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Protein

Soluble calcium-activated nucleotidase 1

Gene

CANT1

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

Functioni

Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP (PubMed:12234496, PubMed:15248776, PubMed:15006348, PubMed:16835225). Involved in proteoglycan synthesis (PubMed:22539336).5 Publications

Catalytic activityi

A nucleoside diphosphate + H2O = a nucleoside phosphate + phosphate.3 Publications

Cofactori

Ca2+4 Publications

pH dependencei

Optimum pH is 6.8.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei160Important for dimer formation1 Publication1
Metal bindingi168Calcium; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi169CalciumCombined sources2 Publications1
Sitei200Important for dimer formation1 Publication1
Sitei202Important for dimer formation1 Publication1
Metal bindingi215Calcium; via carbonyl oxygenCombined sources2 Publications1
Sitei256Important for dimer formation1 Publication1
Metal bindingi284Calcium; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi345Calcium; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi396Calcium; via carbonyl oxygenCombined sources2 Publications1

GO - Molecular functioni

  • adenosine-diphosphatase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • guanosine-diphosphatase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • signal transducer activity Source: UniProtKB
  • uridine-diphosphatase activity Source: GO_Central

GO - Biological processi

  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • proteoglycan biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS15974-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Soluble calcium-activated nucleotidase 1 (EC:3.6.1.64 Publications)
Short name:
SCAN-1
Alternative name(s):
Apyrase homolog
Putative MAPK-activating protein PM09
Putative NF-kappa-B-activating protein 107
Gene namesi
Name:CANT1
Synonyms:SHAPY
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:19721. CANT1.

Subcellular locationi

  • Endoplasmic reticulum membrane 1 Publication; Single-pass type II membrane protein 1 Publication
  • Golgi apparatusGolgi stack membrane 1 Publication; Single-pass type II membrane protein 1 Publication
  • Cell membrane 1 Publication

  • Note: Processed form: Secreted.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 44CytoplasmicSequence analysisAdd BLAST44
Transmembranei45 – 62Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST18
Topological domaini63 – 401LumenalSequence analysisAdd BLAST339

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • Golgi cisterna membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Desbuquois dysplasia 1 (DBQD1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA chondrodysplasia characterized by severe prenatal and postnatal growth retardation (less than -5 SD), joint laxity, short extremities, progressive scoliosis, round face, midface hypoplasia, prominent bulging eyes. The main radiologic features are short long bones with metaphyseal splay, a 'Swedish key' appearance of the proximal femur (exaggerated trochanter), and advance carpal and tarsal bone age. Two forms of Desbuquois dysplasia are distinguished on the basis of the presence or absence of characteristic hand anomalies: an extra ossification center distal to the second metacarpal, delta phalanx, bifid distal thumb phalanx, and phalangeal dislocations.
See also OMIM:251450
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_068655112D → E in DBQD1. 1 PublicationCorresponds to variant rs749246739dbSNPEnsembl.1
Natural variantiVAR_068656125W → C in DBQD1; severely affects activity. 1 PublicationCorresponds to variant rs587776898dbSNPEnsembl.1
Natural variantiVAR_068657165M → T in DBQD1; severely affects activity. 1 Publication1
Natural variantiVAR_068658224L → P in DBQD1; affects protein stability and secretion. 1 PublicationCorresponds to variant rs150181226dbSNPEnsembl.1
Natural variantiVAR_068659226V → M in DBQD1; severely affects activity. 2 PublicationsCorresponds to variant rs377546036dbSNPEnsembl.1
Natural variantiVAR_062980299P → L in DBQD1. 1 PublicationCorresponds to variant rs267606700dbSNPEnsembl.1
Natural variantiVAR_062981300R → C in DBQD1; severely affects activity. 2 PublicationsCorresponds to variant rs267606701dbSNPEnsembl.1
Natural variantiVAR_062982300R → H in DBQD1. 2 PublicationsCorresponds to variant rs267606699dbSNPEnsembl.1
Natural variantiVAR_068660303S → R in DBQD1. 1 Publication1
Natural variantiVAR_068662360A → D in DBQD1; affects protein secretion. 1 PublicationCorresponds to variant rs387907081dbSNPEnsembl.1
Natural variantiVAR_068663374I → N in DBQD1. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi60C → S: Loss of dimer formation. 1 Publication1
Mutagenesisi112D → A: Reduces activity by 99%. 1 Publication1
Mutagenesisi114D → A: Reduces activity by 99%. 2 Publications1
Mutagenesisi139S → C: Reduces GDPase and ADPase activities 1.7-fold. Severe loss of dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi152G → E: Slightly reduced activity. 1 Publication1
Mutagenesisi160E → Y: Increases GDPase activity 2-fold and ADPase activity 5-fold. Forms dimer even at suboptimal Ca(2+) concentrations. 2 Publications1
Mutagenesisi163R → A: Reduces activity by 98%. 1 Publication1
Mutagenesisi166E → Q: Reduces activity by 95%. 1 Publication1
Mutagenesisi168S → A: Reduces activity by over 99.9%. 1 Publication1
Mutagenesisi169D → N: Reduces activity by 96%. 1 Publication1
Mutagenesisi181D → A: Loss of activity. 1 Publication1
Mutagenesisi182D → N: Reduces activity by over 99.9%. 1 Publication1
Mutagenesisi200I → C: Reduces GDPase activity 2-fold and ADPase activity 2.5-fold. No effect on dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi202S → C: Reduces GDPase activity 1.7-fold and ADPase activity 1.5-fold. No effect on dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi205D → A: Slightly reduced activity. 1 Publication1
Mutagenesisi215E → Q: Reduces activity by 99%. 1 Publication1
Mutagenesisi246E → M: Increases activity 5-fold. 1 Publication1
Mutagenesisi256S → C: No effect on GDPase and ADPase activities. No effect on dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi287C → S: Reduces GDPase and ADPase activities 1.3-fold. 1 Publication1
Mutagenesisi301R → A: Reduces activity by 99%. 2 Publications1
Mutagenesisi308S → C: Reduces GDPase activity 1.3-fold and ADPase activity 2-fold. Severe loss of dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi317A → C: Reduces GDPase activity 1.7-fold and ADPase activity 1.5-fold. Severe loss of dimer formation; when associated with S-287. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi124583.
MalaCardsiCANT1.
MIMi251450. phenotype.
OpenTargetsiENSG00000171302.
Orphaneti1425. Desbuquois syndrome.
PharmGKBiPA134984439.

Chemistry databases

DrugBankiDB03754. Tris.

Polymorphism and mutation databases

BioMutaiCANT1.
DMDMi66774052.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002099251 – 401Soluble calcium-activated nucleotidase 1Add BLAST401

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi60Interchain1 Publication
Glycosylationi88N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8WVQ1.
MaxQBiQ8WVQ1.
PaxDbiQ8WVQ1.
PeptideAtlasiQ8WVQ1.
PRIDEiQ8WVQ1.

PTM databases

iPTMnetiQ8WVQ1.
PhosphoSitePlusiQ8WVQ1.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000171302.
CleanExiHS_CANT1.
ExpressionAtlasiQ8WVQ1. baseline and differential.
GenevisibleiQ8WVQ1. HS.

Organism-specific databases

HPAiHPA019627.
HPA019639.
HPA022818.

Interactioni

Subunit structurei

Monomer (PubMed:12234496, PubMed:15006348). Homodimer; dimerization is Ca2+-dependent (PubMed:16835225). Homodimer; disulfide-linked (membrane form) (PubMed:16835225).3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi125875. 16 interactors.
STRINGi9606.ENSP00000307674.

Structurei

Secondary structure

1401
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi92 – 94Combined sources3
Beta strandi97 – 99Combined sources3
Beta strandi102 – 112Combined sources11
Helixi114 – 117Combined sources4
Beta strandi125 – 137Combined sources13
Beta strandi143 – 147Combined sources5
Beta strandi152 – 157Combined sources6
Beta strandi158 – 160Combined sources3
Beta strandi167 – 173Combined sources7
Beta strandi176 – 181Combined sources6
Turni182 – 184Combined sources3
Beta strandi186 – 191Combined sources6
Beta strandi194 – 200Combined sources7
Turni204 – 207Combined sources4
Beta strandi208 – 211Combined sources4
Beta strandi216 – 220Combined sources5
Beta strandi223 – 227Combined sources5
Beta strandi240 – 242Combined sources3
Helixi244 – 246Combined sources3
Beta strandi247 – 251Combined sources5
Beta strandi257 – 261Combined sources5
Helixi263 – 272Combined sources10
Beta strandi280 – 282Combined sources3
Beta strandi286 – 289Combined sources4
Turni290 – 293Combined sources4
Beta strandi294 – 297Combined sources4
Beta strandi300 – 305Combined sources6
Helixi309 – 312Combined sources4
Beta strandi319 – 323Combined sources5
Beta strandi330 – 334Combined sources5
Beta strandi342 – 349Combined sources8
Beta strandi357 – 366Combined sources10
Beta strandi369 – 378Combined sources10
Beta strandi383 – 400Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S18X-ray1.70A/B71-401[»]
1S1DX-ray1.60A/B71-401[»]
2H2NX-ray2.30A/B69-401[»]
2H2UX-ray2.40A/B69-401[»]
ProteinModelPortaliQ8WVQ1.
SMRiQ8WVQ1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WVQ1.

Family & Domainsi

Sequence similaritiesi

Belongs to the apyrase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4494. Eukaryota.
ENOG410XS4T. LUCA.
GeneTreeiENSGT00390000012872.
HOGENOMiHOG000008129.
HOVERGENiHBG059824.
InParanoidiQ8WVQ1.
KOiK12304.
OMAiVVPTHGF.
OrthoDBiEOG091G0DL5.
PhylomeDBiQ8WVQ1.
TreeFamiTF315248.

Family and domain databases

InterProiIPR009283. Apyrase.
[Graphical view]
PANTHERiPTHR13023. PTHR13023. 1 hit.
PfamiPF06079. Apyrase. 1 hit.
[Graphical view]
SUPFAMiSSF101887. SSF101887. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WVQ1-1) [UniParc]FASTAAdd to basket

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

« Hide

        10         20         30         40         50
MPVQLSEHPE WNESMHSLRI SVGGLPVLAS MTKAADPRFR PRWKVILTFF
60 70 80 90 100
VGAAILWLLC SHRPAPGRPP THNAHNWRLG QAPANWYNDT YPLSPPQRTP
110 120 130 140 150
AGIRYRIAVI ADLDTESRAQ EENTWFSYLK KGYLTLSDSG DKVAVEWDKD
160 170 180 190 200
HGVLESHLAE KGRGMELSDL IVFNGKLYSV DDRTGVVYQI EGSKAVPWVI
210 220 230 240 250
LSDGDGTVEK GFKAEWLAVK DERLYVGGLG KEWTTTTGDV VNENPEWVKV
260 270 280 290 300
VGYKGSVDHE NWVSNYNALR AAAGIQPPGY LIHESACWSD TLQRWFFLPR
310 320 330 340 350
RASQERYSEK DDERKGANLL LSASPDFGDI AVSHVGAVVP THGFSSFKFI
360 370 380 390 400
PNTDDQIIVA LKSEEDSGRV ASYIMAFTLD GRFLLPETKI GSVKYEGIEF

I
Length:401
Mass (Da):44,840
Last modified:March 1, 2002 - v1
Checksum:i5B78EB24C0B2C4CA
GO
Isoform 2 (identifier: Q8WVQ1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     220-245: KDERLYVGGLGKEWTTTTGDVVNENP → REIVRKRWRLVKQVSHVGVLGQWIQR
     246-401: Missing.

Show »
Length:245
Mass (Da):27,762
Checksum:i0D53611DA70ADCAF
GO
Isoform 3 (identifier: Q8WVQ1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     41-91: Missing.

Note: No experimental confirmation available.
Show »
Length:350
Mass (Da):38,946
Checksum:i3E074A6D59449646
GO

Sequence cautioni

The sequence AAM94564 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_068655112D → E in DBQD1. 1 PublicationCorresponds to variant rs749246739dbSNPEnsembl.1
Natural variantiVAR_068656125W → C in DBQD1; severely affects activity. 1 PublicationCorresponds to variant rs587776898dbSNPEnsembl.1
Natural variantiVAR_068657165M → T in DBQD1; severely affects activity. 1 Publication1
Natural variantiVAR_068658224L → P in DBQD1; affects protein stability and secretion. 1 PublicationCorresponds to variant rs150181226dbSNPEnsembl.1
Natural variantiVAR_068659226V → M in DBQD1; severely affects activity. 2 PublicationsCorresponds to variant rs377546036dbSNPEnsembl.1
Natural variantiVAR_062980299P → L in DBQD1. 1 PublicationCorresponds to variant rs267606700dbSNPEnsembl.1
Natural variantiVAR_062981300R → C in DBQD1; severely affects activity. 2 PublicationsCorresponds to variant rs267606701dbSNPEnsembl.1
Natural variantiVAR_062982300R → H in DBQD1. 2 PublicationsCorresponds to variant rs267606699dbSNPEnsembl.1
Natural variantiVAR_068660303S → R in DBQD1. 1 Publication1
Natural variantiVAR_068661323A → T Polymorphism; does not affect activity. 1 PublicationCorresponds to variant rs9903215dbSNPEnsembl.1
Natural variantiVAR_068662360A → D in DBQD1; affects protein secretion. 1 PublicationCorresponds to variant rs387907081dbSNPEnsembl.1
Natural variantiVAR_068663374I → N in DBQD1. 1 Publication1
Natural variantiVAR_068664391G → E Polymorphism; does not affect activity. 1 PublicationCorresponds to variant rs34082669dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05426041 – 91Missing in isoform 3. 1 PublicationAdd BLAST51
Alternative sequenceiVSP_013760220 – 245KDERL…VNENP → REIVRKRWRLVKQVSHVGVL GQWIQR in isoform 2. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_013761246 – 401Missing in isoform 2. 1 PublicationAdd BLAST156

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF328554 mRNA. Translation: AAM94564.1. Different initiation.
AB097006 mRNA. Translation: BAC77359.1.
AB097033 mRNA. Translation: BAC77386.1.
AK074687 mRNA. Translation: BAC11139.1.
AK295930 mRNA. Translation: BAG58716.1.
BC005104 mRNA. Translation: AAH05104.1.
BC017655 mRNA. Translation: AAH17655.1.
BC065038 mRNA. Translation: AAH65038.1.
AJ312208 mRNA. Translation: CAC85468.1.
CCDSiCCDS11760.1. [Q8WVQ1-1]
RefSeqiNP_001153244.1. NM_001159772.1. [Q8WVQ1-1]
NP_001153245.1. NM_001159773.1. [Q8WVQ1-1]
NP_620148.1. NM_138793.3. [Q8WVQ1-1]
XP_005257078.1. XM_005257021.1. [Q8WVQ1-1]
XP_005257079.1. XM_005257022.1. [Q8WVQ1-1]
XP_006721746.1. XM_006721683.1. [Q8WVQ1-1]
XP_011522593.1. XM_011524291.1. [Q8WVQ1-1]
XP_011522595.1. XM_011524293.1. [Q8WVQ1-1]
XP_011522596.1. XM_011524294.1. [Q8WVQ1-1]
XP_011522597.1. XM_011524295.2. [Q8WVQ1-1]
UniGeneiHs.8859.

Genome annotation databases

EnsembliENST00000302345; ENSP00000307674; ENSG00000171302. [Q8WVQ1-1]
ENST00000392446; ENSP00000376241; ENSG00000171302. [Q8WVQ1-1]
ENST00000591773; ENSP00000467437; ENSG00000171302. [Q8WVQ1-1]
ENST00000620915; ENSP00000477798; ENSG00000171302. [Q8WVQ1-1]
GeneIDi124583.
KEGGihsa:124583.
UCSCiuc002jwj.4. human. [Q8WVQ1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF328554 mRNA. Translation: AAM94564.1. Different initiation.
AB097006 mRNA. Translation: BAC77359.1.
AB097033 mRNA. Translation: BAC77386.1.
AK074687 mRNA. Translation: BAC11139.1.
AK295930 mRNA. Translation: BAG58716.1.
BC005104 mRNA. Translation: AAH05104.1.
BC017655 mRNA. Translation: AAH17655.1.
BC065038 mRNA. Translation: AAH65038.1.
AJ312208 mRNA. Translation: CAC85468.1.
CCDSiCCDS11760.1. [Q8WVQ1-1]
RefSeqiNP_001153244.1. NM_001159772.1. [Q8WVQ1-1]
NP_001153245.1. NM_001159773.1. [Q8WVQ1-1]
NP_620148.1. NM_138793.3. [Q8WVQ1-1]
XP_005257078.1. XM_005257021.1. [Q8WVQ1-1]
XP_005257079.1. XM_005257022.1. [Q8WVQ1-1]
XP_006721746.1. XM_006721683.1. [Q8WVQ1-1]
XP_011522593.1. XM_011524291.1. [Q8WVQ1-1]
XP_011522595.1. XM_011524293.1. [Q8WVQ1-1]
XP_011522596.1. XM_011524294.1. [Q8WVQ1-1]
XP_011522597.1. XM_011524295.2. [Q8WVQ1-1]
UniGeneiHs.8859.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S18X-ray1.70A/B71-401[»]
1S1DX-ray1.60A/B71-401[»]
2H2NX-ray2.30A/B69-401[»]
2H2UX-ray2.40A/B69-401[»]
ProteinModelPortaliQ8WVQ1.
SMRiQ8WVQ1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125875. 16 interactors.
STRINGi9606.ENSP00000307674.

Chemistry databases

DrugBankiDB03754. Tris.

PTM databases

iPTMnetiQ8WVQ1.
PhosphoSitePlusiQ8WVQ1.

Polymorphism and mutation databases

BioMutaiCANT1.
DMDMi66774052.

Proteomic databases

EPDiQ8WVQ1.
MaxQBiQ8WVQ1.
PaxDbiQ8WVQ1.
PeptideAtlasiQ8WVQ1.
PRIDEiQ8WVQ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302345; ENSP00000307674; ENSG00000171302. [Q8WVQ1-1]
ENST00000392446; ENSP00000376241; ENSG00000171302. [Q8WVQ1-1]
ENST00000591773; ENSP00000467437; ENSG00000171302. [Q8WVQ1-1]
ENST00000620915; ENSP00000477798; ENSG00000171302. [Q8WVQ1-1]
GeneIDi124583.
KEGGihsa:124583.
UCSCiuc002jwj.4. human. [Q8WVQ1-1]

Organism-specific databases

CTDi124583.
DisGeNETi124583.
GeneCardsiCANT1.
HGNCiHGNC:19721. CANT1.
HPAiHPA019627.
HPA019639.
HPA022818.
MalaCardsiCANT1.
MIMi251450. phenotype.
613165. gene.
neXtProtiNX_Q8WVQ1.
OpenTargetsiENSG00000171302.
Orphaneti1425. Desbuquois syndrome.
PharmGKBiPA134984439.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4494. Eukaryota.
ENOG410XS4T. LUCA.
GeneTreeiENSGT00390000012872.
HOGENOMiHOG000008129.
HOVERGENiHBG059824.
InParanoidiQ8WVQ1.
KOiK12304.
OMAiVVPTHGF.
OrthoDBiEOG091G0DL5.
PhylomeDBiQ8WVQ1.
TreeFamiTF315248.

Enzyme and pathway databases

BioCyciZFISH:HS15974-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiCANT1. human.
EvolutionaryTraceiQ8WVQ1.
GeneWikiiCANT1.
GenomeRNAii124583.
PROiQ8WVQ1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171302.
CleanExiHS_CANT1.
ExpressionAtlasiQ8WVQ1. baseline and differential.
GenevisibleiQ8WVQ1. HS.

Family and domain databases

InterProiIPR009283. Apyrase.
[Graphical view]
PANTHERiPTHR13023. PTHR13023. 1 hit.
PfamiPF06079. Apyrase. 1 hit.
[Graphical view]
SUPFAMiSSF101887. SSF101887. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCANT1_HUMAN
AccessioniPrimary (citable) accession number: Q8WVQ1
Secondary accession number(s): B4DJ54
, Q7Z2J7, Q8NG05, Q8NHP0, Q9BSD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: March 1, 2002
Last modified: November 30, 2016
This is version 130 of the entry and version 1 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

Miscellaneous

Not inhibited by azide.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

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 one 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.