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P52961 (NAR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1

EC=2.4.2.31
Alternative name(s):
ADP-ribosyltransferase C2 and C3 toxin-like 1
Short name=ARTC1
Mono(ADP-ribosyl)transferase 1
CD_antigen=CD296
Gene names
Name:ART1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Has ADP-ribosyltransferase activity toward GLP1R. Ref.6

Catalytic activity

NAD+ + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine.

Subcellular location

Sarcoplasmic reticulum membrane; Lipid-anchorGPI-anchor.

Sequence similarities

Belongs to the Arg-specific ADP-ribosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 295273GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1
PRO_0000019311
Propeptide296 – 32732Removed in mature form Potential
PRO_0000019312

Sites

Active site2471 By similarity
Binding site1211NAD By similarity
Binding site1791NAD By similarity
Binding site2331NAD By similarity

Amino acid modifications

Lipidation2951GPI-anchor amidated serine Potential
Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 277 By similarity
Disulfide bond174 ↔ 224 By similarity

Natural variations

Natural variant1051P → L.
Corresponds to variant rs35123761 [ dbSNP | Ensembl ].
VAR_034125
Natural variant1261P → R.
Corresponds to variant rs35619488 [ dbSNP | Ensembl ].
VAR_034126
Natural variant2571L → P. Ref.1
Corresponds to variant rs2280134 [ dbSNP | Ensembl ].
VAR_053526

Sequences

Sequence LengthMass (Da)Tools
P52961 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: 8FDC568197031EA5

FASTA32736,335
        10         20         30         40         50         60 
MQMPAMMSLL LVSVGLMEAL QAQSHPITRR DLFSQEIQLD MALASFDDQY AGCAAAMTAA 

        70         80         90        100        110        120 
LPDLNHTEFQ ANQVYADSWT LASSQWQERQ ARWPEWSLSP TRPSPPPLGF RDEHGVALLA 

       130        140        150        160        170        180 
YTANSPLHKE FNAAVREAGR SRAHYLHHFS FKTLHFLLTE ALQLLGSGQR PPRCHQVFRG 

       190        200        210        220        230        240 
VHGLRFRPAG PRATVRLGGF ASASLKHVAA QQFGEDTFFG IWTCLGAPIK GYSFFPGEEE 

       250        260        270        280        290        300 
VLIPPFETFQ VINASRLAQG PARIYLRALG KHSTYNCEYI KDKKCKSGPC HLDNSAMGQS 

       310        320 
PLSAVWSLLL LLWFLVVRAF PDGPGLL 

« Hide

References

« Hide 'large scale' references
[1]"Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases."
Okazaki I.J., Zolkiewska A., Nightingale M.S., Moss J.
Biochemistry 33:12828-12836(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-257.
Tissue: Skeletal muscle.
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
[4]"Conservation of the ART gene family across mammalian species."
Kuehl M., Glowacki G., Haag F., Koch-Nolte F.
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-223.
[5]"Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[6]"Glucagon like-peptide-1 receptor is covalently modified by endogenous mono-ADP-ribosyltransferase."
Dezelak M., Bavec A.
Mol. Biol. Rep. 39:4375-4381(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S74683 mRNA. Translation: AAB32387.1.
CH471158 Genomic DNA. Translation: EAX02559.1.
BC069102 mRNA. Translation: AAH69102.1.
BC111729 mRNA. Translation: AAI11730.1.
AJ291430 mRNA. Translation: CAC69964.1.
CCDSCCDS7744.1.
PIRA55966.
RefSeqNP_004305.2. NM_004314.2.
XP_005252990.1. XM_005252933.2.
UniGeneHs.382188.

3D structure databases

ProteinModelPortalP52961.
SMRP52961. Positions 37-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000250693.

Chemistry

ChEMBLCHEMBL2158.
DrugBankDB00102. Becaplermin.

PTM databases

PhosphoSiteP52961.

Polymorphism databases

DMDM206729882.

Proteomic databases

PaxDbP52961.
PRIDEP52961.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250693; ENSP00000250693; ENSG00000129744.
GeneID417.
KEGGhsa:417.
UCSCuc001lye.1. human.

Organism-specific databases

CTD417.
GeneCardsGC11P003666.
H-InvDBHIX0035913.
HGNCHGNC:723. ART1.
HPAHPA051148.
MIM601625. gene.
neXtProtNX_P52961.
PharmGKBPA25014.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40339.
HOGENOMHOG000273888.
HOVERGENHBG004464.
InParanoidP52961.
KOK06716.
OMACLGAPIK.
OrthoDBEOG7D85WV.
PhylomeDBP52961.
TreeFamTF335356.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeP52961.
CleanExHS_ART1.
GenevestigatorP52961.

Family and domain databases

InterProIPR000768. ART.
[Graphical view]
PANTHERPTHR10339. PTHR10339. 1 hit.
PfamPF01129. ART. 1 hit.
[Graphical view]
PRINTSPR00970. RIBTRNSFRASE.
PROSITEPS01291. ART. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi417.
NextBio1763.
PROP52961.
SOURCESearch...

Entry information

Entry nameNAR1_HUMAN
AccessionPrimary (citable) accession number: P52961
Secondary accession number(s): Q6NTD2, Q96KT9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries