CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002012
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serum albumin 
Protein Synonyms/Alias
 BSA; Bos d 6 
Gene Name
 ALB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Bos taurus (Bovine) 
NCBI Taxa ID
 9913 
Lysine Modification
Position
Peptide
Type
References
28VFRRDTHKSEIAHRFglycation[1, 2]
36SEIAHRFKDLGEEHFglycation[1, 2, 3]
75NELTEFAKTCVADESglycation[1]
88ESHAGCEKSLHTLFGglycation[1, 2]
100LFGDELCKVASLRETglycation[4]
117DMADCCEKQEPERNEglycation[2]
130NECFLSHKDDSPDLPglycation[4]
151NTLCDEFKADEKKFWglycation[4]
156EFKADEKKFWGKYLYglycation[2]
160DEKKFWGKYLYEIARglycation[2, 3]
183ELLYYANKYNGVFQEglycation[4]
204KGACLLPKIETMREKglycation[2, 4]
228LRCASIQKFGERALKglycation[2]
235KFGERALKAWSVARLacetylation[5]
235KFGERALKAWSVARLglycation[2, 3]
248RLSQKFPKAEFVEVTglycation[4]
256AEFVEVTKLVTDLTKglycation[2, 3]
263KLVTDLTKVHKECCHglycation[4]
266TDLTKVHKECCHGDLglycation[2]
285DDRADLAKYICDNQDglycation[2]
297NQDTISSKLKECCDKglycation[1]
299DTISSKLKECCDKPLglycation[1]
309CDKPLLEKSHCIAEVglycation[4]
346CKNYQEAKDAFLGSFglycation[2]
374SVLLRLAKEYEATLEglycation[2]
399CYSTVFDKLKHLVDEglycation[1, 2]
401STVFDKLKHLVDEPQglycation[2, 3]
412DEPQNLIKQNCDQFEglycation[1, 2, 4]
420QNCDQFEKLGEYGFQglycation[1, 2]
437LIVRYTRKVPQVSTPacetylation[5]
437LIVRYTRKVPQVSTPglycation[1, 2]
455EVSRSLGKVGTRCCTglycation[1, 2]
489RLCVLHEKTPVSEKVglycation[1]
495EKTPVSEKVTKCCTEglycation[1, 2, 4]
498PVSEKVTKCCTESLVglycation[1, 2]
523PDETYVPKAFDEKLFglycation[1, 2]
528VPKAFDEKLFTFHADglycation[1]
548DTEKQIKKQTALVELglycation[1, 2, 3, 6]
561ELLKHKPKATEEQLKglycation[1, 2]
568KATEEQLKTVMENFVglycation[1, 2]
580NFVAFVDKCCAADDKglycation[4]
587KCCAADDKEACFAVEglycation[1]
Reference
 [1] Site specificity of glycation and carboxymethylation of bovine serum albumin by fructose.
 Hinton DJ, Ames JM.
 Amino Acids. 2006 Jun;30(4):425-34. [PMID: 16583308]
 [2] Analysis of amadori peptides enriched by boronic acid affinity chromatography.
 Frolov A, Hoffmann R.
 Ann N Y Acad Sci. 2008 Apr;1126:253-6. [PMID: 18448825]
 [3] Fragmentation behavior of glycated peptides derived from D-glucose, D-fructose and D-ribose in tandem mass spectrometry.
 Frolov A, Hoffmann P, Hoffmann R.
 J Mass Spectrom. 2006 Nov;41(11):1459-69. [PMID: 17063450]
 [4] Identification of AGE-precursors and AGE formation in glycation-induced BSA peptides.
 Ahmad W, Li L, Deng Y.
 BMB Rep. 2008 Jul 31;41(7):516-22. [PMID: 18682035]
 [5] The application of a hypothesis-driven strategy to the sensitive detection and location of acetylated lysine residues.
 Griffiths JR, Unwin RD, Evans CA, Leech SH, Corfe BM, Whetton AD.
 J Am Soc Mass Spectrom. 2007 Aug;18(8):1423-8. [PMID: 17543536]
 [6] Primary sequence and glycation at lysine-548 of bovine serum albumin.
 Wada Y.
 J Mass Spectrom. 1996 Mar;31(3):263-6. [PMID: 8799278
Functional Description
 Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. 
Sequence Annotation
 DOMAIN 19 209 Albumin 1.
 DOMAIN 210 402 Albumin 2.
 DOMAIN 403 600 Albumin 3.
 METAL 27 27 Copper (By similarity).
 METAL 91 91 Zinc (By similarity).
 METAL 123 123 Zinc (By similarity).
 METAL 270 270 Zinc (By similarity).
 METAL 272 272 Zinc (By similarity).
 MOD_RES 82 82 Phosphoserine (By similarity).
 MOD_RES 442 442 Phosphoserine (By similarity).
 MOD_RES 443 443 Phosphothreonine (By similarity).
 MOD_RES 445 445 Phosphothreonine (By similarity).
 DISULFID 77 86
 DISULFID 99 115
 DISULFID 114 125
 DISULFID 147 192
 DISULFID 191 200
 DISULFID 223 269
 DISULFID 268 276
 DISULFID 288 302
 DISULFID 301 312
 DISULFID 339 384
 DISULFID 383 392
 DISULFID 415 461
 DISULFID 460 471
 DISULFID 484 500
 DISULFID 499 510
 DISULFID 537 582
 DISULFID 581 590  
Keyword
 3D-structure; Allergen; Cleavage on pair of basic residues; Complete proteome; Copper; Direct protein sequencing; Disulfide bond; Lipid-binding; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 607 AA 
Protein Sequence
MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFKDLGE EHFKGLVLIA FSQYLQQCPF 60
DEHVKLVNEL TEFAKTCVAD ESHAGCEKSL HTLFGDELCK VASLRETYGD MADCCEKQEP 120
ERNECFLSHK DDSPDLPKLK PDPNTLCDEF KADEKKFWGK YLYEIARRHP YFYAPELLYY 180
ANKYNGVFQE CCQAEDKGAC LLPKIETMRE KVLASSARQR LRCASIQKFG ERALKAWSVA 240
RLSQKFPKAE FVEVTKLVTD LTKVHKECCH GDLLECADDR ADLAKYICDN QDTISSKLKE 300
CCDKPLLEKS HCIAEVEKDA IPENLPPLTA DFAEDKDVCK NYQEAKDAFL GSFLYEYSRR 360
HPEYAVSVLL RLAKEYEATL EECCAKDDPH ACYSTVFDKL KHLVDEPQNL IKQNCDQFEK 420
LGEYGFQNAL IVRYTRKVPQ VSTPTLVEVS RSLGKVGTRC CTKPESERMP CTEDYLSLIL 480
NRLCVLHEKT PVSEKVTKCC TESLVNRRPC FSALTPDETY VPKAFDEKLF TFHADICTLP 540
DTEKQIKKQT ALVELLKHKP KATEEQLKTV MENFVAFVDK CCAADDKEAC FAVEGPKLVV 600
STQTALA 607 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005576; C:extracellular region; TAS:Reactome.
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0043234; C:protein complex; ISS:UniProtKB.
 GO:0003677; F:DNA binding; ISS:UniProtKB.
 GO:0008144; F:drug binding; ISS:UniProtKB.
 GO:0005504; F:fatty acid binding; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0019825; F:oxygen binding; IEA:Compara.
 GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
 GO:0015643; F:toxic substance binding; ISS:UniProtKB.
 GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
 GO:0019836; P:hemolysis by symbiont of host erythrocytes; ISS:UniProtKB.
 GO:0051659; P:maintenance of mitochondrion location; ISS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
 GO:0006810; P:transport; IEA:InterPro. 
Interpro
 IPR000264; ALB/AFP/VDB.
 IPR001703; Alpha-fetoprotein.
 IPR020858; Serum_albumin-like.
 IPR021177; Serum_albumin/AFP.
 IPR020857; Serum_albumin_CS.
 IPR014760; Serum_albumin_N. 
Pfam
 PF00273; Serum_albumin 
SMART
 SM00103; ALBUMIN 
PROSITE
 PS00212; ALBUMIN_1
 PS51438; ALBUMIN_2 
PRINTS
 PR00803; AFETOPROTEIN.
 PR00802; SERUMALBUMIN.