CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004018
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serotransferrin 
Protein Synonyms/Alias
 Transferrin; Beta-1 metal-binding globulin; Liver regeneration-related protein LRRG03; Siderophilin 
Gene Name
 Tf 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
26AVPDKTVKWCAVSEHacetylation[1]
46ISFRDHMKTVLPADGacetylation[1]
134QLNQLQGKKSCHTGLacetylation[1]
225GGDVAFVKHTTIFEVacetylation[1]
252LCLDNTRKPVDQYEDacetylation[1]
278VARNGDGKEDLIWEIacetylation[1]
295VAQEHFGKGKSKDFQacetylation[1]
299HFGKGKSKDFQLFGSacetylation[1]
310LFGSPLGKDLLFKDSacetylation[1]
315LGKDLLFKDSAFGLLacetylation[1]
466SINWNNLKGKKSCHTacetylation[1]
553KGDVAFVKHQTVLENacetylation[1]
564VLENTNGKNTAAWAKacetylation[1]
629AQKDLFWKGDKDCTGacetylation[1]
646CLFRSSTKDLLFRDDacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
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 360 683 Transferrin-like 2.
 METAL 82 82 Iron 1 (By similarity).
 METAL 114 114 Iron 1 (By similarity).
 METAL 207 207 Iron 1 (By similarity).
 METAL 268 268 Iron 1 (By similarity).
 METAL 410 410 Iron 2 (By similarity).
 METAL 447 447 Iron 2 (By similarity).
 METAL 536 536 Iron 2 (By similarity).
 METAL 604 604 Iron 2 (By similarity).
 BINDING 139 139 Carbonate 1 (By similarity).
 BINDING 143 143 Carbonate 1 (By similarity).
 BINDING 145 145 Carbonate 1; via amide nitrogen (By
 BINDING 146 146 Carbonate 1; via amide nitrogen (By
 BINDING 473 473 Carbonate 2 (By similarity).
 BINDING 477 477 Carbonate 2 (By similarity).
 BINDING 479 479 Carbonate 2; via amide nitrogen (By
 BINDING 480 480 Carbonate 2; via amide nitrogen (By
 MOD_RES 42 42 Omega-N-methylated arginine.
 CARBOHYD 512 512 N-linked (GlcNAc...) (Potential).
 DISULFID 28 67 By similarity.
 DISULFID 38 58 By similarity.
 DISULFID 137 213 By similarity.
 DISULFID 156 350 By similarity.
 DISULFID 177 193 By similarity.
 DISULFID 180 196 By similarity.
 DISULFID 190 198 By similarity.
 DISULFID 246 260 By similarity.
 DISULFID 363 395 By similarity.
 DISULFID 373 386 By similarity.
 DISULFID 420 693 By similarity.
 DISULFID 435 656 By similarity.
 DISULFID 471 542 By similarity.
 DISULFID 495 684 By similarity.
 DISULFID 505 519 By similarity.
 DISULFID 516 525 By similarity.
 DISULFID 582 596 By similarity.
 DISULFID 634 639 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport; Metal-binding; Methylation; Reference proteome; Repeat; Secreted; Signal; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 698 AA 
Protein Sequence
MRFAVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP ADGPRLACVK 60
KTSYQDCIKA ISGGEADAIT LDGGWVYDAG LTPNNLKPVA AEFYGSLEHP QTHYLAVAVV 120
KKGTDFQLNQ LQGKKSCHTG LGRSAGWIIP IGLLFCNLPE PRKPLEKAVA SFFSGSCVPC 180
ADPVAFPQLC QLCPGCGCSP TQPFFGYVGA FKCLRDGGGD VAFVKHTTIF EVLPQKADRD 240
QYELLCLDNT RKPVDQYEDC YLARIPSHAV VARNGDGKED LIWEILKVAQ EHFGKGKSKD 300
FQLFGSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHSYVT AIRNQREGVC PEGSIDSAPV 360
KWCALSHQER AKCDEWSVSS NGQIECESAE STEDCIDKIV NGEADAMSLD GGHAYIAGQC 420
GLVPVMAENY DISSCTNPQS DVFPKGYYAV AVVKASDSSI NWNNLKGKKS CHTGVDRTAG 480
WNIPMGLLFS RINHCKFDEF FSQGCAPGYK KNSTLCDLCI GPAKCAPNNR EGYNGYTGAF 540
QCLVEKGDVA FVKHQTVLEN TNGKNTAAWA KDLKQEDFQL LCPDGTKKPV TEFATCHLAQ 600
APNHVVVSRK EKAARVSTVL TAQKDLFWKG DKDCTGNFCL FRSSTKDLLF RDDTKCLTKL 660
PEGTTYEEYL GAEYLQAVGN IRKCSTSRLL EACTFHKS 698 
Gene Ontology
 GO:0005604; C:basement membrane; IDA:RGD.
 GO:0005615; C:extracellular space; IDA:RGD.
 GO:0008199; F:ferric iron binding; IDA:RGD.
 GO:0015091; F:ferric iron transmembrane transporter activity; IDA:RGD.
 GO:0006953; P:acute-phase response; IEP:RGD.
 GO:0006879; P:cellular iron ion homeostasis; TAS:RGD.
 GO:0071320; P:cellular response to cAMP; IEP:UniProtKB.
 GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:UniProtKB.
 GO:0006917; P:induction of apoptosis; ISS:UniProtKB.
 GO:0031643; P:positive regulation of myelination; IDA:RGD.
 GO:0001666; P:response to hypoxia; IEP:RGD. 
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.