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P02768 (ALBU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 205. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serum albumin
Gene names
Name:ALB
ORF Names:GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length609 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. Ref.32

Subcellular location

Secreted.

Tissue specificity

Plasma.

Post-translational modification

Kenitra variant is partially O-glycosylated at Thr-620. It has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606.

Glycated in diabetic patients.

Phosphorylation sites are present in the extracellular medium.

Acetylated on Lys-223 by acetylsalicylic acid. Ref.25

Polymorphism

A variant structure of albumin could lead to increased binding of zinc resulting in an asymptomatic augmentation of zinc concentration in the blood. The sequence shown is that of variant albumin A.

Involvement in disease

Dysalbuminemic hyperthyroxinemia (DH) [MIM:103600]: A disorder characterized by abnormally elevated levels of total serum thyroxine (T4) in euthyroid patients. It is due to abnormal serum albumin that binds T4 with enhanced affinity.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.61 Ref.62 Ref.63 Ref.64

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Contains 3 albumin domains.

Caution

A peptide arising from positions 166 to 174 was originally (Ref.23 and Ref.24) termed neurotensin-related peptide (NRP) or kinetensin and was thought to regulate fat digestion, lipid absorption, and blood flow.

Sequence caution

The sequence AAF22034.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAF69644.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAG35503.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
   LigandCopper
Lipid-binding
Metal-binding
Zinc
   PTMCleavage on pair of basic residues
Disulfide bond
Glycation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid and bile salt transport

Traceable author statement. Source: Reactome

bile acid metabolic process

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cellular response to starvation

Inferred from direct assay PubMed 16245148. Source: UniProtKB

hemolysis by symbiont of host erythrocytes

Inferred from direct assay PubMed 16394536. Source: UniProtKB

lipoprotein metabolic process

Traceable author statement. Source: Reactome

maintenance of mitochondrion location

Inferred from direct assay PubMed 16153637. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay PubMed 16153637. Source: UniProtKB

negative regulation of programmed cell death

Non-traceable author statement PubMed 14726550. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

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

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

small molecule metabolic process

Traceable author statement. Source: Reactome

sodium-independent organic anion transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement PubMed 12617161. Source: UniProtKB

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 19996109. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

protein complex

Inferred from direct assay PubMed 16283771. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 16405401. Source: UniProtKB

antioxidant activity

Non-traceable author statement PubMed 14726550. Source: UniProtKB

chaperone binding

Inferred from physical interaction PubMed 19996109. Source: BHF-UCL

copper ion binding

Non-traceable author statement PubMed 14726550. Source: UniProtKB

drug binding

Inferred from direct assay PubMed 16169013PubMed 16307046PubMed 16413734PubMed 16413740. Source: UniProtKB

fatty acid binding

Inferred from direct assay PubMed 16289007PubMed 16413837. Source: UniProtKB

pyridoxal phosphate binding

Inferred from direct assay PubMed 16201370. Source: UniProtKB

toxic substance binding

Inferred from direct assay PubMed 16169013. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TFRCP027862EBI-714423,EBI-355727

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P02768-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P02768-2)

The sequence of this isoform differs from the canonical sequence as follows:
     43-234: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Propeptide19 – 224
PRO_0000001067
Chain25 – 609585Serum albumin
PRO_0000001068

Regions

Domain19 – 210192Albumin 1
Domain211 – 403193Albumin 2
Domain404 – 601198Albumin 3

Sites

Metal binding271Copper By similarity
Metal binding911Zinc
Metal binding1231Zinc
Metal binding2711Zinc
Metal binding2731Zinc
Binding site2641Bilirubin
Site281Not glycated
Site441Not glycated
Site651Not glycated
Site881Not glycated
Site971Not glycated
Site1171Not glycated
Site1301Not glycated
Site1601Not glycated
Site1831Not glycated
Site1981Not glycated
Site2051Not glycated
Site2141Not glycated
Site2191Not glycated
Site2231Aspirin-acetylated lysine
Site2291Not glycated
Site2361Not glycated
Site2641Not glycated
Site2861Not glycated
Site2981Not glycated
Site3101Not glycated
Site3831Not glycated
Site3961Not glycated
Site4131Not glycated
Site4261Not glycated
Site4381Not glycated
Site4561Not glycated
Site4601Not glycated
Site4901Not glycated
Site4991Not glycated
Site5241Not glycated
Site5431Not glycated
Site5481Not glycated
Site5621Not glycated
Site5651Not glycated
Site5811Not glycated
Site5841Not glycated
Site5881Not glycated
Site5981Not glycated

Amino acid modifications

Modified residue821Phosphoserine Ref.33
Modified residue4431Phosphoserine Ref.34
Modified residue4441Phosphothreonine Ref.34
Modified residue4461Phosphothreonine Ref.34
Glycosylation361N-linked (Glc) (glycation) Probable
Glycosylation751N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation1611N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation1861N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation2231N-linked (Glc) (glycation); in vitro Ref.29 Ref.31
Glycosylation2491N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation2571N-linked (Glc) (glycation) Probable
Glycosylation3001N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation3051N-linked (Glc) (glycation) Ref.31
Glycosylation3371N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation3411N-linked (Glc) (glycation) Probable
Glycosylation3421N-linked (GlcNAc...); in variant Redhill
CAR_000226
Glycosylation3471N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation3751N-linked (Glc) (glycation) Probable
Glycosylation4021N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation4371N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation4631N-linked (Glc) (glycation) Ref.31
Glycosylation4681N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation5181N-linked (GlcNAc...); in variant Casebrook
CAR_000069
Glycosylation5491N-linked (Glc) (glycation) Ref.26 Ref.29 Ref.30 Ref.31
Glycosylation5581N-linked (Glc) (glycation) Probable
Glycosylation5601N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation5691N-linked (Glc) (glycation); in vitro Ref.26
Glycosylation5971N-linked (Glc) (glycation); in vitro Ref.26
Disulfide bond77 ↔ 86 Ref.27
Disulfide bond99 ↔ 115 Ref.27
Disulfide bond114 ↔ 125 Ref.27
Disulfide bond148 ↔ 193 Ref.27
Disulfide bond192 ↔ 201 Ref.27
Disulfide bond224 ↔ 270 Ref.27
Disulfide bond269 ↔ 277 Ref.27
Disulfide bond289 ↔ 303 Ref.27
Disulfide bond302 ↔ 313 Ref.27
Disulfide bond340 ↔ 385 Ref.27
Disulfide bond384 ↔ 393 Ref.27
Disulfide bond416 ↔ 462 Ref.27
Disulfide bond461 ↔ 472 Ref.27
Disulfide bond485 ↔ 501 Ref.27
Disulfide bond500 ↔ 511 Ref.27
Disulfide bond538 ↔ 583 Ref.27
Disulfide bond582 ↔ 591 Ref.27

Natural variations

Alternative sequence43 – 234192Missing in isoform 2.
VSP_021275
Natural variant231R → C in Redhill/Malmo-I/Tradate; associated with T-344 in Redhill. Ref.56
VAR_000499
Natural variant231R → H in Fukuoka-2/Lille/Taipei/Varese/Komagome-3. Ref.47 Ref.51 Ref.53
VAR_000500
Natural variant241R → L in Jaffna.
VAR_000501
Natural variant241R → P in Takefu/Honolulu-1. Ref.49
VAR_000502
Natural variant241R → Q in Christchurch/Honolulu-2. Ref.47 Ref.48 Ref.49
VAR_000503
Natural variant251D → V in Bleinheim/Iowa city-2. Ref.53
VAR_000504
Natural variant271H → Q in Nagasaki-3. Ref.46
VAR_000505
Natural variant271H → Y in Larino. Ref.11 Ref.60
VAR_000506
Natural variant731F → Y. Ref.65
VAR_010657
Natural variant841E → K in Torino. Ref.51
VAR_000507
Natural variant871D → N in Malmo-95/Dalakarlia. Ref.56
VAR_000508
Natural variant901L → P in DH. Ref.64
VAR_013011
Natural variant1061E → K in Vibo Valentia. Ref.51
VAR_000509
Natural variant1211E → G. Ref.2
VAR_014290
Natural variant1381R → G in Yanomama-2.
VAR_000510
Natural variant1431E → K in Nagoya. Ref.49
VAR_000511
Natural variant1461V → E in Tregasio.
VAR_013012
Natural variant1521H → R in Komagome-2. Ref.53
VAR_000512
Natural variant2011C → F in Hawkes bay. Ref.58
VAR_000513
Natural variant2151A → T.
Corresponds to variant rs3210154 [ dbSNP | Ensembl ].
VAR_014291
Natural variant2151A → V.
Corresponds to variant rs3204504 [ dbSNP | Ensembl ].
VAR_014292
Natural variant2201Q → L.
Corresponds to variant rs3210163 [ dbSNP | Ensembl ].
VAR_014293
Natural variant2421R → H in DH. Ref.61 Ref.62 Ref.63
VAR_000514
Natural variant2421R → P in DH.
VAR_013013
Natural variant2491K → Q in Tradate-2. Ref.60
VAR_000515
Natural variant2641K → E in Herborn. Ref.57
VAR_000516
Natural variant2921Q → R in Malmo-10. Ref.56
VAR_000517
Natural variant2931D → G in Nagasaki-1. Ref.48
VAR_000518
Natural variant3001K → N in Caserta. Ref.60
VAR_000519
Natural variant3371K → N in Canterbury/New Guinea/Tagliacozzo/Cuneo/Cooperstown. Ref.44 Ref.47 Ref.49
VAR_000520
Natural variant3381D → G in Bergamo.
VAR_013014
Natural variant3381D → V in Brest.
VAR_013015
Natural variant3421N → K in Malmo-47. Ref.56
VAR_000521
Natural variant3441A → T in Redhill; associated with C-23.
VAR_000522
Natural variant3451E → K in Roma.
VAR_000523
Natural variant3571E → K in Sondrio. Ref.55
VAR_000524
Natural variant3781E → K in Hiroshima-1. Ref.5 Ref.48
VAR_000525
Natural variant3821E → K in Coari I/Porto Alegre.
VAR_000526
Natural variant3831K → N in Trieste.
VAR_013016
Natural variant3891D → H in Parklands.
VAR_000527
Natural variant3891D → V in Iowa city-1. Ref.53
VAR_000528
Natural variant3961K → E in Naskapi/Mersin/Komagome-1. Ref.45 Ref.46 Ref.53
VAR_000529
Natural variant3991D → N in Nagasaki-2. Ref.46
VAR_000530
Natural variant4001E → K in Tochigi. Ref.48
VAR_000531
Natural variant4001E → Q in Malmo-5. Ref.56
VAR_000532
Natural variant4061E → K in Hiroshima-2. Ref.48
VAR_000533
Natural variant4201E → K. Ref.1
VAR_014294
Natural variant4341R → C in Liprizzi.
VAR_013017
Natural variant4901K → E.
Corresponds to variant rs1063469 [ dbSNP | Ensembl ].
VAR_014295
Natural variant5031E → K in Dublin.
VAR_000534
Natural variant5181D → N in Casebrook. Ref.54
VAR_000535
Natural variant5251E → K in Manaus-1/Adana/Lambadi/Vancouver. Ref.49
VAR_000536
Natural variant5291E → K in Ortonovo. Ref.59
VAR_000537
Natural variant5571V → M in Maddaloni.
Corresponds to variant rs78284052 [ dbSNP | Ensembl ].
VAR_013018
Natural variant5601K → E in Castel di Sangro.
VAR_000538
Natural variant5651K → E in Maku. Ref.46
VAR_000539
Natural variant5741D → A in Malmo-61. Ref.56
VAR_000541
Natural variant5741D → G in Mexico. Ref.45
VAR_000540
Natural variant5841K → E in Church bay.
VAR_013019
Natural variant5871D → N in Fukuoka-1/Paris-2. Ref.49 Ref.55
VAR_000542
Natural variant5891E → K in Osaka-1. Ref.49
VAR_000543
Natural variant5941E → K in Osaka-2/Phnom Phen/albumin B/Verona. Ref.47 Ref.48 Ref.49
VAR_000544
Natural variant596 – 60914GKKLV…AALGL → PTMRIRERK in Venezia.
VAR_000547
Natural variant5971K → E in Gent/Milano Fast.
VAR_000545
Natural variant5981K → N in Vanves.
VAR_000546
Natural variant599 – 60911LVAASQAALGL → TCCCKSSCLRLITSHLKASQ PTMRIRERK in Kenitra.
VAR_012981

Experimental info

Sequence conflict551L → P in CAH18185. Ref.11
Sequence conflict1221R → S in AAF01333. Ref.4
Sequence conflict1551E → Q AA sequence Ref.18
Sequence conflict1741Y → L AA sequence Ref.23
Sequence conflict1741Y → L AA sequence Ref.24
Sequence conflict1941Q → E AA sequence Ref.18
Sequence conflict327 – 3326PSLAAD → MFVLLC in AAF71067. Ref.10
Sequence conflict4051V → A in AAF71067. Ref.10
Sequence conflict4091Q → E in AAH14308. Ref.14
Sequence conflict4411Q → E in CAA23753. Ref.2
Sequence conflict4661E → G in AAF01333. Ref.4
Sequence conflict488 – 4892HE → EH AA sequence Ref.18
Sequence conflict4901K → R in CAH18185. Ref.11
Sequence conflict5251E → Q AA sequence Ref.18
Sequence conflict5511T → A in CAH18185. Ref.11
Sequence conflict5601K → R in CAH18185. Ref.11
Sequence conflict6041Q → R in AAN17825. Ref.5

Secondary structure

....................................................................................... 609
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: F88FF61DD242E818

FASTA60969,367
        10         20         30         40         50         60 
MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF 

        70         80         90        100        110        120 
EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP 

       130        140        150        160        170        180 
ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF 

       190        200        210        220        230        240 
FAKRYKAAFT ECCQAADKAA CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV 

       250        260        270        280        290        300 
ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK 

       310        320        330        340        350        360 
ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF LGMFLYEYAR 

       370        380        390        400        410        420 
RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE 

       430        440        450        460        470        480 
QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV 

       490        500        510        520        530        540 
LNQLCVLHEK TPVSDRVTKC CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL 

       550        560        570        580        590        600 
SEKERQIKKQ TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV 


AASQAALGL 

« Hide

Isoform 2 [UniParc].

Checksum: 16E764833EEF4E8D
Show »

FASTA41747,360

References

« Hide 'large scale' references
[1]"The sequence of human serum albumin cDNA and its expression in E. coli."
Lawn R.M., Adelman J., Bock S.C., Franke A.E., Houck C.M., Najarian R.C., Seeburg P.H., Wion K.L.
Nucleic Acids Res. 9:6103-6114(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-420.
[2]"Nucleotide sequence and the encoded amino acids of human serum albumin mRNA."
Dugaiczyk A., Law S.W., Dennison O.E.
Proc. Natl. Acad. Sci. U.S.A. 79:71-75(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-121.
[3]"Molecular structure of the human albumin gene is revealed by nucleotide sequence within q11-22 of chromosome 4."
Minghetti P.P., Ruffner D.E., Kuang W.J., Dennison O.E., Hawkins J.W., Beattie W.G., Dugaiczyk A.
J. Biol. Chem. 261:6747-6757(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Human serum albumin."
Yang S., Zhang R.A., Qi Z.W., Yuan Z.Y.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[5]"The cDNA sequences of human serum albumin."
Huang M.C., Wu H.T.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIROSHIMA-1 LYS-378.
[6]"Induction of galactose regulated gene expression in yeast."
Hinchliffe E.
Patent number EP0248637, 09-DEC-1987
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]"High expression HSA in Pichia for Pharmaceutical Use."
Yu Z., Fu Y.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[8]"Cloning and sequence analysis of human albumin gene."
Wang F., Huang L.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[9]"Identification of a human cell growth inhibition gene."
Kim J.W.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[10]"Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs."
Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.
Genome Res. 11:1392-1403(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal liver.
[11]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TYR-27.
Tissue: Liver.
[12]SeattleSNPs variation discovery resource
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[13]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"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] (ISOFORMS 1 AND 2).
Tissue: Liver and Skeletal muscle.
[15]Menaya J., Parrilla R., Ayuso M.S.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-455.
Tissue: Liver.
[16]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167.
[17]"The human albumin gene. Characterization of the 5' and 3' flanking regions and the polymorphic gene transcripts."
Urano Y., Watanabe K., Sakai M., Tamaoki T.
J. Biol. Chem. 261:3244-3251(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
[18]"Complete amino acid sequence of human serum albumin."
Meloun B., Moravek L., Kostka V.
FEBS Lett. 58:134-137(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-609.
[19]Brown J.R., Shockley P., Behrens P.Q.
(In) Bing D.H. (eds.); The chemistry and physiology of the human plasma proteins, pp.23-40, Pergamon Press, New York (1979)
Cited for: PROTEIN SEQUENCE OF 25-609.
[20]"The human myocardial two-dimensional gel protein database: update 1994."
Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-44 AND 480-499.
Tissue: Heart.
[21]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-34.
Tissue: Platelet.
[22]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 45-75; 98-130; 162-183; 239-254; 265-281; 287-298; 348-372; 397-434; 438-452; 500-543; 550-558; 570-581 AND 599-609, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[23]"The amino acid sequence of kinetensin, a novel peptide isolated from pepsin-treated human plasma: homology with human serum albumin, neurotensin and angiotensin."
Mogard M.H., Kobayashi R., Chen C.F., Lee T.D., Reeve J.R. Jr., Shively J.E., Walsh J.H.
Biochem. Biophys. Res. Commun. 136:983-988(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 166-174.
[24]"Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s)."
Carraway R.E., Mitra S.P., Cochrane D.E.
J. Biol. Chem. 262:5968-5973(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 166-174.
[25]"Lysine residue 199 of human serum albumin is modified by acetylsalicylic acid."
Walker J.E.
FEBS Lett. 66:173-175(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 222-229, ASPIRIN-ACETYLATION AT LYS-223.
[26]"Enzymatic digestion and mass spectrometry in the study of advanced glycation end products/peptides."
Lapolla A., Fedele D., Reitano R., Arico N.C., Seraglia R., Traldi P., Marotta E., Tonani R.
J. Am. Soc. Mass Spectrom. 15:496-509(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 250-264, GLYCATION AT LYS-75; LYS-161; LYS-186; LYS-249; LYS-257; LYS-300; LYS-337; LYS-347; LYS-375; LYS-402; LYS-437; LYS-468; LYS-560; LYS-549; LYS-569 AND LYS-597, LACK OF GLYCATION AT LYS-28; LYS-44; LYS-65; LYS-88; LYS-97; LYS-117; LYS-130; LYS-160; LYS-183; LYS-198; LYS-205; LYS-214; LYS-219; LYS-229; LYS-236; LYS-264; LYS-286; LYS-298; LYS-310; LYS-383; LYS-396; LYS-413; LYS-426; LYS-438; LYS-456; LYS-460; LYS-490; LYS-499; LYS-524; LYS-543; LYS-548; LYS-562; LYS-565; LYS-581; LYS-584; LYS-588 AND LYS-598, IDENTIFICATION BY MASS SPECTROMETRY.
[27]"Disulfide bonds in human serum albumin."
Saber M.A., Stockbauer P., Moravek L., Meloun B.
Collect. Czech. Chem. Commun. 42:564-579(1977)
Cited for: DISULFIDE BONDS.
[28]"Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin."
Jacobsen C.
Biochem. J. 171:453-459(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: BILIRUBIN-BINDING SITE.
[29]"The principal site of nonenzymatic glycosylation of human serum albumin in vivo."
Garlick R.L., Mazer J.S.
J. Biol. Chem. 258:6142-6146(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCATION AT LYS-223 AND LYS-549.
[30]"Nonenzymatic glycosylation of human serum albumin alters its conformation and function."
Shaklai N., Garlick R.L., Bunn H.F.
J. Biol. Chem. 259:3812-3817(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCATION AT LYS-549.
[31]"Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites."
Iberg N., Fluckiger R.
J. Biol. Chem. 261:13542-13545(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCATION AT LYS-36; LYS-223; LYS-257; LYS-305; LYS-341; LYS-375; LYS-463; LYS-549 AND LYS-558.
[32]"Albumin as a zinc carrier: properties of its high-affinity zinc-binding site."
Lu J., Stewart A.J., Sadler P.J., Pinheiro T.J., Blindauer C.A.
Biochem. Soc. Trans. 36:1317-1321(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ZINC-BINDING SITES.
[33]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[34]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; THR-444 AND THR-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[35]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Three-dimensional structure of human serum albumin."
Carter D.C., He X.-M., Munson S.H., Twigg P.D., Gernert K.M., Broom M.B., Miller T.Y.
Science 244:1195-1198(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
[37]"Structure of human serum albumin."
Carter D.C., He X.-M.
Science 249:302-303(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS).
[38]"Atomic structure and chemistry of human serum albumin."
He X.-M., Carter D.C.
Nature 358:209-215(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[39]Erratum
He X.-M., Carter D.C.
Nature 364:362-362(1993)
[40]"Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites."
Curry S., Mandelkow H., Brick P., Franks N.
Nat. Struct. Biol. 5:827-835(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[41]"Crystal structure of human serum albumin at 2.5-A resolution."
Sugio S., Kashima A., Mochizuki S., Noda M., Kobayashi K.
Protein Eng. 12:439-446(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[42]"Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures."
Bhattacharya A.A., Curry S., Franks N.P.
J. Biol. Chem. 275:38731-38738(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-609.
[43]"Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids."
Petitpas I., Grune T., Bhattacharya A.A., Curry S.
J. Mol. Biol. 314:955-960(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[44]"Albumin Canterbury (313 Lys-->Asn). A point mutation in the second domain of serum albumin."
Brennan S.O., Herbert P.
Biochim. Biophys. Acta 912:191-197(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CANTERBURY ASN-337.
[45]"Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning."
Takahashi N., Takahashi Y., Blumberg B.S., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 84:4413-4417(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NASKAPI/MERSIN GLU-396 AND MEXICO GLY-574.
[46]"Amino acid substitutions in inherited albumin variants from Amerindian and Japanese populations."
Takshashi N., Takahashi Y., Isobe T., Putnam F.W., Fujita M., Satoh C., Neel J.V.
Proc. Natl. Acad. Sci. U.S.A. 84:8001-8005(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NAGASAKI-3 GLN-27 YANOMAMA-2 GLU-396; NAGASAKI-2 ASN-399 AND MAKU GLU-565.
[47]"Identical structural changes in inherited albumin variants from different populations."
Arai K., Ishioka N., Huss K., Madison J., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 86:434-438(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FUKUOKA-2 HIS-23; CHRISTCHURCH/HONOLULU-2 GLN-24; TAGLIACOZZO ASN-337 AND ALBUMIN B/OSAKA-2/PHNOM PHEN LYS-594.
[48]"Point substitutions in Japanese alloalbumins."
Arai K., Madison J., Huss K., Ishioka N., Satoh C., Fujita M., Neel J.V., Sakurabayashi I., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 86:6092-6096(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HONOLULU-2 GLN-24; NAGASAKI-1 GLY-293; HIROSHIMA-1 LYS-378; TOCHIGI LYS-400; HIROSHIMA-2 LYS-406 AND OSAKA-2 LYS-594.
[49]"Point substitutions in albumin genetic variants from Asia."
Arai K., Madison J., Shimuzu A., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 87:497-501(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HONOLULU-1 PRO-24; HONOLULU-2 GLN-24; NAGOYA LYS-143; NEW GUINEA ASN-337; MANAUS-1/LAMBADI LYS-525; FUKUOKA-1 ASN-587; OSAKA-1 LYS-589 AND OSAKA-2 LYS-594.
[50]"Albumin Redhill (-1 Arg, 320 Ala-->Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site."
Brennan S.O., Myles T., Peach R.J., Donaldson D., George P.M.
Proc. Natl. Acad. Sci. U.S.A. 87:26-30(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT REDHILL.
[51]"Mutations in genetic variants of human serum albumin found in Italy."
Galliano M., Minchiotti L., Porta F., Rossi A., Ferri G., Madison J., Watkins S., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 87:8721-8725(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VARESE HIS-23; TORINO LYS-84 AND VIBO VALENTIA LYS-106.
[52]"A donor splice mutation and a single-base deletion produce two carboxyl-terminal variants of human serum albumin."
Watkins S., Madison J., Davis E., Sakamoto Y., Galliano M., Minchiotti L., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 88:5959-5963(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT VENEZIA.
[53]"Genetic variants of serum albumin in Americans and Japanese."
Madison J., Arai K., Feld R.D., Kyle R.A., Watkins S., Davis E., Matsuda Y., Amaki I., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 88:9853-9857(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS KOMAGOME-3 HIS-23; IOWA CITY-2 VAL-25; KOMAGOME-2 ARG-152; IOWA CITY-1 VAL-389 AND KOMAGOME-1 GLU-396.
[54]"Structural characterization of a glycoprotein variant of human serum albumin: albumin Casebrook (494 Asp-->Asn)."
Peach R.J., Brennan S.O.
Biochim. Biophys. Acta 1097:49-54(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CASEBROOK ASN-518.
[55]"Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions."
Minchiotti L., Galliano M., Stoppini M., Ferri G., Crespeau H., Rochu D., Porta F.
Biochim. Biophys. Acta 1119:232-238(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SONDRIO LYS-357 AND PARIS-2 ASN-587.
[56]"Alloalbuminemia in Sweden: structural study and phenotypic distribution of nine albumin variants."
Carlson J., Sakamoto Y., Laurell C.-B., Madison J., Watkins S., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 89:8225-8229(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MALMO-I CYS-23; MALMO-95 ASN-87; MALMO-10 ARG-292; MALMO-47 LYS-342; MALMO-5 GLN-400 AND MALMO-61 ALA-574.
[57]"The structural characterization and bilirubin-binding properties of albumin Herborn, a [Lys240-->Glu] albumin mutant."
Minchiotti L., Galliano M., Zapponi M.C., Tenni R.
Eur. J. Biochem. 214:437-444(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HERBORN GLU-264.
[58]"Albumin Hawkes Bay; a low level variant caused by loss of a sulphydryl group at position 177."
Brennan S.O., Fellowes A.P.
Biochim. Biophys. Acta 1182:46-50(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAWKES BAY PHE-201.
[59]"Protein and DNA sequence analysis of a 'private' genetic variant: albumin Ortonovo (Glu-505-->Lys)."
Galliano M., Minchiotti L., Iadarola P., Stoppini M., Giagnoni P., Watkins S., Madison J., Putnam F.W.
Biochim. Biophys. Acta 1225:27-32(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ORTONOVO LYS-529.
[60]"Genetic variants of human serum albumin in Italy: point mutants and a carboxyl-terminal variant."
Madison J., Galliano M., Watkins S., Minchiotti L., Porta F., Rossi A., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 91:6476-6480(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LARINO TYR-27; TRADATE-2 GLN-249 AND CASERTA ASN-300.
[61]"An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families."
Sunthornthepvarakul T., Angkeow P., Weiss R.E., Hayashi Y., Retetoff S.
Biochem. Biophys. Res. Commun. 202:781-787(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DH HIS-242.
[62]"Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia."
Rushbrook J.I., Becker E., Schussler G.C., Divino C.M.
J. Clin. Endocrinol. Metab. 80:461-467(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DH HIS-242, PROTEIN SEQUENCE OF 25-51.
[63]"A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred."
Wada N., Chiba H., Shimizu C., Kijima H., Kubo M., Koike T.
J. Clin. Endocrinol. Metab. 82:3246-3250(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DH HIS-242.
[64]"Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect."
Sunthornthepvarakul T., Likitmaskul S., Ngowngarmratana S., Angsusingha K., Kitvitayasak S., Scherberg N.H., Refetoff S.
J. Clin. Endocrinol. Metab. 83:1448-1454(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DH PRO-90.
[65]"Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry I. Profiling an unfractionated tryptic digest."
Spahr C.S., Davis M.T., McGinley M.D., Robinson J.H., Bures E.J., Beierle J., Mort J., Courchesne P.L., Chen K., Wahl R.C., Yu W., Luethy R., Patterson S.D.
Proteomics 1:93-107(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TYR-73, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Urine.
[66]"A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges."
Minchiotti L., Campagnoli M., Rossi A., Cosulich M.E., Monti M., Pucci P., Kragh-Hansen U., Granel B., Disdier P., Weiller P.J., Galliano M.
Eur. J. Biochem. 268:344-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT KENITRA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00494 mRNA. Translation: CAA23753.1.
V00495 mRNA. Translation: CAA23754.1.
M12523 Genomic DNA. Translation: AAA98797.1.
M12523 Genomic DNA. Translation: AAA98798.1.
AF190168 mRNA. Translation: AAF01333.1.
AF542069 mRNA. Translation: AAN17825.1.
A06977 mRNA. Translation: CAA00606.1.
AY728024 mRNA. Translation: AAU21642.1.
DQ986150 mRNA. Translation: ABJ16448.1.
AY544124 mRNA. Translation: AAT11155.1.
AY550967 mRNA. Translation: AAT52213.1.
AF116645 mRNA. Translation: AAF71067.1.
AF118090 mRNA. Translation: AAF22034.1. Different initiation.
AF119840 mRNA. Translation: AAF69594.1.
AF119890 mRNA. Translation: AAF69644.1. Different initiation.
AF130077 mRNA. Translation: AAG35503.1. Different initiation.
CR749331 mRNA. Translation: CAH18185.1.
EF649953 Genomic DNA. Translation: ABS29264.1.
CH471057 Genomic DNA. Translation: EAX05676.1.
BC014308 mRNA. Translation: AAH14308.1.
BC034023 mRNA. Translation: AAH34023.1.
BC036003 mRNA. Translation: AAH36003.1.
BC041789 mRNA. Translation: AAH41789.1.
U22961 mRNA. Translation: AAA64922.1.
AY358313 mRNA. Translation: AAQ89947.1.
AH002596 Genomic DNA. Translation: AAA51688.1.
PIRABHUS. A93743.
RefSeqNP_000468.1. NM_000477.5.
UniGeneHs.418167.
Hs.592379.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AO6X-ray2.50A/B25-609[»]
1BJ5X-ray2.50A25-609[»]
1BKEX-ray3.15A28-608[»]
1BM0X-ray2.50A/B25-609[»]
1E78X-ray2.60A/B25-609[»]
1E7AX-ray2.20A/B25-609[»]
1E7BX-ray2.38A/B25-609[»]
1E7CX-ray2.40A25-609[»]
1E7EX-ray2.50A25-609[»]
1E7FX-ray2.43A25-609[»]
1E7GX-ray2.50A25-609[»]
1E7HX-ray2.43A25-609[»]
1E7IX-ray2.70A25-609[»]
1GNIX-ray2.40A25-609[»]
1GNJX-ray2.60A25-609[»]
1H9ZX-ray2.50A25-609[»]
1HA2X-ray2.50A25-609[»]
1HK1X-ray2.65A25-609[»]
1HK2X-ray2.80A25-609[»]
1HK3X-ray2.80A25-609[»]
1HK4X-ray2.40A25-609[»]
1HK5X-ray2.70A25-609[»]
1N5UX-ray1.90A25-609[»]
1O9XX-ray3.20A25-609[»]
1TF0X-ray2.70A25-596[»]
1UORX-ray2.80A25-609[»]
1YSXNMR-A409-609[»]
2BX8X-ray2.70A/B25-609[»]
2BXAX-ray2.35A/B25-609[»]
2BXBX-ray3.20A/B25-609[»]
2BXCX-ray3.10A/B25-609[»]
2BXDX-ray3.05A/B25-609[»]
2BXEX-ray2.95A/B25-609[»]
2BXFX-ray2.95A/B25-609[»]
2BXGX-ray2.70A/B25-609[»]
2BXHX-ray2.25A/B25-609[»]
2BXIX-ray2.50A25-609[»]
2BXKX-ray2.40A25-609[»]
2BXLX-ray2.60A25-609[»]
2BXMX-ray2.50A25-609[»]
2BXNX-ray2.65A25-609[»]
2BXOX-ray2.60A25-609[»]
2BXPX-ray2.30A25-609[»]
2BXQX-ray2.60A25-609[»]
2ESGX-ray-C25-609[»]
2I2ZX-ray2.70A25-609[»]
2I30X-ray2.90A25-609[»]
2VDBX-ray2.52A30-608[»]
2VUEX-ray2.42A/B25-609[»]
2VUFX-ray3.05A/B25-609[»]
2XSIX-ray2.70A25-609[»]
2XVQX-ray2.90A/B25-609[»]
2XVUX-ray2.60A/B25-609[»]
2XVVX-ray2.40A25-609[»]
2XVWX-ray2.65A25-609[»]
2XW0X-ray2.40A/B25-609[»]
2XW1X-ray2.50A/B25-609[»]
2YDFX-ray2.75A/B25-609[»]
3A73X-ray2.19A/B25-609[»]
3B9LX-ray2.60A25-609[»]
3B9MX-ray2.70A25-609[»]
3CX9X-ray2.80A27-608[»]
3JQZX-ray3.30A/B25-609[»]
3JRYX-ray2.30A/B25-609[»]
3LU6X-ray2.70A/B25-609[»]
3LU7X-ray2.80A/B25-609[»]
3LU8X-ray2.60A/B25-609[»]
3SQJX-ray2.05A/B27-608[»]
3TDLX-ray2.60A25-609[»]
3UIVX-ray2.20A/H25-609[»]
4BKEX-ray2.35A1-609[»]
4E99X-ray2.30A25-609[»]
4EMXX-ray2.30A/B25-609[»]
4G03X-ray2.22A/B25-609[»]
4G04X-ray2.30A/B25-609[»]
4HGKX-ray3.04A/B25-609[»]
4HGMX-ray2.34B25-609[»]
4IW1X-ray2.56A25-609[»]
4IW2X-ray2.41A25-609[»]
4K2CX-ray3.23A/B25-609[»]
4K71X-ray2.40A/D25-609[»]
4L8UX-ray2.01A25-609[»]
4L9KX-ray2.40A/B25-609[»]
4L9QX-ray2.70A/B25-609[»]
4LA0X-ray2.40A/B25-609[»]
4LB2X-ray2.80A/B25-609[»]
4LB9X-ray2.70A25-609[»]
4N0FX-ray3.02D/G/J/M25-609[»]
4N0UX-ray3.80D27-609[»]
DisProtDP00515.
ProteinModelPortalP02768.
SMRP02768. Positions 26-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106715. 159 interactions.
DIPDIP-29902N.
IntActP02768. 154 interactions.
MINTMINT-3004222.

Chemistry

BindingDBP02768.
ChEMBLCHEMBL3253.
DrugBankDB01418. Acenocoumarol.
DB00459. Acitretin.
DB00802. Alfentanil.
DB01370. Aluminium.
DB00995. Auranofin.
DB01402. Bismuth.
DB01197. Captopril.
DB00958. Carboplatin.
DB00456. Cefalotin.
DB01327. Cefazolin.
DB01328. Cefonicid.
DB01329. Cefoperazone.
DB01114. Chlorpheniramine.
DB00477. Chlorpromazine.
DB00537. Ciprofloxacin.
DB01068. Clonazepam.
DB01147. Cloxacillin.
DB00987. Cytarabine.
DB01219. Dantrolene.
DB00586. Diclofenac.
DB00861. Diflunisal.
DB01396. Digitoxin.
DB00655. Estrone.
DB00903. Ethacrynic acid.
DB00749. Etodolac.
DB00712. Flurbiprofen.
DB00743. Gadobenate Dimeglumine.
DB01044. Gatifloxacin.
DB01120. Gliclazide.
DB01159. Halothane.
DB00062. Human Serum Albumin.
DB00070. Hyaluronidase.
DB01050. Ibuprofen.
DB01307. Insulin-detemir.
DB01308. Insulin-glargine.
DB04711. Iodipamide.
DB01009. Ketoprofen.
DB00848. Levamisole.
DB00451. Levothyroxine.
DB00279. Liothyronine.
DB00784. Mefenamic acid.
DB00532. Mephenytoin.
DB00563. Methotrexate.
DB00540. Nortriptyline.
DB00842. Oxazepam.
DB01229. Paclitaxel.
DB00946. Phenprocoumon.
DB01032. Probenecid.
DB00818. Propofol.
DB00165. Pyridoxine.
DB00936. Salicyclic acid.
DB01232. Saquinavir.
DB00096. Serum albumin.
DB00064. Serum albumin iodonated.
DB00815. Sodium lauryl sulfate.
DB00364. Sucralfate.
DB00576. Sulfamethizole.
DB00605. Sulindac.
DB00870. Suprofen.
DB00624. Testosterone.
DB00137. Xanthophyll.

Protein family/group databases

Allergome763. Hom s HSA.

PTM databases

PhosphoSiteP02768.
UniCarbKBP02768.

Polymorphism databases

DMDM113576.

2D gel databases

DOSAC-COBS-2DPAGEP02768.
OGPP02768.
REPRODUCTION-2DPAGEIPI00384697.
IPI00745872.
P02768.
SWISS-2DPAGEP02768.
UCD-2DPAGEP02768.

Proteomic databases

PaxDbP02768.
PRIDEP02768.

Protocols and materials databases

DNASU213.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295897; ENSP00000295897; ENSG00000163631. [P02768-1]
ENST00000509063; ENSP00000422784; ENSG00000163631.
GeneID213.
KEGGhsa:213.
UCSCuc003hgs.4. human. [P02768-1]

Organism-specific databases

CTD213.
GeneCardsGC04P074259.
HGNCHGNC:399. ALB.
HPACAB006262.
MIM103600. gene+phenotype.
neXtProtNX_P02768.
Orphanet86816. Congenital analbuminemia.
276271. Familial dysalbuminemic hyperthyroxinemia.
PharmGKBPA24690.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45992.
HOVERGENHBG004207.
KOK16141.
OMANCDKSLH.
OrthoDBEOG7S4X5C.
PhylomeDBP02768.
TreeFamTF335561.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP02768.
BgeeP02768.
GenevestigatorP02768.

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. human.
EvolutionaryTraceP02768.
GeneWikiSerum_albumin.
GenomeRNAi213.
NextBio862.
PMAP-CutDBP02768.
PROP02768.
SOURCESearch...

Entry information

Entry nameALBU_HUMAN
AccessionPrimary (citable) accession number: P02768
Secondary accession number(s): O95574 expand/collapse secondary AC list , P04277, Q13140, Q645G4, Q68DN5, Q6UXK4, Q86YG0, Q9P157, Q9P1I7, Q9UHS3, Q9UJZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 205 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM