CSTF1_HUMAN - dbPTM
CSTF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSTF1_HUMAN
UniProt AC Q05048
Protein Name Cleavage stimulation factor subunit 1
Gene Name CSTF1
Organism Homo sapiens (Human).
Sequence Length 431
Subcellular Localization Nucleus.
Protein Description One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA..
Protein Sequence MYRTKVGLKDRQQLYKLIISQLLYDGYISIANGLINEIKPQSVCAPSEQLLHLIKLGMENDDTAVQYAIGRSDTVAPGTGIDLEFDADVQTMSPEASEYETCYVTSHKGPCRVATYSRDGQLIATGSADASIKILDTERMLAKSAMPIEVMMNETAQQNMENHPVIRTLYDHVDEVTCLAFHPTEQILASGSRDYTLKLFDYSKPSAKRAFKYIQEAEMLRSISFHPSGDFILVGTQHPTLRLYDINTFQCFVSCNPQDQHTDAICSVNYNSSANMYVTGSKDGCIKLWDGVSNRCITTFEKAHDGAEVCSAIFSKNSKYILSSGKDSVAKLWEISTGRTLVRYTGAGLSGRQVHRTQAVFNHTEDYVLLPDERTISLCCWDSRTAERRNLLSLGHNNIVRCIVHSPTNPGFMTCSDDFRARFWYRRSTTD
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
58SulfoxidationLHLIKLGMENDDTAV
HHHHHHCCCCCCHHH		6.7021406390
63PhosphorylationLGMENDDTAVQYAIG
HCCCCCCHHHHHHHC		31.4321945579
67PhosphorylationNDDTAVQYAIGRSDT
CCCHHHHHHHCCCCC		8.1221945579
143UbiquitinationDTERMLAKSAMPIEV
CHHHHHHHHCCCHHH		34.48-
195PhosphorylationLASGSRDYTLKLFDY
HCCCCCCEEEEECCC		16.92-
198UbiquitinationGSRDYTLKLFDYSKP
CCCCEEEEECCCCCH		39.0329967540
204AcetylationLKLFDYSKPSAKRAF
EEECCCCCHHHHHHH		36.4426051181
204UbiquitinationLKLFDYSKPSAKRAF
EEECCCCCHHHHHHH		36.4422817900
208UbiquitinationDYSKPSAKRAFKYIQ
CCCCHHHHHHHHHHH		48.9022817900
208AcetylationDYSKPSAKRAFKYIQ
CCCCHHHHHHHHHHH		48.9025953088
273O-linked_GlycosylationCSVNYNSSANMYVTG
EEEECCCCCCEEEEE		21.74OGP
287UbiquitinationGSKDGCIKLWDGVSN
ECCCCEEEEECCCCC		47.8329967540
287AcetylationGSKDGCIKLWDGVSN
ECCCCEEEEECCCCC		47.8326051181
302AcetylationRCITTFEKAHDGAEV
EEEEECHHCCCHHHH		46.9926051181
315PhosphorylationEVCSAIFSKNSKYIL
HHHHHHHCCCCCEEE		25.4724719451
316UbiquitinationVCSAIFSKNSKYILS
HHHHHHCCCCCEEEC		55.2629967540
319UbiquitinationAIFSKNSKYILSSGK
HHHCCCCCEEECCCC		45.7827667366
319AcetylationAIFSKNSKYILSSGK
HHHCCCCCEEECCCC		45.7826051181
326AcetylationKYILSSGKDSVAKLW
CEEECCCCHHHHHHH		49.1026051181
3262-HydroxyisobutyrylationKYILSSGKDSVAKLW
CEEECCCCHHHHHHH		49.10-
326UbiquitinationKYILSSGKDSVAKLW
CEEECCCCHHHHHHH		49.1029967540
364PhosphorylationTQAVFNHTEDYVLLP
EEHCCCCCCCEEECC		31.4922210691
367PhosphorylationVFNHTEDYVLLPDER
CCCCCCCEEECCCCC		6.1722817900
393PhosphorylationAERRNLLSLGHNNIV
HHHHHHHHCCCCCEE		35.16-
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 CSTF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSTF1_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 CSTF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BARD1_HUMANBARD1physical
10477523
BARD1_HUMANBARD1physical
11257228
BARD1_HUMANBARD1physical
18842000
PARN_HUMANPARNphysical
20379136
BARD1_HUMANBARD1physical
20379136
CSTF3_HUMANCSTF3physical
26344197
DCNL1_HUMANDCUN1D1physical
26344197
DLDH_HUMANDLDphysical
26344197
DAAF5_HUMANDNAAF5physical
26344197
HPBP1_HUMANHSPBP1physical
26344197
MK03_HUMANMAPK3physical
26344197
NMD3_HUMANNMD3physical
26344197
PEPL1_HUMANNPEPL1physical
26344197
TADBP_HUMANTARDBPphysical
26344197
TTC27_HUMANTTC27physical
26344197
XPO6_HUMANXPO6physical
26344197
BARD1_HUMANBARD1physical
27591253
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 CSTF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-367, AND MASSSPECTROMETRY.

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