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Q3LIE5

- ADPRM_HUMAN

UniProt

Q3LIE5 - ADPRM_HUMAN

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Protein

Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase

Gene

ADPRM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline and CDP-ethanolamine, but not other non-reducing ADP-sugars or CDP-glucose. May be involved in immune cell signaling as suggested by the second-messenger role of ADP-ribose, which activates TRPM2 as a mediator of oxidative/nitrosative stress (By similarity).By similarity

Catalytic activityi

CDP-choline + H2O = CMP + phosphocholine.
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate.
CDP-glycerol + H2O = CMP + sn-glycerol 3-phosphate.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi25 – 251Zinc 1By similarity
Metal bindingi27 – 271Zinc 1By similarity
Metal bindingi74 – 741Zinc 1By similarity
Metal bindingi74 – 741Zinc 2By similarity
Metal bindingi110 – 1101Zinc 2By similarity
Metal bindingi241 – 2411Zinc 2By similarity
Metal bindingi278 – 2781Zinc 2By similarity
Metal bindingi280 – 2801Zinc 1By similarity

GO - Molecular functioni

  1. ADP-ribose diphosphatase activity Source: UniProtKB-EC
  2. CDP-glycerol diphosphatase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase (EC:3.6.1.13, EC:3.6.1.16, EC:3.6.1.53)
Alternative name(s):
ADPRibase-Mn
CDP-choline phosphohydrolase
Gene namesi
Name:ADPRM
Synonyms:C17orf48
ORF Names:MDS006, Nbla03831
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:30925. ADPRM.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672231.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342Manganese-dependent ADP-ribose/CDP-alcohol diphosphatasePRO_0000286567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ3LIE5.
PaxDbiQ3LIE5.
PRIDEiQ3LIE5.

PTM databases

PhosphoSiteiQ3LIE5.

Expressioni

Gene expression databases

BgeeiQ3LIE5.
CleanExiHS_C17orf48.
ExpressionAtlasiQ3LIE5. baseline and differential.
GenevestigatoriQ3LIE5.

Organism-specific databases

HPAiHPA023265.
HPA023820.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi121302. 1 interaction.
STRINGi9606.ENSP00000369099.

Structurei

3D structure databases

ProteinModelPortaliQ3LIE5.
SMRiQ3LIE5. Positions 17-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ADPRibase-Mn family.Curated

Phylogenomic databases

eggNOGiCOG1409.
GeneTreeiENSGT00390000014667.
HOGENOMiHOG000154875.
HOVERGENiHBG100432.
InParanoidiQ3LIE5.
KOiK01517.
OMAiLAWNYRD.
OrthoDBiEOG757CXK.
PhylomeDBiQ3LIE5.
TreeFamiTF331229.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3LIE5-1) [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
MDDKPNPEAL SDSSERLFSF GVIADVQFAD LEDGFNFQGT RRRYYRHSLL
60 70 80 90 100
HLQGAIEDWN NESSMPCCVL QLGDIIDGYN AQYNASKKSL ELVMDMFKRL
110 120 130 140 150
KVPVHHTWGN HEFYNFSREY LTHSKLNTKF LEDQIVHHPE TMPSEDYYAY
160 170 180 190 200
HFVPFPKFRF ILLDAYDLSV LGVDQSSPKY EQCMKILREH NPNTELNSPQ
210 220 230 240 250
GLSEPQFVQF NGGFSQEQLN WLNEVLTFSD TNQEKVVIVS HLPIYPDASD
260 270 280 290 300
NVCLAWNYRD ALAVIWSHEC VVCFFAGHTH DGGYSEDPFG VYHVNLEGVI
310 320 330 340
ETAPDSQAFG TVHVYPDKMM LKGRGRVPDR IMNYKKERAF HC
Length:342
Mass (Da):39,529
Last modified:November 8, 2005 - v1
Checksum:i2DBD4499D9DA2AC2
GO
Isoform 2 (identifier: Q3LIE5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     202-205: LSEP → ELFL
     206-342: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:205
Mass (Da):24,010
Checksum:iC830ED5DC8F1C833
GO

Sequence cautioni

The sequence AAF87317.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131F → S in BAF85318. (PubMed:15489334)Curated
Sequence conflicti202 – 2021L → F in AAF87317. (PubMed:12880961)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921L → R.
Corresponds to variant rs34940296 [ dbSNP | Ensembl ].
VAR_032125
Natural varianti337 – 3371E → G.
Corresponds to variant rs406446 [ dbSNP | Ensembl ].
VAR_032126

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei202 – 2054LSEP → ELFL in isoform 2. 2 PublicationsVSP_025092
Alternative sequencei206 – 342137Missing in isoform 2. 2 PublicationsVSP_025093Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073393 mRNA. Translation: BAE45723.1.
AK292629 mRNA. Translation: BAF85318.1.
CH471108 Genomic DNA. Translation: EAW89995.1.
CH471108 Genomic DNA. Translation: EAW89996.1.
BC001294 mRNA. Translation: AAH01294.1.
BC070155 mRNA. Translation: AAH70155.1.
AF168715 mRNA. Translation: AAF87317.1. Frameshift.
CCDSiCCDS11159.2. [Q3LIE5-1]
RefSeqiNP_064618.3. NM_020233.4. [Q3LIE5-1]
UniGeneiHs.47668.
Hs.708369.

Genome annotation databases

EnsembliENST00000379774; ENSP00000369099; ENSG00000170222. [Q3LIE5-1]
ENST00000468843; ENSP00000431622; ENSG00000170222. [Q3LIE5-3]
GeneIDi56985.
KEGGihsa:56985.
UCSCiuc002gmt.3. human. [Q3LIE5-1]

Polymorphism databases

DMDMi121942723.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073393 mRNA. Translation: BAE45723.1 .
AK292629 mRNA. Translation: BAF85318.1 .
CH471108 Genomic DNA. Translation: EAW89995.1 .
CH471108 Genomic DNA. Translation: EAW89996.1 .
BC001294 mRNA. Translation: AAH01294.1 .
BC070155 mRNA. Translation: AAH70155.1 .
AF168715 mRNA. Translation: AAF87317.1 . Frameshift.
CCDSi CCDS11159.2. [Q3LIE5-1 ]
RefSeqi NP_064618.3. NM_020233.4. [Q3LIE5-1 ]
UniGenei Hs.47668.
Hs.708369.

3D structure databases

ProteinModelPortali Q3LIE5.
SMRi Q3LIE5. Positions 17-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121302. 1 interaction.
STRINGi 9606.ENSP00000369099.

PTM databases

PhosphoSitei Q3LIE5.

Polymorphism databases

DMDMi 121942723.

Proteomic databases

MaxQBi Q3LIE5.
PaxDbi Q3LIE5.
PRIDEi Q3LIE5.

Protocols and materials databases

DNASUi 56985.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379774 ; ENSP00000369099 ; ENSG00000170222 . [Q3LIE5-1 ]
ENST00000468843 ; ENSP00000431622 ; ENSG00000170222 . [Q3LIE5-3 ]
GeneIDi 56985.
KEGGi hsa:56985.
UCSCi uc002gmt.3. human. [Q3LIE5-1 ]

Organism-specific databases

CTDi 56985.
GeneCardsi GC17P010600.
HGNCi HGNC:30925. ADPRM.
HPAi HPA023265.
HPA023820.
neXtProti NX_Q3LIE5.
PharmGKBi PA142672231.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1409.
GeneTreei ENSGT00390000014667.
HOGENOMi HOG000154875.
HOVERGENi HBG100432.
InParanoidi Q3LIE5.
KOi K01517.
OMAi LAWNYRD.
OrthoDBi EOG757CXK.
PhylomeDBi Q3LIE5.
TreeFami TF331229.

Miscellaneous databases

GenomeRNAii 56985.
NextBioi 62667.
PROi Q3LIE5.

Gene expression databases

Bgeei Q3LIE5.
CleanExi HS_C17orf48.
ExpressionAtlasi Q3LIE5. baseline and differential.
Genevestigatori Q3LIE5.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
    Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
    Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Neuroblastoma.
  2. "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] (ISOFORM 2).
    Tissue: Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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 2).
    Tissue: Placenta and Testis.
  5. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
    Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J., Gu J., Huang Q., Yu Y., Xu S., Ren S., Fu G.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-217 (ISOFORM 1).
    Tissue: Hematopoietic stem cell.
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiADPRM_HUMAN
AccessioniPrimary (citable) accession number: Q3LIE5
Secondary accession number(s): A8K9B4
, D3DTS4, Q9BVD4, Q9NRU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: November 8, 2005
Last modified: November 26, 2014
This is version 83 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

Keywords - Technical termi

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3