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Q8WVQ1

- CANT1_HUMAN

UniProt

Q8WVQ1 - CANT1_HUMAN

Protein

Soluble calcium-activated nucleotidase 1

Gene

CANT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    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. Involved in proteoglycan synthesis.3 Publications

    Catalytic activityi

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

    Cofactori

    Calcium.2 Publications

    pH dependencei

    Optimum pH is 6.8.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi168 – 1681Calcium
    Metal bindingi215 – 2151Calcium
    Metal bindingi284 – 2841Calcium
    Metal bindingi345 – 3451Calcium
    Metal bindingi396 – 3961Calcium

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. signal transducer activity Source: UniProtKB
    3. uridine-diphosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    2. proteoglycan biosynthetic process Source: UniProtKB
    3. signal transduction Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Soluble calcium-activated nucleotidase 1 (EC:3.6.1.6)
    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
    ProteomesiUP000005640: 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
    Note: Processed form: Secreted.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi cisterna membrane Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Desbuquois dysplasia 1 (DBQD1) [MIM:251450]: A 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.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121D → E in DBQD1. 1 Publication
    VAR_068655
    Natural varianti125 – 1251W → C in DBQD1; severely affects activity. 1 Publication
    VAR_068656
    Natural varianti165 – 1651M → T in DBQD1; severely affects activity. 1 Publication
    VAR_068657
    Natural varianti224 – 2241L → P in DBQD1; affects protein stability and secretion. 1 Publication
    Corresponds to variant rs150181226 [ dbSNP | Ensembl ].
    VAR_068658
    Natural varianti226 – 2261V → M in DBQD1; severely affects activity. 2 Publications
    VAR_068659
    Natural varianti299 – 2991P → L in DBQD1. 1 Publication
    VAR_062980
    Natural varianti300 – 3001R → C in DBQD1; severely affects activity. 1 Publication
    VAR_062981
    Natural varianti300 – 3001R → H in DBQD1. 2 Publications
    VAR_062982
    Natural varianti303 – 3031S → R in DBQD1. 1 Publication
    VAR_068660
    Natural varianti360 – 3601A → D in DBQD1; affects protein secretion. 1 Publication
    VAR_068662
    Natural varianti374 – 3741I → N in DBQD1. 1 Publication
    VAR_068663

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi112 – 1121D → A: Reduces activity by 99%. 1 Publication
    Mutagenesisi114 – 1141D → A: Reduces activity by 99%. 2 Publications
    Mutagenesisi152 – 1521G → E: Slightly reduced activity. 1 Publication
    Mutagenesisi160 – 1601E → Y: Increases GDPase activity 2-fold and ADPase activity 5-fold. 1 Publication
    Mutagenesisi163 – 1631R → A: Reduces activity by 98%. 1 Publication
    Mutagenesisi166 – 1661E → Q: Reduces activity by 95%. 1 Publication
    Mutagenesisi168 – 1681S → A: Reduces activity by over 99.9%. 1 Publication
    Mutagenesisi169 – 1691D → N: Reduces activity by 96%. 1 Publication
    Mutagenesisi181 – 1811D → A: Loss of activity. 1 Publication
    Mutagenesisi182 – 1821D → N: Reduces activity by over 99.9%. 1 Publication
    Mutagenesisi205 – 2051D → A: Slightly reduced activity. 1 Publication
    Mutagenesisi215 – 2151E → Q: Reduces activity by 99%. 1 Publication
    Mutagenesisi246 – 2461E → M: Increases activity 5-fold. 1 Publication
    Mutagenesisi301 – 3011R → A: Reduces activity by 99%. 2 Publications

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi251450. phenotype.
    Orphaneti1425. Desbuquois syndrome.
    PharmGKBiPA134984439.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 401401Soluble calcium-activated nucleotidase 1PRO_0000209925Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ8WVQ1.
    PaxDbiQ8WVQ1.
    PRIDEiQ8WVQ1.

    PTM databases

    PhosphoSiteiQ8WVQ1.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ8WVQ1.
    BgeeiQ8WVQ1.
    CleanExiHS_CANT1.
    GenevestigatoriQ8WVQ1.

    Organism-specific databases

    HPAiHPA019627.
    HPA019639.
    HPA022818.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi125875. 2 interactions.
    STRINGi9606.ENSP00000307674.

    Structurei

    Secondary structure

    1
    401
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi92 – 943
    Beta strandi97 – 993
    Beta strandi102 – 11211
    Helixi114 – 1174
    Beta strandi125 – 13713
    Beta strandi143 – 1475
    Beta strandi152 – 1576
    Beta strandi158 – 1603
    Beta strandi167 – 1737
    Beta strandi176 – 1816
    Turni182 – 1843
    Beta strandi186 – 1916
    Beta strandi194 – 2007
    Turni204 – 2074
    Beta strandi208 – 2114
    Beta strandi216 – 2205
    Beta strandi223 – 2275
    Beta strandi240 – 2423
    Helixi244 – 2463
    Beta strandi247 – 2515
    Beta strandi257 – 2615
    Helixi263 – 27210
    Beta strandi280 – 2823
    Beta strandi286 – 2894
    Turni290 – 2934
    Beta strandi294 – 2974
    Beta strandi300 – 3056
    Helixi309 – 3124
    Beta strandi319 – 3235
    Beta strandi330 – 3345
    Beta strandi342 – 3498
    Beta strandi357 – 36610
    Beta strandi369 – 37810
    Beta strandi383 – 40018

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 85-401.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WVQ1.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4444CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini63 – 401339LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei45 – 6218Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the apyrase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG264398.
    HOGENOMiHOG000008129.
    HOVERGENiHBG059824.
    InParanoidiQ8WVQ1.
    KOiK12304.
    OMAiVVPTHGF.
    OrthoDBiEOG7T1RBF.
    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. Align

    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

    MPVQLSEHPE WNESMHSLRI SVGGLPVLAS MTKAADPRFR PRWKVILTFF    50
    VGAAILWLLC SHRPAPGRPP THNAHNWRLG QAPANWYNDT YPLSPPQRTP 100
    AGIRYRIAVI ADLDTESRAQ EENTWFSYLK KGYLTLSDSG DKVAVEWDKD 150
    HGVLESHLAE KGRGMELSDL IVFNGKLYSV DDRTGVVYQI EGSKAVPWVI 200
    LSDGDGTVEK GFKAEWLAVK DERLYVGGLG KEWTTTTGDV VNENPEWVKV 250
    VGYKGSVDHE NWVSNYNALR AAAGIQPPGY LIHESACWSD TLQRWFFLPR 300
    RASQERYSEK DDERKGANLL LSASPDFGDI AVSHVGAVVP THGFSSFKFI 350
    PNTDDQIIVA LKSEEDSGRV ASYIMAFTLD GRFLLPETKI GSVKYEGIEF 400
    I 401
    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 AAM94564.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121D → E in DBQD1. 1 Publication
    VAR_068655
    Natural varianti125 – 1251W → C in DBQD1; severely affects activity. 1 Publication
    VAR_068656
    Natural varianti165 – 1651M → T in DBQD1; severely affects activity. 1 Publication
    VAR_068657
    Natural varianti224 – 2241L → P in DBQD1; affects protein stability and secretion. 1 Publication
    Corresponds to variant rs150181226 [ dbSNP | Ensembl ].
    VAR_068658
    Natural varianti226 – 2261V → M in DBQD1; severely affects activity. 2 Publications
    VAR_068659
    Natural varianti299 – 2991P → L in DBQD1. 1 Publication
    VAR_062980
    Natural varianti300 – 3001R → C in DBQD1; severely affects activity. 1 Publication
    VAR_062981
    Natural varianti300 – 3001R → H in DBQD1. 2 Publications
    VAR_062982
    Natural varianti303 – 3031S → R in DBQD1. 1 Publication
    VAR_068660
    Natural varianti323 – 3231A → T Polymorphism that does not affect activity.
    Corresponds to variant rs9903215 [ dbSNP | Ensembl ].
    VAR_068661
    Natural varianti360 – 3601A → D in DBQD1; affects protein secretion. 1 Publication
    VAR_068662
    Natural varianti374 – 3741I → N in DBQD1. 1 Publication
    VAR_068663
    Natural varianti391 – 3911G → E Polymorphism that does not affect activity.
    Corresponds to variant rs34082669 [ dbSNP | Ensembl ].
    VAR_068664

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei41 – 9151Missing in isoform 3. 1 PublicationVSP_054260Add
    BLAST
    Alternative sequencei220 – 24526KDERL…VNENP → REIVRKRWRLVKQVSHVGVL GQWIQR in isoform 2. 1 PublicationVSP_013760Add
    BLAST
    Alternative sequencei246 – 401156Missing in isoform 2. 1 PublicationVSP_013761Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_005257077.1. XM_005257020.1. [Q8WVQ1-1]
    XP_005257078.1. XM_005257021.1. [Q8WVQ1-1]
    XP_005257079.1. XM_005257022.1. [Q8WVQ1-1]
    XP_006721745.1. XM_006721682.1. [Q8WVQ1-1]
    XP_006721746.1. XM_006721683.1. [Q8WVQ1-1]
    UniGeneiHs.8859.

    Genome annotation databases

    EnsembliENST00000302345; ENSP00000307674; ENSG00000171302. [Q8WVQ1-1]
    ENST00000392446; ENSP00000376241; ENSG00000171302. [Q8WVQ1-1]
    ENST00000591773; ENSP00000467437; ENSG00000171302. [Q8WVQ1-1]
    GeneIDi124583.
    KEGGihsa:124583.
    UCSCiuc002jwj.3. human. [Q8WVQ1-1]

    Polymorphism databases

    DMDMi66774052.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11760.1. [Q8WVQ1-1 ]
    RefSeqi NP_001153244.1. NM_001159772.1. [Q8WVQ1-1 ]
    NP_001153245.1. NM_001159773.1. [Q8WVQ1-1 ]
    NP_620148.1. NM_138793.3. [Q8WVQ1-1 ]
    XP_005257077.1. XM_005257020.1. [Q8WVQ1-1 ]
    XP_005257078.1. XM_005257021.1. [Q8WVQ1-1 ]
    XP_005257079.1. XM_005257022.1. [Q8WVQ1-1 ]
    XP_006721745.1. XM_006721682.1. [Q8WVQ1-1 ]
    XP_006721746.1. XM_006721683.1. [Q8WVQ1-1 ]
    UniGenei Hs.8859.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S18 X-ray 1.70 A/B 71-401 [» ]
    1S1D X-ray 1.60 A/B 71-401 [» ]
    2H2N X-ray 2.30 A/B 69-401 [» ]
    2H2U X-ray 2.40 A/B 69-401 [» ]
    ProteinModelPortali Q8WVQ1.
    SMRi Q8WVQ1. Positions 85-401.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125875. 2 interactions.
    STRINGi 9606.ENSP00000307674.

    PTM databases

    PhosphoSitei Q8WVQ1.

    Polymorphism databases

    DMDMi 66774052.

    Proteomic databases

    MaxQBi Q8WVQ1.
    PaxDbi Q8WVQ1.
    PRIDEi Q8WVQ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302345 ; ENSP00000307674 ; ENSG00000171302 . [Q8WVQ1-1 ]
    ENST00000392446 ; ENSP00000376241 ; ENSG00000171302 . [Q8WVQ1-1 ]
    ENST00000591773 ; ENSP00000467437 ; ENSG00000171302 . [Q8WVQ1-1 ]
    GeneIDi 124583.
    KEGGi hsa:124583.
    UCSCi uc002jwj.3. human. [Q8WVQ1-1 ]

    Organism-specific databases

    CTDi 124583.
    GeneCardsi GC17M076987.
    HGNCi HGNC:19721. CANT1.
    HPAi HPA019627.
    HPA019639.
    HPA022818.
    MIMi 251450. phenotype.
    613165. gene.
    neXtProti NX_Q8WVQ1.
    Orphaneti 1425. Desbuquois syndrome.
    PharmGKBi PA134984439.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264398.
    HOGENOMi HOG000008129.
    HOVERGENi HBG059824.
    InParanoidi Q8WVQ1.
    KOi K12304.
    OMAi VVPTHGF.
    OrthoDBi EOG7T1RBF.
    PhylomeDBi Q8WVQ1.
    TreeFami TF315248.

    Miscellaneous databases

    EvolutionaryTracei Q8WVQ1.
    GeneWikii CANT1.
    GenomeRNAii 124583.
    NextBioi 35472441.
    PROi Q8WVQ1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WVQ1.
    Bgeei Q8WVQ1.
    CleanExi HS_CANT1.
    Genevestigatori Q8WVQ1.

    Family and domain databases

    InterProi IPR009283. Apyrase.
    [Graphical view ]
    PANTHERi PTHR13023. PTHR13023. 1 hit.
    Pfami PF06079. Apyrase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101887. SSF101887. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases."
      Smith T., Hicks-Berger C., Kim S., Kirley T.
      Arch. Biochem. Biophys. 406:105-115(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, COFACTOR, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
      Tissue: Mammary tumor.
    2. "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
      Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
      Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Lung fibroblast.
    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.
      , 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] (ISOFORMS 1 AND 3).
      Tissue: Mammary gland and Substantia nigra.
    4. "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] (ISOFORM 1).
      Tissue: Ovary, Pancreas and Skin.
    5. "Cloning, expression, and functional characterization of a Ca2+-dependent endoplasmic reticulum nucleoside diphosphatase."
      Failer B.U., Braun N., Zimmermann H.
      J. Biol. Chem. 277:36978-36986(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 141-401 (ISOFORM 1).
      Tissue: Brain.
    6. "Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change."
      Yang M., Kirley T.L.
      Biochemistry 43:9185-9194(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, MUTAGENESIS OF ASP-114; GLY-152; GLU-160; ARG-163; ASP-181; ASP-205 AND ARG-301.
    7. Cited for: INVOLVEMENT IN DBQD1.
    8. Cited for: FUNCTION IN PROTEOGLYCAN SYNTHESIS, VARIANTS DBQD1 HIS-300; ARG-303 AND ASN-374.
    9. "Structure and protein design of a human platelet function inhibitor."
      Dai J., Liu J., Deng Y., Smith T.M., Lu M.
      Cell 116:649-659(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 71-401 IN COMPLEX WITH SUBSTRATE ANALOG AND CALCIUM IONS, MUTAGENESIS OF ASP-112; ASP-114; GLU-166; SER-168; ASP-169; ASP-182; GLU-215; GLU-246 AND ARG-301.
    10. Cited for: VARIANTS DBQD1 LEU-299; CYS-300 AND HIS-300.
    11. "Desbuquois dysplasia type I and fetal hydrops due to novel mutations in the CANT1 gene."
      Laccone F., Schoner K., Krabichler B., Kluge B., Schwerdtfeger R., Schulze B., Zschocke J., Rehder H.
      Eur. J. Hum. Genet. 19:1133-1137(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DBQD1 GLU-112.
    12. Cited for: VARIANT DBQD1 MET-226.
    13. Cited for: VARIANTS DBQD1 CYS-125; THR-165; PRO-224; MET-226 AND ASP-360, CHARACTERIZATION OF VARIANTS DBQD1 CYS-125; THR-165; PRO-224; MET-226; CYS-300 AND ASP-360, CHARACTERIZATION OF VARIANTS THR-323 AND GLU-391.

    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: October 1, 2014
    This is version 109 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

    External Data

    Dasty 3