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Protein

Low molecular weight phosphotyrosine protein phosphatase

Gene

Acp1

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

Functioni

Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.By similarity

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.By similarity
A phosphate monoester + H2O = an alcohol + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei13 – 131NucleophileBy similarity
Active sitei19 – 191By similarity
Active sitei130 – 1301Proton donorBy similarity

GO - Molecular functioni

  • acid phosphatase activity Source: MGI
  • non-membrane spanning protein tyrosine phosphatase activity Source: InterPro
  • phosphatase activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Low molecular weight phosphotyrosine protein phosphatase (EC:3.1.3.48)
Short name:
LMW-PTP
Short name:
LMW-PTPase
Alternative name(s):
Low molecular weight cytosolic acid phosphatase (EC:3.1.3.2)
Gene namesi
Name:Acp1
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:87881. Acp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 158157Low molecular weight phosphotyrosine protein phosphatasePRO_0000046559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei132 – 1321PhosphotyrosineBy similarity
Modified residuei133 – 1331PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9D358.
PaxDbiQ9D358.
PRIDEiQ9D358.

2D gel databases

REPRODUCTION-2DPAGEQ9D358.

PTM databases

PhosphoSiteiQ9D358.

Expressioni

Tissue specificityi

Widely expressed with highest levels in brain and liver and lowest levels in muscle.1 Publication

Gene expression databases

BgeeiQ9D358.
CleanExiMM_ACP1.
ExpressionAtlasiQ9D358. baseline and differential.
GenevisibleiQ9D358. MM.

Interactioni

Subunit structurei

Interacts with the SH3 domain of SPTAN1. Interacts with EPHA2; dephosphorylates EPHA2. Interacts with EPHB1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi197927. 1 interaction.
IntActiQ9D358. 2 interactions.
MINTiMINT-1855654.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1812Combined sources
Helixi19 – 3315Combined sources
Helixi37 – 393Combined sources
Beta strandi40 – 4910Combined sources
Turni50 – 534Combined sources
Helixi58 – 669Combined sources
Helixi80 – 856Combined sources
Beta strandi87 – 937Combined sources
Helixi94 – 10512Combined sources
Beta strandi113 – 1164Combined sources
Helixi117 – 1204Combined sources
Helixi136 – 15722Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P4UX-ray1.90A/B/C/D2-158[»]
ProteinModelPortaliQ9D358.
SMRiQ9D358. Positions 6-158.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0394.
GeneTreeiENSGT00500000044891.
HOGENOMiHOG000273094.
HOVERGENiHBG007540.
InParanoidiQ9D358.
KOiK14394.
OrthoDBiEOG7QZGCG.
PhylomeDBiQ9D358.
TreeFamiTF353727.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF15. PTHR11717:SF15. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 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 11 Publication (identifier: Q9D358-1) [UniParc]FASTAAdd to basket

Also known as: m-IF11 Publication

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
MAEVGSKSVL FVCLGNICRS PIAEAVFRKL VTDEKVSDNW RIDSAATSTY
60 70 80 90 100
EVGNPPDYRG QNCMRKHGIH MQHIARQITK EDFATFDYIL CMDESNLRDL
110 120 130 140 150
NRKSNQVKNC KAKIELLGSY DPQKQLIIED PYYGNDSDFE VVYQQCLRCC

KAFLEKTY
Length:158
Mass (Da):18,192
Last modified:January 23, 2007 - v3
Checksum:iA374BE5C183226AE
GO
Isoform 21 Publication (identifier: Q9D358-2) [UniParc]FASTAAdd to basket

Also known as: m-IF21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     41-74: RIDSAATSTYEVGNPPDYRGQNCMRKHGIHMQHI → AIDSSAVSDWNVGRPPDPRAVSCLRNRGISTAHK

Show »
Length:158
Mass (Da):17,941
Checksum:iA2A1AF4BF774889E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141L → P.1 Publication
Natural varianti157 – 1571T → P.1 Publication
Isoform 21 Publication (identifier: Q9D358-2)
Natural varianti67 – 671R → H.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei41 – 7434RIDSA…HMQHI → AIDSSAVSDWNVGRPPDPRA VSCLRNRGISTAHK in isoform 2. 3 PublicationsVSP_050726Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17343 mRNA. Translation: CAA76753.1.
Y17344 mRNA. Translation: CAA76754.1.
Y17345 mRNA. Translation: CAA76755.1.
AK014603 mRNA. Translation: BAB29458.1.
AK018329 mRNA. Translation: BAB31164.1.
AK019186 mRNA. Translation: BAB31593.1.
AK082955 mRNA. Translation: BAC38707.1.
BC039744 mRNA. Translation: AAH39744.1.
CCDSiCCDS36427.1. [Q9D358-1]
CCDS49045.1. [Q9D358-2]
RefSeqiNP_001103709.1. NM_001110239.1.
NP_067305.2. NM_021330.4. [Q9D358-1]
XP_006542863.1. XM_006542800.2. [Q9D358-1]
UniGeneiMm.359831.

Genome annotation databases

EnsembliENSMUST00000062740; ENSMUSP00000106509; ENSMUSG00000044573. [Q9D358-1]
GeneIDi102642088.
11431.
KEGGimmu:102642088.
mmu:11431.
UCSCiuc007ngw.2. mouse. [Q9D358-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17343 mRNA. Translation: CAA76753.1.
Y17344 mRNA. Translation: CAA76754.1.
Y17345 mRNA. Translation: CAA76755.1.
AK014603 mRNA. Translation: BAB29458.1.
AK018329 mRNA. Translation: BAB31164.1.
AK019186 mRNA. Translation: BAB31593.1.
AK082955 mRNA. Translation: BAC38707.1.
BC039744 mRNA. Translation: AAH39744.1.
CCDSiCCDS36427.1. [Q9D358-1]
CCDS49045.1. [Q9D358-2]
RefSeqiNP_001103709.1. NM_001110239.1.
NP_067305.2. NM_021330.4. [Q9D358-1]
XP_006542863.1. XM_006542800.2. [Q9D358-1]
UniGeneiMm.359831.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P4UX-ray1.90A/B/C/D2-158[»]
ProteinModelPortaliQ9D358.
SMRiQ9D358. Positions 6-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197927. 1 interaction.
IntActiQ9D358. 2 interactions.
MINTiMINT-1855654.

PTM databases

PhosphoSiteiQ9D358.

2D gel databases

REPRODUCTION-2DPAGEQ9D358.

Proteomic databases

MaxQBiQ9D358.
PaxDbiQ9D358.
PRIDEiQ9D358.

Protocols and materials databases

DNASUi11431.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062740; ENSMUSP00000106509; ENSMUSG00000044573. [Q9D358-1]
GeneIDi102642088.
11431.
KEGGimmu:102642088.
mmu:11431.
UCSCiuc007ngw.2. mouse. [Q9D358-1]

Organism-specific databases

CTDi52.
MGIiMGI:87881. Acp1.

Phylogenomic databases

eggNOGiCOG0394.
GeneTreeiENSGT00500000044891.
HOGENOMiHOG000273094.
HOVERGENiHBG007540.
InParanoidiQ9D358.
KOiK14394.
OrthoDBiEOG7QZGCG.
PhylomeDBiQ9D358.
TreeFamiTF353727.

Miscellaneous databases

NextBioi278712.
PROiQ9D358.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D358.
CleanExiMM_ACP1.
ExpressionAtlasiQ9D358. baseline and differential.
GenevisibleiQ9D358. MM.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF15. PTHR11717:SF15. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of murine low molecular weight phosphotyrosine protein phosphatase cDNA: identification of a new isoform."
    Magherini F., Giannoni E., Raugei G., Cirri P., Paoli P., Modesti A., Camici G., Ramponi G.
    FEBS Lett. 437:263-266(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANTS PRO-14 AND PRO-157.
    Tissue: LiverImported.
  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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo, Skin and Spinal cord.
  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] (ISOFORM 2).
    Strain: FVB/NImported.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-158.

Entry informationi

Entry nameiPPAC_MOUSE
AccessioniPrimary (citable) accession number: Q9D358
Secondary accession number(s): O88739, O88740, Q9QWF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.