Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02768

- ALBU_HUMAN

UniProt

P02768 - ALBU_HUMAN

Protein

Serum albumin

Gene

ALB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 210 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi27 – 271CopperBy similarity
    Sitei28 – 281Not glycated
    Sitei44 – 441Not glycated
    Sitei65 – 651Not glycated
    Sitei88 – 881Not glycated
    Metal bindingi91 – 911Zinc
    Sitei97 – 971Not glycated
    Sitei117 – 1171Not glycated
    Metal bindingi123 – 1231Zinc
    Sitei130 – 1301Not glycated
    Sitei160 – 1601Not glycated
    Sitei183 – 1831Not glycated
    Sitei198 – 1981Not glycated
    Sitei205 – 2051Not glycated
    Sitei214 – 2141Not glycated
    Sitei219 – 2191Not glycated
    Sitei223 – 2231Aspirin-acetylated lysine
    Sitei229 – 2291Not glycated
    Sitei236 – 2361Not glycated
    Binding sitei264 – 2641Bilirubin
    Sitei264 – 2641Not glycated
    Metal bindingi271 – 2711Zinc
    Metal bindingi273 – 2731Zinc
    Sitei286 – 2861Not glycated
    Sitei298 – 2981Not glycated
    Sitei310 – 3101Not glycated
    Sitei383 – 3831Not glycated
    Sitei396 – 3961Not glycated
    Sitei413 – 4131Not glycated
    Sitei426 – 4261Not glycated
    Sitei438 – 4381Not glycated
    Sitei456 – 4561Not glycated
    Sitei460 – 4601Not glycated
    Sitei490 – 4901Not glycated
    Sitei499 – 4991Not glycated
    Sitei524 – 5241Not glycated
    Sitei543 – 5431Not glycated
    Sitei548 – 5481Not glycated
    Sitei562 – 5621Not glycated
    Sitei565 – 5651Not glycated
    Sitei581 – 5811Not glycated
    Sitei584 – 5841Not glycated
    Sitei588 – 5881Not glycated
    Sitei598 – 5981Not glycated

    GO - Molecular functioni

    1. antioxidant activity Source: UniProtKB
    2. chaperone binding Source: BHF-UCL
    3. copper ion binding Source: UniProtKB
    4. DNA binding Source: UniProtKB
    5. drug binding Source: UniProtKB
    6. fatty acid binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. pyridoxal phosphate binding Source: UniProtKB
    9. toxic substance binding Source: UniProtKB
    10. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. bile acid and bile salt transport Source: Reactome
    2. bile acid metabolic process Source: Reactome
    3. blood coagulation Source: Reactome
    4. cellular response to starvation Source: UniProtKB
    5. hemolysis by symbiont of host erythrocytes Source: UniProtKB
    6. lipoprotein metabolic process Source: Reactome
    7. maintenance of mitochondrion location Source: UniProtKB
    8. negative regulation of apoptotic process Source: UniProtKB
    9. negative regulation of programmed cell death Source: UniProtKB
    10. platelet activation Source: Reactome
    11. platelet degranulation Source: Reactome
    12. positive regulation of circadian sleep/wake cycle, non-REM sleep Source: Ensembl
    13. response to mercury ion Source: Ensembl
    14. response to nutrient Source: Ensembl
    15. response to organic substance Source: Ensembl
    16. response to platinum ion Source: Ensembl
    17. retina homeostasis Source: UniProt
    18. small molecule metabolic process Source: Reactome
    19. sodium-independent organic anion transport Source: Reactome
    20. transmembrane transport Source: Reactome
    21. transport Source: UniProtKB

    Keywords - Ligandi

    Copper, Lipid-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_11042. Recycling of bile acids and salts.
    REACT_13621. HDL-mediated lipid transport.
    REACT_160163. Scavenging of heme from plasma.
    REACT_23988. Transport of organic anions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serum albumin
    Gene namesi
    Name:ALB
    ORF Names:GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:399. ALB.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: Ensembl
    2. blood microparticle Source: UniProt
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: BHF-UCL
    5. extracellular vesicular exosome Source: UniProtKB
    6. nucleus Source: UniProt
    7. platelet alpha granule lumen Source: Reactome
    8. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901L → P in DH. 1 Publication
    VAR_013011
    Natural varianti242 – 2421R → H in DH. 3 Publications
    VAR_000514
    Natural varianti242 – 2421R → P in DH.
    VAR_013013

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi103600. gene+phenotype.
    Orphaneti86816. Congenital analbuminemia.
    276271. Familial dysalbuminemic hyperthyroxinemia.
    PharmGKBiPA24690.

    Protein family/group databases

    Allergomei763. Hom s HSA.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Propeptidei19 – 224PRO_0000001067
    Chaini25 – 609585Serum albuminPRO_0000001068Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361N-linked (Glc) (glycation)Curated
    Glycosylationi75 – 751N-linked (Glc) (glycation); in vitro
    Disulfide bondi77 ↔ 861 PublicationPROSITE-ProRule annotation
    Modified residuei82 – 821Phosphoserine1 Publication
    Disulfide bondi99 ↔ 1151 PublicationPROSITE-ProRule annotation
    Disulfide bondi114 ↔ 1251 PublicationPROSITE-ProRule annotation
    Disulfide bondi148 ↔ 1931 PublicationPROSITE-ProRule annotation
    Glycosylationi161 – 1611N-linked (Glc) (glycation); in vitro
    Glycosylationi186 – 1861N-linked (Glc) (glycation); in vitro
    Disulfide bondi192 ↔ 2011 PublicationPROSITE-ProRule annotation
    Glycosylationi223 – 2231N-linked (Glc) (glycation); in vitro
    Disulfide bondi224 ↔ 2701 PublicationPROSITE-ProRule annotation
    Glycosylationi249 – 2491N-linked (Glc) (glycation); in vitro
    Glycosylationi257 – 2571N-linked (Glc) (glycation)Curated
    Disulfide bondi269 ↔ 2771 PublicationPROSITE-ProRule annotation
    Disulfide bondi289 ↔ 3031 PublicationPROSITE-ProRule annotation
    Glycosylationi300 – 3001N-linked (Glc) (glycation); in vitro
    Disulfide bondi302 ↔ 3131 PublicationPROSITE-ProRule annotation
    Glycosylationi305 – 3051N-linked (Glc) (glycation)
    Glycosylationi337 – 3371N-linked (Glc) (glycation); in vitro
    Disulfide bondi340 ↔ 3851 PublicationPROSITE-ProRule annotation
    Glycosylationi341 – 3411N-linked (Glc) (glycation)Curated
    Glycosylationi342 – 3421N-linked (GlcNAc...); in variant RedhillCAR_000226
    Glycosylationi347 – 3471N-linked (Glc) (glycation); in vitro
    Glycosylationi375 – 3751N-linked (Glc) (glycation)Curated
    Disulfide bondi384 ↔ 3931 PublicationPROSITE-ProRule annotation
    Glycosylationi402 – 4021N-linked (Glc) (glycation); in vitro
    Disulfide bondi416 ↔ 4621 PublicationPROSITE-ProRule annotation
    Glycosylationi437 – 4371N-linked (Glc) (glycation); in vitro
    Modified residuei443 – 4431Phosphoserine1 Publication
    Modified residuei444 – 4441Phosphothreonine1 Publication
    Modified residuei446 – 4461Phosphothreonine1 Publication
    Disulfide bondi461 ↔ 4721 PublicationPROSITE-ProRule annotation
    Glycosylationi463 – 4631N-linked (Glc) (glycation)
    Glycosylationi468 – 4681N-linked (Glc) (glycation); in vitro
    Disulfide bondi485 ↔ 5011 PublicationPROSITE-ProRule annotation
    Disulfide bondi500 ↔ 5111 PublicationPROSITE-ProRule annotation
    Glycosylationi518 – 5181N-linked (GlcNAc...); in variant CasebrookCAR_000069
    Disulfide bondi538 ↔ 5831 PublicationPROSITE-ProRule annotation
    Glycosylationi549 – 5491N-linked (Glc) (glycation)
    Glycosylationi558 – 5581N-linked (Glc) (glycation)Curated
    Glycosylationi560 – 5601N-linked (Glc) (glycation); in vitro
    Glycosylationi569 – 5691N-linked (Glc) (glycation); in vitro
    Disulfide bondi582 ↔ 5911 PublicationPROSITE-ProRule annotation
    Glycosylationi597 – 5971N-linked (Glc) (glycation); in vitro

    Post-translational modificationi

    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.2 Publications
    Acetylated on Lys-223 by acetylsalicylic acid.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP02768.
    PaxDbiP02768.
    PRIDEiP02768.

    2D gel databases

    DOSAC-COBS-2DPAGEP02768.
    OGPiP02768.
    REPRODUCTION-2DPAGEIPI00384697.
    IPI00745872.
    P02768.
    SWISS-2DPAGEP02768.
    UCD-2DPAGEP02768.

    PTM databases

    PhosphoSiteiP02768.
    UniCarbKBiP02768.

    Miscellaneous databases

    PMAP-CutDBP02768.

    Expressioni

    Tissue specificityi

    Plasma.

    Gene expression databases

    ArrayExpressiP02768.
    BgeeiP02768.
    GenevestigatoriP02768.

    Organism-specific databases

    HPAiCAB006262.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TFRCP027862EBI-714423,EBI-355727

    Protein-protein interaction databases

    BioGridi106715. 156 interactions.
    DIPiDIP-29902N.
    IntActiP02768. 159 interactions.
    MINTiMINT-3004222.

    Structurei

    Secondary structure

    1
    609
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 389
    Helixi40 – 5415
    Beta strandi55 – 584
    Helixi60 – 7920
    Turni84 – 874
    Helixi90 – 9910
    Turni101 – 1033
    Helixi104 – 1085
    Helixi109 – 1168
    Helixi119 – 12810
    Beta strandi130 – 1323
    Helixi144 – 15310
    Helixi155 – 16915
    Beta strandi170 – 1734
    Helixi175 – 19218
    Beta strandi195 – 1973
    Helixi198 – 23033
    Helixi232 – 24615
    Beta strandi248 – 2503
    Helixi252 – 27120
    Helixi274 – 28916
    Helixi290 – 2945
    Helixi297 – 2993
    Helixi300 – 3034
    Helixi307 – 3159
    Helixi330 – 3334
    Beta strandi336 – 3383
    Helixi339 – 3457
    Helixi347 – 36014
    Beta strandi363 – 3653
    Helixi367 – 38418
    Beta strandi387 – 3893
    Helixi390 – 3945
    Helixi397 – 42226
    Helixi424 – 43815
    Beta strandi440 – 4423
    Helixi444 – 46118
    Beta strandi462 – 4643
    Helixi466 – 48823
    Beta strandi489 – 4913
    Helixi495 – 5028
    Turni505 – 5073
    Helixi508 – 5136
    Beta strandi519 – 5213
    Helixi529 – 5313
    Helixi535 – 5384
    Helixi542 – 55918
    Beta strandi561 – 5633
    Helixi565 – 58319
    Beta strandi584 – 5874
    Helixi588 – 5903
    Turni591 – 5933
    Helixi594 – 60613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00515.
    ProteinModelPortaliP02768.
    SMRiP02768. Positions 26-608.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02768.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 210192Albumin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini211 – 403193Albumin 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.
    HOVERGENiHBG004207.
    KOiK16141.
    OMAiNCDKSLH.
    OrthoDBiEOG7S4X5C.
    PhylomeDBiP02768.
    TreeFamiTF335561.

    Family and domain databases

    InterProiIPR000264. ALB/AFP/VDB.
    IPR020858. Serum_albumin-like.
    IPR021177. Serum_albumin/AFP.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P02768-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA    50
    FAQYLQQCPF EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT 100
    VATLRETYGE MADCCAKQEP ERNECFLQHK DDNPNLPRLV RPEVDVMCTA 150
    FHDNEETFLK KYLYEIARRH PYFYAPELLF FAKRYKAAFT ECCQAADKAA 200
    CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV ARLSQRFPKA 250
    EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK 300
    ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF 350
    LGMFLYEYAR RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE 400
    FKPLVEEPQN LIKQNCELFE QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV 450
    SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV LNQLCVLHEK TPVSDRVTKC 500
    CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL SEKERQIKKQ 550
    TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV 600
    AASQAALGL 609
    Length:609
    Mass (Da):69,367
    Last modified:April 1, 1990 - v2
    Checksum:iF88FF61DD242E818
    GO
    Isoform 2 (identifier: P02768-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:417
    Mass (Da):47,360
    Checksum:i16E764833EEF4E8D
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551L → P in CAH18185. (PubMed:17974005)Curated
    Sequence conflicti122 – 1221R → S in AAF01333. 1 PublicationCurated
    Sequence conflicti155 – 1551E → Q AA sequence (PubMed:1225573)Curated
    Sequence conflicti174 – 1741Y → L AA sequence (PubMed:3087352)Curated
    Sequence conflicti174 – 1741Y → L AA sequence (PubMed:2437111)Curated
    Sequence conflicti194 – 1941Q → E AA sequence (PubMed:1225573)Curated
    Sequence conflicti327 – 3326PSLAAD → MFVLLC in AAF71067. (PubMed:11483580)Curated
    Sequence conflicti405 – 4051V → A in AAF71067. (PubMed:11483580)Curated
    Sequence conflicti409 – 4091Q → E in AAH14308. (PubMed:15489334)Curated
    Sequence conflicti441 – 4411Q → E in CAA23753. (PubMed:6275391)Curated
    Sequence conflicti466 – 4661E → G in AAF01333. 1 PublicationCurated
    Sequence conflicti488 – 4892HE → EH AA sequence (PubMed:1225573)Curated
    Sequence conflicti490 – 4901K → R in CAH18185. (PubMed:17974005)Curated
    Sequence conflicti525 – 5251E → Q AA sequence (PubMed:1225573)Curated
    Sequence conflicti551 – 5511T → A in CAH18185. (PubMed:17974005)Curated
    Sequence conflicti560 – 5601K → R in CAH18185. (PubMed:17974005)Curated
    Sequence conflicti604 – 6041Q → R in AAN17825. 1 PublicationCurated

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231R → C in Redhill/Malmo-I/Tradate; associated with T-344 in Redhill. 1 Publication
    VAR_000499
    Natural varianti23 – 231R → H in Fukuoka-2/Lille/Taipei/Varese/Komagome-3. 3 Publications
    VAR_000500
    Natural varianti24 – 241R → L in Jaffna.
    VAR_000501
    Natural varianti24 – 241R → P in Takefu/Honolulu-1. 1 Publication
    VAR_000502
    Natural varianti24 – 241R → Q in Christchurch/Honolulu-2. 3 Publications
    VAR_000503
    Natural varianti25 – 251D → V in Bleinheim/Iowa city-2. 1 Publication
    VAR_000504
    Natural varianti27 – 271H → Q in Nagasaki-3.
    VAR_000505
    Natural varianti27 – 271H → Y in Larino. 2 Publications
    VAR_000506
    Natural varianti73 – 731F → Y.1 Publication
    VAR_010657
    Natural varianti84 – 841E → K in Torino. 1 Publication
    VAR_000507
    Natural varianti87 – 871D → N in Malmo-95/Dalakarlia. 1 Publication
    VAR_000508
    Natural varianti90 – 901L → P in DH. 1 Publication
    VAR_013011
    Natural varianti106 – 1061E → K in Vibo Valentia. 1 Publication
    VAR_000509
    Natural varianti121 – 1211E → G.1 Publication
    VAR_014290
    Natural varianti138 – 1381R → G in Yanomama-2.
    VAR_000510
    Natural varianti143 – 1431E → K in Nagoya. 1 Publication
    VAR_000511
    Natural varianti146 – 1461V → E in Tregasio.
    VAR_013012
    Natural varianti152 – 1521H → R in Komagome-2. 1 Publication
    VAR_000512
    Natural varianti201 – 2011C → F in Hawkes bay. 1 Publication
    VAR_000513
    Natural varianti215 – 2151A → T.
    Corresponds to variant rs3210154 [ dbSNP | Ensembl ].
    VAR_014291
    Natural varianti215 – 2151A → V.
    Corresponds to variant rs3204504 [ dbSNP | Ensembl ].
    VAR_014292
    Natural varianti220 – 2201Q → L.
    Corresponds to variant rs3210163 [ dbSNP | Ensembl ].
    VAR_014293
    Natural varianti242 – 2421R → H in DH. 3 Publications
    VAR_000514
    Natural varianti242 – 2421R → P in DH.
    VAR_013013
    Natural varianti249 – 2491K → Q in Tradate-2. 1 Publication
    VAR_000515
    Natural varianti264 – 2641K → E in Herborn. 1 Publication
    VAR_000516
    Natural varianti292 – 2921Q → R in Malmo-10. 1 Publication
    VAR_000517
    Natural varianti293 – 2931D → G in Nagasaki-1. 1 Publication
    VAR_000518
    Natural varianti300 – 3001K → N in Caserta. 1 Publication
    VAR_000519
    Natural varianti337 – 3371K → N in Canterbury/New Guinea/Tagliacozzo/Cuneo/Cooperstown. 3 Publications
    VAR_000520
    Natural varianti338 – 3381D → G in Bergamo.
    VAR_013014
    Natural varianti338 – 3381D → V in Brest.
    VAR_013015
    Natural varianti342 – 3421N → K in Malmo-47. 1 Publication
    VAR_000521
    Natural varianti344 – 3441A → T in Redhill; associated with C-23.
    VAR_000522
    Natural varianti345 – 3451E → K in Roma.
    VAR_000523
    Natural varianti357 – 3571E → K in Sondrio. 1 Publication
    VAR_000524
    Natural varianti378 – 3781E → K in Hiroshima-1. 2 Publications
    VAR_000525
    Natural varianti382 – 3821E → K in Coari I/Porto Alegre.
    VAR_000526
    Natural varianti383 – 3831K → N in Trieste.
    VAR_013016
    Natural varianti389 – 3891D → H in Parklands.
    VAR_000527
    Natural varianti389 – 3891D → V in Iowa city-1. 1 Publication
    VAR_000528
    Natural varianti396 – 3961K → E in Naskapi/Mersin/Komagome-1. 3 Publications
    VAR_000529
    Natural varianti399 – 3991D → N in Nagasaki-2. 1 Publication
    VAR_000530
    Natural varianti400 – 4001E → K in Tochigi. 1 Publication
    VAR_000531
    Natural varianti400 – 4001E → Q in Malmo-5. 1 Publication
    VAR_000532
    Natural varianti406 – 4061E → K in Hiroshima-2. 1 Publication
    VAR_000533
    Natural varianti420 – 4201E → K.1 Publication
    VAR_014294
    Natural varianti434 – 4341R → C in Liprizzi.
    VAR_013017
    Natural varianti490 – 4901K → E.
    Corresponds to variant rs1063469 [ dbSNP | Ensembl ].
    VAR_014295
    Natural varianti503 – 5031E → K in Dublin.
    VAR_000534
    Natural varianti518 – 5181D → N in Casebrook. 1 Publication
    VAR_000535
    Natural varianti525 – 5251E → K in Manaus-1/Adana/Lambadi/Vancouver. 1 Publication
    VAR_000536
    Natural varianti529 – 5291E → K in Ortonovo. 1 Publication
    VAR_000537
    Natural varianti557 – 5571V → M in Maddaloni.
    Corresponds to variant rs78284052 [ dbSNP | Ensembl ].
    VAR_013018
    Natural varianti560 – 5601K → E in Castel di Sangro.
    VAR_000538
    Natural varianti565 – 5651K → E in Maku. 1 Publication
    VAR_000539
    Natural varianti574 – 5741D → A in Malmo-61. 1 Publication
    VAR_000541
    Natural varianti574 – 5741D → G in Mexico. 1 Publication
    VAR_000540
    Natural varianti584 – 5841K → E in Church bay.
    VAR_013019
    Natural varianti587 – 5871D → N in Fukuoka-1/Paris-2. 2 Publications
    VAR_000542
    Natural varianti589 – 5891E → K in Osaka-1. 1 Publication
    VAR_000543
    Natural varianti594 – 5941E → K in Osaka-2/Phnom Phen/albumin B/Verona. 3 Publications
    VAR_000544
    Natural varianti596 – 60914GKKLV…AALGL → PTMRIRERK in Venezia.
    VAR_000547Add
    BLAST
    Natural varianti597 – 5971K → E in Gent/Milano Fast.
    VAR_000545
    Natural varianti598 – 5981K → N in Vanves.
    VAR_000546
    Natural varianti599 – 60911LVAASQAALGL → TCCCKSSCLRLITSHLKASQ PTMRIRERK in Kenitra.
    VAR_012981Add
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei43 – 234192Missing in isoform 2. 2 PublicationsVSP_021275Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS3555.1. [P02768-1]
    PIRiA93743. ABHUS.
    RefSeqiNP_000468.1. NM_000477.5. [P02768-1]
    UniGeneiHs.418167.
    Hs.592379.

    Genome annotation databases

    EnsembliENST00000295897; ENSP00000295897; ENSG00000163631. [P02768-1]
    ENST00000509063; ENSP00000422784; ENSG00000163631.
    GeneIDi213.
    KEGGihsa:213.
    UCSCiuc003hgs.4. human. [P02768-1]

    Polymorphism databases

    DMDMi113576.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Albumin Website
    Wikipedia

    Serum albumin entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS3555.1. [P02768-1 ]
    PIRi A93743. ABHUS.
    RefSeqi NP_000468.1. NM_000477.5. [P02768-1 ]
    UniGenei Hs.418167.
    Hs.592379.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AO6 X-ray 2.50 A/B 25-609 [» ]
    1BJ5 X-ray 2.50 A 25-609 [» ]
    1BKE X-ray 3.15 A 28-608 [» ]
    1BM0 X-ray 2.50 A/B 25-609 [» ]
    1E78 X-ray 2.60 A/B 25-609 [» ]
    1E7A X-ray 2.20 A/B 25-609 [» ]
    1E7B X-ray 2.38 A/B 25-609 [» ]
    1E7C X-ray 2.40 A 25-609 [» ]
    1E7E X-ray 2.50 A 25-609 [» ]
    1E7F X-ray 2.43 A 25-609 [» ]
    1E7G X-ray 2.50 A 25-609 [» ]
    1E7H X-ray 2.43 A 25-609 [» ]
    1E7I X-ray 2.70 A 25-609 [» ]
    1GNI X-ray 2.40 A 25-609 [» ]
    1GNJ X-ray 2.60 A 25-609 [» ]
    1H9Z X-ray 2.50 A 25-609 [» ]
    1HA2 X-ray 2.50 A 25-609 [» ]
    1HK1 X-ray 2.65 A 25-609 [» ]
    1HK2 X-ray 2.80 A 25-609 [» ]
    1HK3 X-ray 2.80 A 25-609 [» ]
    1HK4 X-ray 2.40 A 25-609 [» ]
    1HK5 X-ray 2.70 A 25-609 [» ]
    1N5U X-ray 1.90 A 25-609 [» ]
    1O9X X-ray 3.20 A 25-609 [» ]
    1TF0 X-ray 2.70 A 25-596 [» ]
    1UOR X-ray 2.80 A 25-609 [» ]
    1YSX NMR - A 409-609 [» ]
    2BX8 X-ray 2.70 A/B 25-609 [» ]
    2BXA X-ray 2.35 A/B 25-609 [» ]
    2BXB X-ray 3.20 A/B 25-609 [» ]
    2BXC X-ray 3.10 A/B 25-609 [» ]
    2BXD X-ray 3.05 A/B 25-609 [» ]
    2BXE X-ray 2.95 A/B 25-609 [» ]
    2BXF X-ray 2.95 A/B 25-609 [» ]
    2BXG X-ray 2.70 A/B 25-609 [» ]
    2BXH X-ray 2.25 A/B 25-609 [» ]
    2BXI X-ray 2.50 A 25-609 [» ]
    2BXK X-ray 2.40 A 25-609 [» ]
    2BXL X-ray 2.60 A 25-609 [» ]
    2BXM X-ray 2.50 A 25-609 [» ]
    2BXN X-ray 2.65 A 25-609 [» ]
    2BXO X-ray 2.60 A 25-609 [» ]
    2BXP X-ray 2.30 A 25-609 [» ]
    2BXQ X-ray 2.60 A 25-609 [» ]
    2ESG X-ray - C 25-609 [» ]
    2I2Z X-ray 2.70 A 25-609 [» ]
    2I30 X-ray 2.90 A 25-609 [» ]
    2VDB X-ray 2.52 A 30-608 [» ]
    2VUE X-ray 2.42 A/B 25-609 [» ]
    2VUF X-ray 3.05 A/B 25-609 [» ]
    2XSI X-ray 2.70 A 25-609 [» ]
    2XVQ X-ray 2.90 A/B 25-609 [» ]
    2XVU X-ray 2.60 A/B 25-609 [» ]
    2XVV X-ray 2.40 A 25-609 [» ]
    2XVW X-ray 2.65 A 25-609 [» ]
    2XW0 X-ray 2.40 A/B 25-609 [» ]
    2XW1 X-ray 2.50 A/B 25-609 [» ]
    2YDF X-ray 2.75 A/B 25-609 [» ]
    3A73 X-ray 2.19 A/B 25-609 [» ]
    3B9L X-ray 2.60 A 25-609 [» ]
    3B9M X-ray 2.70 A 25-609 [» ]
    3CX9 X-ray 2.80 A 27-608 [» ]
    3JQZ X-ray 3.30 A/B 25-609 [» ]
    3JRY X-ray 2.30 A/B 25-609 [» ]
    3LU6 X-ray 2.70 A/B 25-609 [» ]
    3LU7 X-ray 2.80 A/B 25-609 [» ]
    3LU8 X-ray 2.60 A/B 25-609 [» ]
    3SQJ X-ray 2.05 A/B 27-608 [» ]
    3TDL X-ray 2.60 A 25-609 [» ]
    3UIV X-ray 2.20 A/H 25-609 [» ]
    4BKE X-ray 2.35 A 1-609 [» ]
    4E99 X-ray 2.30 A 25-609 [» ]
    4EMX X-ray 2.30 A/B 25-609 [» ]
    4G03 X-ray 2.22 A/B 25-609 [» ]
    4G04 X-ray 2.30 A/B 25-609 [» ]
    4HGK X-ray 3.04 A/B 25-609 [» ]
    4HGM X-ray 2.34 B 25-609 [» ]
    4IW1 X-ray 2.56 A 25-609 [» ]
    4IW2 X-ray 2.41 A 25-609 [» ]
    4K2C X-ray 3.23 A/B 25-609 [» ]
    4K71 X-ray 2.40 A/D 25-609 [» ]
    4L8U X-ray 2.01 A 25-609 [» ]
    4L9K X-ray 2.40 A/B 25-609 [» ]
    4L9Q X-ray 2.70 A/B 25-609 [» ]
    4LA0 X-ray 2.40 A/B 25-609 [» ]
    4LB2 X-ray 2.80 A/B 25-609 [» ]
    4LB9 X-ray 2.70 A 25-609 [» ]
    4N0F X-ray 3.02 D/G/J/M 25-609 [» ]
    4N0U X-ray 3.80 D 27-609 [» ]
    DisProti DP00515.
    ProteinModelPortali P02768.
    SMRi P02768. Positions 26-608.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106715. 156 interactions.
    DIPi DIP-29902N.
    IntActi P02768. 159 interactions.
    MINTi MINT-3004222.

    Chemistry

    BindingDBi P02768.
    ChEMBLi CHEMBL3253.
    DrugBanki DB05812. Abiraterone.
    DB01418. Acenocoumarol.
    DB01614. Acepromazine.
    DB00945. Acetylsalicylic acid.
    DB00459. Acitretin.
    DB00802. Alfentanil.
    DB00321. Amitriptyline.
    DB00415. Ampicillin.
    DB00995. Auranofin.
    DB07402. Azapropazone.
    DB01294. Bismuth Subsalicylate.
    DB08907. Canagliflozin.
    DB01197. Captopril.
    DB00456. Cefalotin.
    DB01327. Cefazolin.
    DB00274. Cefmetazole.
    DB01328. Cefonicid.
    DB01329. Cefoperazone.
    DB01330. Cefotetan.
    DB00430. Cefpiramide.
    DB01212. Ceftriaxone.
    DB00482. Celecoxib.
    DB00567. Cephalexin.
    DB00477. Chlorpromazine.
    DB01242. Clomipramine.
    DB01068. Clonazepam.
    DB01147. Cloxacillin.
    DB01189. Desflurane.
    DB00829. Diazepam.
    DB00586. Diclofenac.
    DB00861. Diflunisal.
    DB01396. Digitoxin.
    DB04855. Dronedarone.
    DB00228. Enflurane.
    DB08899. Enzalutamide.
    DB00530. Erlotinib.
    DB00783. Estradiol.
    DB00655. Estrone.
    DB04574. Estropipate.
    DB00903. Ethacrynic acid.
    DB00749. Etodolac.
    DB00573. Fenoprofen.
    DB00544. Fluorouracil.
    DB00472. Fluoxetine.
    DB00712. Flurbiprofen.
    DB01320. Fosphenytoin.
    DB06716. Fospropofol.
    DB00695. Furosemide.
    DB00743. Gadobenate Dimeglumine.
    DB06705. Gadofosveset trisodium.
    DB01044. Gatifloxacin.
    DB00317. Gefitinib.
    DB01120. Gliclazide.
    DB01016. Glyburide.
    DB01159. Halothane.
    DB00070. Hyaluronidase.
    DB01050. Ibuprofen.
    DB00619. Imatinib.
    DB00328. Indomethacin.
    DB01307. Insulin Detemir.
    DB04711. Iodipamide.
    DB00762. Irinotecan.
    DB00753. Isoflurane.
    DB08820. Ivacaftor.
    DB01587. Ketazolam.
    DB01009. Ketoprofen.
    DB00451. Levothyroxine.
    DB00279. Liothyronine.
    DB01583. Liotrix.
    DB00678. Losartan.
    DB08932. MACITENTAN.
    DB01397. Magnesium salicylate.
    DB00931. Methacycline.
    DB00563. Methotrexate.
    DB06710. Methyltestosterone.
    DB08893. Mirabegron.
    DB00688. Mycophenolate mofetil.
    DB01183. Naloxone.
    DB00788. Naproxen.
    DB00731. Nateglinide.
    DB00717. Norethindrone.
    DB00540. Nortriptyline.
    DB00334. Olanzapine.
    DB00776. Oxcarbazepine.
    DB00454. Pethidine.
    DB00946. Phenprocoumon.
    DB00252. Phenytoin.
    DB01621. Pipotiazine.
    DB00554. Piroxicam.
    DB08860. Pitavastatin.
    DB06209. Prasugrel.
    DB00635. Prednisone.
    DB01032. Probenecid.
    DB00818. Propofol.
    DB00912. Repaglinide.
    DB00412. Rosiglitazone.
    DB01098. Rosuvastatin.
    DB06201. Rufinamide.
    DB00936. Salicylic acid.
    DB01232. Saquinavir.
    DB01236. Sevoflurane.
    DB06290. SIMEPREVIR.
    DB00815. Sodium lauryl sulfate.
    DB00364. Sucralfate.
    DB01581. Sulfamerazine.
    DB01582. Sulfamethazine.
    DB00576. Sulfamethizole.
    DB01015. Sulfamethoxazole.
    DB00605. Sulindac.
    DB00864. Tacrolimus.
    DB05521. Telaprevir.
    DB00624. Testosterone.
    DB00759. Tetracycline.
    DB01622. Thioproperazine.
    DB01623. Thiothixene.
    DB01056. Tocainide.
    DB08895. Tofacitinib.
    DB00177. Valsartan.
    DB05294. Vandetanib.
    DB08881. Vemurafenib.
    DB08828. Vismodegib.
    DB00682. Warfarin.
    DB00137. Xanthophyll.
    DB00495. Zidovudine.

    Protein family/group databases

    Allergomei 763. Hom s HSA.

    PTM databases

    PhosphoSitei P02768.
    UniCarbKBi P02768.

    Polymorphism databases

    DMDMi 113576.

    2D gel databases

    DOSAC-COBS-2DPAGE P02768.
    OGPi P02768.
    REPRODUCTION-2DPAGE IPI00384697.
    IPI00745872.
    P02768.
    SWISS-2DPAGE P02768.
    UCD-2DPAGE P02768.

    Proteomic databases

    MaxQBi P02768.
    PaxDbi P02768.
    PRIDEi P02768.

    Protocols and materials databases

    DNASUi 213.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295897 ; ENSP00000295897 ; ENSG00000163631 . [P02768-1 ]
    ENST00000509063 ; ENSP00000422784 ; ENSG00000163631 .
    GeneIDi 213.
    KEGGi hsa:213.
    UCSCi uc003hgs.4. human. [P02768-1 ]

    Organism-specific databases

    CTDi 213.
    GeneCardsi GC04P074259.
    HGNCi HGNC:399. ALB.
    HPAi CAB006262.
    MIMi 103600. gene+phenotype.
    neXtProti NX_P02768.
    Orphaneti 86816. Congenital analbuminemia.
    276271. Familial dysalbuminemic hyperthyroxinemia.
    PharmGKBi PA24690.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45992.
    HOVERGENi HBG004207.
    KOi K16141.
    OMAi NCDKSLH.
    OrthoDBi EOG7S4X5C.
    PhylomeDBi P02768.
    TreeFami TF335561.

    Enzyme and pathway databases

    Reactomei REACT_11042. Recycling of bile acids and salts.
    REACT_13621. HDL-mediated lipid transport.
    REACT_160163. Scavenging of heme from plasma.
    REACT_23988. Transport of organic anions.

    Miscellaneous databases

    ChiTaRSi ALB. human.
    EvolutionaryTracei P02768.
    GeneWikii Serum_albumin.
    GenomeRNAii 213.
    NextBioi 862.
    PMAP-CutDB P02768.
    PROi P02768.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02768.
    Bgeei P02768.
    Genevestigatori P02768.

    Family and domain databases

    InterProi IPR000264. ALB/AFP/VDB.
    IPR020858. Serum_albumin-like.
    IPR021177. Serum_albumin/AFP.
    IPR020857. Serum_albumin_CS.
    IPR014760. Serum_albumin_N.
    [Graphical view ]
    Pfami PF00273. Serum_albumin. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF002520. Serum_albumin_subgroup. 1 hit.
    PRINTSi PR00802. SERUMALBUMIN.
    SMARTi SM00103. ALBUMIN. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48552. SSF48552. 3 hits.
    PROSITEi PS00212. ALBUMIN_1. 3 hits.
    PS51438. ALBUMIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiALBU_HUMAN
    AccessioniPrimary (citable) accession number: P02768
    Secondary accession number(s): O95574
    , P04277, Q13140, Q645G4, Q68DN5, Q6UXK4, Q86YG0, Q9P157, Q9P1I7, Q9UHS3, Q9UJZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 210 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Caution

    A peptide arising from positions 166 to 174 was originally (PubMed:3087352 and PubMed:2437111) termed neurotensin-related peptide (NRP) or kinetensin and was thought to regulate fat digestion, lipid absorption, and blood flow.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3