CPSF7_HUMAN - dbPTM
CPSF7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPSF7_HUMAN
UniProt AC Q8N684
Protein Name Cleavage and polyadenylation specificity factor subunit 7 {ECO:0000305}
Gene Name CPSF7 {ECO:0000312|HGNC:HGNC:30098}
Organism Homo sapiens (Human).
Sequence Length 471
Subcellular Localization Nucleus . Cytoplasm . Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460).
Protein Description Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. [PubMed: 8626397]
Protein Sequence MSEGVDLIDIYADEEFNQDPEFNNTDQIDLYDDVLTATSQPSDDRSSSTEPPPPVRQEPSPKPNNKTPAILYTYSGLRNRRAAVYVGSFSWWTTDQQLIQVIRSIGVYDVVELKFAENRANGQSKGYAEVVVASENSVHKLLELLPGKVLNGEKVDVRPATRQNLSQFEAQARKRECVRVPRGGIPPRAHSRDSSDSADGRATPSENLVPSSARVDKPPSVLPYFNRPPSALPLMGLPPPPIPPPPPLSSSFGVPPPPPGIHYQHLMPPPPRLPPHLAVPPPGAIPPALHLNPAFFPPPNATVGPPPDTYMKASAPYNHHGSRDSGPPPSTVSEAEFEDIMKRNRAISSSAISKAVSGASAGDYSDAIETLLTAIAVIKQSRVANDERCRVLISSLKDCLHGIEAKSYSVGASGSSSRKRHRSRERSPSRSRESSRRHRDLLHNEDRHDDYFQERNREHERHRDRERDRHH
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
31PhosphorylationNTDQIDLYDDVLTAT
CCCCCCCCCHHHHCC		13.32-
36PhosphorylationDLYDDVLTATSQPSD
CCCCHHHHCCCCCCC		27.9526074081
38PhosphorylationYDDVLTATSQPSDDR
CCHHHHCCCCCCCCC		23.7426074081
39PhosphorylationDDVLTATSQPSDDRS
CHHHHCCCCCCCCCC		37.3226074081
42PhosphorylationLTATSQPSDDRSSST
HHCCCCCCCCCCCCC		44.5026074081
46PhosphorylationSQPSDDRSSSTEPPP
CCCCCCCCCCCCCCC		35.3230266825
47PhosphorylationQPSDDRSSSTEPPPP
CCCCCCCCCCCCCCC		42.0230266825
48PhosphorylationPSDDRSSSTEPPPPV
CCCCCCCCCCCCCCC		37.7330266825
49PhosphorylationSDDRSSSTEPPPPVR
CCCCCCCCCCCCCCC		55.2330266825
60PhosphorylationPPVRQEPSPKPNNKT
CCCCCCCCCCCCCCC		44.8225159151
67PhosphorylationSPKPNNKTPAILYTY
CCCCCCCCCEEEEEE		21.7828464451
72PhosphorylationNKTPAILYTYSGLRN
CCCCEEEEEECCCCC		9.4921945579
73PhosphorylationKTPAILYTYSGLRNR
CCCEEEEEECCCCCC		14.0421945579
74PhosphorylationTPAILYTYSGLRNRR
CCEEEEEECCCCCCC		6.2821945579
75PhosphorylationPAILYTYSGLRNRRA
CEEEEEECCCCCCCE		24.4521945579
89 (in isoform 3)Phosphorylation-6.11-
90PhosphorylationAVYVGSFSWWTTDQQ
EEEEECCCCCCCHHH		24.3319664995
90 (in isoform 3)Phosphorylation-24.33-
91 (in isoform 3)Phosphorylation-8.4024719451
103 (in isoform 3)Phosphorylation-24.3024719451
115 (in isoform 3)Phosphorylation-18.8627642862
117 (in isoform 3)Phosphorylation-50.8327642862
124PhosphorylationENRANGQSKGYAEVV
ECCCCCCCCCCEEEE		29.4621712546
127PhosphorylationANGQSKGYAEVVVAS
CCCCCCCCEEEEEEC		11.8821712546
134PhosphorylationYAEVVVASENSVHKL
CEEEEEECCCHHHHH		26.2121712546
140UbiquitinationASENSVHKLLELLPG
ECCCHHHHHHHHCCC		53.24-
1482-HydroxyisobutyrylationLLELLPGKVLNGEKV
HHHHCCCCCCCCCCC		41.43-
148SumoylationLLELLPGKVLNGEKV
HHHHCCCCCCCCCCC		41.43-
148UbiquitinationLLELLPGKVLNGEKV
HHHHCCCCCCCCCCC		41.4321890473
148 (in isoform 1)Ubiquitination-41.4321890473
148 (in isoform 2)Ubiquitination-41.4321890473
151 (in isoform 3)Phosphorylation-60.6127642862
154AcetylationGKVLNGEKVDVRPAT
CCCCCCCCCCCCHHH		45.1725953088
154UbiquitinationGKVLNGEKVDVRPAT
CCCCCCCCCCCCHHH		45.17-
166PhosphorylationPATRQNLSQFEAQAR
HHHHCCHHHHHHHHH		40.1328555341
182 (in isoform 2)Phosphorylation-53.7824275569
186UbiquitinationRVPRGGIPPRAHSRD
ECCCCCCCCCCCCCC		18.6621890473
186 (in isoform 2)Phosphorylation-18.6627762562
188 (in isoform 2)Phosphorylation-39.3129116813
191PhosphorylationGIPPRAHSRDSSDSA
CCCCCCCCCCCCCCC		36.4830576142
191 (in isoform 3)Ubiquitination-36.48-
194PhosphorylationPRAHSRDSSDSADGR
CCCCCCCCCCCCCCC		34.6319664994
195PhosphorylationRAHSRDSSDSADGRA
CCCCCCCCCCCCCCC		39.6119664994
197PhosphorylationHSRDSSDSADGRATP
CCCCCCCCCCCCCCC		30.1523927012
203PhosphorylationDSADGRATPSENLVP
CCCCCCCCCCHHCCC		26.4529255136
205PhosphorylationADGRATPSENLVPSS
CCCCCCCCHHCCCCC		34.4622167270
211PhosphorylationPSENLVPSSARVDKP
CCHHCCCCCCCCCCC		29.2023927012
212O-linked_GlycosylationSENLVPSSARVDKPP
CHHCCCCCCCCCCCC		17.6428510447
212PhosphorylationSENLVPSSARVDKPP
CHHCCCCCCCCCCCC		17.6423927012
234 (in isoform 3)Phosphorylation-4.4124719451
237 (in isoform 3)Phosphorylation-3.4224719451
238 (in isoform 3)Phosphorylation-33.3527251275
240 (in isoform 3)Phosphorylation-37.2024719451
246 (in isoform 3)Phosphorylation-48.5124719451
248 (in isoform 3)Phosphorylation-10.79-
309PhosphorylationTVGPPPDTYMKASAP
CCCCCCCCCCCCCCC		31.1524260401
310PhosphorylationVGPPPDTYMKASAPY
CCCCCCCCCCCCCCC		12.1924260401
314PhosphorylationPDTYMKASAPYNHHG
CCCCCCCCCCCCCCC		25.0228555341
317PhosphorylationYMKASAPYNHHGSRD
CCCCCCCCCCCCCCC		27.1828555341
322PhosphorylationAPYNHHGSRDSGPPP
CCCCCCCCCCCCCCC		28.6720068231
325PhosphorylationNHHGSRDSGPPPSTV
CCCCCCCCCCCCCCC		52.6825159151
330PhosphorylationRDSGPPPSTVSEAEF
CCCCCCCCCCCHHHH		47.4127732954
333PhosphorylationGPPPSTVSEAEFEDI
CCCCCCCCHHHHHHH		31.04-
342AcetylationAEFEDIMKRNRAISS
HHHHHHHHHCHHHCH		47.0226051181
342UbiquitinationAEFEDIMKRNRAISS
HHHHHHHHHCHHHCH		47.02-
348O-linked_GlycosylationMKRNRAISSSAISKA
HHHCHHHCHHHHHHH		19.7728510447
348PhosphorylationMKRNRAISSSAISKA
HHHCHHHCHHHHHHH		19.7723312004
349PhosphorylationKRNRAISSSAISKAV
HHCHHHCHHHHHHHH		20.0623312004
350PhosphorylationRNRAISSSAISKAVS
HCHHHCHHHHHHHHH		23.8823312004
354SumoylationISSSAISKAVSGASA
HCHHHHHHHHHCCCC		46.8528112733
365PhosphorylationGASAGDYSDAIETLL
CCCCCCHHHHHHHHH		25.8820068231
365 (in isoform 3)Phosphorylation-25.8827251275
368 (in isoform 3)Phosphorylation-5.0924719451
379UbiquitinationLTAIAVIKQSRVAND
HHHHHHHHHHHCCCH		35.31-
394PhosphorylationERCRVLISSLKDCLH
HHHHHHHHHHHHHHC		26.0030266825
395PhosphorylationRCRVLISSLKDCLHG
HHHHHHHHHHHHHCC		32.2324719451
397AcetylationRVLISSLKDCLHGIE
HHHHHHHHHHHCCCC		48.6323749302
397MalonylationRVLISSLKDCLHGIE
HHHHHHHHHHHCCCC		48.6326320211
397UbiquitinationRVLISSLKDCLHGIE
HHHHHHHHHHHCCCC		48.63-
407PhosphorylationLHGIEAKSYSVGASG
HCCCCEECCCCCCCC		29.6827251275
408NitrationHGIEAKSYSVGASGS
CCCCEECCCCCCCCC		13.48-
408PhosphorylationHGIEAKSYSVGASGS
CCCCEECCCCCCCCC		13.4820068231
409PhosphorylationGIEAKSYSVGASGSS
CCCEECCCCCCCCCH		22.5925159151
413PhosphorylationKSYSVGASGSSSRKR
ECCCCCCCCCHHHHH		33.0225159151
415PhosphorylationYSVGASGSSSRKRHR
CCCCCCCCHHHHHHH		23.7325159151
416PhosphorylationSVGASGSSSRKRHRS
CCCCCCCHHHHHHHC		37.3723401153
417PhosphorylationVGASGSSSRKRHRSR
CCCCCCHHHHHHHCC		43.4421815630
423PhosphorylationSSRKRHRSRERSPSR
HHHHHHHCCCCCCCC		32.1617081983
427PhosphorylationRHRSRERSPSRSRES
HHHCCCCCCCCCHHH		23.6030576142
429PhosphorylationRSRERSPSRSRESSR
HCCCCCCCCCHHHHH		44.1020068231
431PhosphorylationRERSPSRSRESSRRH
CCCCCCCCHHHHHHH		44.7420068231
434PhosphorylationSPSRSRESSRRHRDL
CCCCCHHHHHHHHHH		28.2126074081
435PhosphorylationPSRSRESSRRHRDLL
CCCCHHHHHHHHHHH		28.6926074081
437 (in isoform 3)Phosphorylation-31.0127251275
438 (in isoform 3)Phosphorylation-26.8824719451
447MethylationDLLHNEDRHDDYFQE
HHHCCCCCCHHHHHH		29.02-
451PhosphorylationNEDRHDDYFQERNRE
CCCCCHHHHHHHHHH		17.1428796482
452 (in isoform 3)Phosphorylation-8.6024719451
456 (in isoform 3)Phosphorylation-53.6027251275
459 (in isoform 3)Phosphorylation-33.87-
460 (in isoform 3)Phosphorylation-45.49-
466 (in isoform 3)Phosphorylation-64.32-
470 (in isoform 3)Phosphorylation-34.99-
472 (in isoform 3)Phosphorylation--
494 (in isoform 3)Phosphorylation-27642862
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 CPSF7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPSF7_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 CPSF7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ROA1_HUMANHNRNPA1physical
22939629
UBP2L_HUMANUBAP2Lphysical
22939629
TPM2_HUMANTPM2physical
22939629
NDUS2_HUMANNDUFS2physical
22939629
MCM2_HUMANMCM2physical
22939629
RT31_HUMANMRPS31physical
22939629
NU133_HUMANNUP133physical
22939629
RS19_HUMANRPS19physical
22939629
ODO1_HUMANOGDHphysical
22939629
ERGI3_HUMANERGIC3physical
22939629
CPSF5_HUMANNUDT21physical
26344197
CPSF5_HUMANNUDT21physical
26496610
CPSF6_HUMANCPSF6physical
26496610
WWP2_HUMANWWP2physical
26496610
ZN766_HUMANZNF766physical
26496610
BRNP1_HUMANBRINP1physical
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 CPSF7_HUMAN

loading...

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-48 AND THR-203, AND MASSSPECTROMETRY.
"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 THR-203 AND SER-413, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND SER-429, ANDMASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-72 AND THR-73, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory