TRFE_MOUSE - dbPTM
TRFE_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRFE_MOUSE
UniProt AC Q921I1
Protein Name Serotransferrin
Gene Name Tf
Organism Mus musculus (Mouse).
Sequence Length 697
Subcellular Localization Secreted.
Protein Description Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation..
Protein Sequence MRLTVGALLACAALGLCLAVPDKTVKWCAVSEHENTKCISFRDHMKTVLPPDGPRLACVKKTSYPDCIKAISASEADAMTLDGGWVYDAGLTPNNLKPVAAEFYGSVEHPQTYYYAVAVVKKGTDFQLNQLEGKKSCHTGLGRSAGWVIPIGLLFCKLSEPRSPLEKAVSSFFSGSCVPCADPVAFPKLCQLCPGCGCSSTQPFFGYVGAFKCLKDGGGDVAFVKHTTIFEVLPEKADRDQYELLCLDNTRKPVDQYEDCYLARIPSHAVVARKNNGKEDLIWEILKVAQEHFGKGKSKDFQLFSSPLGKDLLFKDSAFGLLRVPPRMDYRLYLGHNYVTAIRNQQEGVCPEGSIDNSPVKWCALSHLERTKCDEWSIISEGKIECESAETTEDCIEKIVNGEADAMTLDGGHAYIAGQCGLVPVMAEYYESSNCAIPSQQGIFPKGYYAVAVVKASDTSITWNNLKGKKSCHTGVDRTAGWNIPMGMLYNRINHCKFDEFFSQGCAPGYEKNSTLCDLCIGPLKCAPNNKEEYNGYTGAFRCLVEKGDVAFVKHQTVLDNTEGKNPAEWAKNLKQEDFELLCPDGTRKPVKDFASCHLAQAPNHVVVSRKEKAARVKAVLTSQETLFGGSDCTGNFCLFKSTTKDLLFRDDTKCFVKLPEGTTPEKYLGAEYMQSVGNMRKCSTSRLLEACTFHKH
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
42MethylationNTKCISFRDHMKTVL
CCEEEEEHHHHCCCC		26.57-
58S-palmitoylationPDGPRLACVKKTSYP
CCCCCEEEEEECCCH		5.6626165157
67S-palmitoylationKKTSYPDCIKAISAS
EECCCHHHHHHHCCH		2.7326165157
134AcetylationQLNQLEGKKSCHTGL
CCHHCCCCCCCCCCC		31.9419865995
134UbiquitinationQLNQLEGKKSCHTGL
CCHHCCCCCCCCCCC		31.94-
137GlutathionylationQLEGKKSCHTGLGRS
HCCCCCCCCCCCCCC		4.5924333276
144PhosphorylationCHTGLGRSAGWVIPI
CCCCCCCCCCEEEEE		29.3624719451
156S-palmitoylationIPIGLLFCKLSEPRS
EEEEEEEEECCCCCC		4.3528526873
163PhosphorylationCKLSEPRSPLEKAVS
EECCCCCCHHHHHHH		44.5524719451
170PhosphorylationSPLEKAVSSFFSGSC
CHHHHHHHHHHCCCC		26.7023984901
171PhosphorylationPLEKAVSSFFSGSCV
HHHHHHHHHHCCCCC		24.5823984901
174PhosphorylationKAVSSFFSGSCVPCA
HHHHHHHCCCCCCCC		27.9923984901
176PhosphorylationVSSFFSGSCVPCADP
HHHHHCCCCCCCCCC		15.6723984901
177S-palmitoylationSSFFSGSCVPCADPV
HHHHCCCCCCCCCCC		4.5226165157
207PhosphorylationSTQPFFGYVGAFKCL
CCCCCCCEEEEEEEE		7.2024719451
213S-palmitoylationGYVGAFKCLKDGGGD
CEEEEEEEEECCCCC		4.6326165157
225AcetylationGGDVAFVKHTTIFEV
CCCEEEEEECEEEEE		28.8722902405
252UbiquitinationLCLDNTRKPVDQYED
EEECCCCCCCHHCCC		47.56-
260S-palmitoylationPVDQYEDCYLARIPS
CCHHCCCCEEECCCC		1.6826165157
278UbiquitinationVARKNNGKEDLIWEI
EEECCCCCHHHHHHH		50.61-
297AcetylationQEHFGKGKSKDFQLF
HHHHCCCCCCCCEEE		58.7922902405
299UbiquitinationHFGKGKSKDFQLFSS
HHCCCCCCCCEEECC		67.0827667366
305PhosphorylationSKDFQLFSSPLGKDL
CCCCEEECCCCCCCC		39.3723984901
306PhosphorylationKDFQLFSSPLGKDLL
CCCEEECCCCCCCCC		19.4623984901
310SuccinylationLFSSPLGKDLLFKDS
EECCCCCCCCCCCCC		53.5423954790
310UbiquitinationLFSSPLGKDLLFKDS
EECCCCCCCCCCCCC		53.54-
310AcetylationLFSSPLGKDLLFKDS
EECCCCCCCCCCCCC		53.5423954790
315UbiquitinationLGKDLLFKDSAFGLL
CCCCCCCCCCCCCCC		51.23-
315AcetylationLGKDLLFKDSAFGLL
CCCCCCCCCCCCCCC		51.2321728379
340PhosphorylationYLGHNYVTAIRNQQE
EECCCHHHHHHCCCC		13.1524719451
373S-palmitoylationSHLERTKCDEWSIIS
HCHHCCCCCCCEEEE		5.9128526873
388PhosphorylationEGKIECESAETTEDC
CCEEEECCCCCHHHH		42.96-
467SuccinylationSITWNNLKGKKSCHT
CCEECCCCCCCCCCC		71.4623954790
467UbiquitinationSITWNNLKGKKSCHT
CCEECCCCCCCCCCC		71.46-
474PhosphorylationKGKKSCHTGVDRTAG
CCCCCCCCCCCCCCC		43.1328059163
506S-palmitoylationDEFFSQGCAPGYEKN
HHHHHCCCCCCCCCC		2.9928526873
513N-linked_GlycosylationCAPGYEKNSTLCDLC
CCCCCCCCCCHHHHH		28.4317330941
526S-palmitoylationLCIGPLKCAPNNKEE
HHCCEEEECCCCCCH		11.3826165157
531UbiquitinationLKCAPNNKEEYNGYT
EEECCCCCCHHCCCC		59.57-
537PhosphorylationNKEEYNGYTGAFRCL
CCCHHCCCCCCEEHE		9.8124719451
543S-palmitoylationGYTGAFRCLVEKGDV
CCCCCEEHEEECCCE		3.9426165157
554UbiquitinationKGDVAFVKHQTVLDN
CCCEEEEECEEECCC		24.44-
554AcetylationKGDVAFVKHQTVLDN
CCCEEEEECEEECCC		24.4423954790
572AcetylationKNPAEWAKNLKQEDF
CCHHHHHHHCCHHHC		64.9823954790
583S-palmitoylationQEDFELLCPDGTRKP
HHHCEEECCCCCCCC		4.5126165157
597S-palmitoylationPVKDFASCHLAQAPN
CCHHHHHCCCCCCCC		2.4628526873
655S-palmitoylationLFRDDTKCFVKLPEG
EECCCCCEEEECCCC		5.2826165157
667UbiquitinationPEGTTPEKYLGAEYM
CCCCCHHHHCCHHHH		47.15-
684PhosphorylationVGNMRKCSTSRLLEA
HCCCCCCCHHHHHHH		32.24-
692S-palmitoylationTSRLLEACTFHKH--
HHHHHHHHCCCCC--		2.8126165157
696AcetylationLEACTFHKH------
HHHHCCCCC------		46.9823201123
696UbiquitinationLEACTFHKH------
HHHHCCCCC------		46.9822790023
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 TRFE_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.";
Bernhard O.K., Kapp E.A., Simpson R.J.;
J. Proteome Res. 6:987-995(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-513, AND MASSSPECTROMETRY.

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