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UniProtKB/Swiss-Prot entry P24666


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PPAC_HUMAN
Primary accession number P24666
Secondary accession numbers P24667 Q16035 Q16036 Q16725 Q53RU0
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 101)
Name and origin of the protein
Protein name Low molecular weight phosphotyrosine protein phosphatase
Synonyms LMW-PTPase
LMW-PTP
EC 3.1.3.48
Low molecular weight cytosolic acid phosphatase
EC 3.1.3.2
Red cell acid phosphatase 1
Adipocyte acid phosphatase
Gene name
Name: ACP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE (ALLELE B; ISOFORMS 1 AND 2).
PubMed=1939112 [NCBI, ExPASy, EBI, Israel, Japan]
Dissing J., Johnsen A.H., Sensabaugh G.F.;
"Human red cell acid phosphatase (ACP1). The amino acid sequence of the two isozymes Bf and Bs encoded by the ACP1*B allele.";
J. Biol. Chem. 266:20619-20625(1991).
[2]
PROTEIN SEQUENCE (ALLELES A AND C; ISOFORMS 1 AND 2).
DOI=10.1016/0167-4838(92)90155-7; PubMed=1627603 [NCBI, ExPASy, EBI, Israel, Japan]
Dissing J., Johnsen A.H.;
"Human red cell acid phosphatase (ACP1): the primary structure of the two pairs of isozymes encoded by the ACP1*A and ACP1*C alleles.";
Biochim. Biophys. Acta 1121:261-268(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=1587862 [NCBI, ExPASy, EBI, Israel, Japan]
Wo Y.-Y.P., McCormack A.L., Shabonowitz J., Hunt D.F., Davis J.P., Mitchell G.L., van Etten R.L.;
"Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase.";
J. Biol. Chem. 267:10856-10865(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/geno.1995.9893; PubMed=8586411 [NCBI, ExPASy, EBI, Israel, Japan]
Bryson G.L.M., Massa H., Trask B.J., van Etten R.L.;
"Gene structure, sequence, and chromosomal localization of the human red cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene, ACP1.";
Genomics 30:133-140(1995).
[5]
NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
TISSUE=Adipocyte;
PubMed=1304913 [NCBI, ExPASy, EBI, Israel, Japan]
Shekels L.L., Smith A.J., van Etten R.L., Bernlohr D.A.;
"Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase.";
Protein Sci. 1:710-721(1992).
[6]
NUCLEOTIDE SEQUENCE (ISOFORM 2), TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-132 AND TYR-133, AND MUTAGENESIS OF CYS-13; TYR-132 AND TYR-133.
DOI=10.1074/jbc.272.39.24480; PubMed=9038134 [NCBI, ExPASy, EBI, Israel, Japan]
Tailor P., Gilman J., Williams S., Couture C., Mustelin T.;
"Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132.";
J. Biol. Chem. 272:5371-5374(1997).
[7]
NUCLEOTIDE SEQUENCE (ISOFORM 3).
PubMed=10336608 [NCBI, ExPASy, EBI, Israel, Japan]
Tailor P., Gilman J., Williams S., Mustelin T.;
"A novel isoform of the low molecular weight phosphotyrosine phosphatase, LMPTP-C, arising from alternative mRNA splicing.";
Eur. J. Biochem. 262:277-282(1999).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.;
"NEDO human cDNA sequencing project.";
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
PROTEIN SEQUENCE OF 42-59, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-158 (ISOFORMS 1/2).
TISSUE=Blood;
DOI=10.1093/hmg/2.7.1079-a; PubMed=8364553 [NCBI, ExPASy, EBI, Israel, Japan]
Sensabaugh G.F., Lazaruk K.A.;
"A TaqI site identifies the *A allele at the ACP1 locus.";
Hum. Mol. Genet. 2:1079-1079(1993).
[15]
INTERACTION WITH SPTAN1.
DOI=10.1128/MCB.22.10.3527-3536.2002; PubMed=11971983 [NCBI, ExPASy, EBI, Israel, Japan]
Nicolas G., Fournier C.M., Galand C., Malbert-Colas L., Bournier O., Kroviarski Y., Bourgeois M., Camonis J.H., Dhermy D., Grandchamp B., Lecomte M.-C.;
"Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain.";
Mol. Cell. Biol. 22:3527-3536(2002).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[18]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1074/jbc.273.34.21714; PubMed=9705307 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang M., Stauffacher C.V., Lin D., van Etten R.L.;
"Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity.";
J. Biol. Chem. 273:21714-21720(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M83653; AAB59354.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M83654; AAB59355.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U25849; AAC52067.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U25847; AAC52067.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U25848; AAC52067.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S62884; AAB27085.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S62885; AAB27086.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M87545; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
BT007136; AAP35800.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291861; BAF84550.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC079779; AAY14958.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471053; EAX01112.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007422; AAH07422.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L06508; AAB59628.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38148; A38148.
B38148; B38148.
RefSeq NP_004291.1; -.
NP_009030.1; -.
UniGene Hs.558296
3D structure databases
PDB
1XWW; X-ray; 1.63 A; A=1-158.[ExPASy / RCSB / EBI]
5PNT; X-ray; 2.20 A; A=1-158.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1XWW; -.
5PNT; -.
ModBase P24666.
Protein-protein interaction databases
IntAct P24666; -.
PTM databases
PhosphoSite P24666; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00218847; -.
IPI00219861; -.
Organism-specific databases
H-InvDB HIX0001778; -.
HGNC HGNC:122; ACP1.
GenAtlas ACP1.
HPA HPA016754; -.
MIM 171500; gene. [NCBI / EBI]
PharmGKB PA24446; -.
GeneCards P24666.
Gene expression databases
ArrayExpress P24666; -.
CleanEx HS_ACP1; -.
GermOnline ENSG00000143727; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0003993; Molecular function: acid phosphatase activity (traceable author statement from ProtInc).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004726; Molecular function: non-membrane spanning protein tyrosine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0006470; Biological process: protein amino acid dephosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000106; Tyr_Pase_low_mol_wt.
IPR002115; Tyr_Pase_low_mol_wt_mml.
Graphical view of domain structure.
PANTHER PTHR11717; Low_mwt_PTPase; 1.
Pfam PF01451; LMWPc; 1.
Pfam graphical view of domain structure.
PRINTS PR00719; LMWPTPASE.
PR00720; MAMMALPTPASE.
SMART SM00226; LMWPc; 1.
SMART graphical view of domain structure.
ProtoNet P24666.
Genome annotation databases
Ensembl ENSG00000143727; Homo sapiens. [Contig view]
GeneID 52; -.
Phylogenomic databases
HOVERGEN P24666; -.
Other
NextBio 205; -.
SOURCE ACP1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing; Hydrolase; Phosphoprotein; Polymorphism; Protein phosphatase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   158  157     Low molecular weight phosphotyrosine protein phosphatase. PRO_0000046558
ACT_SITE   13    13        Nucleophile (By similarity). 
ACT_SITE   19    19        By similarity. 
ACT_SITE   130   130        Proton donor (By similarity). 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   132   132        Phosphotyrosine. 
MOD_RES   133   133        Phosphotyrosine. 
VAR_SEQ   41    74        RVDSAATSGYEIGNPPDYRGQSCMKRHGIPMSHV -> VIDSGAVSDWNVGRSPDPRAVSCLRNHGIHTAHK (in isoform 2). VSP_010087
VAR_SEQ   41    74        Missing (in isoform 3). VSP_010088
VARIANT   106   106  1     Q -> R (in allele ACP1*A). VAR_006171 [3D]
MUTAGEN   13    13        C->S: Inactive. 
MUTAGEN   132   132        Y->F: Reduced phosphorylation and activity. 
MUTAGEN   133   133        Y->F: Reduced phosphorylation. No effect on activity. 
CONFLICT   2     6        AEQAT -> PRRGR (in Ref. 5; AAB27086). 
CONFLICT   13    20        CLGNICRS -> PARREAAR (in Ref. 5; AAB27085). 
CONFLICT   32    32        T -> W (in Ref. 1 and 2). 
STRAND   7    18  12      
HELIX   19    33  15      
HELIX   37    39  3      
STRAND   40    49  10      
TURN   50    53  4      
HELIX   58    66  9      
HELIX   80    85  6      
STRAND   87    93  7      
HELIX   94   105  12      
STRAND   113   116  4      
HELIX   117   120  4      
HELIX   136   156  21      
Sequence information
Length: 158 AA [This is the length of the unprocessed precursor] Molecular weight: 18042 Da [This is the MW of the unprocessed precursor] CRC64: 46617BD799313EED [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW RVDSAATSGY EIGNPPDYRG 

        70         80         90        100        110        120 
QSCMKRHGIP MSHVARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY 

       130        140        150 
DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH 

P24666 in FASTA format

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