCFVEFHEHRHAAAALAAMNGRKIMGKEVKVNWATTPSSQKKDTSSSTVVSTQRSQDHFHVFVGDLSPEITTEDIKAAFAPFGRISDARVVKDMATGKSKGYGFVSFFNKWDAENAIQQMGGQWLGGRQIRTNWATRKPPAPKSTYESNTKQLSYDEVVNQSSPSNCTVYCGGVTSGLTEQLMRQTFSPFGQIMEIRVFPDKGYSFVRFNSHESAAHAIVSVNGTTIEGHVVKCYWGKETLDMINPVQQQNQIGYPQPYGQWGQWYGNAQQIGQYMPNGWQVPAYGMYGQAWNQQGFNQTQSSAPWMGPNYGVQPPQGQNGSMLPNQPSGYRVAGYETQ
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-------MEDEMPKT
-------CCCCCCCE		15.3522814378
8PhosphorylationMEDEMPKTLYVGNLS
CCCCCCCEEEECCCC		19.9028152594
10PhosphorylationDEMPKTLYVGNLSRD
CCCCCEEEECCCCHH		16.1428152594
12UbiquitinationMPKTLYVGNLSRDVT
CCCEEEECCCCHHHH		18.7932142685
15PhosphorylationTLYVGNLSRDVTEAL
EEEECCCCHHHHHHH		30.3628152594
23UbiquitinationRDVTEALILQLFSQI
HHHHHHHHHHHHHHH		2.7227667366
40UbiquitinationCKNCKMIMDTAGNDP
CCCCCEEEECCCCCC		3.1532142685
42UbiquitinationNCKMIMDTAGNDPYC
CCCEEEECCCCCCEE		21.0532142685
48PhosphorylationDTAGNDPYCFVEFHE
ECCCCCCEEEEEECC		11.0327811184
51UbiquitinationGNDPYCFVEFHEHRH
CCCCEEEEEECCHHH		7.3927667366
53UbiquitinationDPYCFVEFHEHRHAA
CCEEEEEECCHHHHH		7.4332015554
77UbiquitinationKIMGKEVKVNWATTP
EECCEEEEEEEECCC		30.8332142685
79UbiquitinationMGKEVKVNWATTPSS
CCEEEEEEEECCCCC		19.5632142685
82PhosphorylationEVKVNWATTPSSQKK
EEEEEEECCCCCCCC		30.7428857561
83PhosphorylationVKVNWATTPSSQKKD
EEEEEECCCCCCCCC		17.2721815630
85PhosphorylationVNWATTPSSQKKDTS
EEEECCCCCCCCCCC		43.2225159151
86PhosphorylationNWATTPSSQKKDTSS
EEECCCCCCCCCCCC		47.4225159151
88UbiquitinationATTPSSQKKDTSSST
ECCCCCCCCCCCCCE		55.3427667366
88AcetylationATTPSSQKKDTSSST
ECCCCCCCCCCCCCE		55.3425953088
89UbiquitinationTTPSSQKKDTSSSTV
CCCCCCCCCCCCCEE		59.6129967540
90UbiquitinationTPSSQKKDTSSSTVV
CCCCCCCCCCCCEEE		59.8832015554
91PhosphorylationPSSQKKDTSSSTVVS
CCCCCCCCCCCEEEE		39.1121406692
92PhosphorylationSSQKKDTSSSTVVST
CCCCCCCCCCEEEEE		32.2121406692
93PhosphorylationSQKKDTSSSTVVSTQ
CCCCCCCCCEEEEEE		31.9221406692
94PhosphorylationQKKDTSSSTVVSTQR
CCCCCCCCEEEEEEC		25.6221406692
95PhosphorylationKKDTSSSTVVSTQRS
CCCCCCCEEEEEECC		27.2021406692
98PhosphorylationTSSSTVVSTQRSQDH
CCCCEEEEEECCCCC		17.9325159151
99PhosphorylationSSSTVVSTQRSQDHF
CCCEEEEEECCCCCE		19.1821815630
102PhosphorylationTVVSTQRSQDHFHVF
EEEEEECCCCCEEEE		30.0926714015
103PhosphorylationVVSTQRSQDHFHVFV
EEEEECCCCCEEEEE		50.84-
114PhosphorylationHVFVGDLSPEITTED
EEEECCCCCCCCHHH		25.8120068231
131MethylationAAFAPFGRISDARVV
HHHCCCCCCCCCEEE		26.14115918441
143PhosphorylationRVVKDMATGKSKGYG
EEEEHHCCCCCCCCC		38.2122210691
145AcetylationVKDMATGKSKGYGFV
EEHHCCCCCCCCCEE		44.6425953088
149PhosphorylationATGKSKGYGFVSFFN
CCCCCCCCCEEEEEC		15.8920090780
191PhosphorylationRKPPAPKSTYESNTK
CCCCCCCCCCCCCCC		34.8528796482
192PhosphorylationKPPAPKSTYESNTKQ
CCCCCCCCCCCCCCC		37.1228796482
193PhosphorylationPPAPKSTYESNTKQL
CCCCCCCCCCCCCCC		25.1728796482
195PhosphorylationAPKSTYESNTKQLSY
CCCCCCCCCCCCCCH		39.1128796482
197PhosphorylationKSTYESNTKQLSYDE
CCCCCCCCCCCCHHH		29.4628796482
209PhosphorylationYDEVVNQSSPSNCTV
HHHHHCCCCCCCCEE		38.7316094384
210PhosphorylationDEVVNQSSPSNCTVY
HHHHCCCCCCCCEEE		23.6816094384
235PhosphorylationQLMRQTFSPFGQIME
HHHHHHCCCCCCEEE		23.7827050516
241SulfoxidationFSPFGQIMEIRVFPD
CCCCCCEEEEEECCC		2.4221406390
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 TIA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIA1_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 TIA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FASTK_HUMANFASTKphysical
7544399
WDR6_HUMANWDR6physical
19910486
LC7L2_HUMANLUC7L2physical
26344197
MPI_HUMANMPIphysical
26344197
PCBP1_HUMANPCBP1physical
26344197
PCBP2_HUMANPCBP2physical
26344197
PIPNB_HUMANPITPNBphysical
26344197
SMD1_HUMANSNRPD1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604454Welander distal myopathy (WDM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TIA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-210, ANDMASS SPECTROMETRY.

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