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P22748 (CAH4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

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

Names and origin

Protein namesRecommended name:
Carbonic anhydrase 4

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase IV
Carbonic anhydrase IV
Short name=CA-IV
Gene names
Name:CA4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid. Ref.20

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Enzyme regulation

Activated by histamine, L-adrenaline, D-phenylalanine, L- and D-histidine. Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide and Foscarnet (phosphonoformate trisodium salt). Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Subunit structure

Interacts with SLC4A4. Ref.20

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Ref.9.

Tissue specificity

Expressed in the endothelium of the choriocapillaris in eyes (at protein level). Not expressed in the retinal epithelium at detectable levels. Ref.20

Involvement in disease

Retinitis pigmentosa 17 (RP17) [MIM:600852]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry. Defective acid overload removal from retina and retinal epithelium, due to mutant CA4, is responsible for photoreceptor degeneration, indicating that impaired pH homeostasis is the most likely cause underlying the RP17 phenotype. Ref.20

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Biophysicochemical properties

Kinetic parameters:

KM=21.5 mM for CO2 Ref.17

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Retinitis pigmentosa
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbicarbonate transport

Inferred from mutant phenotype Ref.20. Source: DFLAT

one-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

organ development

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 17409381. Source: DFLAT

anchored component of external side of plasma membrane

Inferred from direct assay PubMed 17409381. Source: DFLAT

apical plasma membrane

Inferred from direct assay PubMed 17409381. Source: DFLAT

brush border membrane

Inferred from direct assay PubMed 17409381. Source: DFLAT

cell surface

Inferred from direct assay Ref.20. Source: DFLAT

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay PubMed 17409381. Source: DFLAT

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

membrane

Traceable author statement PubMed 6811592. Source: ProtInc

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17409381. Source: DFLAT

plasma membrane

Inferred from direct assay Ref.20. Source: UniProtKB

rough endoplasmic reticulum

Inferred from direct assay PubMed 17409381. Source: DFLAT

sarcolemma

Inferred from electronic annotation. Source: Ensembl

sarcoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

secretory granule membrane

Inferred from direct assay PubMed 17409381. Source: DFLAT

trans-Golgi network

Inferred from direct assay PubMed 17409381. Source: DFLAT

transport vesicle membrane

Inferred from direct assay PubMed 17409381. Source: DFLAT

   Molecular_functioncarbonate dehydratase activity

Traceable author statement. Source: Reactome

protein binding

Inferred from physical interaction Ref.20. Source: DFLAT

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.7
Chain19 – 284266Carbonic anhydrase 4
PRO_0000004226
Propeptide285 – 31228Removed in mature form
PRO_0000004227

Regions

Region225 – 2262Substrate binding Probable

Sites

Active site881Proton acceptor By similarity
Metal binding1151Zinc; catalytic
Metal binding1171Zinc; catalytic
Metal binding1401Zinc; catalytic

Amino acid modifications

Lipidation2841GPI-anchor amidated serine Ref.9
Disulfide bond24 ↔ 36 Ref.8
Disulfide bond46 ↔ 229 Ref.8

Natural variations

Natural variant141R → W in RP17; abolishes interaction with SLC4A4. Impaired SLC4A4 cotransporter activity stimulation. Ref.20
VAR_024749
Natural variant2191R → S in RP17; no catalytic activity. Impaired SLC4A4 cotransporter activity stimulation. Ref.20
VAR_024750
Natural variant2371V → L.
Corresponds to variant rs2229178 [ dbSNP | Ensembl ].
VAR_048680

Experimental info

Mutagenesis2841S → F: Loss of C-terminal domain removal and inactivation. Ref.9
Sequence conflict241C → E AA sequence Ref.7

Secondary structure

................................................ 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22748 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: EF5F182474ABE9B0

FASTA31235,032
        10         20         30         40         50         60 
MRMLLALLAL SAARPSASAE SHWCYEVQAE SSNYPCLVPV KWGGNCQKDR QSPINIVTTK 

        70         80         90        100        110        120 
AKVDKKLGRF FFSGYDKKQT WTVQNNGHSV MMLLENKASI SGGGLPAPYQ AKQLHLHWSD 

       130        140        150        160        170        180 
LPYKGSEHSL DGEHFAMEMH IVHEKEKGTS RNVKEAQDPE DEIAVLAFLV EAGTQVNEGF 

       190        200        210        220        230        240 
QPLVEALSNI PKPEMSTTMA ESSLLDLLPK EEKLRHYFRY LGSLTTPTCD EKVVWTVFRE 

       250        260        270        280        290        300 
PIQLHREQIL AFSQKLYYDK EQTVSMKDNV RPLQQLGQRT VIKSGAPGRP LPWALPALLG 

       310 
PMLACLLAGF LR 

« Hide

References

« Hide 'large scale' references
[1]"Human carbonic anhydrase IV: cDNA cloning, sequence comparison, and expression in COS cell membranes."
Okuyama T., Sato S., Zhu X.L., Waheed A., Sly W.S.
Proc. Natl. Acad. Sci. U.S.A. 89:1315-1319(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic organization and localization of gene for human carbonic anhydrase IV to chromosome 17q."
Okuyama T., Batanian J.R., Sly W.S.
Genomics 16:678-684(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Brain and Placenta.
[7]"Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney."
Zhu X.L., Sly W.S.
J. Biol. Chem. 265:8795-8801(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-35; 113-123 AND 233-239.
Tissue: Lung.
[8]"Carbonic anhydrase IV: purification of a secretory form of the recombinant human enzyme and identification of the positions and importance of its disulfide bonds."
Waheed A., Okuyama T., Heyduk T., Sly W.S.
Arch. Biochem. Biophys. 333:432-438(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[9]"Carbonic anhydrase IV: role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activity."
Okuyama T., Waheed A., Kusumoto W., Zhu X.L., Sly W.S.
Arch. Biochem. Biophys. 320:315-322(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR AT SER-284, MUTAGENESIS OF SER-284.
[10]"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.
[11]"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.
[12]"Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste."
Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G.
Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[13]"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.
[14]"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: ENZYME REGULATION.
[15]"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.
[16]"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.
[17]"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.
[18]"Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution."
Stams T., Nair S.K., Okuyama T., Waheed A., Sly W.S., Christianson D.W.
Proc. Natl. Acad. Sci. U.S.A. 93:13589-13594(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 19-284 IN COMPLEX WITH ZINC ION.
[19]"Thioether benzenesulfonamide inhibitors of carbonic anhydrases II and IV: structure-based drug design, synthesis, and biological evaluation."
Vernier W.F., Chong W., Rewolinski D., Greasley S., Pauly T.A., Shaw M., Dinh D.M., Ferre R.A.A., Meador J.W. III, Nukui S., Ornelas M., Paz R.L., Reyner E.
Bioorg. Med. Chem. 18:3307-3319(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 19-284 IN COMPLEX WITH INHIBITORS.
[20]"Mutant carbonic anhydrase 4 impairs pH regulation and causes retinal photoreceptor degeneration."
Yang Z., Alvarez B.V., Chakarova C., Jiang L., Karan G., Frederick J.M., Zhao Y., Sauve Y., Li X., Zrenner E., Wissinger B., Den Hollander A.I., Katz B., Baehr W., Cremers F.P., Casey J.R., Bhattacharya S.S., Zhang K.
Hum. Mol. Genet. 14:255-265(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP17 TRP-14 AND SER-219, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH SLC4A4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83670 mRNA. Translation: AAA35630.1.
L10955 expand/collapse EMBL AC list , L10951, L10953, L10954 Genomic DNA. Translation: AAA35625.1. Sequence problems.
L10955, L10954 Genomic DNA. Translation: AAA35626.1. Sequence problems.
AK289715 mRNA. Translation: BAF82404.1.
CR541766 mRNA. Translation: CAG46565.1.
CH471109 Genomic DNA. Translation: EAW94362.1.
BC057792 mRNA. Translation: AAH57792.1.
BC069649 mRNA. Translation: AAH69649.1.
BC074768 mRNA. Translation: AAH74768.1.
CCDSCCDS11624.1.
PIRCRHU4. A45745.
RefSeqNP_000708.1. NM_000717.3.
UniGeneHs.89485.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZNCX-ray2.80A/B19-284[»]
3F7BX-ray2.05A/B19-284[»]
3F7UX-ray2.00A/B/C/D19-284[»]
3FW3X-ray1.72A/B19-284[»]
ProteinModelPortalP22748.
SMRP22748. Positions 23-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107217. 4 interactions.
IntActP22748. 4 interactions.
STRING9606.ENSP00000300900.

Chemistry

BindingDBP22748.
ChEMBLCHEMBL2095180.
DrugBankDB00436. Bendroflumethiazide.
DB00562. Benzthiazide.
DB00880. Chlorothiazide.
DB00606. Cyclothiazide.
DB01119. Diazoxide.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00232. Methyclothiazide.
DB01325. Quinethazone.
DB00273. Topiramate.
DB01021. Trichlormethiazide.
GuidetoPHARMACOLOGY2599.

PTM databases

PhosphoSiteP22748.

Polymorphism databases

DMDM115465.

Proteomic databases

PaxDbP22748.
PRIDEP22748.

Protocols and materials databases

DNASU762.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300900; ENSP00000300900; ENSG00000167434.
GeneID762.
KEGGhsa:762.
UCSCuc002iym.4. human.

Organism-specific databases

CTD762.
GeneCardsGC17P058227.
GeneReviewsCA4.
HGNCHGNC:1375. CA4.
HPAHPA011089.
HPA017258.
MIM114760. gene.
600852. phenotype.
neXtProtNX_P22748.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA25991.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3338.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP22748.
KOK18246.
OMAKGTSRNV.
OrthoDBEOG7MD4QN.
PhylomeDBP22748.
TreeFamTF316425.

Enzyme and pathway databases

BRENDA4.2.1.1. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP22748.

Gene expression databases

ArrayExpressP22748.
BgeeP22748.
CleanExHS_CA4.
GenevestigatorP22748.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF95. PTHR18952:SF95. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. SSF51069. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22748.
GeneWikiCarbonic_anhydrase_4.
GenomeRNAi762.
NextBio3082.
PROP22748.
SOURCESearch...

Entry information

Entry nameCAH4_HUMAN
AccessionPrimary (citable) accession number: P22748
Secondary accession number(s): Q6FHI7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM