PAIP1_HUMAN - dbPTM
PAIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAIP1_HUMAN
UniProt AC Q9H074
Protein Name Polyadenylate-binding protein-interacting protein 1
Gene Name PAIP1
Organism Homo sapiens (Human).
Sequence Length 479
Subcellular Localization Cytoplasm .
Protein Description Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain..
Protein Sequence MSDGFDRAPGAGRGRSRGLGRGGGGPEGGGFPNGAGPAERARHQPPQPKAPGFLQPPPLRQPRTTPPPGAQCEVPASPQRPSRPGALPEQTRPLRAPPSSQDKIPQQNSESAMAKPQVVVAPVLMSKLSVNAPEFYPSGYSSSYTESYEDGCEDYPTLSEYVQDFLNHLTEQPGSFETEIEQFAETLNGCVTTDDALQELVELIYQQATSIPNFSYMGARLCNYLSHHLTISPQSGNFRQLLLQRCRTEYEVKDQAAKGDEVTRKRFHAFVLFLGELYLNLEIKGTNGQVTRADILQVGLRELLNALFSNPMDDNLICAVKLLKLTGSVLEDAWKEKGKMDMEEIIQRIENVVLDANCSRDVKQMLLKLVELRSSNWGRVHATSTYREATPENDPNYFMNEPTFYTSDGVPFTAADPDYQEKYQELLEREDFFPDYEENGTDLSGAGDPYLDDIDDEMDPEIEEAYEKFCLESERKRKQ
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
2Phosphorylation------MSDGFDRAP
------CCCCCCCCC		46.57-
2 (in isoform 2)Phosphorylation-46.5725159151
2 (in isoform 3)Acetylation-46.5722223895
7Methylation-MSDGFDRAPGAGRG
-CCCCCCCCCCCCCC		40.18115486371
12 (in isoform 2)Phosphorylation-38.1922210691
13DimethylationDRAPGAGRGRSRGLG
CCCCCCCCCCCCCCC		36.50-
13MethylationDRAPGAGRGRSRGLG
CCCCCCCCCCCCCCC		36.50115486375
15DimethylationAPGAGRGRSRGLGRG
CCCCCCCCCCCCCCC		23.09-
15MethylationAPGAGRGRSRGLGRG
CCCCCCCCCCCCCCC		23.09115486379
17MethylationGAGRGRSRGLGRGGG
CCCCCCCCCCCCCCC		42.8980701973
17DimethylationGAGRGRSRGLGRGGG
CCCCCCCCCCCCCCC		42.89-
20 (in isoform 2)Phosphorylation-29.0722210691
21DimethylationGRSRGLGRGGGGPEG
CCCCCCCCCCCCCCC		45.70-
21 (in isoform 2)Phosphorylation-45.7022210691
21MethylationGRSRGLGRGGGGPEG
CCCCCCCCCCCCCCC		45.7024129315
36UbiquitinationGGFPNGAGPAERARH
CCCCCCCCHHHHHCC		24.2923000965
42MethylationAGPAERARHQPPQPK
CCHHHHHCCCCCCCC		34.88115486367
64PhosphorylationPPLRQPRTTPPPGAQ
CCCCCCCCCCCCCCC		50.7923403867
65PhosphorylationPLRQPRTTPPPGAQC
CCCCCCCCCCCCCCC		34.7727732954
77PhosphorylationAQCEVPASPQRPSRP
CCCCCCCCCCCCCCC		18.5921712546
82PhosphorylationPASPQRPSRPGALPE
CCCCCCCCCCCCCCC		53.9827732954
91PhosphorylationPGALPEQTRPLRAPP
CCCCCCCCCCCCCCC		32.3723312004
99PhosphorylationRPLRAPPSSQDKIPQ
CCCCCCCCCCCCCCC		39.30-
100PhosphorylationPLRAPPSSQDKIPQQ
CCCCCCCCCCCCCCC		48.4420068231
109PhosphorylationDKIPQQNSESAMAKP
CCCCCCCCCHHHCCC		28.7023312004
111PhosphorylationIPQQNSESAMAKPQV
CCCCCCCHHHCCCCE		24.1423312004
115UbiquitinationNSESAMAKPQVVVAP
CCCHHHCCCCEEEEH		23.9323000965
129PhosphorylationPVLMSKLSVNAPEFY
HHHHHCCCCCCCCCC		19.6426657352
141UbiquitinationEFYPSGYSSSYTESY
CCCCCCCCCCCCCCC		19.1424816145
155PhosphorylationYEDGCEDYPTLSEYV
CCCCCCCCCCHHHHH		3.9422817900
174UbiquitinationNHLTEQPGSFETEIE
HHHHCCCCCHHHHHH		44.6624816145
223UbiquitinationYMGARLCNYLSHHLT
HHHHHHHHHHHHHCE		45.4332015554
227UbiquitinationRLCNYLSHHLTISPQ
HHHHHHHHHCEECCC		19.8529967540
230PhosphorylationNYLSHHLTISPQSGN
HHHHHHCEECCCCCC		18.30-
251UbiquitinationQRCRTEYEVKDQAAK
HHHCCHHHHHHHHHC		36.5423000965
253UbiquitinationCRTEYEVKDQAAKGD
HCCHHHHHHHHHCCC		31.9824816145
256UbiquitinationEYEVKDQAAKGDEVT
HHHHHHHHHCCCHHH		22.6721890473
256UbiquitinationEYEVKDQAAKGDEVT
HHHHHHHHHCCCHHH		22.6723000965
260UbiquitinationKDQAAKGDEVTRKRF
HHHHHCCCHHHHHHH		46.6229967540
284UbiquitinationLYLNLEIKGTNGQVT
HHHCEEEECCCCCEE		50.7523000965
289 (in isoform 2)Ubiquitination-35.1621890473
289UbiquitinationEIKGTNGQVTRADIL
EEECCCCCEEHHHHH		35.1623000965
312SulfoxidationNALFSNPMDDNLICA
HHHHCCCCCCHHHHH		13.6330846556
335UbiquitinationSVLEDAWKEKGKMDM
CHHHHHHHHHCCCCH		51.7932015554
339MalonylationDAWKEKGKMDMEEII
HHHHHHCCCCHHHHH		42.6826320211
339UbiquitinationDAWKEKGKMDMEEII
HHHHHHCCCCHHHHH		42.6829967540
3392-HydroxyisobutyrylationDAWKEKGKMDMEEII
HHHHHHCCCCHHHHH		42.68-
359PhosphorylationVVLDANCSRDVKQML
HHHCCCCCHHHHHHH		31.1821712546
3632-HydroxyisobutyrylationANCSRDVKQMLLKLV
CCCCHHHHHHHHHHH		33.99-
363UbiquitinationANCSRDVKQMLLKLV
CCCCHHHHHHHHHHH		33.9923000965
363AcetylationANCSRDVKQMLLKLV
CCCCHHHHHHHHHHH		33.9927452117
368UbiquitinationDVKQMLLKLVELRSS
HHHHHHHHHHHHHHC		46.6723000965
368 (in isoform 1)Ubiquitination-46.6721890473
386NitrationRVHATSTYREATPEN
CCEEEEEEECCCCCC		13.26-
386PhosphorylationRVHATSTYREATPEN
CCEEEEEEECCCCCC		13.26-
390PhosphorylationTSTYREATPENDPNY
EEEEECCCCCCCCCC		26.7828348404
397PhosphorylationTPENDPNYFMNEPTF
CCCCCCCCCCCCCCE		15.0322817900
399SulfoxidationENDPNYFMNEPTFYT
CCCCCCCCCCCCEEC		3.8130846556
405PhosphorylationFMNEPTFYTSDGVPF
CCCCCCEECCCCCCC		14.0722817900
423PhosphorylationDPDYQEKYQELLERE
CHHHHHHHHHHHHCC		13.3828796482
436PhosphorylationREDFFPDYEENGTDL
CCCCCCCHHHHCCCC		25.9427642862
473PhosphorylationYEKFCLESERKRKQ-
HHHHHHHHHHHHCC-		29.7425159151
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
-KUbiquitinationE3 ubiquitin ligaseWWP2O00308
PMID:25266661
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAIP1_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 PAIP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PABP1_HUMANPABPC1physical
11997512
PABP1_HUMANPABPC1physical
9548260
IF4A1_HUMANEIF4A1physical
9548260
CSDE1_HUMANCSDE1physical
11051545
HNRPQ_HUMANSYNCRIPphysical
11051545
PABP1_HUMANPABPC1physical
11051545
HNRPD_HUMANHNRNPDphysical
11051545
PABP1_HUMANPABPC1physical
11287654
UBR5_HUMANUBR5physical
11287654
RENT2_HUMANUPF2physical
22939629
PABP1_HUMANPABPC1physical
25266661
WWP2_HUMANWWP2physical
25266661
MKRN2_HUMANMKRN2physical
26186194
STAU2_HUMANSTAU2physical
26186194
PAP1L_HUMANPABPC1Lphysical
26186194
ZCHC3_HUMANZCCHC3physical
26186194
SPB1_HUMANFTSJ3physical
26186194
RS15_HUMANRPS15physical
26186194
H2AX_HUMANH2AFXphysical
26186194
SF3B4_HUMANSF3B4physical
26186194
PAIP2_HUMANPAIP2physical
26186194
EIF3B_HUMANEIF3Bphysical
24396066
EIF3G_HUMANEIF3Gphysical
24396066
PABP1_HUMANPABPC1physical
24396066
EIF3A_HUMANEIF3Aphysical
24396066
PAP1L_HUMANPABPC1Lphysical
28514442
MKRN2_HUMANMKRN2physical
28514442
ZCHC3_HUMANZCCHC3physical
28514442
H2AX_HUMANH2AFXphysical
28514442
STAU2_HUMANSTAU2physical
28514442
PAIP2_HUMANPAIP2physical
28514442
SREK1_HUMANSREK1physical
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 PAIP1_HUMAN

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Related Literatures of Post-Translational Modification

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