PAPD5_HUMAN - dbPTM
PAPD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAPD5_HUMAN
UniProt AC Q8NDF8
Protein Name Non-canonical poly(A) RNA polymerase PAPD5
Gene Name PAPD5
Organism Homo sapiens (Human).
Sequence Length 572
Subcellular Localization Nucleus . Nucleus, nucleolus . Cytoplasm . Predominantly expressed in the cytoplasm (PubMed:18172165).
Protein Description Catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro). Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion..
Protein Sequence MYRSGERLLGSHALPAEQRDFLPLETTNNNNNHHQPGAWARRAGSSASSPPSASSSPHPSAAVPAADPADSASGSSNKRKRDNKASGGRAAGGGRADGGGVVYSGTPWKRRNYNQGVVGLHEEISDFYEYMSPRPEEEKMRMEVVNRIESVIKELWPSADVQIFGSFKTGLYLPTSDIDLVVFGKWENLPLWTLEEALRKHKVADEDSVKVLDKATVPIIKLTDSFTEVKVDISFNVQNGVRAADLIKDFTKKYPVLPYLVLVLKQFLLQRDLNEVFTGGIGSYSLFLMAVSFLQLHPREDACIPNTNYGVLLIEFFELYGRHFNYLKTGIRIKDGGSYVAKDEVQKNMLDGYRPSMLYIEDPLQPGNDVGRSSYGAMQVKQAFDYAYVVLSHAVSPIAKYYPNNETESILGRIIRVTDEVATYRDWISKQWGLKNRPEPSCNGPVSSSSATQSSSSDVDSDATPCKTPKQLLCRPSTGNRVGSQDVSLESSQAVGKMQSTQTTNTSNSTNKSQHGSARLFRSSSKGFQGTTQTSHGSLMTNKQHQGKSNNQYYHGKKRKHKRDAPLSDLCR
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
11PhosphorylationSGERLLGSHALPAEQ
CCCCCCCCCCCCHHH		12.9328555341
45PhosphorylationAWARRAGSSASSPPS
HHHHHCCCCCCCCCC		23.0323401153
45 (in isoform 3)Phosphorylation-23.0321406692
46PhosphorylationWARRAGSSASSPPSA
HHHHCCCCCCCCCCC		31.1123927012
48PhosphorylationRRAGSSASSPPSASS
HHCCCCCCCCCCCCC		45.3823401153
48 (in isoform 3)Phosphorylation-45.3821406692
49PhosphorylationRAGSSASSPPSASSS
HCCCCCCCCCCCCCC		40.3123927012
52PhosphorylationSSASSPPSASSSPHP
CCCCCCCCCCCCCCC		44.1423927012
54PhosphorylationASSPPSASSSPHPSA
CCCCCCCCCCCCCCC		35.3723927012
55PhosphorylationSSPPSASSSPHPSAA
CCCCCCCCCCCCCCC		47.8323927012
56PhosphorylationSPPSASSSPHPSAAV
CCCCCCCCCCCCCCC		25.4023927012
56 (in isoform 3)Phosphorylation-25.4021406692
60PhosphorylationASSSPHPSAAVPAAD
CCCCCCCCCCCCCCC		26.3123927012
71PhosphorylationPAADPADSASGSSNK
CCCCCCCCCCCCCCC		26.8320363803
73PhosphorylationADPADSASGSSNKRK
CCCCCCCCCCCCCCC		43.0623927012
75PhosphorylationPADSASGSSNKRKRD
CCCCCCCCCCCCCCC		28.3923927012
76PhosphorylationADSASGSSNKRKRDN
CCCCCCCCCCCCCCC		50.3120363803
106PhosphorylationGGVVYSGTPWKRRNY
CCEEECCCCCCCCCC		21.7525627689
109UbiquitinationVYSGTPWKRRNYNQG
EECCCCCCCCCCCCC		42.56-
112PhosphorylationGTPWKRRNYNQGVVG
CCCCCCCCCCCCCCC		44.11-
113PhosphorylationTPWKRRNYNQGVVGL
CCCCCCCCCCCCCCC		13.67-
116PhosphorylationKRRNYNQGVVGLHEE
CCCCCCCCCCCCCHH		16.67-
153 (in isoform 5)Phosphorylation-44.6029083192
154 (in isoform 5)Phosphorylation-44.9629083192
155 (in isoform 5)Phosphorylation-7.4729083192
159 (in isoform 5)Phosphorylation-19.5329083192
188UbiquitinationVVFGKWENLPLWTLE
EEEECCCCCCCCCHH		45.93-
210AcetylationVADEDSVKVLDKATV
CCCHHHCEEHHHCCC		40.8226051181
210MethylationVADEDSVKVLDKATV
CCCHHHCEEHHHCCC		40.82115974607
214UbiquitinationDSVKVLDKATVPIIK
HHCEEHHHCCCEEEE		41.62-
289MethylationGSYSLFLMAVSFLQL
HHHHHHHHHHHHHHH		2.44-
289UbiquitinationGSYSLFLMAVSFLQL
HHHHHHHHHHHHHHH		2.44-
293UbiquitinationLFLMAVSFLQLHPRE
HHHHHHHHHHHCCCC		3.97-
300UbiquitinationFLQLHPREDACIPNT
HHHHCCCCCCCCCCC		55.18-
327UbiquitinationYGRHFNYLKTGIRIK
HHHHCCCCCCCEEEC		4.14-
342SumoylationDGGSYVAKDEVQKNM
CCCCEECCHHHHHCC		44.36-
375PhosphorylationNDVGRSSYGAMQVKQ
CCCCCHHCCCHHHHH		15.3429496907
413UbiquitinationETESILGRIIRVTDE
HHHHHHHHHHHHCHH		20.09-
421SumoylationIIRVTDEVATYRDWI
HHHHCHHHHHHHHHH		5.55-
421UbiquitinationIIRVTDEVATYRDWI
HHHHCHHHHHHHHHH		5.55-
426UbiquitinationDEVATYRDWISKQWG
HHHHHHHHHHHHHHC		36.33-
450PhosphorylationNGPVSSSSATQSSSS
CCCCCCCCCCCCCCC		36.9630576142
452PhosphorylationPVSSSSATQSSSSDV
CCCCCCCCCCCCCCC		30.8230576142
454PhosphorylationSSSSATQSSSSDVDS
CCCCCCCCCCCCCCC		28.0328348404
455PhosphorylationSSSATQSSSSDVDSD
CCCCCCCCCCCCCCC		24.8423663014
456PhosphorylationSSATQSSSSDVDSDA
CCCCCCCCCCCCCCC		35.4923663014
457PhosphorylationSATQSSSSDVDSDAT
CCCCCCCCCCCCCCC		43.5323663014
461PhosphorylationSSSSDVDSDATPCKT
CCCCCCCCCCCCCCC		29.0623663014
464 (in isoform 3)Phosphorylation-33.9225159151
470SumoylationATPCKTPKQLLCRPS
CCCCCCCCEEEECCC		59.8328112733
477PhosphorylationKQLLCRPSTGNRVGS
CEEEECCCCCCCCCC		29.6025159151
477 (in isoform 3)Phosphorylation-29.60-
478PhosphorylationQLLCRPSTGNRVGSQ
EEEECCCCCCCCCCC		40.9525627689
484PhosphorylationSTGNRVGSQDVSLES
CCCCCCCCCCEECHH		21.9825159151
485 (in isoform 3)Phosphorylation-49.5528111955
486 (in isoform 3)Phosphorylation-33.4028111955
488PhosphorylationRVGSQDVSLESSQAV
CCCCCCEECHHHCCH		34.4125159151
488 (in isoform 3)Phosphorylation-34.4128111955
489 (in isoform 3)Phosphorylation-8.1128111955
490 (in isoform 3)Phosphorylation-40.6228111955
491PhosphorylationSQDVSLESSQAVGKM
CCCEECHHHCCHHCE		32.8019691289
492PhosphorylationQDVSLESSQAVGKMQ
CCEECHHHCCHHCEE		16.8819691289
494 (in isoform 3)Phosphorylation-17.6128111955
495 (in isoform 3)Phosphorylation-6.1628111955
496 (in isoform 3)Phosphorylation-23.8023663014
497SumoylationESSQAVGKMQSTQTT
HHHCCHHCEEECEEE		27.45-
497SumoylationESSQAVGKMQSTQTT
HHHCCHHCEEECEEE		27.4528112733
497 (in isoform 3)Phosphorylation-27.4523663014
499 (in isoform 3)Phosphorylation-46.9823663014
501 (in isoform 3)Phosphorylation-17.0323663014
502 (in isoform 3)Phosphorylation-52.1223663014
503 (in isoform 3)Phosphorylation-23.3123663014
504 (in isoform 3)Phosphorylation-27.0423663014
508 (in isoform 3)Phosphorylation-51.3023663014
509PhosphorylationQTTNTSNSTNKSQHG
EEECCCCCCCCCCCC		32.8830576142
510PhosphorylationTTNTSNSTNKSQHGS
EECCCCCCCCCCCCC		51.4125627689
511 (in isoform 3)Phosphorylation-41.6323663014
512SumoylationNTSNSTNKSQHGSAR
CCCCCCCCCCCCCEE		52.1328112733
513PhosphorylationTSNSTNKSQHGSARL
CCCCCCCCCCCCEEE		29.4930576142
515 (in isoform 3)Phosphorylation-38.9928111955
523PhosphorylationGSARLFRSSSKGFQG
CCEEEECCCCCCCCC		31.4628857561
524PhosphorylationSARLFRSSSKGFQGT
CEEEECCCCCCCCCC		31.6429116813
525PhosphorylationARLFRSSSKGFQGTT
EEEECCCCCCCCCCE		37.7423401153
526SumoylationRLFRSSSKGFQGTTQ
EEECCCCCCCCCCEE		66.7428112733
531PhosphorylationSSKGFQGTTQTSHGS
CCCCCCCCEECCCCC		12.6329978859
532PhosphorylationSKGFQGTTQTSHGSL
CCCCCCCEECCCCCE		36.3529978859
534PhosphorylationGFQGTTQTSHGSLMT
CCCCCEECCCCCEEC		22.1629978859
535PhosphorylationFQGTTQTSHGSLMTN
CCCCEECCCCCEECC		18.9429978859
536PhosphorylationQGTTQTSHGSLMTNK
CCCEECCCCCEECCC		33.0027251275
538PhosphorylationTTQTSHGSLMTNKQH
CEECCCCCEECCCEE		15.0028555341
549PhosphorylationNKQHQGKSNNQYYHG
CCEECCCCCCCCCCC		48.0826074081
553PhosphorylationQGKSNNQYYHGKKRK
CCCCCCCCCCCCCCC		10.2726074081
554PhosphorylationGKSNNQYYHGKKRKH
CCCCCCCCCCCCCCC		8.3726074081
564 (in isoform 5)Phosphorylation-58.2928111955
565 (in isoform 5)Phosphorylation-15.8028111955
567 (in isoform 5)Phosphorylation-7.1528111955
568 (in isoform 5)Phosphorylation-27.7228111955
569 (in isoform 5)Phosphorylation-58.4328111955
573 (in isoform 5)Phosphorylation-28111955
574 (in isoform 5)Phosphorylation-28111955
575 (in isoform 5)Phosphorylation-23663014
576 (in isoform 5)Phosphorylation-23663014
578 (in isoform 5)Phosphorylation-23663014
580 (in isoform 5)Phosphorylation-23663014
581 (in isoform 5)Phosphorylation-23663014
582 (in isoform 5)Phosphorylation-23663014
583 (in isoform 5)Phosphorylation-23663014
587 (in isoform 5)Phosphorylation-23663014
590 (in isoform 5)Phosphorylation-23663014
594 (in isoform 5)Phosphorylation-28111955
603Phosphorylation--------------------------------------
--------------------------------------		-
610Phosphorylation---------------------------------------------
---------------------------------------------		19691289
614Phosphorylation-------------------------------------------------
-------------------------------------------------		-
623Sumoylation----------------------------------------------------------
----------------------------------------------------------		-
650Phosphorylation-------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------		-
651Phosphorylation--------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------		-
657Phosphorylation--------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------		-
669Ubiquitination--------------------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------------------		-
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 PAPD5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAPD5_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 PAPD5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZCHC7_HUMANZCCHC7physical
21878619
DIAP2_HUMANDIAPH2physical
26496610
K2C6A_HUMANKRT6Aphysical
26496610
K2C6B_HUMANKRT6Bphysical
26496610
NUMA1_HUMANNUMA1physical
26496610
PSMD2_HUMANPSMD2physical
26496610
SMCA4_HUMANSMARCA4physical
26496610
MPZL1_HUMANMPZL1physical
26496610
BCL7B_HUMANBCL7Bphysical
26496610
MED17_HUMANMED17physical
26496610
RCL1_HUMANRCL1physical
26496610
RBM6_HUMANRBM6physical
26496610
RPP38_HUMANRPP38physical
26496610
EHD1_HUMANEHD1physical
26496610
SF3B2_HUMANSF3B2physical
26496610
NNTM_HUMANNNTphysical
26496610
TECT3_HUMANTCTN3physical
26496610
RABL6_HUMANRABL6physical
26496610
TOM22_HUMANTOMM22physical
26496610
NUD18_HUMANNUDT18physical
26496610
ASCC2_HUMANASCC2physical
26496610
CHD6_HUMANCHD6physical
26496610
U119B_HUMANUNC119Bphysical
26496610
ZSC25_HUMANZSCAN25physical
26496610
RSBNL_HUMANRSBN1Lphysical
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 PAPD5_HUMAN

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Related Literatures of Post-Translational Modification
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 SER-484, AND MASSSPECTROMETRY.

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