T2FA_MOUSE - dbPTM
T2FA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T2FA_MOUSE
UniProt AC Q3THK3
Protein Name General transcription factor IIF subunit 1
Gene Name Gtf2f1
Organism Mus musculus (Mouse).
Sequence Length 508
Subcellular Localization Nucleus.
Protein Description TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation (By similarity)..
Protein Sequence MAALGSSSQNVTEYVVRVPKNTAKRYNIMAFNAADKVNFATWNQARLERDLSNKKIYQEEEMPESGAGSEFNRKLREEARRKKYGIVLKEFRPEDQPWLLRVNGKSGRKFKGIKKGGVTENTAYYIFTQCADGAFEAFPVQNWYNFTPLARHRTLTAEEAEEEWERRNKVLNHFSIMQQRRLKDQDQDEDEEEKEKRSRKKPSELRIHDLEDDLEMSSDASDASGEEGSRTSKAKKKAPVTKAGRKKKKKKGSDDEAFEDSDDGDFEGQEVDYMSDGSSSSPDETEGKPKVPQQEDGPKGVDEQSESSEESEEEKPPEEDKEEEEEKKAPTPQEKKRRKDSSDDSDSSEESDIDSETSSALFMAKKKTPPKRERKPSGGSSKGTSRPGTPSAEAASTSSTLRAAASKLEQGKRTSETPAAKRLRMDTGPQSLSGKSTPSSGDVQVTEDAVRRYLTRKPMTTKDLLKKFQTKKTGLSSEQTVNVLAQILKRLNPERKMIGDKMHFSLKE
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
2Acetylation------MAALGSSSQ
------CCCCCCCCC		16.05-
54AcetylationLERDLSNKKIYQEEE
HHHHHCCCCCCCCCC		36.857624199
74AcetylationAGSEFNRKLREEARR
CCHHHHHHHHHHHHH		53.667624211
154PhosphorylationTPLARHRTLTAEEAE
CCCCCCCCCCHHHHH		23.4925266776
156PhosphorylationLARHRTLTAEEAEEE
CCCCCCCCHHHHHHH		31.2625266776
217PhosphorylationLEDDLEMSSDASDAS
HHHHHHHCCCCCCCC		18.7221082442
218PhosphorylationEDDLEMSSDASDASG
HHHHHHCCCCCCCCC		35.5721082442
221PhosphorylationLEMSSDASDASGEEG
HHHCCCCCCCCCCCC		38.4121082442
224PhosphorylationSSDASDASGEEGSRT
CCCCCCCCCCCCCCC		52.2921082442
229PhosphorylationDASGEEGSRTSKAKK
CCCCCCCCCCCHHHH		35.3521149613
305PhosphorylationPKGVDEQSESSEESE
CCCCCCCCCCCCCCC		37.0823684622
307PhosphorylationGVDEQSESSEESEEE
CCCCCCCCCCCCCCC		48.5823684622
308PhosphorylationVDEQSESSEESEEEK
CCCCCCCCCCCCCCC		41.1323684622
311PhosphorylationQSESSEESEEEKPPE
CCCCCCCCCCCCCCH		46.3823684622
331PhosphorylationEEEKKAPTPQEKKRR
HHHHHCCCHHHHHHH		42.3325521595
341PhosphorylationEKKRRKDSSDDSDSS
HHHHHCCCCCCCCCC		38.4119854140
342PhosphorylationKKRRKDSSDDSDSSE
HHHHCCCCCCCCCCC		56.4219854140
345PhosphorylationRKDSSDDSDSSEESD
HCCCCCCCCCCCHHH		44.3719854140
347PhosphorylationDSSDDSDSSEESDID
CCCCCCCCCCHHHCC		43.5319854140
348PhosphorylationSSDDSDSSEESDIDS
CCCCCCCCCHHHCCH		50.8323608596
351PhosphorylationDSDSSEESDIDSETS
CCCCCCHHHCCHHHH		35.5019854140
355PhosphorylationSEESDIDSETSSALF
CCHHHCCHHHHHHHH		43.0123608596
357PhosphorylationESDIDSETSSALFMA
HHHCCHHHHHHHHHH		31.7523608596
368PhosphorylationLFMAKKKTPPKRERK
HHHHCCCCCCCCCCC		54.42-
377PhosphorylationPKRERKPSGGSSKGT
CCCCCCCCCCCCCCC		59.8425266776
380PhosphorylationERKPSGGSSKGTSRP
CCCCCCCCCCCCCCC		32.1924899341
381PhosphorylationRKPSGGSSKGTSRPG
CCCCCCCCCCCCCCC		38.0821183079
384PhosphorylationSGGSSKGTSRPGTPS
CCCCCCCCCCCCCCC		25.8725521595
385PhosphorylationGGSSKGTSRPGTPSA
CCCCCCCCCCCCCCH		45.1827087446
389PhosphorylationKGTSRPGTPSAEAAS
CCCCCCCCCCHHHHC		19.4327087446
391PhosphorylationTSRPGTPSAEAASTS
CCCCCCCCHHHHCCH		38.2825521595
396PhosphorylationTPSAEAASTSSTLRA
CCCHHHHCCHHHHHH		35.5525619855
397PhosphorylationPSAEAASTSSTLRAA
CCHHHHCCHHHHHHH		23.2125619855
398PhosphorylationSAEAASTSSTLRAAA
CHHHHCCHHHHHHHH		20.8725619855
399PhosphorylationAEAASTSSTLRAAAS
HHHHCCHHHHHHHHH		31.3925619855
400PhosphorylationEAASTSSTLRAAASK
HHHCCHHHHHHHHHH		21.7425619855
406PhosphorylationSTLRAAASKLEQGKR
HHHHHHHHHHHHCCC		32.8026643407
407AcetylationTLRAAASKLEQGKRT
HHHHHHHHHHHCCCC		51.8523806337
413MethylationSKLEQGKRTSETPAA
HHHHHCCCCCCCHHH		50.76-
425OxidationPAAKRLRMDTGPQSL
HHHHHHHCCCCCCCC		6.8217242355
427PhosphorylationAKRLRMDTGPQSLSG
HHHHHCCCCCCCCCC		41.2225168779
431PhosphorylationRMDTGPQSLSGKSTP
HCCCCCCCCCCCCCC		27.8625168779
433PhosphorylationDTGPQSLSGKSTPSS
CCCCCCCCCCCCCCC		49.8025521595
436PhosphorylationPQSLSGKSTPSSGDV
CCCCCCCCCCCCCCC		49.4227087446
437PhosphorylationQSLSGKSTPSSGDVQ
CCCCCCCCCCCCCCC		30.5825521595
439PhosphorylationLSGKSTPSSGDVQVT
CCCCCCCCCCCCCCC		47.2221082442
440PhosphorylationSGKSTPSSGDVQVTE
CCCCCCCCCCCCCCH		39.9721082442
446PhosphorylationSSGDVQVTEDAVRRY
CCCCCCCCHHHHHHH		15.8525367039
461PhosphorylationLTRKPMTTKDLLKKF
HHCCCCCHHHHHHHH		19.1319854140
505PhosphorylationIGDKMHFSLKE----
CCCCCCCCCCC----		24.69-
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 T2FA_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T2FA_MOUSE !!
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 T2FA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of T2FA_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of T2FA_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221AND SER-224, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-331, AND MASSSPECTROMETRY.

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