dbPTM

TFR1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFR1_MOUSE
UniProt AC	Q62351
Protein Name	Transferrin receptor protein 1
Gene Name	Tfrc
Organism	Mus musculus (Mouse).
Sequence Length	763
Subcellular Localization	Cell membrane Single-pass type II membrane protein . Melanosome .
Protein Description	Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). Upon stimulation, positively regulates T and B cell proliferation through iron uptake. [PubMed: 26642240]
Protein Sequence	MMDQARSAFSNLFGGEPLSYTRFSLARQVDGDNSHVEMKLAADEEENADNNMKASVRKPKRFNGRLCFAAIALVIFFLIGFMSGYLGYCKRVEQKEECVKLAETEETDKSETMETEDVPTSSRLYWADLKTLLSEKLNSIEFADTIKQLSQNTYTPREAGSQKDESLAYYIENQFHEFKFSKVWRDEHYVKIQVKSSIGQNMVTIVQSNGNLDPVESPEGYVAFSKPTEVSGKLVHANFGTKKDFEELSYSVNGSLVIVRAGEITFAEKVANAQSFNAIGVLIYMDKNKFPVVEADLALFGHAHLGTGDPYTPGFPSFNHTQFPPSQSSGLPNIPVQTISRAAAEKLFGKMEGSCPARWNIDSSCKLELSQNQNVKLIVKNVLKERRILNIFGVIKGYEEPDRYVVVGAQRDALGAGVAAKSSVGTGLLLKLAQVFSDMISKDGFRPSRSIIFASWTAGDFGAVGATEWLEGYLSSLHLKAFTYINLDKVVLGTSNFKVSASPLLYTLMGKIMQDVKHPVDGKSLYRDSNWISKVEKLSFDNAAYPFLAYSGIPAVSFCFCEDADYPYLGTRLDTYEALTQKVPQLNQMVRTAAEVAGQLIIKLTHDVELNLDYEMYNSKLLSFMKDLNQFKTDIRDMGLSLQWLYSARGDYFRATSRLTTDFHNAEKTNRFVMREINDRIMKVEYHFLSPYVSPRESPFRHIFWGSGSHTLSALVENLKLRQKNITAFNETLFRNQLALATWTIQGVANALSGDIWNIDNEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MMDQARSAFSNLFG -CHHHHHHHHHHHHC	36.36	22499769
10	Phosphorylation	DQARSAFSNLFGGEP HHHHHHHHHHHCCCC	32.13	-
19	Phosphorylation	LFGGEPLSYTRFSLA HHCCCCCCEEEEEEE	34.86	21082442
20	Phosphorylation	FGGEPLSYTRFSLAR HCCCCCCEEEEEEEE	15.04	18515860
21	Phosphorylation	GGEPLSYTRFSLARQ CCCCCCEEEEEEEEE	23.12	18515860
24	Phosphorylation	PLSYTRFSLARQVDG CCCEEEEEEEEECCC	20.16	26239621
34	Phosphorylation	RQVDGDNSHVEMKLA EECCCCCCCEEEEEE	33.38	25521595
39	Ubiquitination	DNSHVEMKLAADEEE CCCCEEEEEECCCHH	22.82	-
53	Ubiquitination	ENADNNMKASVRKPK HCCCCCCCCCCCCCC	39.37	-
55	Phosphorylation	ADNNMKASVRKPKRF CCCCCCCCCCCCCHH	19.55	25266776
67	S-palmitoylation	KRFNGRLCFAAIALV CHHCHHHHHHHHHHH	1.78	-
104	O-linked_Glycosylation	ECVKLAETEETDKSE HHHHHHHCCCCCCCC	33.25	-
134	Phosphorylation	ADLKTLLSEKLNSIE HHHHHHHHHHHCHHH	35.48	23737553
253	N-linked_Glycosylation	EELSYSVNGSLVIVR HHHEEEECCEEEEEE	28.53	-
319	N-linked_Glycosylation	TPGFPSFNHTQFPPS CCCCCCCCCCCCCCC	41.45	-
354	Phosphorylation	LFGKMEGSCPARWNI HHCCCCCCCCCCCCC	12.01	21659604
370	Phosphorylation	SSCKLELSQNQNVKL CCCEEEECCCCCCEE	20.08	21659604
437	Phosphorylation	LKLAQVFSDMISKDG HHHHHHHHHHHCCCC	27.67	29899451
500	Phosphorylation	GTSNFKVSASPLLYT ECCCCEEECHHHHHH	24.50	26060331
502	Phosphorylation	SNFKVSASPLLYTLM CCCEEECHHHHHHHH	14.47	26060331
506	Phosphorylation	VSASPLLYTLMGKIM EECHHHHHHHHHHHH	12.90	26060331
507	Phosphorylation	SASPLLYTLMGKIMQ ECHHHHHHHHHHHHC	15.39	26060331
619	Phosphorylation	LDYEMYNSKLLSFMK CCHHHHHHHHHHHHH	13.75	28285833
623	Phosphorylation	MYNSKLLSFMKDLNQ HHHHHHHHHHHHHHH	33.46	28285833
725	N-linked_Glycosylation	NLKLRQKNITAFNET HHHHHHCCCCCCHHH	28.62	19349973
730	N-linked_Glycosylation	QKNITAFNETLFRNQ HCCCCCCHHHHHHCH	38.59	19349973

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
-	K	Ubiquitination	E3 ubiquitin ligase	Marchf1	Q6NZQ8	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	MARCHF2	Q99M02	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TFR1_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 TFR1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TFR1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TFR1_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-725 AND ASN-730, AND MASSSPECTROMETRY.	19349973 [Abstract]
Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASSSPECTROMETRY.	17947660 [Abstract]