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Protein

Phospholysine phosphohistidine inorganic pyrophosphate phosphatase

Gene

Lhpp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Phosphatase that hydrolyzes imidodiphosphate, 3-phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency (By similarity).By similarity

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171MagnesiumBy similarity
Metal bindingi19 – 191Magnesium; via carbonyl oxygenBy similarity
Binding sitei189 – 1891SubstrateBy similarity
Metal bindingi214 – 2141MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-73817. Purine ribonucleoside monophosphate biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (EC:3.1.3.-, EC:3.6.1.1)
Gene namesi
Name:Lhpp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1923679. Lhpp.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Phospholysine phosphohistidine inorganic pyrophosphate phosphatasePRO_0000305075Add
BLAST

Proteomic databases

EPDiQ9D7I5.
MaxQBiQ9D7I5.
PaxDbiQ9D7I5.
PeptideAtlasiQ9D7I5.
PRIDEiQ9D7I5.

PTM databases

iPTMnetiQ9D7I5.
PhosphoSiteiQ9D7I5.

Expressioni

Gene expression databases

BgeeiQ9D7I5.
CleanExiMM_2310007H09RIK.
GenevisibleiQ9D7I5. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9D7I5. 1 interaction.
MINTiMINT-4127446.
STRINGi10090.ENSMUSP00000033241.

Structurei

3D structure databases

ProteinModelPortaliQ9D7I5.
SMRiQ9D7I5. Positions 1-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 193Substrate bindingBy similarity
Regioni54 – 552Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the HAD-like hydrolase superfamily.Curated

Phylogenomic databases

eggNOGiKOG3040. Eukaryota.
COG0647. LUCA.
GeneTreeiENSGT00510000046678.
HOGENOMiHOG000068106.
HOVERGENiHBG075146.
InParanoidiQ9D7I5.
KOiK11725.
OMAiRPYLLIH.
OrthoDBiEOG7P2XT1.
PhylomeDBiQ9D7I5.
TreeFamiTF314344.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR006355. HAD-SF_hydro_IIA_hyp2.
IPR023215. NPhePase-like_dom.
[Graphical view]
PfamiPF13344. Hydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01458. HAD-SF-IIA-hyp3. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9D7I5-1) [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
MAAWAERLTG VRGVLLDISG VLCDSSASGA TAIAGSVEAV ARLKQSPLKV
60 70 80 90 100
RFCTNESQKS LRELVGVLQQ LGFDISEEEV TAPAPATCQI LKERGLRPHL
110 120 130 140 150
LIHEGVRSEF DDIDMSNPNC VVIADAGEAF SYQNMNRAFQ VLMELENPVL
160 170 180 190 200
ISLGKGRYYK ETSGLMLDVG GYMKALEYAC GIKAEVVGKP SPEFFKSALQ
210 220 230 240 250
AIGVEAHQAI MIGDDIVGDV GGAQQCGMRA LQVRTGKFRP GDEHHPEVQA
260 270
DGYVDNLAEA VDLLLKYTDK
Length:270
Mass (Da):29,144
Last modified:June 1, 2001 - v1
Checksum:i19A258715AA668B5
GO
Isoform 2 (identifier: Q9D7I5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     241-242: GD → RC
     243-270: Missing.

Note: No experimental confirmation available.
Show »
Length:242
Mass (Da):26,066
Checksum:iDB88C89EB1A9A690
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei241 – 2422GD → RC in isoform 2. 1 PublicationVSP_028214
Alternative sequencei243 – 27028Missing in isoform 2. 1 PublicationVSP_028215Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009207 mRNA. Translation: BAB26140.1.
AK140229 mRNA. Translation: BAE24290.1.
BC065789 mRNA. Translation: AAH65789.1.
CCDSiCCDS21925.1. [Q9D7I5-1]
RefSeqiNP_083885.1. NM_029609.1. [Q9D7I5-1]
UniGeneiMm.276721.

Genome annotation databases

EnsembliENSMUST00000033241; ENSMUSP00000033241; ENSMUSG00000030946. [Q9D7I5-1]
GeneIDi76429.
KEGGimmu:76429.
UCSCiuc009kce.1. mouse. [Q9D7I5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009207 mRNA. Translation: BAB26140.1.
AK140229 mRNA. Translation: BAE24290.1.
BC065789 mRNA. Translation: AAH65789.1.
CCDSiCCDS21925.1. [Q9D7I5-1]
RefSeqiNP_083885.1. NM_029609.1. [Q9D7I5-1]
UniGeneiMm.276721.

3D structure databases

ProteinModelPortaliQ9D7I5.
SMRiQ9D7I5. Positions 1-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D7I5. 1 interaction.
MINTiMINT-4127446.
STRINGi10090.ENSMUSP00000033241.

PTM databases

iPTMnetiQ9D7I5.
PhosphoSiteiQ9D7I5.

Proteomic databases

EPDiQ9D7I5.
MaxQBiQ9D7I5.
PaxDbiQ9D7I5.
PeptideAtlasiQ9D7I5.
PRIDEiQ9D7I5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033241; ENSMUSP00000033241; ENSMUSG00000030946. [Q9D7I5-1]
GeneIDi76429.
KEGGimmu:76429.
UCSCiuc009kce.1. mouse. [Q9D7I5-1]

Organism-specific databases

CTDi64077.
MGIiMGI:1923679. Lhpp.

Phylogenomic databases

eggNOGiKOG3040. Eukaryota.
COG0647. LUCA.
GeneTreeiENSGT00510000046678.
HOGENOMiHOG000068106.
HOVERGENiHBG075146.
InParanoidiQ9D7I5.
KOiK11725.
OMAiRPYLLIH.
OrthoDBiEOG7P2XT1.
PhylomeDBiQ9D7I5.
TreeFamiTF314344.

Enzyme and pathway databases

ReactomeiR-MMU-73817. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

PROiQ9D7I5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D7I5.
CleanExiMM_2310007H09RIK.
GenevisibleiQ9D7I5. MM.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR006355. HAD-SF_hydro_IIA_hyp2.
IPR023215. NPhePase-like_dom.
[Graphical view]
PfamiPF13344. Hydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01458. HAD-SF-IIA-hyp3. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Tongue.
  2. "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).
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiLHPP_MOUSE
AccessioniPrimary (citable) accession number: Q9D7I5
Secondary accession number(s): Q3USP1, Q6P070
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 103 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.