P02768 (ALBU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serum albumin

Gene names

Name:	ALB
ORF Names:	GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca2+, Na+, K+, fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. Ref.33
Subcellular location	Secreted.
Tissue specificity	Plasma. Ref.35
Post-translational modification	Kenitra variant is partially O-glycosylated at Thr-620. It has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606. Glycated in diabetic patients. Phosphorylation sites are present in the extracelllular medium. Acetylated on Lys-223 by acetylsalicylic acid.
Polymorphism	A variant structure of albumin could lead to increased binding of zinc resulting in an asymptomatic augmentation of zinc concentration in the blood. The sequence shown is that of variant albumin A.
Involvement in disease	Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T4. It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population. Ref.64 Ref.65 Ref.66 Ref.67
Sequence similarities	Belongs to the ALB/AFP/VDB family. Contains 3 albumin domains.
Caution	A peptide arising from positions 166 to 174 was originally (Ref.23 and Ref.24) termed neurotensin-related peptide (NRP) or kinetensin and was thought to regulates fat digestion, lipid absorption, and blood flow.
Sequence caution	The sequence AAF22034.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAF69644.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAG35503.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat Signal
Ligand	Copper Lipid-binding Metal-binding Zinc
PTM	Cleavage on pair of basic residues Disulfide bond Glycation Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	bile acid and bile salt transport Traceable author statement. Source: Reactome bile acid metabolic process Traceable author statement. Source: Reactome cellular response to starvation Inferred from direct assay. Source: UniProtKB hemolysis by symbiont of host erythrocytes Inferred from direct assay. Source: UniProtKB lipoprotein metabolic process Traceable author statement. Source: Reactome maintenance of mitochondrion location Inferred from direct assay. Source: UniProtKB negative regulation of apoptotic process Inferred from direct assay. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome sodium-independent organic anion transport Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome
Cellular component	extracellular space Inferred from direct assay. Source: BHF-UCL platelet alpha granule lumen Traceable author statement. Source: Reactome protein complex Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from direct assay. Source: UniProtKB antioxidant activity Non-traceable author statement. Source: UniProtKB chaperone binding Inferred from physical interaction. Source: BHF-UCL copper ion binding Non-traceable author statement. Source: UniProtKB drug binding Inferred from direct assay. Source: UniProtKB fatty acid binding Inferred from direct assay. Source: UniProtKB pyridoxal phosphate binding Inferred from direct assay. Source: UniProtKB toxin binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P02768-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P02768-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Propeptide

19 – 22

4

PRO_0000001067

Chain

25 – 609

585

Serum albumin

PRO_0000001068

Regions

Domain

19 – 210

192

Albumin 1

Domain

211 – 403

193

Albumin 2

Domain

404 – 601

198

Albumin 3

Sites

Metal binding

27

1

Copper By similarity

Metal binding

91

1

Zinc

Metal binding

123

1

Zinc

Metal binding

271

1

Zinc

Metal binding

273

1

Zinc

Binding site

264

1

Bilirubin

Site

28

1

Not glycated

Site

44

1

Not glycated

Site

65

1

Not glycated

Site

88

1

Not glycated

Site

97

1

Not glycated

Site

117

1

Not glycated

Site

130

1

Not glycated

Site

160

1

Not glycated

Site

183

1

Not glycated

Site

198

1

Not glycated

Site

205

1

Not glycated

Site

214

1

Not glycated

Site

219

1

Not glycated

Site

223

1

Aspirin-acetylated lysine

Site

229

1

Not glycated

Site

236

1

Not glycated

Site

264

1

Not glycated

Site

286

1

Not glycated

Site

298

1

Not glycated

Site

310

1

Not glycated

Site

383

1

Not glycated

Site

396

1

Not glycated

Site

413

1

Not glycated

Site

426

1

Not glycated

Site

438

1

Not glycated

Site

456

1

Not glycated

Site

460

1

Not glycated

Site

490

1

Not glycated

Site

499

1

Not glycated

Site

524

1

Not glycated

Site

543

1

Not glycated

Site

548

1

Not glycated

Site

562

1

Not glycated

Site

565

1

Not glycated

Site

581

1

Not glycated

Site

584

1

Not glycated

Site

588

1

Not glycated

Site

598

1

Not glycated

Amino acid modifications

Modified residue

82

1

Phosphoserine Ref.34

Modified residue

108

1

Phosphotyrosine Ref.32

Modified residue

164

1

Phosphotyrosine Ref.32 Ref.36

Modified residue

294

1

Phosphoserine Ref.35

Modified residue

297

1

Phosphoserine Ref.35

Modified residue

443

1

Phosphoserine Ref.37

Modified residue

444

1

Phosphothreonine Ref.37

Modified residue

446

1

Phosphothreonine Ref.37

Glycosylation

36

1

N-linked (Glc) (glycation) Probable

Glycosylation

75

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

161

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

186

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

223

1

N-linked (Glc) (glycation); in vitro Ref.29 Ref.31

Glycosylation

249

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

257

1

N-linked (Glc) (glycation) Probable

Glycosylation

300

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

305

1

N-linked (Glc) (glycation) Ref.31

Glycosylation

337

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

341

1

N-linked (Glc) (glycation) Probable

Glycosylation

342

1

N-linked (GlcNAc...); in variant Redhill

CAR_000226

Glycosylation

347

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

375

1

N-linked (Glc) (glycation) Probable

Glycosylation

402

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

437

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

463

1

N-linked (Glc) (glycation) Ref.31

Glycosylation

468

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

518

1

N-linked (GlcNAc...); in variant Casebrook

CAR_000069

Glycosylation

549

1

N-linked (Glc) (glycation) Ref.26 Ref.29 Ref.30 Ref.31

Glycosylation

558

1

N-linked (Glc) (glycation) Probable

Glycosylation

560

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

569

1

N-linked (Glc) (glycation); in vitro Ref.26

Glycosylation

597

1

N-linked (Glc) (glycation); in vitro Ref.26

Disulfide bond

77 ↔ 86

Ref.27

Disulfide bond

99 ↔ 115

Ref.27

Disulfide bond

114 ↔ 125

Ref.27

Disulfide bond

148 ↔ 193

Ref.27

Disulfide bond

192 ↔ 201

Ref.27

Disulfide bond

224 ↔ 270

Ref.27

Disulfide bond

269 ↔ 277

Ref.27

Disulfide bond

289 ↔ 303

Ref.27

Disulfide bond

302 ↔ 313

Ref.27

Disulfide bond

340 ↔ 385

Ref.27

Disulfide bond

384 ↔ 393

Ref.27

Disulfide bond

416 ↔ 462

Ref.27

Disulfide bond

461 ↔ 472

Ref.27

Disulfide bond

485 ↔ 501

Ref.27

Disulfide bond

500 ↔ 511

Ref.27

Disulfide bond

538 ↔ 583

Ref.27

Disulfide bond

582 ↔ 591

Ref.27

Natural variations

Alternative sequence

43 – 234

192

Missing in isoform 2.

VSP_021275

Natural variant

23

1

R → C in Redhill/Malmo-I/Tradate; associated with T-344 in Redhill. Ref.59

VAR_000499

Natural variant

23

1

R → H in Fukuoka-2/Lille/Taipei/Varese/Komagome-3. Ref.50 Ref.54 Ref.56

VAR_000500

Natural variant

24

1

R → L in Jaffna.

VAR_000501

Natural variant

24

1

R → P in Takefu/Honolulu-1. Ref.52

VAR_000502

Natural variant

24

1

R → Q in Christchurch/Honolulu-2. Ref.50 Ref.51 Ref.52

VAR_000503

Natural variant

25

1

D → V in Bleinheim/Iowa city-2. Ref.56

VAR_000504

Natural variant

27

1

H → Q in Nagasaki-3. Ref.49

VAR_000505

Natural variant

27

1

H → Y in Larino. Ref.11 Ref.63

VAR_000506

Natural variant

73

1

F → Y Ref.68

VAR_010657

Natural variant

84

1

E → K in Torino. Ref.54

VAR_000507

Natural variant

87

1

D → N in Malmo-95/Dalakarlia. Ref.59

VAR_000508

Natural variant

90

1

L → P in FDH. Ref.67

VAR_013011

Natural variant

106

1

E → K in Vibo Valentia. Ref.54

VAR_000509

Natural variant

121

1

E → G Ref.2

VAR_014290

Natural variant

138

1

R → G in Yanomama-2.

VAR_000510

Natural variant

143

1

E → K in Nagoya. Ref.52

VAR_000511

Natural variant

146

1

V → E in Tregasio.

VAR_013012

Natural variant

152

1

H → R in Komagome-2. Ref.56

VAR_000512

Natural variant

201

1

C → F in Hawkes bay. Ref.61

VAR_000513

Natural variant

215

1

A → T. [dbSNP:rs3210154]

VAR_014291

Natural variant

215

1

A → V. [dbSNP:rs3204504]

VAR_014292

Natural variant

220

1

Q → L. [dbSNP:rs3210163]

VAR_014293

Natural variant

242

1

R → H in FDH. Ref.64 Ref.65 Ref.66

VAR_000514

Natural variant

242

1

R → P in FDH.

VAR_013013

Natural variant

249

1

K → Q in Tradate-2. Ref.63

VAR_000515

Natural variant

264

1

K → E in Herborn. Ref.60

VAR_000516

Natural variant

292

1

Q → R in Malmo-10. Ref.59

VAR_000517

Natural variant

293

1

D → G in Nagasaki-1. Ref.51

VAR_000518

Natural variant

300

1

K → N in Caserta. Ref.63

VAR_000519

Natural variant

337

1

K → N in Canterbury/New Guinea/Tagliacozzo/Cuneo/Cooperstown. Ref.47 Ref.50 Ref.52

VAR_000520

Natural variant

338

1

D → G in Bergamo.

VAR_013014

Natural variant

338

1

D → V in Brest.

VAR_013015

Natural variant

342

1

N → K in Malmo-47. Ref.59

VAR_000521

Natural variant

344

1

A → T in Redhill; associated with C-23.

VAR_000522

Natural variant

345

1

E → K in Roma.

VAR_000523

Natural variant

357

1

E → K in Sondrio. Ref.58

VAR_000524

Natural variant

378

1

E → K in Hiroshima-1. Ref.5 Ref.51

VAR_000525

Natural variant

382

1

E → K in Coari I/Porto Alegre.

VAR_000526

Natural variant

383

1

K → N in Trieste.

VAR_013016

Natural variant

389

1

D → H in Parklands.

VAR_000527

Natural variant

389

1

D → V in Iowa city-1. Ref.56

VAR_000528

Natural variant

396

1

K → E in Naskapi/Mersin/Komagome-1. Ref.48 Ref.49 Ref.56

VAR_000529

Natural variant

399

1

D → N in Nagasaki-2. Ref.49

VAR_000530

Natural variant

400

1

E → K in Tochigi. Ref.51

VAR_000531

Natural variant

400

1

E → Q in Malmo-5. Ref.59

VAR_000532

Natural variant

406

1

E → K in Hiroshima-2. Ref.51

VAR_000533

Natural variant

420

1

E → K Ref.1

VAR_014294

Natural variant

434

1

R → C in Liprizzi.

VAR_013017

Natural variant

490

1

K → E. [dbSNP:rs1063469]

VAR_014295

Natural variant

503

1

E → K in Dublin.

VAR_000534

Natural variant

518

1

D → N in Casebrook. Ref.57

VAR_000535

Natural variant

525

1

E → K in Manaus-1/Adana/Lambadi/Vancouver. Ref.52

VAR_000536

Natural variant

529

1

E → K in Ortonovo. Ref.62

VAR_000537

Natural variant

557

1

V → M in Maddaloni.

VAR_013018

Natural variant

560

1

K → E in Castel di Sangro.

VAR_000538

Natural variant

565

1

K → E in Maku. Ref.49

VAR_000539

Natural variant

574

1

D → A in Malmo-61. Ref.59

VAR_000541

Natural variant

574

1

D → G in Mexico. Ref.48

VAR_000540

Natural variant

584

1

K → E in Church bay.

VAR_013019

Natural variant

587

1

D → N in Fukuoka-1/Paris-2. Ref.52 Ref.58

VAR_000542

Natural variant

589

1

E → K in Osaka-1. Ref.52

VAR_000543

Natural variant

594

1

E → K in Osaka-2/Phnom Phen/albumin B/Verona. Ref.50 Ref.51 Ref.52

VAR_000544

Natural variant

596 – 609

14

GKKLV…AALGL → PTMRIRERK in Venezia.

VAR_000547

Natural variant

597

1

K → E in Gent/Milano Fast.

VAR_000545

Natural variant

598

1

K → N in Vanves.

VAR_000546

Natural variant

599 – 609

11

LVAASQAALGL → TCCCKSSCLRLITSHLKASQ PTMRIRERK in Kenitra.

VAR_012981

Experimental info

Sequence conflict

55

1

L → P in CAH18185. Ref.11

Sequence conflict

122

1

R → S in AAF01333. Ref.4

Sequence conflict

155

1

E → Q AA sequence Ref.18

Sequence conflict

174

1

Y → L AA sequence Ref.23

Sequence conflict

174

1

Y → L AA sequence Ref.24

Sequence conflict

194

1

Q → E AA sequence Ref.18

Sequence conflict

327 – 332

6

PSLAAD → MFVLLC in AAF71067. Ref.10

Sequence conflict

405

1

V → A in AAF71067. Ref.10

Sequence conflict

409

1

Q → E in AAH14308. Ref.14

Sequence conflict

441

1

Q → E in CAA23753. Ref.2

Sequence conflict

466

1

E → G in AAF01333. Ref.4

Sequence conflict

488 – 489

2

HE → EH AA sequence Ref.18

Sequence conflict

490

1

K → R in CAH18185. Ref.11

Sequence conflict

525

1

E → Q AA sequence Ref.18

Sequence conflict

551

1

T → A in CAH18185. Ref.11

Sequence conflict

560

1

K → R in CAH18185. Ref.11

Sequence conflict

604

1

Q → R in AAN17825. Ref.5

Secondary structure

1

.

.

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609

Helix Strand Turn

Details...

Helix

31 – 54

24

Helix

60 – 79

20

Beta strand

83 – 85

3

Helix

90 – 102

13

Helix

105 – 108

4

Helix

111 – 115

5

Turn

119 – 123

5

Helix

124 – 128

5

Helix

144 – 153

10

Helix

155 – 167

13

Helix

175 – 192

18

Beta strand

195 – 197

3

Helix

198 – 230

33

Helix

232 – 246

15

Helix

252 – 271

20

Helix

274 – 290

17

Helix

292 – 295

4

Helix

300 – 303

4

Helix

307 – 314

8

Helix

330 – 333

4

Helix

339 – 345

7

Helix

347 – 360

14

Helix

367 – 385

19

Helix

390 – 393

4

Helix

394 – 397

4

Helix

398 – 438

41

Helix

444 – 461

18

Helix

466 – 490

25

Helix

495 – 503

9

Helix

508 – 514

7

Helix

528 – 530

3

Helix

535 – 539

5

Helix

542 – 559

18

Beta strand

561 – 563

3

Helix

567 – 584

18

Helix

591 – 605

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 1, 1990. Version 2. Checksum: F88FF61DD242E818	FASTA	609	69,367
	10 20 30 40 50 60 MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF 70 80 90 100 110 120 EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP 130 140 150 160 170 180 ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF 190 200 210 220 230 240 FAKRYKAAFT ECCQAADKAA CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV 250 260 270 280 290 300 ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK 310 320 330 340 350 360 ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF LGMFLYEYAR 370 380 390 400 410 420 RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE 430 440 450 460 470 480 QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV 490 500 510 520 530 540 LNQLCVLHEK TPVSDRVTKC CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL 550 560 570 580 590 600 SEKERQIKKQ TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV AASQAALGL
	Isoform 2 [UniParc]. Checksum: 16E764833EEF4E8D	FASTA	417	47,360
	10 20 30 40 50 60 MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKAWAVAR LSQRFPKAEF 70 80 90 100 110 120 AEVSKLVTDL TKVHTECCHG DLLECADDRA DLAKYICENQ DSISSKLKEC CEKPLLEKSH 130 140 150 160 170 180 CIAEVENDEM PADLPSLAAD FVESKDVCKN YAEAKDVFLG MFLYEYARRH PDYSVVLLLR 190 200 210 220 230 240 LAKTYETTLE KCCAAADPHE CYAKVFDEFK PLVEEPQNLI KQNCELFEQL GEYKFQNALL 250 260 270 280 290 300 VRYTKKVPQV STPTLVEVSR NLGKVGSKCC KHPEAKRMPC AEDYLSVVLN QLCVLHEKTP 310 320 330 340 350 360 VSDRVTKCCT ESLVNRRPCF SALEVDETYV PKEFNAETFT FHADICTLSE KERQIKKQTA 370 380 390 400 410 LVELVKHKPK ATKEQLKAVM DDFAAFVEKC CKADDKETCF AEEGKKLVAA SQAALGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of human serum albumin cDNA and its expression in E. coli." Lawn R.M., Adelman J., Bock S.C., Franke A.E., Houck C.M., Najarian R.C., Seeburg P.H., Wion K.L. Nucleic Acids Res. 9:6103-6114(1981) [PubMed: 6171778] [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: 6275391] [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: 3009475] [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: 11483580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Fetal liver.
[11]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TYR-27. Tissue: Liver.
[12]	SeattleSNPs variation discovery resource Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[13]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Liver and Skeletal muscle.
[15]	Menaya J., Parrilla R., Ayuso M.S. Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-455. Tissue: Liver.
[16]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167.
[17]	"The human albumin gene. Characterization of the 5' and 3' flanking regions and the polymorphic gene transcripts." Urano Y., Watanabe K., Sakai M., Tamaoki T. J. Biol. Chem. 261:3244-3251(1986) [PubMed: 2419329] [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: 1225573] [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: 7895732] [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: 12665801] [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, 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: 3087352] [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: 2437111] [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: 955075] [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: 15047055] [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, 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: 656055] [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: 6853480] [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: 6706980] [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: 3759977] [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]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108 AND TYR-164, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[33]	"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: 19021548] [Abstract] Cited for: FUNCTION, ZINC-BINDING SITES.
[34]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, MASS SPECTROMETRY. Tissue: Liver.
[35]	"An initial characterization of the serum phosphoproteome." Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A., Liotta L.A., Petricoin E.F. III J. Proteome Res. 8:5523-5531(2009) [PubMed: 19824718] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-297, TISSUE SPECIFICITY, MASS SPECTROMETRY. Tissue: Serum.
[36]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-164, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[37]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; THR-444 AND THR-446, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[38]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]	"Three-dimensional structure of human serum albumin." Carter D.C., He X.-M., Munson S.H., Twigg P.D., Gernert K.M., Broom M.B., Miller T.Y. Science 244:1195-1198(1989) [PubMed: 2727704] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
[40]	"Structure of human serum albumin." Carter D.C., He X.-M. Science 249:302-303(1990) [PubMed: 2374930] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS).
[41]	"Atomic structure and chemistry of human serum albumin." He X.-M., Carter D.C. Nature 358:209-215(1992) [PubMed: 1630489] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[42]	Erratum He X.-M., Carter D.C. Nature 364:362-362(1993)
[43]	"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: 9731778] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[44]	"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: 10388840] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[45]	"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: 10940303] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-609.
[46]	"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: 11743713] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[47]	"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: 3828358] [Abstract] Cited for: VARIANT CANTERBURY ASN-337.
[48]	"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: 3474609] [Abstract] Cited for: VARIANTS NASKAPI/MERSIN GLU-396 AND MEXICO GLY-574.
[49]	"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: 3479777] [Abstract] Cited for: VARIANTS NAGASAKI-3 GLN-27 YANOMAMA-2 GLU-396; NAGASAKI-2 ASN-399 AND MAKU GLU-565.
[50]	"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: 2911589] [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.
[51]	"Point substitutions in Japanese alloalbumins." Arai K., Madison J., Huss K., Ishioka N., Satoh C., Fujita M., Neel J.V., Sakurabayashi I., Putnam F.W. Proc. Natl. Acad. Sci. U.S.A. 86:6092-6096(1989) [PubMed: 2762316] [Abstract] Cited for: VARIANTS HONOLULU-2 GLN-24; NAGASAKI-1 GLY-293; HIROSHIMA-1 LYS-378; TOCHIGI LYS-400; HIROSHIMA-2 LYS-406 AND OSAKA-2 LYS-594.
[52]	"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: 2404284] [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.
[53]	"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: 2104980] [Abstract] Cited for: CHARACTERIZATION OF VARIANT REDHILL.
[54]	"Mutations in genetic variants of human serum albumin found in Italy." Galliano M., Minchiotti L., Porta F., Rossi A., Ferri G., Madison J., Watkins S., Putnam F.W. Proc. Natl. Acad. Sci. U.S.A. 87:8721-8725(1990) [PubMed: 2247440] [Abstract] Cited for: VARIANTS VARESE HIS-23; TORINO LYS-84 AND VIBO VALENTIA LYS-106.
[55]	"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: 2068071] [Abstract] Cited for: CHARACTERIZATION OF VARIANT VENEZIA.
[56]	"Genetic variants of serum albumin in Americans and Japanese." Madison J., Arai K., Feld R.D., Kyle R.A., Watkins S., Davis E., Matsuda Y., Amaki I., Putnam F.W. Proc. Natl. Acad. Sci. U.S.A. 88:9853-9857(1991) [PubMed: 1946412] [Abstract] Cited for: VARIANTS KOMAGOME-3 HIS-23; IOWA CITY-2 VAL-25; KOMAGOME-2 ARG-152; IOWA CITY-1 VAL-389 AND KOMAGOME-1 GLU-396.
[57]	"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: 1859851] [Abstract] Cited for: VARIANT CASEBROOK ASN-518.
[58]	"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: 1347703] [Abstract] Cited for: VARIANTS SONDRIO LYS-357 AND PARIS-2 ASN-587.
[59]	"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: 1518850] [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.
[60]	"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: 8513793] [Abstract] Cited for: VARIANT HERBORN GLU-264.
[61]	"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: 8347685] [Abstract] Cited for: VARIANT HAWKES BAY PHE-201.
[62]	"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: 7902134] [Abstract] Cited for: VARIANT ORTONOVO LYS-529.
[63]	"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: 8022807] [Abstract] Cited for: VARIANTS LARINO TYR-27; TRADATE-2 GLN-249 AND CASERTA ASN-300.
[64]	"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: 8048949] [Abstract] Cited for: VARIANT FDH HIS-242.
[65]	"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: 7852505] [Abstract] Cited for: VARIANT FDH HIS-242, PROTEIN SEQUENCE OF 25-51.
[66]	"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: 9329347] [Abstract] Cited for: VARIANT FDH HIS-242.
[67]	"Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect." Sunthornthepvarakul T., Likitmaskul S., Ngowngarmratana S., Angsusingha K., Kitvitayasak S., Scherberg N.H., Refetoff S. J. Clin. Endocrinol. Metab. 83:1448-1454(1998) [PubMed: 9589637] [Abstract] Cited for: VARIANT FDH PRO-90.
[68]	"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: 11680902] [Abstract] Cited for: VARIANT TYR-73, MASS SPECTROMETRY. Tissue: Urine.
[69]	"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: 11168369] [Abstract] Cited for: CHARACTERIZATION OF VARIANT KENITRA.
+	Additional computationally mapped references.

Web resources

Albumin Website

Wikipedia

Serum albumin entry

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00494 mRNA. Translation: CAA23753.1.
V00495 mRNA. Translation: CAA23754.1.
M12523 Genomic DNA. Translation: AAA98797.1.
M12523 Genomic DNA. Translation: AAA98798.1.
AF190168 mRNA. Translation: AAF01333.1.
AF542069 mRNA. Translation: AAN17825.1.
A06977 mRNA. Translation: CAA00606.1.
AY728024 mRNA. Translation: AAU21642.1.
DQ986150 mRNA. Translation: ABJ16448.1.
AY544124 mRNA. Translation: AAT11155.1.
AY550967 mRNA. Translation: AAT52213.1.
AF116645 mRNA. Translation: AAF71067.1.
AF118090 mRNA. Translation: AAF22034.1. Different initiation.
AF119840 mRNA. Translation: AAF69594.1.
AF119890 mRNA. Translation: AAF69644.1. Different initiation.
AF130077 mRNA. Translation: AAG35503.1. Different initiation.
CR749331 mRNA. Translation: CAH18185.1.
EF649953 Genomic DNA. Translation: ABS29264.1.
CH471057 Genomic DNA. Translation: EAX05676.1.
BC014308 mRNA. Translation: AAH14308.1.
BC034023 mRNA. Translation: AAH34023.1.
BC036003 mRNA. Translation: AAH36003.1.
BC041789 mRNA. Translation: AAH41789.1.
U22961 mRNA. Translation: AAA64922.1.
AY358313 mRNA. Translation: AAQ89947.1.
M13075 Genomic DNA. Translation: AAA51688.1.

IPI

IPI00384697.
IPI00745872.

PIR

ABHUS. A93743.

RefSeq

NP_000468.1. NM_000477.5.

UniGene

Hs.418167.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P02768.

SMR

P02768. Positions 26-608.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29902N.

IntAct

P02768. 150 interactions.

MINT

MINT-3004222.

STRING

P02768.

Protein family/group databases

Allergome

763. Hom s HSA.

PTM databases

GlycoSuiteDB

P02768.

PhosphoSite

P02768.

Polymorphism databases

DMDM

113576.

2D gel databases

SWISS-2DPAGE

P02768.

Cornea-2DPAGE

P02768.

DOSAC-COBS-2DPAGE

P02768.

OGP

P02768.

REPRODUCTION-2DPAGE

IPI00384697.
IPI00745872.
P02768.

Siena-2DPAGE

P02768.

UCD-2DPAGE

P02768.

Proteomic databases

PRIDE

P02768.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295897; ENSP00000295897; ENSG00000163631.

GeneID

213.

KEGG

hsa:213.

UCSC

uc003hgs.2. human.
uc003hgu.2. human.

Organism-specific databases

CTD

213.

GeneCards

GC04P074259.

H-InvDB

HIX0004278.

HGNC

HGNC:399. ALB.

HPA

CAB006262.

MIM

103600. gene+phenotype.

neXtProt

NX_P02768.

Orphanet

86816. Congenital analbuminemia.

PharmGKB

PA24690.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14937.

HOVERGEN

HBG004207.

OrthoDB

EOG4Z0B55.

PhylomeDB

P02768.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.

Reactome

REACT_15518. Transmembrane transport of small molecules.
REACT_22258. Metabolism of lipids and lipoproteins.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P02768.

Bgee

P02768.

Genevestigator

P02768.

GermOnline

ENSG00000163631. Homo sapiens.

Family and domain databases

InterPro

IPR000264. Serum_albumin.
IPR020858. Serum_albumin-like.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
IPR021177. Serum_albumin_subgr.
[Graphical view]

Pfam

PF00273. Serum_albumin. 3 hits.
[Graphical view]

PIRSF

PIRSF002520. Serum_albumin_subgroup. 1 hit.

PRINTS

PR00802. SERUMALBUMIN.

SMART

SM00103. ALBUMIN. 3 hits.
[Graphical view]

SUPFAM

SSF48552. Serum_albumin. 3 hits.

PROSITE

PS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01418. Acenocoumarol.
DB00459. Acitretin.
DB00802. Alfentanil.
DB01370. Aluminium.
DB00995. Auranofin.
DB01402. Bismuth.
DB01197. Captopril.
DB00958. Carboplatin.
DB00456. Cefalotin.
DB01327. Cefazolin.
DB01328. Cefonicid.
DB01329. Cefoperazone.
DB01114. Chlorpheniramine.
DB00477. Chlorpromazine.
DB00537. Ciprofloxacin.
DB01068. Clonazepam.
DB01147. Cloxacillin.
DB00987. Cytarabine.
DB01219. Dantrolene.
DB00586. Diclofenac.
DB00861. Diflunisal.
DB01396. Digitoxin.
DB00655. Estrone.
DB00903. Ethacrynic acid.
DB00749. Etodolac.
DB00712. Flurbiprofen.
DB00743. Gadobenate Dimeglumine.
DB01044. Gatifloxacin.
DB01120. Gliclazide.
DB01159. Halothane.
DB00062. Human Serum Albumin.
DB00070. Hyaluronidase.
DB01050. Ibuprofen.
DB01307. Insulin-detemir.
DB01308. Insulin-glargine.
DB04711. Iodipamide.
DB01009. Ketoprofen.
DB00848. Levamisole.
DB00451. Levothyroxine.
DB00279. Liothyronine.
DB00784. Mefenamic acid.
DB00532. Mephenytoin.
DB00563. Methotrexate.
DB00540. Nortriptyline.
DB00842. Oxazepam.
DB01229. Paclitaxel.
DB00946. Phenprocoumon.
DB01032. Probenecid.
DB00818. Propofol.
DB00165. Pyridoxine.
DB00936. Salicyclic acid.
DB01232. Saquinavir.
DB00096. Serum albumin.
DB00064. Serum albumin iodonated.
DB00815. Sodium lauryl sulfate.
DB00364. Sucralfate.
DB00576. Sulfamethizole.
DB00605. Sulindac.
DB00870. Suprofen.
DB00624. Testosterone.
DB00137. Xanthophyll.

NextBio

862.

PMAP-CutDB

P02768.

SOURCE

Search...

Entry information

Entry name

ALBU_HUMAN

Accession

Primary (citable) accession number: P02768
Secondary accession number(s): O95574 , P04277, Q13140, Q645G4, Q68DN5, Q6UXK4, Q86YG0, Q9P157, Q9P1I7, Q9UHS3, Q9UJZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 179 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.