CPSF2_HUMAN - dbPTM
CPSF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPSF2_HUMAN
UniProt AC Q9P2I0
Protein Name Cleavage and polyadenylation specificity factor subunit 2
Gene Name CPSF2
Organism Homo sapiens (Human).
Sequence Length 782
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. Involved in the histone 3' end pre-mRNA processing..
Protein Sequence MTSIIKLTTLSGVQEESALCYLLQVDEFRFLLDCGWDEHFSMDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKLGLNCAIYATIPVYKMGQMFMYDLYQSRHNTEDFTLFTLDDVDAAFDKIQQLKFSQIVNLKGKGHGLSITPLPAGHMIGGTIWKIVKDGEEEIVYAVDFNHKREIHLNGCSLEMLSRPSLLITDSFNATYVQPRRKQRDEQLLTNVLETLRGDGNVLIAVDTAGRVLELAQLLDQIWRTKDAGLGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEDKRNNPFQFRHLSLCHGLSDLARVPSPKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLARFLIDNPSEKITEIELRKRVKLEGKELEEYLEKEKLKKEAAKKLEQSKEADIDSSDESDIEEDIDQPSAHKTKHDLMMKGEGSRKGSFFKQAKKSYPMFPAPEERIKWDEYGEIIKPEDFLVPELQATEEEKSKLESGLTNGDEPMDQDLSDVPTKCISTTESIEIKARVTYIDYEGRSDGDSIKKIINQMKPRQLIIVHGPPEASQDLAECCRAFGGKDIKVYMPKLHETVDATSETHIYQVRLKDSLVSSLQFCKAKDAELAWIDGVLDMRVSKVDTGVILEEGELKDDGEDSEMQVEAPSDSSVIAQQKAMKSLFGDDEKETGEESEIIPTLEPLPPHEVPGHQSVFMNEPRLSDFKQVLLREGIQAEFVGGVLVCNNQVAVRRTETGRIGLEGCLCQDFYRIRDLLYEQYAIV
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
3Phosphorylation-----MTSIIKLTTL
-----CCCEEEEEEC		22.4824719451
47PhosphorylationFSMDIIDSLRKHVHQ
CCHHHHHHHHHHHHH		21.4726091039
50AcetylationDIIDSLRKHVHQIDA
HHHHHHHHHHHHCCE		56.1026051181
87PhosphorylationLNCAIYATIPVYKMG
CCCEEEEEEEEHHHC		14.61-
130UbiquitinationFDKIQQLKFSQIVNL
HHHHHHCCCHHEECC		38.3421906983
130UbiquitinationFDKIQQLKFSQIVNL
HHHHHHCCCHHEECC		38.3421890473
138UbiquitinationFSQIVNLKGKGHGLS
CHHEECCCCCCCCCC		54.06-
140UbiquitinationQIVNLKGKGHGLSIT
HEECCCCCCCCCCCC		46.26-
179UbiquitinationYAVDFNHKREIHLNG
EEEECCCCEEEEECC		53.48-
221PhosphorylationQRDEQLLTNVLETLR
HHHHHHHHHHHHHHC		31.6925159151
226PhosphorylationLLTNVLETLRGDGNV
HHHHHHHHHCCCCCE		20.0025159151
239PhosphorylationNVLIAVDTAGRVLEL
CEEEEEECHHHHHHH		25.14-
257UbiquitinationLDQIWRTKDAGLGVY
HHHHHCCCCCCCCHH		36.69-
288PhosphorylationKSQVEWMSDKLMRCF
HHHHHHHHHHHHHHH		32.4420860994
290AcetylationQVEWMSDKLMRCFED
HHHHHHHHHHHHHHC		36.5525953088
298AcetylationLMRCFEDKRNNPFQF
HHHHHHCCCCCCHHH		50.2426051181
311GlutathionylationQFRHLSLCHGLSDLA
HHHHHHHHCCHHHHH		1.8322555962
322PhosphorylationSDLARVPSPKVVLAS
HHHHCCCCCCEEEEC		34.2024719451
324UbiquitinationLARVPSPKVVLASQP
HHCCCCCCEEEECCC		49.68-
335GlutathionylationASQPDLECGFSRDLF
ECCCCCCCCCCHHHE		9.6722555962
375UbiquitinationLIDNPSEKITEIELR
HCCCCCCCEEHHHHH		60.3021906983
390UbiquitinationKRVKLEGKELEEYLE
HHHCCCCHHHHHHHH		50.1521906983
395PhosphorylationEGKELEEYLEKEKLK
CCHHHHHHHHHHHHH		15.7020068231
398UbiquitinationELEEYLEKEKLKKEA
HHHHHHHHHHHHHHH		58.51-
412PhosphorylationAAKKLEQSKEADIDS
HHHHHHHHHHCCCCC		24.0828111955
419PhosphorylationSKEADIDSSDESDIE
HHHCCCCCCCHHHHH		39.7718707149
420PhosphorylationKEADIDSSDESDIEE
HHCCCCCCCHHHHHH		41.4718707149
423PhosphorylationDIDSSDESDIEEDID
CCCCCCHHHHHHCCC		49.2125159151
433PhosphorylationEEDIDQPSAHKTKHD
HHCCCCCCHHHCHHH		37.0524702127
438UbiquitinationQPSAHKTKHDLMMKG
CCCHHHCHHHHHHCC		39.67-
444AcetylationTKHDLMMKGEGSRKG
CHHHHHHCCCCCCCC		39.5825953088
448PhosphorylationLMMKGEGSRKGSFFK
HHHCCCCCCCCCHHH		26.90-
452PhosphorylationGEGSRKGSFFKQAKK
CCCCCCCCHHHHHHH		30.4629970186
460PhosphorylationFFKQAKKSYPMFPAP
HHHHHHHHCCCCCCC		33.4923917254
461PhosphorylationFKQAKKSYPMFPAPE
HHHHHHHCCCCCCCH		13.9523186163
472UbiquitinationPAPEERIKWDEYGEI
CCCHHHCCHHHCCCC		55.61-
476PhosphorylationERIKWDEYGEIIKPE
HHCCHHHCCCCCCHH		20.0027642862
481UbiquitinationDEYGEIIKPEDFLVP
HHCCCCCCHHHCCCC		48.27-
493PhosphorylationLVPELQATEEEKSKL
CCCCCCCCHHHHHHH		30.85-
498PhosphorylationQATEEEKSKLESGLT
CCCHHHHHHHHHCCC		45.8328555341
499UbiquitinationATEEEKSKLESGLTN
CCHHHHHHHHHCCCC		68.3021906983
551UbiquitinationSDGDSIKKIINQMKP
CCHHHHHHHHHHCCC		47.34-
557UbiquitinationKKIINQMKPRQLIIV
HHHHHHCCCCEEEEE		27.56-
584UbiquitinationCCRAFGGKDIKVYMP
HHHHHCCCEEEEECC		57.57-
587UbiquitinationAFGGKDIKVYMPKLH
HHCCCEEEEECCCCH		37.1321890473
600PhosphorylationLHETVDATSETHIYQ
CHHEECCCCCCEEEE		23.7228152594
601PhosphorylationHETVDATSETHIYQV
HHEECCCCCCEEEEE		42.0728152594
603PhosphorylationTVDATSETHIYQVRL
EECCCCCCEEEEEEE		17.2228152594
606PhosphorylationATSETHIYQVRLKDS
CCCCCEEEEEEEHHH		8.0528152594
609MethylationETHIYQVRLKDSLVS
CCEEEEEEEHHHHHH		22.09-
611UbiquitinationHIYQVRLKDSLVSSL
EEEEEEEHHHHHHHH		34.41-
621GlutathionylationLVSSLQFCKAKDAEL
HHHHHHHHCCCCCCE		2.4322555962
624UbiquitinationSLQFCKAKDAELAWI
HHHHHCCCCCCEEEE		42.86-
641UbiquitinationVLDMRVSKVDTGVIL
EEEEEEEEECCCEEE		41.07-
644PhosphorylationMRVSKVDTGVILEEG
EEEEEECCCEEEEEC		36.0127251275
660PhosphorylationLKDDGEDSEMQVEAP
CCCCCCCCCEEEECC		30.5720164059
668PhosphorylationEMQVEAPSDSSVIAQ
CEEEECCCCCHHHHH		58.1130108239
670PhosphorylationQVEAPSDSSVIAQQK
EEECCCCCHHHHHHH		30.7330108239
671PhosphorylationVEAPSDSSVIAQQKA
EECCCCCHHHHHHHH		23.6430108239
677AcetylationSSVIAQQKAMKSLFG
CHHHHHHHHHHHHHC		38.0726051181
677UbiquitinationSSVIAQQKAMKSLFG
CHHHHHHHHHHHHHC		38.07-
680UbiquitinationIAQQKAMKSLFGDDE
HHHHHHHHHHHCCCC		49.20-
680AcetylationIAQQKAMKSLFGDDE
HHHHHHHHHHHCCCC		49.2023954790
725UbiquitinationEPRLSDFKQVLLREG
CCCHHHHHHHHHHCC		44.4821890473
725MalonylationEPRLSDFKQVLLREG
CCCHHHHHHHHHHCC		44.4826320211
725UbiquitinationEPRLSDFKQVLLREG
CCCHHHHHHHHHHCC		44.4821890473
725AcetylationEPRLSDFKQVLLREG
CCCHHHHHHHHHHCC		44.4825953088
776PhosphorylationYRIRDLLYEQYAIV-
HHHHHHHHHHHCCC-		14.32-
779PhosphorylationRDLLYEQYAIV----
HHHHHHHHCCC----		6.07-
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 CPSF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPSF2_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 CPSF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSTFT_HUMANCSTF2Tphysical
14749727
CPSF3_HUMANCPSF3physical
22939629
FIP1_HUMANFIP1L1physical
22939629
WDR33_HUMANWDR33physical
22939629
SMCA4_HUMANSMARCA4physical
22939629
MED17_HUMANMED17physical
22939629
TF3C6_HUMANGTF3C6physical
22939629
RBP1_HUMANRALBP1physical
22939629
TF3C3_HUMANGTF3C3physical
22939629
SMRD3_HUMANSMARCD3physical
22939629
DPOE3_HUMANPOLE3physical
22939629
SYMPK_HUMANSYMPKphysical
18688255
CSTF2_HUMANCSTF2physical
18688255
CPSF3_HUMANCPSF3physical
18688255
CSTF2_HUMANCSTF2physical
26344197
FIP1_HUMANFIP1L1physical
26344197
ISY1_HUMANISY1physical
26344197
PAPOA_HUMANPAPOLAphysical
26344197
SPT5H_HUMANSUPT5Hphysical
26344197
SYMPK_HUMANSYMPKphysical
26344197
FIP1_HUMANFIP1L1physical
14749727
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 CPSF2_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-419; SER-420 ANDSER-423, 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-419; SER-420 ANDSER-423, 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-419; SER-420; SER-423AND SER-660, AND MASS SPECTROMETRY.
"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 TYR-395; SER-419; SER-420AND SER-423, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, AND MASSSPECTROMETRY.

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