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Protein

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2

Gene

BST1

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

Functioni

Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth.1 Publication

Catalytic activityi

NAD+ + H2O = ADP-D-ribose + nicotinamide.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei109Crucial for NAD binding and catalysis1
Sitei172Crucial for NAD binding and catalysis1
Sitei210Crucial for NAD binding and catalysis1

GO - Molecular functioni

GO - Biological processi

  • humoral immune response Source: ParkinsonsUK-UCL
  • NAD metabolic process Source: Reactome
  • neutrophil degranulation Source: Reactome
  • positive regulation of B cell proliferation Source: GO_Central
  • positive regulation of cell proliferation Source: ParkinsonsUK-UCL
  • regulation of actin cytoskeleton organization Source: ParkinsonsUK-UCL
  • regulation of calcium-mediated signaling Source: ParkinsonsUK-UCL
  • regulation of cell-matrix adhesion Source: ParkinsonsUK-UCL
  • regulation of cellular extravasation Source: ParkinsonsUK-UCL
  • regulation of inflammatory response Source: ParkinsonsUK-UCL
  • regulation of integrin-mediated signaling pathway Source: ParkinsonsUK-UCL
  • regulation of neutrophil chemotaxis Source: ParkinsonsUK-UCL
  • regulation of peptidyl-tyrosine phosphorylation Source: ParkinsonsUK-UCL
  • regulation of superoxide metabolic process Source: ParkinsonsUK-UCL
  • signal transduction Source: ParkinsonsUK-UCL

Keywordsi

Molecular functionHydrolase, Transferase
LigandNAD, NADP

Enzyme and pathway databases

ReactomeiR-HSA-163125 Post-translational modification: synthesis of GPI-anchored proteins
R-HSA-196807 Nicotinate metabolism
R-HSA-6798695 Neutrophil degranulation

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2 (EC:3.2.2.6)
Alternative name(s):
ADP-ribosyl cyclase 2
Bone marrow stromal antigen 1
Short name:
BST-1
Cyclic ADP-ribose hydrolase 2
Short name:
cADPr hydrolase 2
CD_antigen: CD157
Gene namesi
Name:BST1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000109743.10
HGNCiHGNC:1118 BST1
MIMi600387 gene
neXtProtiNX_Q10588

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi683
OpenTargetsiENSG00000109743
PharmGKBiPA25435

Chemistry databases

DrugBankiDB01660 Adenosine-5'-Diphosphate Monothiophosphate
DB02483 Etheno-Nad
DB03732 Etheno-Nadp
DB02701 Nicotinamide
DB03227 Nicotinamide Mononucleotide

Polymorphism and mutation databases

BioMutaiBST1
DMDMi116241273

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000000403229 – 293ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2Add BLAST265
PropeptideiPRO_0000004033294 – 318Removed in mature formSequence analysisAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 67
Glycosylationi66N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi83 ↔ 163
Glycosylationi95N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi144 ↔ 157
Glycosylationi148N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi192N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi238 ↔ 259
Disulfide bondi271 ↔ 280
Lipidationi293GPI-anchor amidated alanineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ10588
PaxDbiQ10588
PeptideAtlasiQ10588
PRIDEiQ10588

PTM databases

iPTMnetiQ10588
PhosphoSitePlusiQ10588

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSG00000109743
CleanExiHS_BST1
ExpressionAtlasiQ10588 baseline and differential
GenevisibleiQ10588 HS

Organism-specific databases

HPAiHPA050121

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi107148, 14 interactors
IntActiQ10588, 2 interactors
STRINGi9606.ENSP00000265016

Structurei

Secondary structure

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 57Combined sources15
Helixi60 – 62Combined sources3
Helixi67 – 74Combined sources8
Helixi75 – 78Combined sources4
Helixi87 – 90Combined sources4
Helixi91 – 97Combined sources7
Beta strandi106 – 111Combined sources6
Helixi113 – 120Combined sources8
Turni121 – 124Combined sources4
Helixi129 – 131Combined sources3
Helixi133 – 136Combined sources4
Turni137 – 140Combined sources4
Beta strandi147 – 152Combined sources6
Beta strandi154 – 157Combined sources4
Turni160 – 162Combined sources3
Helixi167 – 181Combined sources15
Beta strandi185 – 192Combined sources8
Beta strandi202 – 204Combined sources3
Helixi205 – 209Combined sources5
Helixi211 – 213Combined sources3
Helixi216 – 218Combined sources3
Beta strandi219 – 227Combined sources9
Helixi242 – 252Combined sources11
Beta strandi257 – 261Combined sources5
Helixi264 – 271Combined sources8
Helixi278 – 280Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ISFX-ray2.50A/B33-297[»]
1ISGX-ray2.60A/B33-297[»]
1ISHX-ray2.40A/B33-297[»]
1ISIX-ray2.10A/B33-297[»]
1ISJX-ray2.30A/B33-297[»]
1ISMX-ray3.00A/B33-297[»]
ProteinModelPortaliQ10588
SMRiQ10588
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10588

Family & Domainsi

Sequence similaritiesi

Belongs to the ADP-ribosyl cyclase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IP4Q Eukaryota
ENOG4111W33 LUCA
GeneTreeiENSGT00390000017291
HOGENOMiHOG000293141
HOVERGENiHBG097049
InParanoidiQ10588
KOiK18152
PhylomeDBiQ10588
TreeFamiTF332530

Family and domain databases

CDDicd04759 Rib_hydrolase, 1 hit
InterProiView protein in InterPro
IPR003193 ADP-ribosyl_cyclase
PANTHERiPTHR10912 PTHR10912, 1 hit
PfamiView protein in Pfam
PF02267 Rib_hydrolayse, 1 hit

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q10588-1) [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
MAAQGCAASR LLQLLLQLLL LLLLLAAGGA RARWRGEGTS AHLRDIFLGR
60 70 80 90 100
CAEYRALLSP EQRNKNCTAI WEAFKVALDK DPCSVLPSDY DLFINLSRHS
110 120 130 140 150
IPRDKSLFWE NSHLLVNSFA DNTRRFMPLS DVLYGRVADF LSWCRQKNDS
160 170 180 190 200
GLDYQSCPTS EDCENNPVDS FWKRASIQYS KDSSGVIHVM LNGSEPTGAY
210 220 230 240 250
PIKGFFADYE IPNLQKEKIT RIEIWVMHEI GGPNVESCGE GSMKVLEKRL
260 270 280 290 300
KDMGFQYSCI NDYRPVKLLQ CVDHSTHPDC ALKSAAAATQ RKAPSLYTEQ
310
RAGLIIPLFL VLASRTQL
Length:318
Mass (Da):35,724
Last modified:October 17, 2006 - v2
Checksum:iE0DD04C89A8F4215
GO
Isoform 2 (identifier: Q10588-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     6-63: Missing.

Note: No experimental confirmation available.
Show »
Length:260
Mass (Da):29,326
Checksum:i143EE2A4949B11AB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti36G → A in BAA04885 (PubMed:8202488).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02843877A → V. Corresponds to variant dbSNP:rs2302466Ensembl.1
Natural variantiVAR_028439101I → V. Corresponds to variant dbSNP:rs6840615Ensembl.1
Natural variantiVAR_021964125R → H. Corresponds to variant dbSNP:rs2302465Ensembl.1
Natural variantiVAR_021965145R → Q. Corresponds to variant dbSNP:rs2302464Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0555076 – 63Missing in isoform 2. 1 PublicationAdd BLAST58

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21878 mRNA Translation: BAA04885.1
AB175627 mRNA Translation: BAE92566.1
BT019502 mRNA Translation: AAV38309.1
AK312497 mRNA Translation: BAG35399.1
AC114744 Genomic DNA Translation: AAY40930.1
CH471069 Genomic DNA Translation: EAW92744.1
BC012095 mRNA Translation: AAH12095.1
CCDSiCCDS3416.1 [Q10588-1]
PIRiI59301
RefSeqiNP_004325.2, NM_004334.2 [Q10588-1]
XP_011512183.1, XM_011513881.2 [Q10588-2]
UniGeneiHs.720344

Genome annotation databases

EnsembliENST00000265016; ENSP00000265016; ENSG00000109743 [Q10588-1]
GeneIDi683
KEGGihsa:683
UCSCiuc003goh.4 human [Q10588-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiBST1_HUMAN
AccessioniPrimary (citable) accession number: Q10588
Secondary accession number(s): B2R6A2
, Q1XII0, Q5U0K0, Q96EN3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: May 23, 2018
This is version 171 of the entry and version 2 of the sequence. See 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, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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