CPSF3_HUMAN - dbPTM
CPSF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPSF3_HUMAN
UniProt AC Q9UKF6
Protein Name Cleavage and polyadenylation specificity factor subunit 3
Gene Name CPSF3
Organism Homo sapiens (Human).
Sequence Length 684
Subcellular Localization Nucleus .
Protein Description Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP-dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner..
Protein Sequence MSAIPAEESDQLLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLILDEYWQNHPELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININNPFVFKHISNLKSMDHFDDIGPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEITTMSGQKLPLKMSVDYISFSAHTDYQQTSEFIRALKPPHVILVHGEQNEMARLKAALIREYEDNDEVHIEVHNPRNTEAVTLNFRGEKLAKVMGFLADKKPEQGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEKPALKVFKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNPKIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVSVKDDSILSVTVDGKTANLNLETRTVECEEGSEDDESLREMVELAAQRLYEALTPVH
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
2Acetylation------MSAIPAEES
------CCCCCHHHC		34.6022223895
2Phosphorylation------MSAIPAEES
------CCCCCHHHC		34.6028634298
9PhosphorylationSAIPAEESDQLLIRP
CCCCHHHCCCEEEEE		23.3528634298
33UbiquitinationSCIILEFKGRKIMLD
EEEEEEECCCEEEEE		48.72-
96PhosphorylationFKGRTFMTHATKAIY
CCCCCHHHHHHHHHH		12.2720860994
108PhosphorylationAIYRWLLSDYVKVSN
HHHHHHHCCCCEECC		25.4022210691
110PhosphorylationYRWLLSDYVKVSNIS
HHHHHCCCCEECCCC		9.9729083192
114PhosphorylationLSDYVKVSNISADDM
HCCCCEECCCCHHHC		23.8022210691
126PhosphorylationDDMLYTETDLEESMD
HHCCEECCCHHHHHH		37.78-
232MethylationTVHDIVNRGGRGLIP
HHHHHHHCCCCCCCC		37.74-
277UbiquitinationYASSLAKKCMAVYQT
CHHHHHHHHHHHHHH		24.52-
292UbiquitinationYVNAMNDKIRKQINI
HHHHHHHHHHHHCCC		39.13-
295UbiquitinationAMNDKIRKQININNP
HHHHHHHHHCCCCCH		60.0321890473
295UbiquitinationAMNDKIRKQININNP
HHHHHHHHHCCCCCH		60.0321890473
306UbiquitinationINNPFVFKHISNLKS
CCCHHHHHHHHCCCC		34.4321890473
306UbiquitinationINNPFVFKHISNLKS
CCCHHHHHHHHCCCC		34.4321890473
312UbiquitinationFKHISNLKSMDHFDD
HHHHHCCCCCCCCCC		48.24-
328PhosphorylationGPSVVMASPGMMQSG
CCHHEECCCCHHCCC		12.1425159151
343PhosphorylationLSRELFESWCTDKRN
CCHHHHHHHHCCCCC		21.8122210691
346PhosphorylationELFESWCTDKRNGVI
HHHHHHHCCCCCCEE		37.9922210691
348AcetylationFESWCTDKRNGVIIA
HHHHHCCCCCCEEEE		29.6126822725
348UbiquitinationFESWCTDKRNGVIIA
HHHHHCCCCCCEEEE		29.61-
369PhosphorylationTLAKHIMSEPEEITT
CHHHHHHCCCCEEEC		49.7728270605
375PhosphorylationMSEPEEITTMSGQKL
HCCCCEEECCCCCCC		21.5228270605
376PhosphorylationSEPEEITTMSGQKLP
CCCCEEECCCCCCCC		18.2729759185
378PhosphorylationPEEITTMSGQKLPLK
CCEEECCCCCCCCCE		35.6629759185
381UbiquitinationITTMSGQKLPLKMSV
EECCCCCCCCCEEEE		56.4421906983
410UbiquitinationSEFIRALKPPHVILV
HHHHHHHCCCEEEEE		56.36-
428UbiquitinationQNEMARLKAALIREY
HHHHHHHHHHHHHHC		26.5121906983
462SumoylationTLNFRGEKLAKVMGF
EEEECHHHHHHHHHH		57.48-
462UbiquitinationTLNFRGEKLAKVMGF
EEEECHHHHHHHHHH		57.48-
462SumoylationTLNFRGEKLAKVMGF
EEEECHHHHHHHHHH		57.4817923699
465SumoylationFRGEKLAKVMGFLAD
ECHHHHHHHHHHHHC		43.10-
465SumoylationFRGEKLAKVMGFLAD
ECHHHHHHHHHHHHC		43.1017923699
465UbiquitinationFRGEKLAKVMGFLAD
ECHHHHHHHHHHHHC		43.10-
473UbiquitinationVMGFLADKKPEQGQR
HHHHHHCCCHHCCCE		65.7021890473
473UbiquitinationVMGFLADKKPEQGQR
HHHHHHCCCHHCCCE		65.7021890473
474UbiquitinationMGFLADKKPEQGQRV
HHHHHCCCHHCCCEE		55.1021890473
474UbiquitinationMGFLADKKPEQGQRV
HHHHHCCCHHCCCEE		55.1021890473
482PhosphorylationPEQGQRVSGILVKRN
HHCCCEEEEEEEECC		23.4625159151
487UbiquitinationRVSGILVKRNFNYHI
EEEEEEEECCCCEEE		37.8721890473
4872-HydroxyisobutyrylationRVSGILVKRNFNYHI
EEEEEEEECCCCEEE		37.87-
487UbiquitinationRVSGILVKRNFNYHI
EEEEEEEECCCCEEE		37.8721890473
492PhosphorylationLVKRNFNYHILSPCD
EEECCCCEEECCCCC		6.0127642862
496PhosphorylationNFNYHILSPCDLSNY
CCCEEECCCCCCCCC		23.9125159151
501PhosphorylationILSPCDLSNYTDLAM
ECCCCCCCCCCHHHH		17.9729978859
503PhosphorylationSPCDLSNYTDLAMST
CCCCCCCCCHHHHHH		9.7728796482
504PhosphorylationPCDLSNYTDLAMSTV
CCCCCCCCHHHHHHC		28.8728796482
509PhosphorylationNYTDLAMSTVKQTQA
CCCHHHHHHCCCCCC		25.1728796482
510PhosphorylationYTDLAMSTVKQTQAI
CCHHHHHHCCCCCCC		20.7328796482
545AcetylationEELEIQEKPALKVFK
HHHHCCCCCHHHEEC		21.1526051181
545SumoylationEELEIQEKPALKVFK
HHHHCCCCCHHHEEC		21.1517923699
545UbiquitinationEELEIQEKPALKVFK
HHHHCCCCCHHHEEC		21.152190698
545SumoylationEELEIQEKPALKVFK
HHHHCCCCCHHHEEC		21.15-
549UbiquitinationIQEKPALKVFKNITV
CCCCCHHHEECCEEE		47.97-
549AcetylationIQEKPALKVFKNITV
CCCCCHHHEECCEEE		47.9726051181
552UbiquitinationKPALKVFKNITVIQE
CCHHHEECCEEEEEC		50.88-
592UbiquitinationLEVQSNPKIRKGAVQ
EEECCCCCCCCCHHH		60.43-
604UbiquitinationAVQKVSKKLEMHVYS
HHHHHHHHHHHHHHH		42.02-
612UbiquitinationLEMHVYSKRLEIMLQ
HHHHHHHHHHHHHHH		43.23-
612AcetylationLEMHVYSKRLEIMLQ
HHHHHHHHHHHHHHH		43.2325953088
633PhosphorylationCVSVKDDSILSVTVD
CEECCCCCEEEEEEC		35.2525159151
636PhosphorylationVKDDSILSVTVDGKT
CCCCCEEEEEECCEE		17.6721406692
638PhosphorylationDDSILSVTVDGKTAN
CCCEEEEEECCEEEE		14.9821406692
652PhosphorylationNLNLETRTVECEEGS
ECEEEECEEECCCCC		28.2422210691
655GlutathionylationLETRTVECEEGSEDD
EEECEEECCCCCCCC		5.1222555962
659PhosphorylationTVECEEGSEDDESLR
EEECCCCCCCCHHHH		40.9223401153
664PhosphorylationEGSEDDESLREMVEL
CCCCCCHHHHHHHHH		39.4630108239
677PhosphorylationELAAQRLYEALTPVH
HHHHHHHHHHHCCCC		11.0128796482
681PhosphorylationQRLYEALTPVH----
HHHHHHHCCCC----		30.2519664994
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 CPSF3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
462KSumoylation

17923699
465KSumoylation

17923699
545KSumoylation

17923699
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 CPSF3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FIP1_HUMANFIP1L1physical
22939629
WDR33_HUMANWDR33physical
22939629
RPA49_HUMANPOLR1Ephysical
22939629
SYMPK_HUMANSYMPKphysical
18688255
CSTF2_HUMANCSTF2physical
18688255
CPSF2_HUMANCPSF2physical
18688255
CPSF2_HUMANCPSF2physical
26344197
DDX23_HUMANDDX23physical
26344197
WDR33_HUMANWDR33physical
26344197
FIP1_HUMANFIP1L1physical
14749727
CSTF1_HUMANCSTF1physical
26496610
CSTF2_HUMANCSTF2physical
26496610
CSTF3_HUMANCSTF3physical
26496610
MARK3_HUMANMARK3physical
26496610
P4HA1_HUMANP4HA1physical
26496610
PDIA1_HUMANP4HBphysical
26496610
SYMPK_HUMANSYMPKphysical
26496610
P4HA2_HUMANP4HA2physical
26496610
LRC41_HUMANLRRC41physical
26496610
CPSF4_HUMANCPSF4physical
26496610
CSTFT_HUMANCSTF2Tphysical
26496610
CPSF1_HUMANCPSF1physical
26496610
PKN3_HUMANPKN3physical
26496610
CPSF2_HUMANCPSF2physical
26496610
WDR33_HUMANWDR33physical
26496610
P3H1_HUMANP3H1physical
26496610
FIP1_HUMANFIP1L1physical
26496610
UBE3D_HUMANUBE3Dphysical
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 CPSF3_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 THR-681, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"Sumoylation modulates the assembly and activity of the pre-mRNA 3'processing complex.";
Vethantham V., Rao N., Manley J.L.;
Mol. Cell. Biol. 27:8848-8858(2007).
Cited for: SUMOYLATION AT LYS-462; LYS-465 AND LYS-545, AND MUTAGENESIS OFLYS-462; LYS-465 AND LYS-545.

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