CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002016
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transferrin receptor protein 1 
Protein Synonyms/Alias
 TR; TfR; TfR1; Trfr; T9; p90; CD71; Transferrin receptor protein 1, serum form; sTfR 
Gene Name
 TFRC 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
39DNSHVEMKLAVDEEEubiquitination[1, 2, 3, 4, 5, 6, 7]
53ENADNNTKANVTKPKubiquitination[2, 5, 6]
58NTKANVTKPKRCSGSubiquitination[2, 6]
128RLYWDDLKRKLSEKLubiquitination[2, 5]
130YWDDLKRKLSEKLDSubiquitination[5]
134LKRKLSEKLDSTDFTubiquitination[5]
145TDFTGTIKLLNENSYubiquitination[2, 5, 6]
161PREAGSQKDENLALYubiquitination[2, 5]
193HFVKIQVKDSAQNSVubiquitination[5]
205NSVIIVDKNGRLVYLubiquitination[2, 5]
224GGYVAYSKAATVTGKubiquitination[2, 5, 6]
231KAATVTGKLVHANFGubiquitination[5]
241HANFGTKKDFEDLYTubiquitination[5]
344ISRAAAEKLFGNMEGubiquitination[5]
358GDCPSDWKTDSTCRMubiquitination[5]
374TSESKNVKLTVSNVLubiquitination[5]
382LTVSNVLKEIKILNIubiquitination[2, 5]
385SNVLKEIKILNIFGVubiquitination[5]
394LNIFGVIKGFVEPDHacetylation[8]
394LNIFGVIKGFVEPDHubiquitination[6]
418AWGPGAAKSGVGTALacetylation[8]
418AWGPGAAKSGVGTALubiquitination[2, 5, 6]
486FTYINLDKAVLGTSNubiquitination[5]
514EKTMQNVKHPVTGQFubiquitination[5]
531QDSNWASKVEKLTLDubiquitination[2, 5]
534NWASKVEKLTLDNAAubiquitination[5]
585ERIPELNKVARAAAEubiquitination[5]
665TDFGNAEKTDRFVMKubiquitination[2, 5]
693LSPYVSPKESPFRHVubiquitination[2, 5]
717PALLENLKLRKQNNGubiquitination[5]
720LENLKLRKQNNGAFNubiquitination[5]
Reference
 [1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional 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). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. 
Sequence Annotation
 DOMAIN 223 313 PA.
 REGION 1 67 Mediates interaction with SH3BP4.
 REGION 569 760 Ligand-binding.
 MOTIF 20 23 Endocytosis signal.
 MOTIF 58 61 Stop-transfer sequence.
 MOTIF 646 648 Cell attachment site; required for
 MOD_RES 20 20 Phosphotyrosine.
 MOD_RES 21 21 Phosphothreonine.
 MOD_RES 24 24 Phosphoserine.
 LIPID 62 62 S-palmitoyl cysteine.
 LIPID 67 67 S-palmitoyl cysteine.
 CARBOHYD 104 104 O-linked (GalNAc...).
 CARBOHYD 251 251 N-linked (GlcNAc...).
 CARBOHYD 317 317 N-linked (GlcNAc...).
 CARBOHYD 727 727 N-linked (GlcNAc...).
 DISULFID 89 89 Interchain.
 DISULFID 98 98 Interchain.  
Keyword
 3D-structure; Cell membrane; Complete proteome; Direct protein sequencing; Disulfide bond; Endocytosis; Glycoprotein; Host-virus interaction; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Secreted; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 760 AA 
Protein Sequence
MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AVDEEENADN NTKANVTKPK 60
RCSGSICYGT IAVIVFFLIG FMIGYLGYCK GVEPKTECER LAGTESPVRE EPGEDFPAAR 120
RLYWDDLKRK LSEKLDSTDF TGTIKLLNEN SYVPREAGSQ KDENLALYVE NQFREFKLSK 180
VWRDQHFVKI QVKDSAQNSV IIVDKNGRLV YLVENPGGYV AYSKAATVTG KLVHANFGTK 240
KDFEDLYTPV NGSIVIVRAG KITFAEKVAN AESLNAIGVL IYMDQTKFPI VNAELSFFGH 300
AHLGTGDPYT PGFPSFNHTQ FPPSRSSGLP NIPVQTISRA AAEKLFGNME GDCPSDWKTD 360
STCRMVTSES KNVKLTVSNV LKEIKILNIF GVIKGFVEPD HYVVVGAQRD AWGPGAAKSG 420
VGTALLLKLA QMFSDMVLKD GFQPSRSIIF ASWSAGDFGS VGATEWLEGY LSSLHLKAFT 480
YINLDKAVLG TSNFKVSASP LLYTLIEKTM QNVKHPVTGQ FLYQDSNWAS KVEKLTLDNA 540
AFPFLAYSGI PAVSFCFCED TDYPYLGTTM DTYKELIERI PELNKVARAA AEVAGQFVIK 600
LTHDVELNLD YERYNSQLLS FVRDLNQYRA DIKEMGLSLQ WLYSARGDFF RATSRLTTDF 660
GNAEKTDRFV MKKLNDRVMR VEYHFLSPYV SPKESPFRHV FWGSGSHTLP ALLENLKLRK 720
QNNGAFNETL FRNQLALATW TIQGAANALS GDVWDIDNEF 760 
Gene Ontology
 GO:0005905; C:coated pit; IDA:UniProtKB.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
 GO:0005768; C:endosome; IDA:MGI.
 GO:0009897; C:external side of plasma membrane; IEA:Compara.
 GO:0005576; C:extracellular region; IDA:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0008233; F:peptidase activity; IEA:InterPro.
 GO:0004998; F:transferrin receptor activity; NAS:UniProtKB.
 GO:0006879; P:cellular iron ion homeostasis; NAS:UniProtKB.
 GO:0030316; P:osteoclast differentiation; IEA:Compara.
 GO:0045780; P:positive regulation of bone resorption; IEA:Compara.
 GO:0006508; P:proteolysis; IEA:InterPro.
 GO:0033572; P:transferrin transport; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR007484; Peptidase_M28.
 IPR003137; Protease-assoc_domain.
 IPR007365; TFR-like_dimer_dom. 
Pfam
 PF02225; PA
 PF04389; Peptidase_M28
 PF04253; TFR_dimer 
SMART
  
PROSITE
  
PRINTS