UniProt Accession

 ALBU_HUMAN; P02768; O95574; P04277; Q13140; Q645G4; Q68DN5; Q6UXK4; Q86YG0; Q9P157; Q9P1I7; Q9UHS3; Q9UJZ0 

Genbank Protein ID

 V00494; V00495; M12523; M12523; AF190168; AF542069; A06977; AY728024; DQ986150; AY544124; AY550967; AF116645; AF118090; AF119840; AF119890; AF130077; CR749331; EF649953; CH471057; BC014308; BC034023; BC036003; BC041789; U22961; AY358313; AH002596 

Genbank Nucleotide ID

 CAA23753.1; CAA23754.1; AAA98797.1; AAA98798.1; AAF01333.1; AAN17825.1; CAA00606.1; AAU21642.1; ABJ16448.1; AAT11155.1; AAT52213.1; AAF71067.1; AAF22034.1; AAF69594.1; AAF69644.1; AAG35503.1; CAH18185.1; ABS29264.1; EAX05676.1; AAH14308.1; AAH34023.1; AAH36003.1; AAH41789.1; AAA64922.1; AAQ89947.1; AAA51688.1 

Protein Name

 Serum albumin 

Protein Synonyms/Alias

  

Gene Name

 ALB 

Gene Synonyms/Alias

 GIG20; GIG42; PRO0903; PRO1708; PRO2044; PRO2619; PRO2675; UNQ696/PRO1341 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
28	VFRRDAHKSEVAHRF	acetylation	[1]
28	VFRRDAHKSEVAHRF	glycation	[2, 3]
36	SEVAHRFKDLGEENF	acetylation	[1]
36	SEVAHRFKDLGEENF	glycation	[4, 5, 6, 7]
44	DLGEENFKALVLIAF	acetylation	[1]
44	DLGEENFKALVLIAF	glycation	[5]
65	CPFEDHVKLVNEVTE	acetylation	[1]
65	CPFEDHVKLVNEVTE	glycation	[5]
75	NEVTEFAKTCVADES	acetylation	[1]
75	NEVTEFAKTCVADES	glycation	[5, 7, 8]
88	ESAENCDKSLHTLFG	acetylation	[1]
88	ESAENCDKSLHTLFG	glycation	[3, 7]
97	LHTLFGDKLCTVATL	acetylation	[1]
97	LHTLFGDKLCTVATL	glycation	[5]
117	EMADCCAKQEPERNE	acetylation	[1]
117	EMADCCAKQEPERNE	glycation	[3]
130	NECFLQHKDDNPNLP	acetylation	[1]
160	DNEETFLKKYLYEIA	acetylation	[1]
160	DNEETFLKKYLYEIA	glycation	[5, 6]
161	NEETFLKKYLYEIAR	acetylation	[1]
161	NEETFLKKYLYEIAR	glycation	[5, 8]
183	PELLFFAKRYKAAFT	acetylation	[1]
183	PELLFFAKRYKAAFT	glycation	[3, 5]
186	LFFAKRYKAAFTECC	acetylation	[1]
186	LFFAKRYKAAFTECC	glycation	[3, 5, 7, 8]
198	ECCQAADKAACLLPK	acetylation	[1]
198	ECCQAADKAACLLPK	glycation	[6, 7]
205	KAACLLPKLDELRDE	acetylation	[1]
205	KAACLLPKLDELRDE	glycation	[6, 7]
214	DELRDEGKASSAKQR	acetylation	[1]
214	DELRDEGKASSAKQR	glycation	[6]
219	EGKASSAKQRLKCAS	acetylation	[1]
219	EGKASSAKQRLKCAS	glycation	[6]
223	SSAKQRLKCASLQKF	acetylation	[1, 9, 10, 11, 12]
223	SSAKQRLKCASLQKF	glycation	[3, 4, 5]
229	LKCASLQKFGERAFK	acetylation	[1]
229	LKCASLQKFGERAFK	glycation	[5]
229	LKCASLQKFGERAFK	ubiquitination	[13]
236	KFGERAFKAWAVARL	acetylation	[1]
249	RLSQRFPKAEFAEVS	acetylation	[1]
249	RLSQRFPKAEFAEVS	glycation	[8]
257	AEFAEVSKLVTDLTK	acetylation	[1, 14]
257	AEFAEVSKLVTDLTK	glycation	[4, 5, 6, 7]
264	KLVTDLTKVHTECCH	acetylation	[1]
286	DDRADLAKYICENQD	acetylation	[1]
286	DDRADLAKYICENQD	glycation	[3, 5, 7]
298	NQDSISSKLKECCEK	acetylation	[1]
298	NQDSISSKLKECCEK	glycation	[2]
300	DSISSKLKECCEKPL	acetylation	[1]
300	DSISSKLKECCEKPL	glycation	[3, 5, 7, 8]
305	KLKECCEKPLLEKSH	acetylation	[1]
305	KLKECCEKPLLEKSH	glycation	[4, 5, 6]
310	CEKPLLEKSHCIAEV	acetylation	[1]
310	CEKPLLEKSHCIAEV	glycation	[6]
337	AADFVESKDVCKNYA	acetylation	[1]
337	AADFVESKDVCKNYA	glycation	[5, 8]
341	VESKDVCKNYAEAKD	acetylation	[1]
341	VESKDVCKNYAEAKD	glycation	[4, 5]
347	CKNYAEAKDVFLGMF	acetylation	[1]
347	CKNYAEAKDVFLGMF	glycation	[3, 5, 8]
375	VLLLRLAKTYETTLE	acetylation	[1]
375	VLLLRLAKTYETTLE	glycation	[4, 5, 7]
383	TYETTLEKCCAAADP	acetylation	[1]
383	TYETTLEKCCAAADP	glycation	[7]
396	DPHECYAKVFDEFKP	acetylation	[1]
396	DPHECYAKVFDEFKP	glycation	[3]
402	AKVFDEFKPLVEEPQ	acetylation	[1, 14]
402	AKVFDEFKPLVEEPQ	glycation	[3, 5, 7, 8]
413	EEPQNLIKQNCELFE	acetylation	[1]
413	EEPQNLIKQNCELFE	glycation	[5]
426	FEQLGEYKFQNALLV	acetylation	[1]
426	FEQLGEYKFQNALLV	glycation	[5, 6]
437	ALLVRYTKKVPQVST	acetylation	[1]
437	ALLVRYTKKVPQVST	glycation	[3, 8]
438	LLVRYTKKVPQVSTP	acetylation	[1]
438	LLVRYTKKVPQVSTP	glycation	[3, 6, 7]
456	EVSRNLGKVGSKCCK	acetylation	[1]
456	EVSRNLGKVGSKCCK	glycation	[3, 5, 6]
460	NLGKVGSKCCKHPEA	acetylation	[1]
460	NLGKVGSKCCKHPEA	glycation	[5, 6]
463	KVGSKCCKHPEAKRM	acetylation	[1]
463	KVGSKCCKHPEAKRM	glycation	[3, 4, 5, 6]
468	CCKHPEAKRMPCAED	acetylation	[1]
468	CCKHPEAKRMPCAED	glycation	[6, 8]
490	QLCVLHEKTPVSDRV	acetylation	[1]
490	QLCVLHEKTPVSDRV	glycation	[6]
499	PVSDRVTKCCTESLV	acetylation	[1]
499	PVSDRVTKCCTESLV	glycation	[3, 5, 6, 7]
524	VDETYVPKEFNAETF	acetylation	[1]
524	VDETYVPKEFNAETF	glycation	[5]
543	DICTLSEKERQIKKQ	acetylation	[1]
543	DICTLSEKERQIKKQ	glycation	[5]
548	SEKERQIKKQTALVE	acetylation	[1]
548	SEKERQIKKQTALVE	glycation	[6]
549	EKERQIKKQTALVEL	acetylation	[1]
549	EKERQIKKQTALVEL	glycation	[3, 4, 5]
558	TALVELVKHKPKATK	acetylation	[1]
558	TALVELVKHKPKATK	glycation	[4]
560	LVELVKHKPKATKEQ	acetylation	[1]
560	LVELVKHKPKATKEQ	glycation	[8]
562	ELVKHKPKATKEQLK	acetylation	[1]
565	KHKPKATKEQLKAVM	acetylation	[1]
565	KHKPKATKEQLKAVM	glycation	[5]
569	KATKEQLKAVMDDFA	acetylation	[1]
569	KATKEQLKAVMDDFA	glycation	[5, 7, 8]
581	DFAAFVEKCCKADDK	acetylation	[1]
581	DFAAFVEKCCKADDK	glycation	[5, 6]
584	AFVEKCCKADDKETC	acetylation	[1]
584	AFVEKCCKADDKETC	glycation	[6]
588	KCCKADDKETCFAEE	acetylation	[1]
588	KCCKADDKETCFAEE	glycation	[6]
597	TCFAEEGKKLVAASQ	acetylation	[1]
597	TCFAEEGKKLVAASQ	glycation	[6, 8]
598	CFAEEGKKLVAASQA	acetylation	[1]
598	CFAEEGKKLVAASQA	glycation	[5]

Reference

 [1] Pseudo-esterase activity of human albumin: slow turnover on tyrosine 411 and stable acetylation of 82 residues including 59 lysines.
 Lockridge O, Xue W, Gaydess A, Grigoryan H, Ding SJ, Schopfer LM, Hinrichs SH, Masson P.
 J Biol Chem. 2008 Aug 15;283(33):22582-90. [PMID: 18577514]
 [2] 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]
 [3] Quantitative analysis of glycation patterns in human serum albumin using 16O/18O-labeling and MALDI-TOF MS.
 Barnaby OS, Cerny RL, Clarke W, Hage DS.
 Clin Chim Acta. 2011 Aug 17;412(17-18):1606-15. [PMID: 21601565]
 [4] Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites.
 Iberg N, Flückiger R.
 J Biol Chem. 1986 Oct 15;261(29):13542-5. [PMID: 3759977]
 [5] Screening and sequencing of glycated proteins by neutral loss scan LC/MS/MS method.
 Gadgil HS, Bondarenko PV, Treuheit MJ, Ren D.
 Anal Chem. 2007 Aug 1;79(15):5991-9. [PMID: 17571855]
 [6] Enrichment of Amadori products derived from the nonenzymatic glycation of proteins using microscale boronate affinity chromatography.
 Takátsy A, Böddi K, Nagy L, Nagy G, Szabó S, Markó L, Wittmann I, Ohmacht R, Ringer T, Bonn GK, Gjerde D, Szabó Z.
 Anal Biochem. 2009 Oct 1;393(1):8-22. [PMID: 19524544]
 [7] Identification and relative quantification of specific glycation sites in human serum albumin.
 Frolov A, Hoffmann R.
 Anal Bioanal Chem. 2010 Jul;397(6):2349-56. [PMID: 20496030]
 [8] Enzymatic digestion and mass spectrometry in the study of advanced glycation end products/peptides.
 Lapolla A, Fedele D, Reitano R, Aricò NC, Seraglia R, Traldi P, Marotta E, Tonani R.
 J Am Soc Mass Spectrom. 2004 Apr;15(4):496-509. [PMID: 15047055]
 [9] Esterase-like activity of human serum albumin: structure-activity relationships for the reactions with phenyl acetates and p-nitrophenyl esters.
 Kurono Y, Maki T, Yotsuyanagi T, Ikeda K.
 Chem Pharm Bull (Tokyo). 1979 Nov;27(11):2781-6. [PMID: 527146]
 [10] Positions in human serum albumin which involve the indole binding site. Sequence of 107-residue fragment.
 Gambhir KK, McMenamy RH, Watson F.
 J Biol Chem. 1975 Sep 10;250(17):6711-9. [PMID: 1158878]
 [11] Structural changes in human serum albumin induced by ingestion of acetylsalicylic acid.
 Hawkins D, Pinckard RN, Crawford IP, Farr RS.
 J Clin Invest. 1969 Mar;48(3):536-42. [PMID: 5773090]
 [12] Studies of the chemical selectivity of hapten, reactivity, and skin sensitization potency. 2. nmr studies of the covalent binding of the (13)c-labeled skin sensitizers 2-[13C]- and 3-[13C]hex-1-ene- and 3-[13C]hexane-1,3-sultones to human serum albumin.
 Meschkat E, Barratt MD, Lepoittevin J.
 Chem Res Toxicol. 2001 Jan;14(1):118-26. [PMID: 11170515]
 [13] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [14] 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

 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 19 210 Albumin 1.
 DOMAIN 211 403 Albumin 2.
 DOMAIN 404 601 Albumin 3.
 METAL 27 27 Copper (By similarity).
 METAL 91 91 Zinc.
 METAL 123 123 Zinc.
 METAL 271 271 Zinc.
 METAL 273 273 Zinc.
 BINDING 264 264 Bilirubin.
 MOD_RES 82 82 Phosphoserine.
 MOD_RES 443 443 Phosphoserine.
 MOD_RES 444 444 Phosphothreonine.
 MOD_RES 446 446 Phosphothreonine.
 CARBOHYD 36 36 N-linked (Glc) (glycation) (Probable).
 CARBOHYD 75 75 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 161 161 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 186 186 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 223 223 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 249 249 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 257 257 N-linked (Glc) (glycation) (Probable).
 CARBOHYD 300 300 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 305 305 N-linked (Glc) (glycation).
 CARBOHYD 337 337 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 341 341 N-linked (Glc) (glycation) (Probable).
 CARBOHYD 342 342 N-linked (GlcNAc...); in variant Redhill.
 CARBOHYD 347 347 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 375 375 N-linked (Glc) (glycation) (Probable).
 CARBOHYD 402 402 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 437 437 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 463 463 N-linked (Glc) (glycation).
 CARBOHYD 468 468 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 518 518 N-linked (GlcNAc...); in variant
 CARBOHYD 549 549 N-linked (Glc) (glycation).
 CARBOHYD 558 558 N-linked (Glc) (glycation) (Probable).
 CARBOHYD 560 560 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 569 569 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 597 597 N-linked (Glc) (glycation); in vitro.
 DISULFID 77 86
 DISULFID 99 115
 DISULFID 114 125
 DISULFID 148 193
 DISULFID 192 201
 DISULFID 224 270
 DISULFID 269 277
 DISULFID 289 303
 DISULFID 302 313
 DISULFID 340 385
 DISULFID 384 393
 DISULFID 416 462
 DISULFID 461 472
 DISULFID 485 501
 DISULFID 500 511
 DISULFID 538 583
 DISULFID 582 591  

Keyword

 3D-structure; Alternative splicing; Cleavage on pair of basic residues; Complete proteome; Copper; Direct protein sequencing; Disease mutation; Disulfide bond; Glycation; Glycoprotein; Lipid-binding; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 609 AA 

Protein Sequence

Gene Ontology

 GO:0005604; C:basement membrane; IEA:Compara.
 GO:0005615; C:extracellular space; IDA:BHF-UCL.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0016209; F:antioxidant activity; NAS:UniProtKB.
 GO:0005507; F:copper ion binding; NAS:UniProtKB.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0008144; F:drug binding; IDA:UniProtKB.
 GO:0005504; F:fatty acid binding; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
 GO:0015643; F:toxic substance binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
 GO:0008206; P:bile acid metabolic process; TAS:Reactome.
 GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
 GO:0019836; P:hemolysis by symbiont of host erythrocytes; IDA:UniProtKB.
 GO:0042157; P:lipoprotein metabolic process; TAS:Reactome.
 GO:0051659; P:maintenance of mitochondrion location; IDA:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Compara.
 GO:0046689; P:response to mercury ion; IEA:Compara.
 GO:0007584; P:response to nutrient; IEA:Compara.
 GO:0010033; P:response to organic substance; IEA:Compara.
 GO:0070541; P:response to platinum ion; IEA:Compara.
 GO:0043252; P:sodium-independent organic anion transport; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome. 

Interpro

 IPR000264; ALB/AFP/VDB.
 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

 PR00802; SERUMALBUMIN.