CPSF4_HUMAN - dbPTM
CPSF4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPSF4_HUMAN
UniProt AC O95639
Protein Name Cleavage and polyadenylation specificity factor subunit 4
Gene Name CPSF4
Organism Homo sapiens (Human).
Sequence Length 269
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. CPSF4 binds RNA polymers with a preference for poly(U)..
Protein Sequence MQEIIASVDHIKFDLEIAVEQQLGAQPLPFPGMDKSGAAVCEFFLKAACGKGGMCPFRHISGEKTVVCKHWLRGLCKKGDQCEFLHEYDMTKMPECYFYSKFGECSNKECPFLHIDPESKIKDCPWYDRGFCKHGPLCRHRHTRRVICVNYLVGFCPEGPSCKFMHPRFELPMGTTEQPPLPQQTQPPAKQSNNPPLQRSSSLIQLTSQNSSPNQQRTPQVIGVMQSQNSSAGNRGPRPLEQVTCYKCGEKGHYANRCTKGHLAFLSGQ
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
7Phosphorylation-MQEIIASVDHIKFD
-CCCCEEECCEEEEE		20.0520068231
7 (in isoform 2)Phosphorylation-20.05-
46MethylationAVCEFFLKAACGKGG
HHHHHHHHHHCCCCC		28.87-
46AcetylationAVCEFFLKAACGKGG
HHHHHHHHHHCCCCC		28.8726051181
46UbiquitinationAVCEFFLKAACGKGG
HHHHHHHHHHCCCCC		28.87-
51UbiquitinationFLKAACGKGGMCPFR
HHHHHCCCCCCCCCE		52.77-
51AcetylationFLKAACGKGGMCPFR
HHHHHCCCCCCCCCE		52.7726051181
51MethylationFLKAACGKGGMCPFR
HHHHHCCCCCCCCCE		52.77-
61PhosphorylationMCPFRHISGEKTVVC
CCCCEECCCCCEEEE		34.4724719451
69AcetylationGEKTVVCKHWLRGLC
CCCEEEEHHHHHHHH		26.6325953088
69MalonylationGEKTVVCKHWLRGLC
CCCEEEEHHHHHHHH		26.6326320211
69UbiquitinationGEKTVVCKHWLRGLC
CCCEEEEHHHHHHHH		26.63-
97PhosphorylationMTKMPECYFYSKFGE
CCCCCCCEEECCCCC		12.14-
101AcetylationPECYFYSKFGECSNK
CCCEEECCCCCCCCC		46.1125953088
108UbiquitinationKFGECSNKECPFLHI
CCCCCCCCCCCCEEC		44.38-
120UbiquitinationLHIDPESKIKDCPWY
EECCCHHHCCCCCCC		52.71-
122AcetylationIDPESKIKDCPWYDR
CCCHHHCCCCCCCCC		57.9526051181
122UbiquitinationIDPESKIKDCPWYDR
CCCHHHCCCCCCCCC		57.95-
133AcetylationWYDRGFCKHGPLCRH
CCCCCCCCCCCCCCC		49.7023749302
133UbiquitinationWYDRGFCKHGPLCRH
CCCCCCCCCCCCCCC		49.70-
173SulfoxidationHPRFELPMGTTEQPP
CCCEECCCCCCCCCC		13.4021406390
193 (in isoform 2)Phosphorylation-63.6328985074
200PhosphorylationNNPPLQRSSSLIQLT
CCCCCCCCHHHHHHH		16.0023927012
201PhosphorylationNPPLQRSSSLIQLTS
CCCCCCCHHHHHHHC		31.2130266825
202PhosphorylationPPLQRSSSLIQLTSQ
CCCCCCHHHHHHHCC		30.6423927012
205 (in isoform 2)Phosphorylation-43.9425159151
207PhosphorylationSSSLIQLTSQNSSPN
CHHHHHHHCCCCCCC		16.3423927012
208PhosphorylationSSLIQLTSQNSSPNQ
HHHHHHHCCCCCCCC		35.6423927012
211PhosphorylationIQLTSQNSSPNQQRT
HHHHCCCCCCCCCCC		39.2625159151
212PhosphorylationQLTSQNSSPNQQRTP
HHHCCCCCCCCCCCC		35.1125159151
218PhosphorylationSSPNQQRTPQVIGVM
CCCCCCCCCEEEEEE		17.4626074081
227PhosphorylationQVIGVMQSQNSSAGN
EEEEEECCCCCCCCC		17.1528857561
230PhosphorylationGVMQSQNSSAGNRGP
EEECCCCCCCCCCCC		17.5825159151
231PhosphorylationVMQSQNSSAGNRGPR
EECCCCCCCCCCCCC		47.9821815630
267PhosphorylationKGHLAFLSGQ-----
CCCHHHHCCC-----		28.7928450419
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 CPSF4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPSF4_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 CPSF4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FIP1_HUMANFIP1L1physical
16189514
CDC73_HUMANCDC73physical
19136632
CSTFT_HUMANCSTF2Tphysical
14749727
FIP1_HUMANFIP1L1physical
25416956
CPSF2_HUMANCPSF2physical
26344197
WDR33_HUMANWDR33physical
26344197
FIP1_HUMANFIP1L1physical
14749727
CBP_HUMANCREBBPphysical
26628108
SMYD2_HUMANSMYD2physical
28514442
WDR33_HUMANWDR33physical
28514442
KLK6_HUMANKLK6physical
28514442
SYMPK_HUMANSYMPKphysical
28514442
FIP1_HUMANFIP1L1physical
28514442
P4HA2_HUMANP4HA2physical
28514442
CPSF2_HUMANCPSF2physical
28514442
CPSF3_HUMANCPSF3physical
28514442
CPSF1_HUMANCPSF1physical
28514442
ANR49_HUMANANKRD49physical
28514442
TTYH1_HUMANTTYH1physical
28514442
CSTF2_HUMANCSTF2physical
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 CPSF4_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-202; SER-211 ANDSER-212, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-202 ANDSER-212, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-212, ANDMASS SPECTROMETRY.

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