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P02768

- ALBU_HUMAN

UniProt

P02768 - ALBU_HUMAN

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Protein

Serum albumin

Gene

ALB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca2+, Na+, K+, fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.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. pyridoxal phosphate binding Source: UniProtKB
  8. toxic substance binding Source: UniProtKB
  9. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP02768.
ExpressionAtlasiP02768. baseline and differential.
GenevestigatoriP02768.

Organism-specific databases

HPAiCAB006262.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106715. 160 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.
GeneTreeiENSGT00390000000113.
HOVERGENiHBG004207.
InParanoidiP02768.
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) [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

        10         20         30         40         50
MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA
60 70 80 90 100
FAQYLQQCPF EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT
110 120 130 140 150
VATLRETYGE MADCCAKQEP ERNECFLQHK DDNPNLPRLV RPEVDVMCTA
160 170 180 190 200
FHDNEETFLK KYLYEIARRH PYFYAPELLF FAKRYKAAFT ECCQAADKAA
210 220 230 240 250
CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV ARLSQRFPKA
260 270 280 290 300
EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK
310 320 330 340 350
ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF
360 370 380 390 400
LGMFLYEYAR RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE
410 420 430 440 450
FKPLVEEPQN LIKQNCELFE QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV
460 470 480 490 500
SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV LNQLCVLHEK TPVSDRVTKC
510 520 530 540 550
CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL SEKERQIKKQ
560 570 580 590 600
TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV

AASQAALGL
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. 160 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.
GeneTreei ENSGT00390000000113.
HOVERGENi HBG004207.
InParanoidi P02768.
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

Bgeei P02768.
ExpressionAtlasi P02768. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 211 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