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Q8WVQ1

- CANT1_HUMAN

UniProt

Q8WVQ1 - CANT1_HUMAN

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Protein
Soluble calcium-activated nucleotidase 1
Gene
CANT1, SHAPY
Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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
Complete GO annotation...

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; Single-pass type II membrane protein. Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein
Note: Processed form: Secreted.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4444Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei45 – 6218Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini63 – 401339Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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.
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.
VAR_068655
Natural varianti125 – 1251W → C in DBQD1; severely affects activity.
VAR_068656
Natural varianti165 – 1651M → T in DBQD1; severely affects activity.
VAR_068657
Natural varianti224 – 2241L → P in DBQD1; affects protein stability and secretion.
Corresponds to variant rs150181226 [ dbSNP | Ensembl ].
VAR_068658
Natural varianti226 – 2261V → M in DBQD1; severely affects activity.
VAR_068659
Natural varianti299 – 2991P → L in DBQD1.
VAR_062980
Natural varianti300 – 3001R → C in DBQD1; severely affects activity.
VAR_062981
Natural varianti300 – 3001R → H in DBQD1.
VAR_062982
Natural varianti303 – 3031S → R in DBQD1.
VAR_068660
Natural varianti360 – 3601A → D in DBQD1; affects protein secretion.
VAR_068662
Natural varianti374 – 3741I → N in DBQD1.
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 1
PRO_0000209925Add
BLAST

Amino acid modifications

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

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.1 Publication

Protein-protein interaction databases

BioGridi125875. 2 interactions.
STRINGi9606.ENSP00000307674.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ8WVQ1.

Family & Domainsi

Sequence similaritiesi

Belongs to the apyrase family.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei41 – 9151Missing in isoform 3.
VSP_054260Add
BLAST
Alternative sequencei220 – 24526KDERL…VNENP → REIVRKRWRLVKQVSHVGVL GQWIQR in isoform 2.
VSP_013760Add
BLAST
Alternative sequencei246 – 401156Missing in isoform 2.
VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 108 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

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