UniProt Accession

 ALBU_MOUSE; P07724; Q3TV03; Q61802; Q8C7C7; Q8C7H3; Q8CG74 

Genbank Protein ID

 AJ011413; AJ277794; AK010025; AK050248; AK050644; AK160487; BC024643; BC049971; M16111; X13060 

Genbank Nucleotide ID

 CAA09617.1; CAC81903.1; BAB26650.1; BAC34145.1; BAC34360.1; BAE35818.1; AAH24643.1; AAH49971.1; AAA37190.1; CAA31458.1 

Protein Name

 Serum albumin 

Protein Synonyms/Alias

  

Gene Name

 Alb 

Gene Synonyms/Alias

 Alb-1; Alb1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
28	VFRREAHKSEIAHRY	acetylation	[1]
65	CSYDEHAKLVQEVTD	ubiquitination	[2]
75	QEVTDFAKTCVADES	acetylation	[3, 4]
88	ESAANCDKSLHTLFG	ubiquitination	[2]
97	LHTLFGDKLCAIPNL	ubiquitination	[2]
205	KESCLTPKLDGVKEK	ubiquitination	[2]
212	KLDGVKEKALVSSVR	ubiquitination	[2]
223	SSVRQRMKCSSMQKF	acetylation	[5]
223	SSVRQRMKCSSMQKF	succinylation	[5]
229	MKCSSMQKFGERAFK	acetylation	[3, 5]
229	MKCSSMQKFGERAFK	succinylation	[5]
236	KFGERAFKAWAVARL	acetylation	[3]
236	KFGERAFKAWAVARL	phosphoglycerylation	[6]
236	KFGERAFKAWAVARL	ubiquitination	[2]
257	ADFAEITKLATDLTK	ubiquitination	[2]
264	KLATDLTKVNKECCH	ubiquitination	[2]
267	TDLTKVNKECCHGDL	acetylation	[7]
305	KLQTCCDKPLLKKAH	acetylation	[3, 4, 7]
305	KLQTCCDKPLLKKAH	ubiquitination	[2]
309	CCDKPLLKKAHCLSE	acetylation	[7]
376	LLLRLAKKYEATLEK	ubiquitination	[2]
413	EEPKNLVKTNCDLYE	ubiquitination	[2]
421	TNCDLYEKLGEYGFQ	acetylation	[8]
438	ILVRYTQKAPQVSTP	ubiquitination	[2]
460	NLGRVGTKCCTLPED	acetylation	[5]
460	NLGRVGTKCCTLPED	succinylation	[5]
490	RVCLLHEKTPVSEHV	ubiquitination	[2]
499	PVSEHVTKCCSGSLV	ubiquitination	[2]
524	VDETYVPKEFKAETF	acetylation	[3]
543	DICTLPEKEKQIKKQ	acetylation	[5]
543	DICTLPEKEKQIKKQ	succinylation	[5]
549	EKEKQIKKQTALAEL	ubiquitination	[2]
588	TCCKAADKDTCFSTE	acetylation	[5, 7]
588	TCCKAADKDTCFSTE	succinylation	[5]

Reference

 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [6] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [7] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [8] 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

 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 19 211 Albumin 1.
 DOMAIN 212 403 Albumin 2.
 DOMAIN 404 601 Albumin 3.
 METAL 27 27 Copper.
 METAL 91 91 Zinc (By similarity).
 METAL 123 123 Zinc (By similarity).
 METAL 271 271 Zinc (By similarity).
 METAL 273 273 Zinc (By similarity).
 MOD_RES 82 82 Phosphoserine (By similarity).
 MOD_RES 443 443 Phosphoserine (By similarity).
 MOD_RES 444 444 Phosphothreonine (By similarity).
 MOD_RES 446 446 Phosphothreonine (By similarity).
 DISULFID 77 86 By similarity.
 DISULFID 99 115 By similarity.
 DISULFID 114 125 By similarity.
 DISULFID 148 193 By similarity.
 DISULFID 192 201 By similarity.
 DISULFID 224 270 By similarity.
 DISULFID 269 277 By similarity.
 DISULFID 289 303 By similarity.
 DISULFID 302 313 By similarity.
 DISULFID 340 385 By similarity.
 DISULFID 384 393 By similarity.
 DISULFID 416 462 By similarity.
 DISULFID 461 472 By similarity.
 DISULFID 485 501 By similarity.
 DISULFID 500 511 By similarity.
 DISULFID 538 583 By similarity.
 DISULFID 582 591 By similarity.  

Keyword

 Cleavage on pair of basic residues; Complete proteome; Copper; Direct protein sequencing; Disulfide bond; Lipid-binding; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 608 AA 

Protein Sequence

Gene Ontology

 GO:0005604; C:basement membrane; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005615; C:extracellular space; IDA:MGI.
 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; IEA:Compara.
 GO:0019825; F:oxygen binding; IEA:Compara.
 GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
 GO:0015643; F:toxic substance binding; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 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: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:0006810; P:transport; IEA:InterPro. 

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.