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Protein

Carbonic anhydrase 9

Gene

CA9

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

Functioni

Reversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia.1 Publication

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Enzyme regulationi

Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA) and Foscarnet (phosphonoformate trisodium salt).4 Publications

pH dependencei

Optimum pH is 6.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei200 – 2001Proton acceptorBy similarity
Metal bindingi226 – 2261Zinc; catalytic
Metal bindingi228 – 2281Zinc; catalytic
Metal bindingi251 – 2511Zinc; catalytic

GO - Molecular functioni

  • carbonate dehydratase activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiREACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_121123. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 9 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase IX
Carbonic anhydrase IX
Short name:
CA-IX
Short name:
CAIX
Membrane antigen MN
P54/58N
Renal cell carcinoma-associated antigen G250
Short name:
RCC-associated antigen G250
pMW1
Gene namesi
Name:CA9
Synonyms:G250, MN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:1383. CA9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini38 – 414377ExtracellularAdd
BLAST
Transmembranei415 – 43521HelicalSequence AnalysisAdd
BLAST
Topological domaini436 – 45924CytoplasmicAdd
BLAST

GO - Cellular componenti

  • basolateral plasma membrane Source: Ensembl
  • integral component of membrane Source: ProtInc
  • microvillus membrane Source: UniProtKB-SubCell
  • nucleolus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25998.

Chemistry

DrugBankiDB00562. Benzthiazide.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00909. Zonisamide.

Polymorphism and mutation databases

BioMutaiCA9.
DMDMi83300925.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 PublicationAdd
BLAST
Chaini38 – 459422Carbonic anhydrase 9PRO_0000004243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi115 – 1151O-linked (GlcNAc...)1 Publication
Disulfide bondi156 ↔ 336
Disulfide bondi174 – 174InterchainCurated
Glycosylationi346 – 3461N-linked (GlcNAc...)2 Publications
Modified residuei449 – 4491Phosphotyrosine1 Publication

Post-translational modificationi

Asn-346 bears high-mannose type glycan structures.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ16790.
PaxDbiQ16790.
PRIDEiQ16790.

PTM databases

PhosphoSiteiQ16790.

Expressioni

Tissue specificityi

Expressed primarily in carcinoma cells lines. Expression is restricted to very few normal tissues and the most abundant expression is found in the epithelial cells of gastric mucosa.

Inductioni

By hypoxia.1 Publication

Gene expression databases

BgeeiQ16790.
CleanExiHS_CA9.
ExpressionAtlasiQ16790. baseline and differential.
GenevisibleiQ16790. HS.

Organism-specific databases

HPAiCAB005100.
CAB017107.
HPA055207.

Interactioni

Subunit structurei

Forms oligomers linked by disulfide bonds.3 Publications

Protein-protein interaction databases

BioGridi107223. 30 interactions.
DIPiDIP-48973N.
STRINGi9606.ENSP00000367608.

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni137 – 1393Combined sources
Beta strandi143 – 1475Combined sources
Helixi149 – 1524Combined sources
Helixi154 – 1574Combined sources
Helixi168 – 1703Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi181 – 1844Combined sources
Beta strandi193 – 1975Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi211 – 2155Combined sources
Beta strandi218 – 22912Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi247 – 25610Combined sources
Helixi262 – 2654Combined sources
Beta strandi271 – 28111Combined sources
Helixi287 – 2937Combined sources
Helixi294 – 2996Combined sources
Beta strandi305 – 3084Combined sources
Helixi313 – 3164Combined sources
Beta strandi324 – 3307Combined sources
Beta strandi338 – 34710Combined sources
Beta strandi349 – 3513Combined sources
Helixi353 – 3619Combined sources
Beta strandi387 – 3893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HKFX-ray2.01P83-91[»]
3IAIX-ray2.20A/B/C/D137-391[»]
ProteinModelPortaliQ16790.
SMRiQ16790. Positions 139-391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16790.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 11275Proteoglycan-like (PG)Add
BLAST
Regioni113 – 414302CatalyticAdd
BLAST
Regioni332 – 3332Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ16790.
KOiK01672.
OMAiSRYFRYE.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ16790.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018429. CA9.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF18. PTHR18952:SF18. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q16790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPLCPSPWL PLLIPAPAPG LTVQLLLSLL LLVPVHPQRL PRMQEDSPLG
60 70 80 90 100
GGSSGEDDPL GEEDLPSEED SPREEDPPGE EDLPGEEDLP GEEDLPEVKP
110 120 130 140 150
KSEEEGSLKL EDLPTVEAPG DPQEPQNNAH RDKEGDDQSH WRYGGDPPWP
160 170 180 190 200
RVSPACAGRF QSPVDIRPQL AAFCPALRPL ELLGFQLPPL PELRLRNNGH
210 220 230 240 250
SVQLTLPPGL EMALGPGREY RALQLHLHWG AAGRPGSEHT VEGHRFPAEI
260 270 280 290 300
HVVHLSTAFA RVDEALGRPG GLAVLAAFLE EGPEENSAYE QLLSRLEEIA
310 320 330 340 350
EEGSETQVPG LDISALLPSD FSRYFQYEGS LTTPPCAQGV IWTVFNQTVM
360 370 380 390 400
LSAKQLHTLS DTLWGPGDSR LQLNFRATQP LNGRVIEASF PAGVDSSPRA
410 420 430 440 450
AEPVQLNSCL AAGDILALVF GLLFAVTSVA FLVQMRRQHR RGTKGGVSYR

PAEVAETGA
Length:459
Mass (Da):49,698
Last modified:December 6, 2005 - v2
Checksum:iBA67195483F0F5CE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331V → M.2 Publications
Corresponds to variant rs2071676 [ dbSNP | Ensembl ].
VAR_010787
Natural varianti326 – 3261Q → R.
Corresponds to variant rs3829078 [ dbSNP | Ensembl ].
VAR_020049

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66839 mRNA. Translation: CAA47315.1.
AJ010588 mRNA. Translation: CAB82444.1.
AL133410, AL357874 Genomic DNA. Translation: CAI10985.1.
AL357874, AL133410 Genomic DNA. Translation: CAI13455.1.
CH471071 Genomic DNA. Translation: EAW58359.1.
BC014950 mRNA. Translation: AAH14950.1.
CCDSiCCDS6585.1.
PIRiI38013.
RefSeqiNP_001207.2. NM_001216.2.
UniGeneiHs.63287.

Genome annotation databases

EnsembliENST00000378357; ENSP00000367608; ENSG00000107159.
GeneIDi768.
KEGGihsa:768.
UCSCiuc003zxo.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66839 mRNA. Translation: CAA47315.1.
AJ010588 mRNA. Translation: CAB82444.1.
AL133410, AL357874 Genomic DNA. Translation: CAI10985.1.
AL357874, AL133410 Genomic DNA. Translation: CAI13455.1.
CH471071 Genomic DNA. Translation: EAW58359.1.
BC014950 mRNA. Translation: AAH14950.1.
CCDSiCCDS6585.1.
PIRiI38013.
RefSeqiNP_001207.2. NM_001216.2.
UniGeneiHs.63287.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HKFX-ray2.01P83-91[»]
3IAIX-ray2.20A/B/C/D137-391[»]
ProteinModelPortaliQ16790.
SMRiQ16790. Positions 139-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107223. 30 interactions.
DIPiDIP-48973N.
STRINGi9606.ENSP00000367608.

Chemistry

BindingDBiQ16790.
ChEMBLiCHEMBL2095180.
DrugBankiDB00562. Benzthiazide.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00909. Zonisamide.

PTM databases

PhosphoSiteiQ16790.

Polymorphism and mutation databases

BioMutaiCA9.
DMDMi83300925.

Proteomic databases

MaxQBiQ16790.
PaxDbiQ16790.
PRIDEiQ16790.

Protocols and materials databases

DNASUi768.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378357; ENSP00000367608; ENSG00000107159.
GeneIDi768.
KEGGihsa:768.
UCSCiuc003zxo.4. human.

Organism-specific databases

CTDi768.
GeneCardsiGC09P035673.
H-InvDBHIX0008019.
HGNCiHGNC:1383. CA9.
HPAiCAB005100.
CAB017107.
HPA055207.
MIMi603179. gene.
neXtProtiNX_Q16790.
PharmGKBiPA25998.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ16790.
KOiK01672.
OMAiSRYFRYE.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ16790.
TreeFamiTF316425.

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiREACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_121123. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTraceiQ16790.
GeneWikiiCarbonic_anhydrase_9.
GenomeRNAii768.
NextBioi3106.
PROiQ16790.
SOURCEiSearch...

Gene expression databases

BgeeiQ16790.
CleanExiHS_CA9.
ExpressionAtlasiQ16790. baseline and differential.
GenevisibleiQ16790. HS.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018429. CA9.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF18. PTHR18952:SF18. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment."
    Pastorek J., Pastorekova S., Callebaut I., Mornon J.-P., Zelnik V., Opavsky R., Zat'Ovicova M., Liao S., Portetelle D., Stanbridge E.J., Zavada J., Burny A., Kettmann R.
    Oncogene 9:2877-2888(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT MET-33.
    Tissue: Carcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Renal cell carcinoma.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANT MET-33.
    Tissue: Colon.
  6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-52.
  7. "A novel quasi-viral agent, MaTu, is a two-component system."
    Pastorekova S., Zavadova Z., Kostal M., Babusikova O., Zavada J.
    Virology 187:620-626(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Expression of MaTu-MN protein in human tumor cultures and in clinical specimens."
    Zavada J., Zavadova Z., Pastorekova S., Ciampor F., Pastorek J., Zelnik V.
    Int. J. Cancer 54:268-274(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "The role of carbonic anhydrase IX overexpression in kidney cancer."
    Dorai T., Sawczuk I.S., Pastorek J., Wiernik P.H., Dutcher J.P.
    Eur. J. Cancer 41:2935-2947(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-449.
  10. "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.
  11. "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.
  12. Cited for: FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346, DISULFIDE BONDS.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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.
  15. "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.
  16. "Stabilization of antibody structure upon association to a human carbonic anhydrase IX epitope studied by X-ray crystallography, microcalorimetry, and molecular dynamics simulations."
    Kral V., Mader P., Collard R., Fabry M., Horejsi M., Rezacova P., Kozisek M., Zavada J., Sedlacek J., Rulisek L., Brynda J.
    Proteins 71:1275-1287(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 83-91 IN COMPLEX WITH SPECIFIC ANTIBODIES.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 137-391 IN COMPLEX WITH ZINC ION AND THE INHIBITOR ACETAZOLAMIDE, GLYCOSYLATION AT ASN-346, DISULFIDE BOND, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiCAH9_HUMAN
AccessioniPrimary (citable) accession number: Q16790
Secondary accession number(s): Q5T4R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: December 6, 2005
Last modified: July 22, 2015
This is version 150 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.