P00915 (CAH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbonic anhydrase 1
EC=4.2.1.1

Alternative name(s):
Carbonate dehydratase I
Carbonic anhydrase B
Short name=CAB
Carbonic anhydrase I
Short name=CA-I

Gene names

Name:

CA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	261 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	Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea. Ref.8
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc.
Enzyme regulation	Activated by histamine, imidazole, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, sulfonamide derivatives such as acetazolamide, benzenesulfonamide and derivatives (4-carboxyethylbenzene-sulfonamide, 4-carboxyethylbenzene-sulfonamide ethyl ester, 4-(acetyl-2-aminoethyl)benzene-sulfonamide, 4-aminoethylbenzene-sulfonamide), and 'prong inhibitors' BR15, BR17, BR22 and BR30. Activated by a short exposition to Foscarnet (phosphonoformate trisodium salt), but inhibited by a long one. Esterase activity weakly reduced by cyanamide. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.24 Ref.25 Ref.26
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.
Biophysicochemical properties	Kinetic parameters: KM=4.0 mM for CO2 Ref.8 Ref.14 KM=15 mM for 4-nitrophenyl acetate

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	bicarbonate transport Traceable author statement. Source: Reactome one-carbon metabolic process Inferred from electronic annotation. Source: InterPro small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA cytosol Traceable author statement. Source: Reactome
Molecular_function	carbonate dehydratase activity Traceable author statement Ref.2. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 261

260

Carbonic anhydrase 1

PRO_0000077409

Regions

Region

200 – 201

2

Substrate binding By similarity

Sites

Active site

65

1

Proton acceptor By similarity

Active site

129

1

By similarity

Metal binding

65

1

Zinc 2; variant Michigan-1

Metal binding

68

1

Zinc 2; variant Michigan-1

Metal binding

95

1

Zinc 1; catalytic Ref.17

Metal binding

97

1

Zinc 1; catalytic Ref.17

Metal binding

120

1

Zinc 1; catalytic Ref.17

Metal binding

201

1

Zinc 2; variant Michigan-1

Binding site

200

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Natural variations

Natural variant

68

1

H → R in variant Michigan-1; confers enhanced esterase activity and an additional zinc binding site. Ref.22 Ref.28

VAR_001378

Natural variant

143

1

A → V.
Corresponds to variant rs7821248 [ dbSNP | Ensembl ].

VAR_048679

Natural variant

254

1

G → R in Guam. Ref.27

VAR_001379

Experimental info

Sequence conflict

75 – 76

2

DN → ND AA sequence Ref.4

Sequence conflict

75 – 76

2

DN → ND AA sequence Ref.5

Secondary structure

1

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261

Helix Strand Turn

Details...

Turn

10 – 12

3

Helix

14 – 19

6

Helix

22 – 25

4

Beta strand

26 – 28

3

Beta strand

32 – 34

3

Turn

36 – 38

3

Beta strand

48 – 51

4

Helix

54 – 56

3

Beta strand

57 – 62

6

Beta strand

67 – 71

5

Beta strand

74 – 82

9

Beta strand

89 – 98

10

Beta strand

100 – 104

5

Beta strand

107 – 110

4

Beta strand

116 – 125

10

Turn

126 – 128

3

Helix

132 – 135

4

Beta strand

141 – 153

13

Helix

156 – 158

3

Helix

159 – 164

6

Helix

165 – 167

3

Beta strand

174 – 176

3

Helix

182 – 185

4

Beta strand

192 – 197

6

Beta strand

208 – 215

8

Beta strand

217 – 219

3

Helix

221 – 228

8

Beta strand

230 – 233

4

Sequences

	Sequence		Length	Mass (Da)
	P00915 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 4959E5FA25E374F8	FASTA	261	28,870
	10 20 30 40 50 60 MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI 70 80 90 100 110 120 INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH 130 140 150 160 170 180 VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF 190 200 210 220 230 240 DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV 250 260 PMQHNNRPTQ PLKGRTVRAS F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human carbonic anhydrase I cDNA." Barlow J.H., Lowe N., Edwards Y.H., Butterworth P.H.W. Nucleic Acids Res. 15:2386-2386(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and methylation patterns of the gene encoding human carbonic anhydrase I." Lowe N., Brady H.J.M., Barlow J.H., Sowden J.C., Edwards M., Butterworth P.H.W. Gene 93:277-283(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas and Spleen.
[4]	"Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)." Giraud N., Marriq C., Laurent-Tabusse G. Biochimie 56:1031-1043(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-261.
[5]	"Amino acid sequence of human erythrocyte carbonic anhydrase B." Andersson B., Nyman P.O., Strid L. Biochem. Biophys. Res. Commun. 48:670-677(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-261.
[6]	"Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B." Lin K.-T.D., Deutsch H.F. J. Biol. Chem. 248:1885-1893(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 12-261.
[7]	"Human carbonic anhydrases. XII. The complete primary structure of the C isozyme." Lin K.-T.D., Deutsch H.F. J. Biol. Chem. 249:2329-2337(1974) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[8]	"Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?" Briganti F., Mangani S., Scozzafava A., Vernaglione G., Supuran C.T. J. Biol. Inorg. Chem. 4:528-536(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme." Temperini C., Scozzafava A., Vullo D., Supuran C.T. Chemistry 12:7057-7066(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[10]	"Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design." Temperini C., Scozzafava A., Vullo D., Supuran C.T. J. Med. Chem. 49:3019-3027(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[11]	"Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV." Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T. Bioorg. Med. Chem. Lett. 17:628-635(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[12]	"A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases." Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T. Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[13]	"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors." Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T. J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[14]	"Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide." Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G. Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Structure of human carbonic anhydrase B. I. Crystallization and heavy atom modifications." Kannan K.K., Fridborg K., Bergsten P.C., Liljas A., Loevgren S., Petef M., Strandberg B., Waara I., Adler L., Falkbring S.O., Goethe P.O., Nyman P.O. J. Mol. Biol. 63:601-604(1972) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260.
[17]	"Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution." Kannan K.K., Notstrand B., Fridborg K., Loevgren S., Ohlsson A., Petef M. Proc. Natl. Acad. Sci. U.S.A. 72:51-55(1975) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[18]	"Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I." Kannan K.K., Ramanadham M., Jones T.A. Ann. N. Y. Acad. Sci. 429:49-60(1984) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION.
[19]	"Differences in anionic inhibition of human carbonic anhydrase I revealed from the structures of iodide and gold cyanide inhibitor complexes." Kumar V., Kannan K.K., Sathyamurthi P. Acta Crystallogr. D 50:731-738(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND INHIBITORS.
[20]	"Enzyme-substrate interactions. Structure of human carbonic anhydrase I complexed with bicarbonate." Kumar V., Kannan K.K. J. Mol. Biol. 241:226-232(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND BICARBONATE.
[21]	"Drug-protein interactions. Refined structures of three sulfonamide drug complexes of human carbonic anhydrase I enzyme." Chakravarty S., Kannan K.K. J. Mol. Biol. 243:298-309(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND INHIBITORS.
[22]	"Crystal structure of a zinc-activated variant of human carbonic anhydrase I, CA I Michigan 1: evidence for a second zinc binding site involving arginine coordination." Ferraroni M., Tilli S., Briganti F., Chegwidden W.R., Supuran C.T., Wiebauer K.E., Tashian R.E., Scozzafava A. Biochemistry 41:6237-6244(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION, VARIANT MICHIGAN-1 ARG-68.
[23]	"Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I." Temperini C., Scozzafava A., Supuran C.T. Bioorg. Med. Chem. Lett. 16:5152-5156(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND ACTIVATORS, ACTIVATION BY IMIDAZOLE AND HISTIDINE.
[24]	"Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with 'two-prong' inhibitors reveal the molecular basis of high affinity." Jude K.M., Banerjee A.L., Haldar M.K., Manokaran S., Roy B., Mallik S., Srivastava D.K., Christianson D.W. J. Am. Chem. Soc. 128:3011-3018(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND INHIBITORS, ENZYME REGULATION.
[25]	"Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I." Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T. Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 6-260 IN COMPLEX WITH ZINC ION AND THE ANTIVIRAL FOSCARNET, ENZYME REGULATION.
[26]	"Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II." Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S., Kooren J., Mallik S., Christianson D.W. J. Am. Chem. Soc. 129:5528-5537(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND INHIBITORS, ENZYME REGULATION.
[27]	"Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam." Omoto K., Ueda S., Goriki K., Takahashi N., Misawa S., Pagaran I.G. Am. J. Hum. Genet. 33:105-111(1981) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GUAM ARG-254.
[28]	"Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I." Chegwidden W.R., Wagner L.E., Venta P.J., Bergenhem N.C.H., Yu Y.-S.L., Tashian R.E. Hum. Mutat. 4:294-296(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MICHIGAN-1 ARG-68.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05014 mRNA. Translation: CAA28663.1.
M33987 mRNA. Translation: AAA51910.1.
BC027890 mRNA. Translation: AAH27890.1.

IPI

IPI00215983.

PIR

CRHU1. JQ0786.

RefSeq

NP_001122301.1. NM_001128829.2.
NP_001122302.1. NM_001128830.2.
NP_001122303.1. NM_001128831.2.
NP_001158302.1. NM_001164830.1.
NP_001729.1. NM_001738.3.

UniGene

Hs.23118.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AZM	X-ray	2.00	A	2-260	[»]
1BZM	X-ray	2.00	A	2-260	[»]
1CRM	X-ray	2.00	A	2-260	[»]
1CZM	X-ray	2.00	A	2-260	[»]
1HCB	X-ray	1.60	A	2-260	[»]
1HUG	X-ray	2.00	A	2-260	[»]
1HUH	X-ray	2.20	A	2-260	[»]
1J9W	X-ray	2.60	A/B	2-260	[»]
1JV0	X-ray	2.00	A/B	2-260	[»]
2CAB	X-ray	2.00	A	2-260	[»]
2FOY	X-ray	1.55	A/B	2-260	[»]
2FW4	X-ray	2.00	A/B	2-260	[»]
2IT4	X-ray	2.00	A/B	6-260	[»]
2NMX	X-ray	1.55	A/B	2-261	[»]
2NN1	X-ray	1.65	A/B	2-260	[»]
2NN7	X-ray	1.85	A/B	2-260	[»]
3LXE	X-ray	1.90	A/B	2-261	[»]
3W6H	X-ray	2.96	A/B	2-261	[»]
3W6I	X-ray	2.69	A/E	2-261	[»]

ProteinModelPortal

P00915.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00915. 1 interaction.

STRING

9606.ENSP00000256119.

PTM databases

PhosphoSite

P00915.

Polymorphism databases

DMDM

115449.

2D gel databases

DOSAC-COBS-2DPAGE

P00915.

REPRODUCTION-2DPAGE

IPI00215983.
P00915.

UCD-2DPAGE

P00915.

Proteomic databases

PaxDb

P00915.

PeptideAtlas

P00915.

PRIDE

P00915.

Protocols and materials databases

DNASU

759.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256119; ENSP00000256119; ENSG00000133742.
ENST00000431316; ENSP00000392338; ENSG00000133742.
ENST00000432364; ENSP00000401551; ENSG00000133742.
ENST00000523022; ENSP00000429798; ENSG00000133742.
ENST00000523953; ENSP00000430656; ENSG00000133742.
ENST00000542576; ENSP00000443517; ENSG00000133742.

GeneID

759.

KEGG

hsa:759.

UCSC

uc003ydh.3. human.

Organism-specific databases

CTD

759.

GeneCards

GC08M086315.

HGNC

HGNC:1368. CA1.

HPA

CAB025790.
HPA006558.

MIM

114800. gene.

neXtProt

NX_P00915.

PharmGKB

PA25984.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3338.

HOGENOM

HOG000112637.

HOVERGEN

HBG002837.

InParanoid

P00915.

KO

K01672.

OMA

HDTSLKP.

OrthoDB

EOG4X97HR.

PhylomeDB

P00915.

Enzyme and pathway databases

BRENDA

4.2.1.1. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P00915.

Gene expression databases

ArrayExpress

P00915.

Bgee

P00915.

CleanEx

HS_CA1.

Genevestigator

P00915.

GermOnline

ENSG00000133742. Homo sapiens.

Family and domain databases

Gene3D

3.10.200.10. 1 hit.

InterPro

IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018442. Carbonic_anhydrase_CA1.
[Graphical view]

PANTHER

PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF30. PTHR18952:SF30. 1 hit.

Pfam

PF00194. Carb_anhydrase. 1 hit.
[Graphical view]

SMART

SM01057. Carb_anhydrase. 1 hit.
[Graphical view]

SUPFAM

SSF51069. Euk_COanhd. 1 hit.

PROSITE

PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00915.

ChEMBL

CHEMBL261.

DrugBank

DB00819. Acetazolamide.
DB00381. Amlodipine.
DB00436. Bendroflumethiazide.
DB00562. Benzthiazide.
DB01194. Brinzolamide.
DB00880. Chlorothiazide.
DB00606. Cyclothiazide.
DB01119. Diazoxide.
DB01144. Dichlorphenamide.
DB01031. Ethinamate.
DB00311. Ethoxzolamide.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB01202. Levetiracetam.
DB00703. Methazolamide.
DB00232. Methyclothiazide.
DB01325. Quinethazone.
DB01021. Trichlormethiazide.
DB00661. Verapamil.
DB00909. Zonisamide.

EvolutionaryTrace

P00915.

GenomeRNAi

759.

NextBio

3070.

SOURCE

Search...

Entry information

Entry name

CAH1_HUMAN

Accession

Primary (citable) accession number: P00915

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 148 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.