CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002017
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serotransferrin 
Protein Synonyms/Alias
 Transferrin; Beta-1 metal-binding globulin; Siderophilin 
Gene Name
 TF 
Gene Synonyms/Alias
 PRO1400 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61PSVACVKKASYLDCIglycation[1]
122YAVAVVKKDSGFQMNglycation[1]
215SGAFKCLKDGAGDVAglycation[1]
225AGDVAFVKHSTIFENglycation[1]
258RKPVDEYKDCHLAQVglycation[1]
297QEHFGKDKSKEFQLFglycation[1]
299HFGKDKSKEFQLFSSglycation[1]
315HGKDLLFKDSAHGFLglycation[1]
359EAPTDECKPVKWCALacetylation[2]
553KGDVAFVKHQTVPQNglycation[1]
659DDTVCLAKLHDRNTYglycation[1]
668HDRNTYEKYLGEEYVglycation[1]
676YLGEEYVKAVGNLRKglycation[1]
683KAVGNLRKCSTSSLLglycation[1]
Reference
 [1] Proteomic profiling of nonenzymatically glycated proteins in human plasma and erythrocyte membranes.
 Zhang Q, Tang N, Schepmoes AA, Phillips LS, Smith RD, Metz TO.
 J Proteome Res. 2008 May;7(5):2025-32. [PMID: 18396901]
 [2] 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
 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. 
Sequence Annotation
 DOMAIN 25 347 Transferrin-like 1.
 DOMAIN 361 683 Transferrin-like 2.
 METAL 82 82 Iron 1.
 METAL 114 114 Iron 1.
 METAL 207 207 Iron 1.
 METAL 268 268 Iron 1.
 METAL 411 411 Iron 2 (By similarity).
 METAL 445 445 Iron 2 (By similarity).
 METAL 536 536 Iron 2 (By similarity).
 METAL 604 604 Iron 2 (By similarity).
 BINDING 139 139 Carbonate 1.
 BINDING 143 143 Carbonate 1.
 BINDING 145 145 Carbonate 1; via amide nitrogen.
 BINDING 146 146 Carbonate 1; via amide nitrogen.
 BINDING 471 471 Carbonate 2 (By similarity).
 BINDING 475 475 Carbonate 2 (By similarity).
 BINDING 477 477 Carbonate 2; via amide nitrogen (By
 BINDING 478 478 Carbonate 2; via amide nitrogen (By
 MOD_RES 42 42 Omega-N-methylated arginine (By
 CARBOHYD 51 51 O-linked (GalNAc...).
 CARBOHYD 432 432 N-linked (GlcNAc...) (complex).
 CARBOHYD 630 630 N-linked (GlcNAc...) (complex).
 DISULFID 28 67
 DISULFID 38 58
 DISULFID 137 213
 DISULFID 156 350
 DISULFID 177 193
 DISULFID 180 196
 DISULFID 190 198
 DISULFID 246 260
 DISULFID 358 615
 DISULFID 364 396
 DISULFID 374 387
 DISULFID 421 693
 DISULFID 437 656
 DISULFID 469 542
 DISULFID 493 684
 DISULFID 503 517
 DISULFID 514 525
 DISULFID 582 596
 DISULFID 634 639  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport; Metal-binding; Methylation; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 698 AA 
Protein Sequence
MRLAVGALLV CAVLGLCLAV PDKTVRWCAV SEHEATKCQS FRDHMKSVIP SDGPSVACVK 60
KASYLDCIRA IAANEADAVT LDAGLVYDAY LAPNNLKPVV AEFYGSKEDP QTFYYAVAVV 120
KKDSGFQMNQ LRGKKSCHTG LGRSAGWNIP IGLLYCDLPE PRKPLEKAVA NFFSGSCAPC 180
ADGTDFPQLC QLCPGCGCST LNQYFGYSGA FKCLKDGAGD VAFVKHSTIF ENLANKADRD 240
QYELLCLDNT RKPVDEYKDC HLAQVPSHTV VARSMGGKED LIWELLNQAQ EHFGKDKSKE 300
FQLFSSPHGK DLLFKDSAHG FLKVPPRMDA KMYLGYEYVT AIRNLREGTC PEAPTDECKP 360
VKWCALSHHE RLKCDEWSVN SVGKIECVSA ETTEDCIAKI MNGEADAMSL DGGFVYIAGK 420
CGLVPVLAEN YNKSDNCEDT PEAGYFAIAV VKKSASDLTW DNLKGKKSCH TAVGRTAGWN 480
IPMGLLYNKI NHCRFDEFFS EGCAPGSKKD SSLCKLCMGS GLNLCEPNNK EGYYGYTGAF 540
RCLVEKGDVA FVKHQTVPQN TGGKNPDPWA KNLNEKDYEL LCLDGTRKPV EEYANCHLAR 600
APNHAVVTRK DKEACVHKIL RQQQHLFGSN VTDCSGNFCL FRSETKDLLF RDDTVCLAKL 660
HDRNTYEKYL GEEYVKAVGN LRKCSTSSLL EACTFRRP 698 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
 GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
 GO:0005905; C:coated pit; IDA:UniProtKB.
 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0030139; C:endocytic vesicle; IDA:MGI.
 GO:0010008; C:endosome membrane; TAS:Reactome.
 GO:0005576; C:extracellular region; NAS:UniProtKB.
 GO:0005770; C:late endosome; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0055037; C:recycling endosome; IDA:UniProtKB.
 GO:0034774; C:secretory granule lumen; TAS:Reactome.
 GO:0008199; F:ferric iron binding; IEA:InterPro.
 GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0033572; P:transferrin transport; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome. 
Interpro
 IPR016357; Transferrin.
 IPR001156; Transferrin_fam.
 IPR018195; Transferrin_Fe_BS. 
Pfam
 PF00405; Transferrin 
SMART
 SM00094; TR_FER 
PROSITE
 PS00205; TRANSFERRIN_LIKE_1
 PS00206; TRANSFERRIN_LIKE_2
 PS00207; TRANSFERRIN_LIKE_3
 PS51408; TRANSFERRIN_LIKE_4 
PRINTS
 PR00422; TRANSFERRIN.