CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002013
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serum albumin 
Protein Synonyms/Alias
  
Gene Name
 Alb 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
28VFRREAHKSEIAHRFacetylation[1]
36SEIAHRFKDLGEQHFacetylation[1]
57AFSQYLQKCPYEEHIacetylation[1]
65CPYEEHIKLVQEVTDacetylation[1]
97IHTLFGDKLCAIPKLacetylation[1]
103DKLCAIPKLRDNYGEacetylation[1]
205KAACLTPKLDAVKEKacetylation[1]
210TPKLDAVKEKALVAAacetylation[1]
212KLDAVKEKALVAAVRacetylation[1]
223AAVRQRMKCSSMQRFacetylation[1]
236RFGERAFKAWAVARMacetylation[1]
257AEFAEITKLATDVTKacetylation[1]
264KLATDVTKINKECCHacetylation[1]
305KLQACCDKPVLQKSQacetylation[1]
341VEDKEVCKNYAEAKDacetylation[1]
375SLLLRLAKKYEATLEacetylation[1]
376LLLRLAKKYEATLEKacetylation[1]
413EEPKNLVKTNCELYEacetylation[1]
421TNCELYEKLGEYGFQacetylation[1]
438VLVRYTQKAPQVSTPacetylation[1]
490RLCVLHEKTPVSEKVacetylation[1]
496EKTPVSEKVTKCCSGacetylation[1]
543DICTLPDKEKQIKKQacetylation[1]
558TALAELVKHKPKATEacetylation[1]
569KATEDQLKTVMGDFAacetylation[1]
588KCCKAADKDNCFATEacetylation[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
 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 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; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 608 AA 
Protein Sequence
MKWVTFLLLL FISGSAFSRG VFRREAHKSE IAHRFKDLGE QHFKGLVLIA FSQYLQKCPY 60
EEHIKLVQEV TDFAKTCVAD ENAENCDKSI HTLFGDKLCA IPKLRDNYGE LADCCAKQEP 120
ERNECFLQHK DDNPNLPPFQ RPEAEAMCTS FQENPTSFLG HYLHEVARRH PYFYAPELLY 180
YAEKYNEVLT QCCTESDKAA CLTPKLDAVK EKALVAAVRQ RMKCSSMQRF GERAFKAWAV 240
ARMSQRFPNA EFAEITKLAT DVTKINKECC HGDLLECADD RAELAKYMCE NQATISSKLQ 300
ACCDKPVLQK SQCLAEIEHD NIPADLPSIA ADFVEDKEVC KNYAEAKDVF LGTFLYEYSR 360
RHPDYSVSLL LRLAKKYEAT LEKCCAEGDP PACYGTVLAE FQPLVEEPKN LVKTNCELYE 420
KLGEYGFQNA VLVRYTQKAP QVSTPTLVEA ARNLGRVGTK CCTLPEAQRL PCVEDYLSAI 480
LNRLCVLHEK TPVSEKVTKC CSGSLVERRP CFSALTVDET YVPKEFKAET FTFHSDICTL 540
PDKEKQIKKQ TALAELVKHK PKATEDQLKT VMGDFAQFVD KCCKAADKDN CFATEGPNLV 600
ARSKEALA 608 
Gene Ontology
 GO:0005604; C:basement membrane; IDA:RGD.
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005615; C:extracellular space; IDA:RGD.
 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: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; IDA:RGD.
 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; IDA:RGD.
 GO:0046689; P:response to mercury ion; IEP:RGD.
 GO:0007584; P:response to nutrient; IEP:RGD.
 GO:0010033; P:response to organic substance; IEP:RGD.
 GO:0070541; P:response to platinum ion; IEP:RGD.
 GO:0006810; P:transport; IEA:InterPro.
 GO:0042311; P:vasodilation; NAS:RGD. 
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.