CSTF3_HUMAN - dbPTM
CSTF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSTF3_HUMAN
UniProt AC Q12996
Protein Name Cleavage stimulation factor subunit 3
Gene Name CSTF3
Organism Homo sapiens (Human).
Sequence Length 717
Subcellular Localization Nucleus.
Protein Description One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs..
Protein Sequence MSGDGATEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKARKTYERLVAQFPSSGRFWKLYIEAEIKAKNYDKVEKLFQRCLMKVLHIDLWKCYLSYVRETKGKLPSYKEKMAQAYDFALDKIGMEIMSYQIWVDYINFLKGVEAVGSYAENQRITAVRRVYQRGCVNPMINIEQLWRDYNKYEEGINIHLAKKMIEDRSRDYMNARRVAKEYETVMKGLDRNAPSVPPQNTPQEAQQVDMWKKYIQWEKSNPLRTEDQTLITKRVMFAYEQCLLVLGHHPDIWYEAAQYLEQSSKLLAEKGDMNNAKLFSDEAANIYERAISTLLKKNMLLYFAYADYEESRMKYEKVHSIYNRLLAIEDIDPTLVYIQYMKFARRAEGIKSGRMIFKKAREDTRTRHHVYVTAALMEYYCSKDKSVAFKIFELGLKKYGDIPEYVLAYIDYLSHLNEDNNTRVLFERVLTSGSLPPEKSGEIWARFLAFESNIGDLASILKVEKRRFTAFKEEYEGKETALLVDRYKFMDLYPCSASELKALGYKDVSRAKLAAIIPDPVVAPSIVPVLKDEVDRKPEYPKPDTQQMIPFQPRHLAPPGLHPVPGGVFPVPPAAVVLMKLLPPPICFQGPFVQVDELMEIFRRCKIPNTVEEAVRIITGGAPELAVEGNGPVESNAVLTKAVKRPNEDSDEDEEKGAVVPPVHDIYRARQQKRIR
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------MSGDGATEQ
------CCCCCHHHH		45.6625849741
2Acetylation------MSGDGATEQ
------CCCCCHHHH		45.6622223895
7Phosphorylation-MSGDGATEQAAEYV
-CCCCCHHHHHHHHC		33.8730108239
13NitrationATEQAAEYVPEKVKK
HHHHHHHHCHHHHHH		19.31-
17UbiquitinationAAEYVPEKVKKAEKK
HHHHCHHHHHHHHHH		53.97-
20UbiquitinationYVPEKVKKAEKKLEE
HCHHHHHHHHHHHHH		65.84-
492-HydroxyisobutyrylationAQNQPIDKARKTYER
HHCCCCHHHHHHHHH		51.30-
49UbiquitinationAQNQPIDKARKTYER
HHCCCCHHHHHHHHH		51.3024816145
49AcetylationAQNQPIDKARKTYER
HHCCCCHHHHHHHHH		51.3026051181
54PhosphorylationIDKARKTYERLVAQF
CHHHHHHHHHHHHHC		11.3324719451
63PhosphorylationRLVAQFPSSGRFWKL
HHHHHCCCCCCCEEE		46.8724719451
64PhosphorylationLVAQFPSSGRFWKLY
HHHHCCCCCCCEEEE		33.9424719451
86UbiquitinationKNYDKVEKLFQRCLM
CCHHHHHHHHHHHHH		58.5529967540
86AcetylationKNYDKVEKLFQRCLM
CCHHHHHHHHHHHHH		58.5527452117
94UbiquitinationLFQRCLMKVLHIDLW
HHHHHHHHHHCHHHH		28.7923000965
104PhosphorylationHIDLWKCYLSYVRET
CHHHHHHHHHHHHHC		8.58-
107PhosphorylationLWKCYLSYVRETKGK
HHHHHHHHHHHCCCC		10.84-
114AcetylationYVRETKGKLPSYKEK
HHHHCCCCCCCHHHH		59.8023749302
121UbiquitinationKLPSYKEKMAQAYDF
CCCCHHHHHHHHHHH		35.0733845483
121MalonylationKLPSYKEKMAQAYDF
CCCCHHHHHHHHHHH		35.0730639696
126PhosphorylationKEKMAQAYDFALDKI
HHHHHHHHHHHHHHH		10.26-
139PhosphorylationKIGMEIMSYQIWVDY
HHCHHHHHHHHHHHH		21.39-
140PhosphorylationIGMEIMSYQIWVDYI
HCHHHHHHHHHHHHH		6.14-
158PhosphorylationKGVEAVGSYAENQRI
HCHHHHHHHHHHCCH		17.9928152594
159PhosphorylationGVEAVGSYAENQRIT
CHHHHHHHHHHCCHH		16.4128152594
159NitrationGVEAVGSYAENQRIT
CHHHHHHHHHHCCHH		16.41-
192AcetylationQLWRDYNKYEEGINI
HHHHHHHHHHHCCCH		48.0526051181
192UbiquitinationQLWRDYNKYEEGINI
HHHHHHHHHHHCCCH		48.0521890473
2032-HydroxyisobutyrylationGINIHLAKKMIEDRS
CCCHHHHHHHHHHHC		49.59-
228AcetylationKEYETVMKGLDRNAP
HHHHHHHHCCCCCCC		52.5725953088
228UbiquitinationKEYETVMKGLDRNAP
HHHHHHHHCCCCCCC		52.5732015554
236PhosphorylationGLDRNAPSVPPQNTP
CCCCCCCCCCCCCCC		44.8629978859
242PhosphorylationPSVPPQNTPQEAQQV
CCCCCCCCCHHHHHH		22.5429978859
261PhosphorylationKYIQWEKSNPLRTED
HHHHHHHCCCCCCCC		31.9721712546
266PhosphorylationEKSNPLRTEDQTLIT
HHCCCCCCCCCCHHH		52.1520068231
270PhosphorylationPLRTEDQTLITKRVM
CCCCCCCCHHHHHHH		32.2320068231
273PhosphorylationTEDQTLITKRVMFAY
CCCCCHHHHHHHHHH		18.8620068231
2742-HydroxyisobutyrylationEDQTLITKRVMFAYE
CCCCHHHHHHHHHHH		35.68-
274UbiquitinationEDQTLITKRVMFAYE
CCCCHHHHHHHHHHH		35.6822817900
3112-HydroxyisobutyrylationSSKLLAEKGDMNNAK
HHHHHHHCCCCCCCC		55.38-
321PhosphorylationMNNAKLFSDEAANIY
CCCCCCCCHHHHHHH		45.00-
328PhosphorylationSDEAANIYERAISTL
CHHHHHHHHHHHHHH		10.1228152594
333PhosphorylationNIYERAISTLLKKNM
HHHHHHHHHHHHHCC		16.4223403867
334PhosphorylationIYERAISTLLKKNML
HHHHHHHHHHHHCCH		29.9623403867
3372-HydroxyisobutyrylationRAISTLLKKNMLLYF
HHHHHHHHHCCHHHH		45.26-
355AcetylationDYEESRMKYEKVHSI
CHHHHHHHHHHHHHH		49.5019809697
356PhosphorylationYEESRMKYEKVHSIY
HHHHHHHHHHHHHHH		16.1930576142
358AcetylationESRMKYEKVHSIYNR
HHHHHHHHHHHHHHH		42.0019809705
361PhosphorylationMKYEKVHSIYNRLLA
HHHHHHHHHHHHHHH		29.7430576142
363PhosphorylationYEKVHSIYNRLLAIE
HHHHHHHHHHHHHHH		9.3930576142
3922-HydroxyisobutyrylationARRAEGIKSGRMIFK
HHHHHCCCCCCEEEH		58.68-
412PhosphorylationTRTRHHVYVTAALME
CCCCCHHHHHHHHHH		6.4224043423
414PhosphorylationTRHHVYVTAALMEYY
CCCHHHHHHHHHHHH		6.6324043423
420PhosphorylationVTAALMEYYCSKDKS
HHHHHHHHHHCCCCC		8.8724043423
421PhosphorylationTAALMEYYCSKDKSV
HHHHHHHHHCCCCCH		4.1224043423
423PhosphorylationALMEYYCSKDKSVAF
HHHHHHHCCCCCHHH		27.9724043423
4262-HydroxyisobutyrylationEYYCSKDKSVAFKIF
HHHHCCCCCHHHHHH		51.03-
427PhosphorylationYYCSKDKSVAFKIFE
HHHCCCCCHHHHHHH		28.8923312004
431UbiquitinationKDKSVAFKIFELGLK
CCCCHHHHHHHCCHH		36.4333845483
431AcetylationKDKSVAFKIFELGLK
CCCCHHHHHHHCCHH		36.4326051181
472PhosphorylationVLFERVLTSGSLPPE
HEEEEHHHCCCCCCC		28.3429396449
473PhosphorylationLFERVLTSGSLPPEK
EEEEHHHCCCCCCCC		23.4029396449
475PhosphorylationERVLTSGSLPPEKSG
EEHHHCCCCCCCCCH		37.1529396449
500PhosphorylationSNIGDLASILKVEKR
CCHHHHHHHHHHHHH		35.4324719451
513AcetylationKRRFTAFKEEYEGKE
HHHCCCCHHHHCCCC		47.3626051181
5132-HydroxyisobutyrylationKRRFTAFKEEYEGKE
HHHCCCCHHHHCCCC		47.36-
5192-HydroxyisobutyrylationFKEEYEGKETALLVD
CHHHHCCCCEEEEEE		39.69-
519UbiquitinationFKEEYEGKETALLVD
CHHHHCCCCEEEEEE		39.6933845483
529UbiquitinationALLVDRYKFMDLYPC
EEEEECHHCCCCCCC		34.8029967540
529AcetylationALLVDRYKFMDLYPC
EEEEECHHCCCCCCC		34.8026051181
534PhosphorylationRYKFMDLYPCSASEL
CHHCCCCCCCCHHHH		9.6422817900
542AcetylationPCSASELKALGYKDV
CCCHHHHHHCCCCCC		37.207408175
546PhosphorylationSELKALGYKDVSRAK
HHHHHCCCCCCCHHH		12.59-
547AcetylationELKALGYKDVSRAKL
HHHHCCCCCCCHHHH		50.2726051181
553UbiquitinationYKDVSRAKLAAIIPD
CCCCCHHHHHHHCCC		37.2333845483
566PhosphorylationPDPVVAPSIVPVLKD
CCCCCCCHHHHHCCC		26.87-
651PhosphorylationRRCKIPNTVEEAVRI
HHCCCCCCHHHHHHH		24.7625599653
676PhosphorylationEGNGPVESNAVLTKA
ECCCCCCCCCCHHHH		30.2626074081
681PhosphorylationVESNAVLTKAVKRPN
CCCCCCHHHHHCCCC		15.4526074081
682AcetylationESNAVLTKAVKRPNE
CCCCCHHHHHCCCCC		47.2023236377
682UbiquitinationESNAVLTKAVKRPNE
CCCCCHHHHHCCCCC		47.2021906983
685UbiquitinationAVLTKAVKRPNEDSD
CCHHHHHCCCCCCCC		67.9822817900
691PhosphorylationVKRPNEDSDEDEEKG
HCCCCCCCCCCHHCC		36.4029255136
708PhosphorylationVPPVHDIYRARQQKR
CCCHHHHHHHHHHHH		12.3224732914
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 CSTF3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSTF3_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 CSTF3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSTFT_HUMANCSTF2Tphysical
22939629
G3P_HUMANGAPDHphysical
22939629
CSTF1_HUMANCSTF1physical
11459828
CSTFT_HUMANCSTF2Tphysical
26344197
PABP1_HUMANPABPC1physical
26344197
PABP3_HUMANPABPC3physical
26344197
PAPOB_HUMANPAPOLBphysical
26344197
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 CSTF3_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-691, AND MASSSPECTROMETRY.
"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-691, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, 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 SER-691, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, 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-691, AND MASSSPECTROMETRY.

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