Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07724 (ALBU_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serum albumin
Gene names
Name:Alb
Synonyms:Alb-1, Alb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca2+, 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.

Subcellular location

Secreted.

Tissue specificity

Plasma.

Post-translational modification

Phosphorylation sites are present in the extracellular medium By similarity.

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Contains 3 albumin domains.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCopper
Lipid-binding
Metal-binding
Zinc
   PTMCleavage on pair of basic residues
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to starvation

Inferred from sequence or structural similarity. Source: UniProtKB

hemolysis by symbiont of host erythrocytes

Inferred from sequence or structural similarity. Source: UniProtKB

maintenance of mitochondrion location

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of circadian sleep/wake cycle, non-REM sleep

Inferred from electronic annotation. Source: Ensembl

response to mercury ion

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to organic substance

Inferred from electronic annotation. Source: Ensembl

response to platinum ion

Inferred from electronic annotation. Source: Ensembl

transport

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 11197537PubMed 15576401PubMed 16880525PubMed 8607965. Source: MGI

extracellular region

Inferred from direct assay PubMed 16106354PubMed 4646766. Source: MGI

extracellular space

Inferred from direct assay PubMed 7798939. Source: MGI

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid binding

Inferred from electronic annotation. Source: Ensembl

oxygen binding

Inferred from electronic annotation. Source: Ensembl

pyridoxal phosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

toxic substance binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Propeptide19 – 224
PRO_0000001073
Chain25 – 608584Serum albumin
PRO_0000001074

Regions

Domain19 – 211193Albumin 1
Domain212 – 403192Albumin 2
Domain404 – 601198Albumin 3

Sites

Metal binding271Copper
Metal binding911Zinc By similarity
Metal binding1231Zinc By similarity
Metal binding2711Zinc By similarity
Metal binding2731Zinc By similarity

Amino acid modifications

Modified residue821Phosphoserine By similarity
Modified residue2291N6-succinyllysine Ref.8
Modified residue4431Phosphoserine By similarity
Modified residue4441Phosphothreonine By similarity
Modified residue4461Phosphothreonine By similarity
Modified residue4601N6-succinyllysine Ref.8
Modified residue5431N6-succinyllysine Ref.8
Modified residue5881N6-succinyllysine Ref.8
Disulfide bond77 ↔ 86 By similarity
Disulfide bond99 ↔ 115 By similarity
Disulfide bond114 ↔ 125 By similarity
Disulfide bond148 ↔ 193 By similarity
Disulfide bond192 ↔ 201 By similarity
Disulfide bond224 ↔ 270 By similarity
Disulfide bond269 ↔ 277 By similarity
Disulfide bond289 ↔ 303 By similarity
Disulfide bond302 ↔ 313 By similarity
Disulfide bond340 ↔ 385 By similarity
Disulfide bond384 ↔ 393 By similarity
Disulfide bond416 ↔ 462 By similarity
Disulfide bond461 ↔ 472 By similarity
Disulfide bond485 ↔ 501 By similarity
Disulfide bond500 ↔ 511 By similarity
Disulfide bond538 ↔ 583 By similarity
Disulfide bond582 ↔ 591 By similarity

Experimental info

Sequence conflict271H → D AA sequence Ref.4
Sequence conflict331H → D AA sequence Ref.4
Sequence conflict331H → N in BAC34360. Ref.2
Sequence conflict411Q → I AA sequence Ref.4
Sequence conflict5611P → H in BAE35818. Ref.2
Sequence conflict6061A → T in BAC34145. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P07724 [UniParc].

Last modified July 15, 1999. Version 3.
Checksum: 292F7C7EED3A61B4

FASTA60868,693
        10         20         30         40         50         60 
MKWVTFLLLL FVSGSAFSRG VFRREAHKSE IAHRYNDLGE QHFKGLVLIA FSQYLQKCSY 

        70         80         90        100        110        120 
DEHAKLVQEV TDFAKTCVAD ESAANCDKSL HTLFGDKLCA IPNLRENYGE LADCCTKQEP 

       130        140        150        160        170        180 
ERNECFLQHK DDNPSLPPFE RPEAEAMCTS FKENPTTFMG HYLHEVARRH PYFYAPELLY 

       190        200        210        220        230        240 
YAEQYNEILT QCCAEADKES CLTPKLDGVK EKALVSSVRQ RMKCSSMQKF GERAFKAWAV 

       250        260        270        280        290        300 
ARLSQTFPNA DFAEITKLAT DLTKVNKECC HGDLLECADD RAELAKYMCE NQATISSKLQ 

       310        320        330        340        350        360 
TCCDKPLLKK AHCLSEVEHD TMPADLPAIA ADFVEDQEVC KNYAEAKDVF LGTFLYEYSR 

       370        380        390        400        410        420 
RHPDYSVSLL LRLAKKYEAT LEKCCAEANP PACYGTVLAE FQPLVEEPKN LVKTNCDLYE 

       430        440        450        460        470        480 
KLGEYGFQNA ILVRYTQKAP QVSTPTLVEA ARNLGRVGTK CCTLPEDQRL PCVEDYLSAI 

       490        500        510        520        530        540 
LNRVCLLHEK TPVSEHVTKC CSGSLVERRP CFSALTVDET YVPKEFKAET FTFHSDICTL 

       550        560        570        580        590        600 
PEKEKQIKKQ TALAELVKHK PKATAEQLKT VMDDFAQFLD TCCKAADKDT CFSTEGPNLV 


TRCKDALA 

« Hide

References

« Hide 'large scale' references
[1]Van Reeth T., Dreze P.L., Gabant P., Szpirer C., Szpirer J.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-205.
Strain: 129/SvEvTacfBr.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver, Stomach, Thymus and Tongue.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney and Liver.
[4]"Mouse liver protein database: a catalog of proteins detected by two-dimensional gel electrophoresis."
Giometti C.S., Taylor J., Tollaksen S.L.
Electrophoresis 13:970-991(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-44.
Tissue: Liver.
[5]Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 35-57; 66-75; 89-105; 243-257; 299-309; 348-372; 422-434; 439-452; 470-483; 509-524; 550-558 AND 570-602, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[6]"The rate of molecular evolution of alpha-fetoprotein approaches that of pseudogenes."
Minghetti P.P., Law S.W., Dugaiczyk A.
Mol. Biol. Evol. 2:347-358(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-516.
[7]"Empty and occupied insertion site of the truncated LINE-1 repeat located in the mouse serum albumin-encoding gene."
Boccaccio C., Deschatrette J., Meunier-Rotival M.
Gene 88:181-186(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 477-551.
Strain: BALB/c.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-229; LYS-460; LYS-543 AND LYS-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ011413 mRNA. Translation: CAA09617.1.
AJ277794 Genomic DNA. Translation: CAC81903.1.
AK010025 mRNA. Translation: BAB26650.1.
AK050248 mRNA. Translation: BAC34145.1.
AK050644 mRNA. Translation: BAC34360.1.
AK160487 mRNA. Translation: BAE35818.1.
BC024643 mRNA. Translation: AAH24643.1.
BC049971 mRNA. Translation: AAH49971.1.
M16111 mRNA. Translation: AAA37190.1.
X13060 Genomic DNA. Translation: CAA31458.1.
CCDSCCDS19412.1.
PIRA05139.
RefSeqNP_033784.2. NM_009654.3.
UniGeneMm.16773.

3D structure databases

ProteinModelPortalP07724.
SMRP07724. Positions 29-585.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198060. 5 interactions.
IntActP07724. 9 interactions.
MINTMINT-1854591.

Chemistry

ChEMBLCHEMBL1075271.

Protein family/group databases

Allergome755. Mus m 4.

PTM databases

PhosphoSiteP07724.

2D gel databases

REPRODUCTION-2DPAGEIPI00131695.
P07724.
Q8CG74.
SWISS-2DPAGEP07724.
UCD-2DPAGEP07724.

Proteomic databases

MaxQBP07724.
PaxDbP07724.
PRIDEP07724.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031314; ENSMUSP00000031314; ENSMUSG00000029368.
GeneID11657.
KEGGmmu:11657.
UCSCuc008yaz.2. mouse.

Organism-specific databases

CTD213.
MGIMGI:87991. Alb.

Phylogenomic databases

eggNOGNOG45992.
HOGENOMHOG000293137.
HOVERGENHBG004207.
InParanoidP07724.
KOK16141.
OMANCDKSLH.
OrthoDBEOG7S4X5C.
PhylomeDBP07724.
TreeFamTF335561.

Gene expression databases

BgeeP07724.
CleanExMM_ALB.
GenevestigatorP07724.

Family and domain databases

InterProIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSPR00802. SERUMALBUMIN.
SMARTSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMSSF48552. SSF48552. 3 hits.
PROSITEPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALB. mouse.
NextBio279275.
PROP07724.
SOURCESearch...

Entry information

Entry nameALBU_MOUSE
AccessionPrimary (citable) accession number: P07724
Secondary accession number(s): Q3TV03 expand/collapse secondary AC list , Q61802, Q8C7C7, Q8C7H3, Q8CG74
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 15, 1999
Last modified: July 9, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot