CSTFT_HUMAN - dbPTM
CSTFT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSTFT_HUMAN
UniProt AC Q9H0L4
Protein Name Cleavage stimulation factor subunit 2 tau variant
Gene Name CSTF2T
Organism Homo sapiens (Human).
Sequence Length 616
Subcellular Localization Nucleus.
Protein Description May play a significant role in AAUAAA-independent mRNA polyadenylation in germ cells. Directly involved in the binding to pre-mRNAs (By similarity)..
Protein Sequence MSSLAVRDPAMDRSLRSVFVGNIPYEATEEQLKDIFSEVGSVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGPAAPIIDSPYGDPIDPEDAPESITRAVASLPPEQMFELMKQMKLCVQNSHQEARNMLLQNPQLAYALLQAQVVMRIMDPEIALKILHRKIHVTPLIPGKSQSVSVSGPGPGPGPGLCPGPNVLLNQQNPPAPQPQHLARRPVKDIPPLMQTPIQGGIPAPGPIPAAVPGAGPGSLTPGGAMQPQLGMPGVGPVPLERGQVQMSDPRAPIPRGPVTPGGLPPRGLLGDAPNDPRGGTLLSVTGEVEPRGYLGPPHQGPPMHHASGHDTRGPSSHEMRGGPLGDPRLLIGEPRGPMIDQRGLPMDGRGGRDSRAMETRAMETEVLETRVMERRGMETCAMETRGMEARGMDARGLEMRGPVPSSRGPMTGGIQGPGPINIGAGGPPQGPRQVPGISGVGNPGAGMQGTGIQGTGMQGAGIQGGGMQGAGIQGVSIQGGGIQGGGIQGASKQGGSQPSSFSPGQSQVTPQDQEKAALIMQVLQLTADQIAMLPPEQRQSILILKEQIQKSTGAS
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------MSSLAVRDP
------CCCCCCCCH		33.7820860994
3Phosphorylation-----MSSLAVRDPA
-----CCCCCCCCHH		21.0320860994
41PhosphorylationDIFSEVGSVVSFRLV
HHHHHHCCEEEEEEE		25.2330387612
44PhosphorylationSEVGSVVSFRLVYDR
HHHCCEEEEEEEEEC		11.5130387612
55UbiquitinationVYDRETGKPKGYGFC
EEECCCCCCCCCCCC		51.48-
57UbiquitinationDRETGKPKGYGFCEY
ECCCCCCCCCCCCCC		69.1524816145
96UbiquitinationVDNAASEKNKEELKS
CCCHHHHHCHHHHHH		71.47-
98UbiquitinationNAASEKNKEELKSLG
CHHHHHCHHHHHHHC		64.7329967540
102UbiquitinationEKNKEELKSLGPAAP
HHCHHHHHHHCCCCC		47.0829967540
113PhosphorylationPAAPIIDSPYGDPID
CCCCCCCCCCCCCCC		15.0426657352
115PhosphorylationAPIIDSPYGDPIDPE
CCCCCCCCCCCCCHH		37.8129632367
145UbiquitinationEQMFELMKQMKLCVQ
HHHHHHHHHHHHHHH		60.9223000965
148UbiquitinationFELMKQMKLCVQNSH
HHHHHHHHHHHHCCH		35.9223000965
189UbiquitinationMDPEIALKILHRKIH
CCHHHHHHHHCCCEE		33.9123000965
194UbiquitinationALKILHRKIHVTPLI
HHHHHCCCEEEEECC		26.8123000965
198PhosphorylationLHRKIHVTPLIPGKS
HCCCEEEEECCCCCC		9.7520068231
205PhosphorylationTPLIPGKSQSVSVSG
EECCCCCCCEEEECC		33.33-
256PhosphorylationDIPPLMQTPIQGGIP
CCCCCCCCCCCCCCC		14.3728348404
279PhosphorylationVPGAGPGSLTPGGAM
CCCCCCCCCCCCCCC		32.0028348404
281PhosphorylationGAGPGSLTPGGAMQP
CCCCCCCCCCCCCCC		22.9128348404
308PhosphorylationERGQVQMSDPRAPIP
CCCCEECCCCCCCCC		27.6328555341
311MethylationQVQMSDPRAPIPRGP
CEECCCCCCCCCCCC		58.97-
316MethylationDPRAPIPRGPVTPGG
CCCCCCCCCCCCCCC		63.87-
320PhosphorylationPIPRGPVTPGGLPPR
CCCCCCCCCCCCCCC		21.2525394399
327DimethylationTPGGLPPRGLLGDAP
CCCCCCCCCCCCCCC		46.59-
327MethylationTPGGLPPRGLLGDAP
CCCCCCCCCCCCCCC		46.59-
338MethylationGDAPNDPRGGTLLSV
CCCCCCCCCCCEEEE		60.06-
341PhosphorylationPNDPRGGTLLSVTGE
CCCCCCCCEEEEECE		27.6120860994
344PhosphorylationPRGGTLLSVTGEVEP
CCCCCEEEEECEECC		22.2720860994
346PhosphorylationGGTLLSVTGEVEPRG
CCCEEEEECEECCCC		25.0120860994
352MethylationVTGEVEPRGYLGPPH
EECEECCCCCCCCCC		32.65-
368PhosphorylationGPPMHHASGHDTRGP
CCCCCCCCCCCCCCC		32.1028348404
372PhosphorylationHHASGHDTRGPSSHE
CCCCCCCCCCCCCCC		31.6729449344
373MethylationHASGHDTRGPSSHEM
CCCCCCCCCCCCCCC		62.17-
381MethylationGPSSHEMRGGPLGDP
CCCCCCCCCCCCCCC		43.88-
389MethylationGGPLGDPRLLIGEPR
CCCCCCCCEECCCCC		47.03-
396MethylationRLLIGEPRGPMIDQR
CEECCCCCCCCCCCC		58.51-
403MethylationRGPMIDQRGLPMDGR
CCCCCCCCCCCCCCC		44.88-
410MethylationRGLPMDGRGGRDSRA
CCCCCCCCCCHHHHH		39.88-
413MethylationPMDGRGGRDSRAMET
CCCCCCCHHHHHHHH		41.37-
420PhosphorylationRDSRAMETRAMETEV
HHHHHHHHHHHHHHH		15.6228509920
423SulfoxidationRAMETRAMETEVLET
HHHHHHHHHHHHHHH		6.2021406390
425PhosphorylationMETRAMETEVLETRV
HHHHHHHHHHHHHHH		20.5028509920
430PhosphorylationMETEVLETRVMERRG
HHHHHHHHHHHHHCC		25.1428509920
440PhosphorylationMERRGMETCAMETRG
HHHCCCCHHHHHHCC		9.1822210691
445PhosphorylationMETCAMETRGMEARG
CCHHHHHHCCHHHCC		21.3122210691
461MethylationDARGLEMRGPVPSSR
CCCCCEECCCCCCCC		36.57-
466PhosphorylationEMRGPVPSSRGPMTG
EECCCCCCCCCCCCC		32.66-
466O-linked_GlycosylationEMRGPVPSSRGPMTG
EECCCCCCCCCCCCC		32.6623301498
467O-linked_GlycosylationMRGPVPSSRGPMTGG
ECCCCCCCCCCCCCC		34.8823301498
467PhosphorylationMRGPVPSSRGPMTGG
ECCCCCCCCCCCCCC		34.88-
472PhosphorylationPSSRGPMTGGIQGPG
CCCCCCCCCCCCCCC		35.0828555341
557PhosphorylationGASKQGGSQPSSFSP
CCCCCCCCCCCCCCC		45.8217525332
560PhosphorylationKQGGSQPSSFSPGQS
CCCCCCCCCCCCCCC		36.0623401153
561PhosphorylationQGGSQPSSFSPGQSQ
CCCCCCCCCCCCCCC		36.1030266825
563PhosphorylationGSQPSSFSPGQSQVT
CCCCCCCCCCCCCCC		30.0322167270
567PhosphorylationSSFSPGQSQVTPQDQ
CCCCCCCCCCCHHHH		32.3117525332
570PhosphorylationSPGQSQVTPQDQEKA
CCCCCCCCHHHHHHH		13.9523927012
601PhosphorylationLPPEQRQSILILKEQ
CCHHHHHHHHHHHHH		22.8821406692
606UbiquitinationRQSILILKEQIQKST
HHHHHHHHHHHHHHH		40.35-
611UbiquitinationILKEQIQKSTGAS--
HHHHHHHHHHCCC--		52.1733845483
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 CSTFT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSTFT_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 CSTFT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBQL1_HUMANUBQLN1physical
16189514
UBQL1_HUMANUBQLN1physical
25416956
CSTF1_HUMANCSTF1physical
26344197
GOGA2_HUMANGOLGA2physical
21516116
CSTF3_HUMANCSTF3physical
28514442
CSTF2_HUMANCSTF2physical
28514442
CSTF1_HUMANCSTF1physical
28514442
SYMPK_HUMANSYMPKphysical
28514442
CRTAP_HUMANCRTAPphysical
28514442
P3H1_HUMANP3H1physical
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 CSTFT_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-563, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557 AND SER-567, ANDMASS 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-563, AND MASSSPECTROMETRY.

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