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Protein

[Protein ADP-ribosylarginine] hydrolase-like protein 1

Gene

Adprhl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Seems not to catalyse the hydrolysis of O-acetyl-ADP-ribose.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
[Protein ADP-ribosylarginine] hydrolase-like protein 1 (EC:3.2.-.-)
Alternative name(s):
ADP-ribosylhydrolase 2
Gene namesi
Name:Adprhl1
Synonyms:Arh2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2442168. Adprhl1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353[Protein ADP-ribosylarginine] hydrolase-like protein 1PRO_0000277607Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BGK2.
PaxDbiQ8BGK2.
PRIDEiQ8BGK2.

PTM databases

iPTMnetiQ8BGK2.
PhosphoSiteiQ8BGK2.

Expressioni

Gene expression databases

BgeeiQ8BGK2.
CleanExiMM_ADPRHL1.
ExpressionAtlasiQ8BGK2. baseline and differential.
GenevisibleiQ8BGK2. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8BGK2. 1 interaction.
MINTiMINT-4110342.
STRINGi10090.ENSMUSP00000033825.

Structurei

3D structure databases

ProteinModelPortaliQ8BGK2.
SMRiQ8BGK2. Positions 1-352.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ADP-ribosylglycohydrolase family.Curated

Phylogenomic databases

eggNOGiENOG410IEA9. Eukaryota.
ENOG410XPXD. LUCA.
GeneTreeiENSGT00530000063627.
HOGENOMiHOG000007974.
HOVERGENiHBG050462.
InParanoidiQ8BGK2.
OMAiVGMRYWQ.
OrthoDBiEOG7SFHWT.
PhylomeDBiQ8BGK2.
TreeFamiTF329417.

Family and domain databases

InterProiIPR012108. ADP-ribosylarg_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
PIRSFiPIRSF016939. ADP_ribslarg_hdr. 1 hit.
SUPFAMiSSF101478. SSF101478. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BGK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKFKAAMLL GSVGDALGYG NICRENSVLG SIQEELQKTG GLDSLVLSPG
60 70 80 90 100
RWPVSDNTIM HMATAEALTT DYWCLDDLYR EMVKRYVETV ETLSEHRPDP
110 120 130 140 150
STIEGCSQLK PDNYLLAWHT PFSEKGSGFG AATKAMCIGM RYWKPERLET
160 170 180 190 200
LIEVSIECGR MTHNHPTGFL GSLCTALFAS YALQGKPLVQ WGREMLKVLP
210 220 230 240 250
LAEEYCRKTI RHMAEYQEHW FYFEAKWQFY LEERKIREDA EDKVTFPDNY
260 270 280 290 300
DAEERDKTYK KWSSEGRGGR RGHDAPMIAY DALLASGSNW TELCQRAMFH
310 320 330 340 350
GGESGATGTI AGCLFGLLHG LATVPRGLYQ ELEHKGRLED LGAALHRLST

EEK
Length:353
Mass (Da):39,885
Last modified:March 1, 2003 - v1
Checksum:i8FDDDECDE80F5D2A
GO

Sequence cautioni

The sequence BAC38332.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ427360 mRNA. Translation: CAD20462.1.
AK081786 mRNA. Translation: BAC38332.1. Different initiation.
AK084501 mRNA. Translation: BAC39199.1.
BC063759 mRNA. Translation: AAH63759.1.
CCDSiCCDS22108.1.
RefSeqiNP_766338.1. NM_172750.3.
UniGeneiMm.132785.

Genome annotation databases

EnsembliENSMUST00000033825; ENSMUSP00000033825; ENSMUSG00000031448.
GeneIDi234072.
KEGGimmu:234072.
UCSCiuc009kxf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ427360 mRNA. Translation: CAD20462.1.
AK081786 mRNA. Translation: BAC38332.1. Different initiation.
AK084501 mRNA. Translation: BAC39199.1.
BC063759 mRNA. Translation: AAH63759.1.
CCDSiCCDS22108.1.
RefSeqiNP_766338.1. NM_172750.3.
UniGeneiMm.132785.

3D structure databases

ProteinModelPortaliQ8BGK2.
SMRiQ8BGK2. Positions 1-352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BGK2. 1 interaction.
MINTiMINT-4110342.
STRINGi10090.ENSMUSP00000033825.

PTM databases

iPTMnetiQ8BGK2.
PhosphoSiteiQ8BGK2.

Proteomic databases

MaxQBiQ8BGK2.
PaxDbiQ8BGK2.
PRIDEiQ8BGK2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033825; ENSMUSP00000033825; ENSMUSG00000031448.
GeneIDi234072.
KEGGimmu:234072.
UCSCiuc009kxf.1. mouse.

Organism-specific databases

CTDi113622.
MGIiMGI:2442168. Adprhl1.

Phylogenomic databases

eggNOGiENOG410IEA9. Eukaryota.
ENOG410XPXD. LUCA.
GeneTreeiENSGT00530000063627.
HOGENOMiHOG000007974.
HOVERGENiHBG050462.
InParanoidiQ8BGK2.
OMAiVGMRYWQ.
OrthoDBiEOG7SFHWT.
PhylomeDBiQ8BGK2.
TreeFamiTF329417.

Miscellaneous databases

NextBioi382002.
PROiQ8BGK2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGK2.
CleanExiMM_ADPRHL1.
ExpressionAtlasiQ8BGK2. baseline and differential.
GenevisibleiQ8BGK2. MM.

Family and domain databases

InterProiIPR012108. ADP-ribosylarg_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
PIRSFiPIRSF016939. ADP_ribslarg_hdr. 1 hit.
SUPFAMiSSF101478. SSF101478. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse."
    Glowacki G., Braren R., Firner K., Nissen M., Kuehl M., Reche P., Bazan J.F., Cetkovic-Cvrlje M., Leiter E., Haag F., Koch-Nolte F.
    Protein Sci. 11:1657-1670(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head and Heart.
  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].
    Tissue: Jaw and Limb.
  4. "The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases."
    Ono T., Kasamatsu A., Oka S., Moss J.
    Proc. Natl. Acad. Sci. U.S.A. 103:16687-16691(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart.

Entry informationi

Entry nameiARHL1_MOUSE
AccessioniPrimary (citable) accession number: Q8BGK2
Secondary accession number(s): Q8C4L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: March 1, 2003
Last modified: January 20, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.