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Protein

Serum albumin

Gene

Alb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Copper
Metal bindingi91 – 911ZincBy similarity
Metal bindingi123 – 1231ZincBy similarity
Metal bindingi271 – 2711ZincBy similarity
Metal bindingi273 – 2731ZincBy similarity

GO - Molecular functioni

  1. chaperone binding Source: MGI
  2. DNA binding Source: UniProtKB
  3. drug binding Source: UniProtKB
  4. fatty acid binding Source: MGI
  5. oxygen binding Source: Ensembl
  6. pyridoxal phosphate binding Source: UniProtKB
  7. toxic substance binding Source: UniProtKB
  8. zinc ion binding Source: Ensembl

GO - Biological processi

  1. cellular response to starvation Source: UniProtKB
  2. hemolysis by symbiont of host erythrocytes Source: UniProtKB
  3. maintenance of mitochondrion location Source: UniProtKB
  4. negative regulation of apoptotic process Source: UniProtKB
  5. positive regulation of circadian sleep/wake cycle, non-REM sleep Source: Ensembl
  6. response to mercury ion Source: Ensembl
  7. response to nutrient Source: Ensembl
  8. response to organic substance Source: Ensembl
  9. response to platinum ion Source: Ensembl
  10. retina homeostasis Source: Ensembl
  11. transport Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Copper, Lipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_300927. Recycling of bile acids and salts.
REACT_303694. Scavenging of heme from plasma.
REACT_307071. Platelet degranulation.
REACT_318911. Transport of organic anions.
REACT_326379. HDL-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum albumin
Gene namesi
Name:Alb
Synonyms:Alb-1, Alb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:87991. Alb.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. blood microparticle Source: MGI
  3. cytoplasm Source: MGI
  4. extracellular region Source: MGI
  5. extracellular space Source: MGI
  6. extracellular vesicular exosome Source: MGI
  7. myelin sheath Source: UniProtKB
  8. nucleus Source: MGI
  9. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei755. Mus m 4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Propeptidei19 – 224PRO_0000001073
Chaini25 – 608584Serum albuminPRO_0000001074Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi77 ↔ 86PROSITE-ProRule annotation
Modified residuei82 – 821PhosphoserineBy similarity
Modified residuei89 – 891PhosphoserineBy similarity
Disulfide bondi99 ↔ 115PROSITE-ProRule annotation
Disulfide bondi114 ↔ 125PROSITE-ProRule annotation
Disulfide bondi148 ↔ 193PROSITE-ProRule annotation
Disulfide bondi192 ↔ 201PROSITE-ProRule annotation
Disulfide bondi224 ↔ 270PROSITE-ProRule annotation
Modified residuei229 – 2291N6-succinyllysine1 Publication
Disulfide bondi269 ↔ 277PROSITE-ProRule annotation
Disulfide bondi289 ↔ 303PROSITE-ProRule annotation
Disulfide bondi302 ↔ 313PROSITE-ProRule annotation
Disulfide bondi340 ↔ 385PROSITE-ProRule annotation
Disulfide bondi384 ↔ 393PROSITE-ProRule annotation
Disulfide bondi416 ↔ 462PROSITE-ProRule annotation
Modified residuei443 – 4431PhosphoserineBy similarity
Modified residuei444 – 4441PhosphothreonineBy similarity
Modified residuei446 – 4461PhosphothreonineBy similarity
Modified residuei460 – 4601N6-succinyllysine1 Publication
Disulfide bondi461 ↔ 472PROSITE-ProRule annotation
Disulfide bondi485 ↔ 501PROSITE-ProRule annotation
Disulfide bondi500 ↔ 511PROSITE-ProRule annotation
Modified residuei513 – 5131PhosphoserineBy similarity
Disulfide bondi538 ↔ 583PROSITE-ProRule annotation
Modified residuei543 – 5431N6-succinyllysine1 Publication
Disulfide bondi582 ↔ 591PROSITE-ProRule annotation
Modified residuei588 – 5881N6-succinyllysine1 Publication

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP07724.
PaxDbiP07724.
PRIDEiP07724.

2D gel databases

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

PTM databases

PhosphoSiteiP07724.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiP07724.
CleanExiMM_ALB.
ExpressionAtlasiP07724. baseline and differential.
GenevestigatoriP07724.

Interactioni

Protein-protein interaction databases

BioGridi198060. 6 interactions.
IntActiP07724. 9 interactions.
MINTiMINT-1854591.

Structurei

3D structure databases

ProteinModelPortaliP07724.
SMRiP07724. Positions 29-585.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 211193Albumin 1PROSITE-ProRule annotationAdd
BLAST
Domaini212 – 403192Albumin 2PROSITE-ProRule annotationAdd
BLAST
Domaini404 – 601198Albumin 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ALB/AFP/VDB family.PROSITE-ProRule annotation
Contains 3 albumin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG45992.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP07724.
KOiK16141.
OMAiNRLCVLH.
OrthoDBiEOG7S4X5C.
PhylomeDBiP07724.
TreeFamiTF335561.

Family and domain databases

InterProiIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP/Afamin.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamiPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSiPR00802. SERUMALBUMIN.
SMARTiSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 3 hits.
PROSITEiPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07724-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWVTFLLLL FVSGSAFSRG VFRREAHKSE IAHRYNDLGE QHFKGLVLIA
60 70 80 90 100
FSQYLQKCSY DEHAKLVQEV TDFAKTCVAD ESAANCDKSL HTLFGDKLCA
110 120 130 140 150
IPNLRENYGE LADCCTKQEP ERNECFLQHK DDNPSLPPFE RPEAEAMCTS
160 170 180 190 200
FKENPTTFMG HYLHEVARRH PYFYAPELLY YAEQYNEILT QCCAEADKES
210 220 230 240 250
CLTPKLDGVK EKALVSSVRQ RMKCSSMQKF GERAFKAWAV ARLSQTFPNA
260 270 280 290 300
DFAEITKLAT DLTKVNKECC HGDLLECADD RAELAKYMCE NQATISSKLQ
310 320 330 340 350
TCCDKPLLKK AHCLSEVEHD TMPADLPAIA ADFVEDQEVC KNYAEAKDVF
360 370 380 390 400
LGTFLYEYSR RHPDYSVSLL LRLAKKYEAT LEKCCAEANP PACYGTVLAE
410 420 430 440 450
FQPLVEEPKN LVKTNCDLYE KLGEYGFQNA ILVRYTQKAP QVSTPTLVEA
460 470 480 490 500
ARNLGRVGTK CCTLPEDQRL PCVEDYLSAI LNRVCLLHEK TPVSEHVTKC
510 520 530 540 550
CSGSLVERRP CFSALTVDET YVPKEFKAET FTFHSDICTL PEKEKQIKKQ
560 570 580 590 600
TALAELVKHK PKATAEQLKT VMDDFAQFLD TCCKAADKDT CFSTEGPNLV

TRCKDALA
Length:608
Mass (Da):68,693
Last modified:July 15, 1999 - v3
Checksum:i292F7C7EED3A61B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271H → D AA sequence (PubMed:1286668).Curated
Sequence conflicti33 – 331H → D AA sequence (PubMed:1286668).Curated
Sequence conflicti33 – 331H → N in BAC34360 (PubMed:16141072).Curated
Sequence conflicti41 – 411Q → I AA sequence (PubMed:1286668).Curated
Sequence conflicti561 – 5611P → H in BAE35818 (PubMed:16141072).Curated
Sequence conflicti606 – 6061A → T in BAC34145 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19412.1.
PIRiA05139.
RefSeqiNP_033784.2. NM_009654.3.
UniGeneiMm.16773.

Genome annotation databases

EnsembliENSMUST00000031314; ENSMUSP00000031314; ENSMUSG00000029368.
GeneIDi11657.
KEGGimmu:11657.
UCSCiuc008yaz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19412.1.
PIRiA05139.
RefSeqiNP_033784.2. NM_009654.3.
UniGeneiMm.16773.

3D structure databases

ProteinModelPortaliP07724.
SMRiP07724. Positions 29-585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198060. 6 interactions.
IntActiP07724. 9 interactions.
MINTiMINT-1854591.

Chemistry

BindingDBiP07724.
ChEMBLiCHEMBL1075271.

Protein family/group databases

Allergomei755. Mus m 4.

PTM databases

PhosphoSiteiP07724.

2D gel databases

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

Proteomic databases

MaxQBiP07724.
PaxDbiP07724.
PRIDEiP07724.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031314; ENSMUSP00000031314; ENSMUSG00000029368.
GeneIDi11657.
KEGGimmu:11657.
UCSCiuc008yaz.2. mouse.

Organism-specific databases

CTDi213.
MGIiMGI:87991. Alb.

Phylogenomic databases

eggNOGiNOG45992.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP07724.
KOiK16141.
OMAiNRLCVLH.
OrthoDBiEOG7S4X5C.
PhylomeDBiP07724.
TreeFamiTF335561.

Enzyme and pathway databases

ReactomeiREACT_300927. Recycling of bile acids and salts.
REACT_303694. Scavenging of heme from plasma.
REACT_307071. Platelet degranulation.
REACT_318911. Transport of organic anions.
REACT_326379. HDL-mediated lipid transport.

Miscellaneous databases

ChiTaRSiAlb. mouse.
NextBioi279275.
PROiP07724.
SOURCEiSearch...

Gene expression databases

BgeeiP07724.
CleanExiMM_ALB.
ExpressionAtlasiP07724. baseline and differential.
GenevestigatoriP07724.

Family and domain databases

InterProiIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP/Afamin.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamiPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSiPR00802. SERUMALBUMIN.
SMARTiSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 3 hits.
PROSITEiPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiALBU_MOUSE
AccessioniPrimary (citable) accession number: P07724
Secondary accession number(s): Q3TV03
, Q61802, Q8C7C7, Q8C7H3, Q8CG74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 15, 1999
Last modified: April 1, 2015
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.