PABP3_HUMAN - dbPTM
PABP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PABP3_HUMAN
UniProt AC Q9H361
Protein Name Polyadenylate-binding protein 3
Gene Name PABPC3
Organism Homo sapiens (Human).
Sequence Length 631
Subcellular Localization Cytoplasm.
Protein Description Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Binds poly(A) with a slightly lower affinity as compared to PABPC1..
Protein Sequence MNPSTPSYPTASLYVGDLHPDVTEAMLYEKFSPAGPILSIRICRDLITSGSSNYAYVNFQHTKDAEHALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFVKNLDKSINNKALYDTVSAFGNILSCNVVCDENGSKGYGFVHFETHEAAERAIKKMNGMLLNGRKVFVGQFKSRKEREAELGARAKEFPNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRTFEQMKQDRITRYQVVNLYVKNLDDGIDDERLRKAFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAYLTNEYMQRMASVRAVPNQRAPPSGYFMTAVPQTQNHAAYYPPSQIARLRPSPRWTAQGARPHPFQNKPSAIRPGAPRVPFSTMRPASSQVPRVMSTQRVANTSTQTVGPRPAAAAAAAATPAVRTVPRYKYAAGVRNPQQHRNAQPQVTMQQLAVHVQGQETLTASRLASAPPQKQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLYMLESPESLRSKVDEAVAVLQAHQAKEATQKAVNSATGVPTV
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
4Phosphorylation----MNPSTPSYPTA
----CCCCCCCCCCC		48.2024043423
5Phosphorylation---MNPSTPSYPTAS
---CCCCCCCCCCCE		19.9424043423
7Phosphorylation-MNPSTPSYPTASLY
-CCCCCCCCCCCEEE		43.7824043423
8PhosphorylationMNPSTPSYPTASLYV
CCCCCCCCCCCEEEC		13.0524043423
10PhosphorylationPSTPSYPTASLYVGD
CCCCCCCCCEEECCC		22.2024043423
12PhosphorylationTPSYPTASLYVGDLH
CCCCCCCEEECCCCC		23.7824043423
14PhosphorylationSYPTASLYVGDLHPD
CCCCCEEECCCCCCC		10.4124043423
23PhosphorylationGDLHPDVTEAMLYEK
CCCCCCCHHHHHHHH		25.9624043423
28PhosphorylationDVTEAMLYEKFSPAG
CCHHHHHHHHCCCCC		12.1824043423
32PhosphorylationAMLYEKFSPAGPILS
HHHHHHCCCCCCEEE		25.5521815630
39PhosphorylationSPAGPILSIRICRDL
CCCCCEEEEEEEHHH		15.5621406692
56PhosphorylationSGSSNYAYVNFQHTK
CCCCCEEEEEEEECC		5.88-
71PhosphorylationDAEHALDTMNFDVIK
CHHHHHHHCCEEEEC		18.1820860994
78UbiquitinationTMNFDVIKGKPVRIM
HCCEEEECCEEEEEE		61.8121890473
80UbiquitinationNFDVIKGKPVRIMWS
CEEEECCEEEEEEEE		35.0221890473
87PhosphorylationKPVRIMWSQRDPSLR
EEEEEEEECCCHHHH		9.6523186163
92PhosphorylationMWSQRDPSLRKSGVG
EEECCCHHHHHCCCC		45.1323403867
104AcetylationGVGNIFVKNLDKSIN
CCCCEEECCCCHHHC		40.8326051181
108UbiquitinationIFVKNLDKSINNKAL
EEECCCCHHHCCHHH		57.30-
140PhosphorylationDENGSKGYGFVHFET
CCCCCCEEEEEEEEH		15.89-
188MethylationAELGARAKEFPNVYI
HHHHHHHHHCCCEEE		55.10116253777
194PhosphorylationAKEFPNVYIKNFGED
HHHCCCEEEECCCCC		16.9022817900
208UbiquitinationDMDDERLKDLFGKFG
CCCHHHHHHHHHHHC		59.62-
213UbiquitinationRLKDLFGKFGPALSV
HHHHHHHHHCCEEEE		39.5521890473
213AcetylationRLKDLFGKFGPALSV
HHHHHHHHHCCEEEE		39.5524638255
219PhosphorylationGKFGPALSVKVMTDE
HHHCCEEEEEEEECC		23.2328450419
221UbiquitinationFGPALSVKVMTDESG
HCCEEEEEEEECCCC		23.94-
224PhosphorylationALSVKVMTDESGKSK
EEEEEEEECCCCCCC		39.3327362937
229UbiquitinationVMTDESGKSKGFGFV
EEECCCCCCCCEEEE		59.2721890473
230PhosphorylationMTDESGKSKGFGFVS
EECCCCCCCCEEEEE		41.3527362937
231UbiquitinationTDESGKSKGFGFVSF
ECCCCCCCCEEEEEE		62.8421890473
237PhosphorylationSKGFGFVSFERHEDA
CCCEEEEEEEEHHHH		21.0921815630
240MethylationFGFVSFERHEDAQKA
EEEEEEEEHHHHHHH		36.16-
246UbiquitinationERHEDAQKAVDEMNG
EEHHHHHHHHHHHCC		52.6921890473
254UbiquitinationAVDEMNGKELNGKQI
HHHHHCCEECCCEEE		54.76-
259AcetylationNGKELNGKQIYVGRA
CCEECCCEEEEECCH		32.23133403
259UbiquitinationNGKELNGKQIYVGRA
CCEECCCEEEEECCH		32.2321890473
262PhosphorylationELNGKQIYVGRAQKK
ECCCEEEEECCHHHH		8.38-
269UbiquitinationYVGRAQKKVERQTEL
EECCHHHHHHHHHHH		36.93-
279PhosphorylationRQTELKRTFEQMKQD
HHHHHHHHHHHHHHH		29.9122210691
284UbiquitinationKRTFEQMKQDRITRY
HHHHHHHHHHHCHHH		49.0621906983
291PhosphorylationKQDRITRYQVVNLYV
HHHHCHHHHEEEEEE		9.3022817900
297PhosphorylationRYQVVNLYVKNLDDG
HHHEEEEEECCCCCC		12.2722817900
309MethylationDDGIDDERLRKAFSP
CCCCCHHHHHHHCCC		46.95-
315PhosphorylationERLRKAFSPFGTITS
HHHHHHCCCCCCEEE		24.95-
322PhosphorylationSPFGTITSAKVMMEG
CCCCCEEEEEEEECC		23.42-
333UbiquitinationMMEGGRSKGFGFVCF
EECCCCCCCCEEEEE		57.8221890473
339S-palmitoylationSKGFGFVCFSSPEEA
CCCCEEEEECCHHHH		2.2729575903
341PhosphorylationGFGFVCFSSPEEATK
CCEEEEECCHHHHHH		39.6025159151
342PhosphorylationFGFVCFSSPEEATKA
CEEEEECCHHHHHHH		18.9725159151
347PhosphorylationFSSPEEATKAVTEMN
ECCHHHHHHHHHHHC		23.8624732914
348UbiquitinationSSPEEATKAVTEMNG
CCHHHHHHHHHHHCC		48.1621890473
360PhosphorylationMNGRIVATKPLYVAL
HCCEEEEEHHHHHHH		23.4628152594
361UbiquitinationNGRIVATKPLYVALA
CCEEEEEHHHHHHHH		24.2421890473
361MethylationNGRIVATKPLYVALA
CCEEEEEHHHHHHHH		24.24-
364PhosphorylationIVATKPLYVALAQRK
EEEEHHHHHHHHHCH		7.6927273156
388PhosphorylationEYMQRMASVRAVPNQ
HHHHHHHHCCCCCCC		11.6424719451
426DimethylationPSQIARLRPSPRWTA
HHHHHHCCCCCCCCC		24.89-
426MethylationPSQIARLRPSPRWTA
HHHHHHCCCCCCCCC		24.89-
428PhosphorylationQIARLRPSPRWTAQG
HHHHCCCCCCCCCCC		22.2117081983
430DimethylationARLRPSPRWTAQGAR
HHCCCCCCCCCCCCC		47.95-
430MethylationARLRPSPRWTAQGAR
HHCCCCCCCCCCCCC		47.95-
437DimethylationRWTAQGARPHPFQNK
CCCCCCCCCCCCCCC		36.56-
437MethylationRWTAQGARPHPFQNK
CCCCCCCCCCCCCCC		36.56-
449MethylationQNKPSAIRPGAPRVP
CCCCCCCCCCCCCCC		24.26-
458PhosphorylationGAPRVPFSTMRPASS
CCCCCCCCCCCCCCC		18.4126657352
459PhosphorylationAPRVPFSTMRPASSQ
CCCCCCCCCCCCCCC		19.9920860994
461DimethylationRVPFSTMRPASSQVP
CCCCCCCCCCCCCCC		24.58-
461MethylationRVPFSTMRPASSQVP
CCCCCCCCCCCCCCC		24.5830762761
464PhosphorylationFSTMRPASSQVPRVM
CCCCCCCCCCCCCEE		24.8026657352
469DimethylationPASSQVPRVMSTQRV
CCCCCCCCEEECCCC		37.60-
469MethylationPASSQVPRVMSTQRV
CCCCCCCCEEECCCC		37.6018601173
472PhosphorylationSQVPRVMSTQRVANT
CCCCCEEECCCCCCC		20.6624719451
480PhosphorylationTQRVANTSTQTVGPR
CCCCCCCCCCCCCCC		20.51-
497PhosphorylationAAAAAAATPAVRTVP
HHHHHHCCHHHCCCC		13.67-
501MethylationAAATPAVRTVPRYKY
HHCCHHHCCCCCCCC		31.92-
502PhosphorylationAATPAVRTVPRYKYA
HCCHHHCCCCCCCCC		28.4124260401
506PhosphorylationAVRTVPRYKYAAGVR
HHCCCCCCCCCCCCC		11.4124260401
508PhosphorylationRTVPRYKYAAGVRNP
CCCCCCCCCCCCCCH		7.8624260401
513MethylationYKYAAGVRNPQQHRN
CCCCCCCCCHHHHCC		48.47-
568SulfoxidationLFPLIQAMHPTLAGK
HHHHHHHHCHHHHHH		1.9231801345
601UbiquitinationSPESLRSKVDEAVAV
CHHHHHHHHHHHHHH		47.47-
624PhosphorylationATQKAVNSATGVPTV
HHHHHHHHHCCCCCC		22.1730108239
626PhosphorylationQKAVNSATGVPTV--
HHHHHHHCCCCCC--		38.2330108239
630O-linked_GlycosylationNSATGVPTV------
HHHCCCCCC------		36.1230620550
630PhosphorylationNSATGVPTV------
HHHCCCCCC------		36.1228985074
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 PABP3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PABP3_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 PABP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NH2L1_HUMANNHP2L1physical
26344197
PAN3_HUMANPAN3physical
26344197
PAPOA_HUMANPAPOLAphysical
26344197
PEBP1_HUMANPEBP1physical
26344197
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 PABP3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-213 AND LYS-259, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364, AND MASSSPECTROMETRY.

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