Full text data of PTP4A1
PTP4A1
(PRL1, PTPCAAX1)
[Confidence: low (only semi-automatic identification from reviews)]
Protein tyrosine phosphatase type IVA 1; 3.1.3.48 (PTP(CAAXI); Protein-tyrosine phosphatase 4a1; Protein-tyrosine phosphatase of regenerating liver 1; PRL-1; Flags: Precursor)
Protein tyrosine phosphatase type IVA 1; 3.1.3.48 (PTP(CAAXI); Protein-tyrosine phosphatase 4a1; Protein-tyrosine phosphatase of regenerating liver 1; PRL-1; Flags: Precursor)
UniProt
Q93096
ID TP4A1_HUMAN Reviewed; 173 AA.
AC Q93096; B2R6C8; O00648; Q49A54;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2005, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Protein tyrosine phosphatase type IVA 1;
DE EC=3.1.3.48;
DE AltName: Full=PTP(CAAXI);
DE AltName: Full=Protein-tyrosine phosphatase 4a1;
DE AltName: Full=Protein-tyrosine phosphatase of regenerating liver 1;
DE Short=PRL-1;
DE Flags: Precursor;
GN Name=PTP4A1; Synonyms=PRL1, PTPCAAX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND ISOPRENYLATION AT
RP CYS-170.
RC TISSUE=Mammary carcinoma;
RX PubMed=9018080; DOI=10.1016/S0304-3835(96)04459-X;
RA Cates C.A., Michael R.L., Stayrook K.R., Harvey K.A., Burke Y.D.,
RA Randall S.K., Crowell P.L., Crowell D.N.;
RT "Prenylation of oncogenic human PTP(CAAX) protein tyrosine
RT phosphatases.";
RL Cancer Lett. 110:49-55(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Regenerating liver;
RX PubMed=9642300; DOI=10.1074/jbc.273.27.17286;
RA Peng Y., Genin A., Spinner N.B., Diamond R.H., Taub R.;
RT "The gene encoding human nuclear protein tyrosine phosphatase, PRL-1.
RT Cloning, chromosomal localization, and identification of an intron
RT enhancer.";
RL J. Biol. Chem. 273:17286-17295(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-163.
RC TISSUE=Lung fibroblast;
RX PubMed=9633825;
RA Dayton M.A., Knobloch T.J.;
RT "Multiple phosphotyrosine phosphatase mRNAs are expressed in the human
RT lung fibroblast cell line WI-38.";
RL Recept. Signal Transduct. 7:241-256(1997).
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10940933;
RX DOI=10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J;
RA Gjoerloff-Wingren A., Saxena M., Han S., Wang X., Alonso A.,
RA Renedo M., Oh P., Williams S., Schnitzer J., Mustelin T.;
RT "Subcellular localization of intracellular protein tyrosine
RT phosphatases in T cells.";
RL Eur. J. Immunol. 30:2412-2421(2000).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-71;
RP ASP-72; CYS-104; CYS-170 AND CYS-171, INTERACTION WITH TUBULIN, AND
RP FUNCTION.
RX PubMed=12235145; DOI=10.1074/jbc.M206407200;
RA Wang J., Kirby C.E., Herbst R.;
RT "The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum
RT and the mitotic spindle and is required for normal mitosis.";
RL J. Biol. Chem. 277:46659-46668(2002).
RN [11]
RP ENZYME REGULATION.
RX PubMed=12516958;
RA Pathak M.K., Dhawan D., Lindner D.J., Borden E.C., Farver C., Yi T.;
RT "Pentamidine is an inhibitor of PRL phosphatases with anticancer
RT activity.";
RL Mol. Cancer Ther. 1:1255-1264(2002).
RN [12]
RP FUNCTION.
RX PubMed=14643450; DOI=10.1016/S0304-3835(03)00517-2;
RA Werner S.R., Lee P.A., DeCamp M.W., Crowell D.N., Randall S.K.,
RA Crowell P.L.;
RT "Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1)
RT by PRL tyrosine phosphatases.";
RL Cancer Lett. 202:201-211(2003).
RN [13]
RP FUNCTION.
RX PubMed=12782572;
RA Zeng Q., Dong J.-M., Guo K., Li J., Tan H.-X., Koh V., Pallen C.J.,
RA Manser E., Hong W.;
RT "PRL-3 and PRL-1 promote cell migration, invasion, and metastasis.";
RL Cancer Res. 63:2716-2722(2003).
RN [14]
RP INDUCTION.
RX PubMed=15501285; DOI=10.1016/j.toxicon.2004.07.018;
RA Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.;
RT "Potential effects of tetrodotoxin exposure to human glial cells
RT postulated using microarray approach.";
RL Toxicon 44:597-608(2004).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF MUTANT SER-104, DISULFIDE
RP BOND, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF THR-13 AND
RP GLN-131, AND MASS SPECTROMETRY.
RX PubMed=15571731; DOI=10.1016/j.jmb.2004.10.061;
RA Jeong D.G., Kim S.J., Kim J.H., Son J.H., Park M.R., Lim S.M.,
RA Yoon T.-S., Ryu S.E.;
RT "Trimeric structure of PRL-1 phosphatase reveals an active enzyme
RT conformation and regulation mechanisms.";
RL J. Mol. Biol. 345:401-413(2005).
CC -!- FUNCTION: Protein tyrosine phosphatase which stimulates
CC progression from G1 into S phase during mitosis. May play a role
CC in the development and maintenance of differentiating epithelial
CC tissues. Enhances cell proliferation, cell motility and invasive
CC activity, and promotes cancer metastasis.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- ENZYME REGULATION: Inhibited by sodium orthovanadate and
CC pentamidine.
CC -!- SUBUNIT: Homotrimer. Interacts with ATF5 (By similarity).
CC Interacts with tubulin.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Early endosome. Endoplasmic
CC reticulum. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Note=And
CC mitotic spindle.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow, lymph nodes, T
CC lymphocytes, spleen, thymus and tonsil. Overexpressed in tumor
CC cell lines.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver.
CC -!- INDUCTION: Strongly down-regulated upon tetrodotoxin treatment.
CC -!- PTM: Farnesylated. Farnesylation is required for membrane
CC targeting. Unfarnesylated forms are shifted into the nucleus.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR EMBL; U48296; AAB40597.1; -; mRNA.
DR EMBL; AF051160; AAC39836.1; -; Genomic_DNA.
DR EMBL; AK312526; BAG35425.1; -; mRNA.
DR EMBL; CR749458; CAH18292.1; -; mRNA.
DR EMBL; AL135905; CAC12761.1; -; Genomic_DNA.
DR EMBL; CH471143; EAW88494.1; -; Genomic_DNA.
DR EMBL; BC023975; AAH23975.1; -; mRNA.
DR EMBL; BC045571; AAH45571.1; -; mRNA.
DR EMBL; U69701; AAB09080.1; -; mRNA.
DR RefSeq; NP_003454.1; NM_003463.4.
DR UniGene; Hs.227777; -.
DR UniGene; Hs.706850; -.
DR PDB; 1RXD; X-ray; 1.90 A; A/B/C=2-160.
DR PDB; 1XM2; X-ray; 2.70 A; A/B/C/D/E/F=1-173.
DR PDBsum; 1RXD; -.
DR PDBsum; 1XM2; -.
DR DisProt; DP00255; -.
DR ProteinModelPortal; Q93096; -.
DR SMR; Q93096; 9-160.
DR IntAct; Q93096; 4.
DR MINT; MINT-194351; -.
DR STRING; 9606.ENSP00000359685; -.
DR BindingDB; Q93096; -.
DR ChEMBL; CHEMBL1075169; -.
DR PhosphoSite; Q93096; -.
DR DMDM; 68566217; -.
DR PaxDb; Q93096; -.
DR PRIDE; Q93096; -.
DR DNASU; 7803; -.
DR Ensembl; ENST00000370651; ENSP00000359685; ENSG00000112245.
DR GeneID; 7803; -.
DR KEGG; hsa:7803; -.
DR UCSC; uc003pek.3; human.
DR CTD; 7803; -.
DR GeneCards; GC06P064279; -.
DR HGNC; HGNC:9634; PTP4A1.
DR HPA; HPA003281; -.
DR MIM; 601585; gene.
DR neXtProt; NX_Q93096; -.
DR PharmGKB; PA33977; -.
DR eggNOG; NOG265664; -.
DR HOGENOM; HOG000231265; -.
DR HOVERGEN; HBG071295; -.
DR InParanoid; Q93096; -.
DR KO; K01104; -.
DR OMA; DKSIAVH; -.
DR OrthoDB; EOG7C8GJD; -.
DR PhylomeDB; Q93096; -.
DR EvolutionaryTrace; Q93096; -.
DR GeneWiki; PTP4A1; -.
DR GenomeRNAi; 7803; -.
DR NextBio; 30184; -.
DR PRO; PR:Q93096; -.
DR ArrayExpress; Q93096; -.
DR Bgee; Q93096; -.
DR CleanEx; HS_PTP4A1; -.
DR Genevestigator; Q93096; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; NAS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; FALSE_NEG.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell membrane; Complete proteome; Cytoplasm;
KW Cytoskeleton; Developmental protein; Disulfide bond;
KW Endoplasmic reticulum; Endosome; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Prenylation; Protein phosphatase; Reference proteome.
FT CHAIN 1 170 Protein tyrosine phosphatase type IVA 1.
FT /FTId=PRO_0000094780.
FT PROPEP 171 173 Removed in mature form (Probable).
FT /FTId=PRO_0000396726.
FT DOMAIN 82 148 Tyrosine-protein phosphatase.
FT REGION 97 132 Interaction with ATF5 (By similarity).
FT REGION 105 110 Phosphate binding.
FT ACT_SITE 72 72 Proton donor (Probable).
FT ACT_SITE 104 104 Phosphocysteine intermediate.
FT BINDING 110 110 Substrate.
FT MOD_RES 170 170 Cysteine methyl ester (Probable).
FT LIPID 170 170 S-farnesyl cysteine.
FT DISULFID 49 104
FT MUTAGEN 13 13 T->F: Reduces trimerization.
FT MUTAGEN 71 71 D->A: No effect on catalytic activity.
FT MUTAGEN 72 72 D->A: 80% loss of catalytic activity;
FT delay in progression through G2/M.
FT MUTAGEN 104 104 C->S: Abolishes enzymatic activity.
FT MUTAGEN 131 131 Q->A: Reduces trimerization.
FT MUTAGEN 170 170 C->S: Redistributes to the nucleus in
FT resting cells, but still locates to the
FT mitotic spindle in dividing cells.
FT Induces defects in cytokinesis.
FT MUTAGEN 171 171 C->S: No effect on subcellular location.
FT STRAND 10 14
FT STRAND 17 21
FT HELIX 27 29
FT HELIX 30 39
FT STRAND 42 47
FT HELIX 56 60
FT STRAND 64 67
FT STRAND 72 74
FT HELIX 78 94
FT STRAND 99 103
FT STRAND 105 108
FT TURN 109 111
FT HELIX 112 121
FT HELIX 126 134
FT HELIX 143 151
SQ SEQUENCE 173 AA; 19815 MW; 702008013D3F3835 CRC64;
MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE ATYDTTLVEK
EGIHVLDWPF DDGAPPSNQI VDDWLSLVKI KFREEPGCCI AVHCVAGLGR APVLVALALI
EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE KYRPKMRLRF KDSNGHRNNC CIQ
//
ID TP4A1_HUMAN Reviewed; 173 AA.
AC Q93096; B2R6C8; O00648; Q49A54;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2005, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Protein tyrosine phosphatase type IVA 1;
DE EC=3.1.3.48;
DE AltName: Full=PTP(CAAXI);
DE AltName: Full=Protein-tyrosine phosphatase 4a1;
DE AltName: Full=Protein-tyrosine phosphatase of regenerating liver 1;
DE Short=PRL-1;
DE Flags: Precursor;
GN Name=PTP4A1; Synonyms=PRL1, PTPCAAX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND ISOPRENYLATION AT
RP CYS-170.
RC TISSUE=Mammary carcinoma;
RX PubMed=9018080; DOI=10.1016/S0304-3835(96)04459-X;
RA Cates C.A., Michael R.L., Stayrook K.R., Harvey K.A., Burke Y.D.,
RA Randall S.K., Crowell P.L., Crowell D.N.;
RT "Prenylation of oncogenic human PTP(CAAX) protein tyrosine
RT phosphatases.";
RL Cancer Lett. 110:49-55(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Regenerating liver;
RX PubMed=9642300; DOI=10.1074/jbc.273.27.17286;
RA Peng Y., Genin A., Spinner N.B., Diamond R.H., Taub R.;
RT "The gene encoding human nuclear protein tyrosine phosphatase, PRL-1.
RT Cloning, chromosomal localization, and identification of an intron
RT enhancer.";
RL J. Biol. Chem. 273:17286-17295(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-163.
RC TISSUE=Lung fibroblast;
RX PubMed=9633825;
RA Dayton M.A., Knobloch T.J.;
RT "Multiple phosphotyrosine phosphatase mRNAs are expressed in the human
RT lung fibroblast cell line WI-38.";
RL Recept. Signal Transduct. 7:241-256(1997).
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10940933;
RX DOI=10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J;
RA Gjoerloff-Wingren A., Saxena M., Han S., Wang X., Alonso A.,
RA Renedo M., Oh P., Williams S., Schnitzer J., Mustelin T.;
RT "Subcellular localization of intracellular protein tyrosine
RT phosphatases in T cells.";
RL Eur. J. Immunol. 30:2412-2421(2000).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-71;
RP ASP-72; CYS-104; CYS-170 AND CYS-171, INTERACTION WITH TUBULIN, AND
RP FUNCTION.
RX PubMed=12235145; DOI=10.1074/jbc.M206407200;
RA Wang J., Kirby C.E., Herbst R.;
RT "The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum
RT and the mitotic spindle and is required for normal mitosis.";
RL J. Biol. Chem. 277:46659-46668(2002).
RN [11]
RP ENZYME REGULATION.
RX PubMed=12516958;
RA Pathak M.K., Dhawan D., Lindner D.J., Borden E.C., Farver C., Yi T.;
RT "Pentamidine is an inhibitor of PRL phosphatases with anticancer
RT activity.";
RL Mol. Cancer Ther. 1:1255-1264(2002).
RN [12]
RP FUNCTION.
RX PubMed=14643450; DOI=10.1016/S0304-3835(03)00517-2;
RA Werner S.R., Lee P.A., DeCamp M.W., Crowell D.N., Randall S.K.,
RA Crowell P.L.;
RT "Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1)
RT by PRL tyrosine phosphatases.";
RL Cancer Lett. 202:201-211(2003).
RN [13]
RP FUNCTION.
RX PubMed=12782572;
RA Zeng Q., Dong J.-M., Guo K., Li J., Tan H.-X., Koh V., Pallen C.J.,
RA Manser E., Hong W.;
RT "PRL-3 and PRL-1 promote cell migration, invasion, and metastasis.";
RL Cancer Res. 63:2716-2722(2003).
RN [14]
RP INDUCTION.
RX PubMed=15501285; DOI=10.1016/j.toxicon.2004.07.018;
RA Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.;
RT "Potential effects of tetrodotoxin exposure to human glial cells
RT postulated using microarray approach.";
RL Toxicon 44:597-608(2004).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF MUTANT SER-104, DISULFIDE
RP BOND, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF THR-13 AND
RP GLN-131, AND MASS SPECTROMETRY.
RX PubMed=15571731; DOI=10.1016/j.jmb.2004.10.061;
RA Jeong D.G., Kim S.J., Kim J.H., Son J.H., Park M.R., Lim S.M.,
RA Yoon T.-S., Ryu S.E.;
RT "Trimeric structure of PRL-1 phosphatase reveals an active enzyme
RT conformation and regulation mechanisms.";
RL J. Mol. Biol. 345:401-413(2005).
CC -!- FUNCTION: Protein tyrosine phosphatase which stimulates
CC progression from G1 into S phase during mitosis. May play a role
CC in the development and maintenance of differentiating epithelial
CC tissues. Enhances cell proliferation, cell motility and invasive
CC activity, and promotes cancer metastasis.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- ENZYME REGULATION: Inhibited by sodium orthovanadate and
CC pentamidine.
CC -!- SUBUNIT: Homotrimer. Interacts with ATF5 (By similarity).
CC Interacts with tubulin.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Early endosome. Endoplasmic
CC reticulum. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Note=And
CC mitotic spindle.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow, lymph nodes, T
CC lymphocytes, spleen, thymus and tonsil. Overexpressed in tumor
CC cell lines.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver.
CC -!- INDUCTION: Strongly down-regulated upon tetrodotoxin treatment.
CC -!- PTM: Farnesylated. Farnesylation is required for membrane
CC targeting. Unfarnesylated forms are shifted into the nucleus.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -----------------------------------------------------------------------
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DR EMBL; U48296; AAB40597.1; -; mRNA.
DR EMBL; AF051160; AAC39836.1; -; Genomic_DNA.
DR EMBL; AK312526; BAG35425.1; -; mRNA.
DR EMBL; CR749458; CAH18292.1; -; mRNA.
DR EMBL; AL135905; CAC12761.1; -; Genomic_DNA.
DR EMBL; CH471143; EAW88494.1; -; Genomic_DNA.
DR EMBL; BC023975; AAH23975.1; -; mRNA.
DR EMBL; BC045571; AAH45571.1; -; mRNA.
DR EMBL; U69701; AAB09080.1; -; mRNA.
DR RefSeq; NP_003454.1; NM_003463.4.
DR UniGene; Hs.227777; -.
DR UniGene; Hs.706850; -.
DR PDB; 1RXD; X-ray; 1.90 A; A/B/C=2-160.
DR PDB; 1XM2; X-ray; 2.70 A; A/B/C/D/E/F=1-173.
DR PDBsum; 1RXD; -.
DR PDBsum; 1XM2; -.
DR DisProt; DP00255; -.
DR ProteinModelPortal; Q93096; -.
DR SMR; Q93096; 9-160.
DR IntAct; Q93096; 4.
DR MINT; MINT-194351; -.
DR STRING; 9606.ENSP00000359685; -.
DR BindingDB; Q93096; -.
DR ChEMBL; CHEMBL1075169; -.
DR PhosphoSite; Q93096; -.
DR DMDM; 68566217; -.
DR PaxDb; Q93096; -.
DR PRIDE; Q93096; -.
DR DNASU; 7803; -.
DR Ensembl; ENST00000370651; ENSP00000359685; ENSG00000112245.
DR GeneID; 7803; -.
DR KEGG; hsa:7803; -.
DR UCSC; uc003pek.3; human.
DR CTD; 7803; -.
DR GeneCards; GC06P064279; -.
DR HGNC; HGNC:9634; PTP4A1.
DR HPA; HPA003281; -.
DR MIM; 601585; gene.
DR neXtProt; NX_Q93096; -.
DR PharmGKB; PA33977; -.
DR eggNOG; NOG265664; -.
DR HOGENOM; HOG000231265; -.
DR HOVERGEN; HBG071295; -.
DR InParanoid; Q93096; -.
DR KO; K01104; -.
DR OMA; DKSIAVH; -.
DR OrthoDB; EOG7C8GJD; -.
DR PhylomeDB; Q93096; -.
DR EvolutionaryTrace; Q93096; -.
DR GeneWiki; PTP4A1; -.
DR GenomeRNAi; 7803; -.
DR NextBio; 30184; -.
DR PRO; PR:Q93096; -.
DR ArrayExpress; Q93096; -.
DR Bgee; Q93096; -.
DR CleanEx; HS_PTP4A1; -.
DR Genevestigator; Q93096; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; NAS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; FALSE_NEG.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell membrane; Complete proteome; Cytoplasm;
KW Cytoskeleton; Developmental protein; Disulfide bond;
KW Endoplasmic reticulum; Endosome; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Prenylation; Protein phosphatase; Reference proteome.
FT CHAIN 1 170 Protein tyrosine phosphatase type IVA 1.
FT /FTId=PRO_0000094780.
FT PROPEP 171 173 Removed in mature form (Probable).
FT /FTId=PRO_0000396726.
FT DOMAIN 82 148 Tyrosine-protein phosphatase.
FT REGION 97 132 Interaction with ATF5 (By similarity).
FT REGION 105 110 Phosphate binding.
FT ACT_SITE 72 72 Proton donor (Probable).
FT ACT_SITE 104 104 Phosphocysteine intermediate.
FT BINDING 110 110 Substrate.
FT MOD_RES 170 170 Cysteine methyl ester (Probable).
FT LIPID 170 170 S-farnesyl cysteine.
FT DISULFID 49 104
FT MUTAGEN 13 13 T->F: Reduces trimerization.
FT MUTAGEN 71 71 D->A: No effect on catalytic activity.
FT MUTAGEN 72 72 D->A: 80% loss of catalytic activity;
FT delay in progression through G2/M.
FT MUTAGEN 104 104 C->S: Abolishes enzymatic activity.
FT MUTAGEN 131 131 Q->A: Reduces trimerization.
FT MUTAGEN 170 170 C->S: Redistributes to the nucleus in
FT resting cells, but still locates to the
FT mitotic spindle in dividing cells.
FT Induces defects in cytokinesis.
FT MUTAGEN 171 171 C->S: No effect on subcellular location.
FT STRAND 10 14
FT STRAND 17 21
FT HELIX 27 29
FT HELIX 30 39
FT STRAND 42 47
FT HELIX 56 60
FT STRAND 64 67
FT STRAND 72 74
FT HELIX 78 94
FT STRAND 99 103
FT STRAND 105 108
FT TURN 109 111
FT HELIX 112 121
FT HELIX 126 134
FT HELIX 143 151
SQ SEQUENCE 173 AA; 19815 MW; 702008013D3F3835 CRC64;
MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE ATYDTTLVEK
EGIHVLDWPF DDGAPPSNQI VDDWLSLVKI KFREEPGCCI AVHCVAGLGR APVLVALALI
EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE KYRPKMRLRF KDSNGHRNNC CIQ
//
MIM
601585
*RECORD*
*FIELD* NO
601585
*FIELD* TI
*601585 PROTEIN-TYROSINE PHOSPHATASE, TYPE 4A, 1; PTP4A1
;;PHOPHATASE OF REGENERATING LIVER 1; PRL1;;
read morePTP(CAAX1)
*FIELD* TX
Cellular processes involving growth, differentiation, and metabolism are
often regulated in part by protein phosphorylation and
dephosphorylation. The protein tyrosine phosphatases (PTPs), which
hydrolyze the phosphate monoesters of tyrosine residues, all share a
common active site motif and are classified into 3 groups. These include
the receptor-like PTPs, the intracellular PTPs, and the dual-specificity
PTPs, which can dephosphorylate at serine and threonine residues as well
as at tyrosines. Diamond et al. (1994) described a PTP from regenerating
rat liver that is a member of a fourth class. The gene, which they
designated Prl1, was one of many immediate-early genes and expressed
mainly in the nucleus. Overexpression of Prl1 in stably transfected
cells resulted in a transformed phenotype, which suggested that it may
play some role in tumorigenesis. By using an in vitro prenylation
screen, Cates et al. (1996) isolated 2 human cDNAs encoding PRL1
homologs, designated PTP(CAAX1) and PTP(CAAX2) (PRL2; 601584), that are
farnesylated in vitro by mammalian farnesyl:protein transferase.
Overexpression of these PTPs in epithelial cells caused a transformed
phenotype in cultured cells and tumor growth in nude mice. The authors
concluded that PTP(CAAX1) and PTP(CAAX2) represent a novel class of
isoprenylated, oncogenic PTPs. Peng et al. (1998) reported that the
human PTP(CAAX1) gene, or PRL1, is composed of 6 exons and contains 2
promoters. The predicted mouse, rat, and human PRL1 proteins are
identical. Zeng et al. (1998) determined that the human PRL1 and PRL2
proteins share 87% amino acid sequence identity.
By FISH, Peng et al. (1998) mapped the PRL1 gene to 6q12.
*FIELD* SA
Montagna et al. (1995)
*FIELD* RF
1. Cates, C. A.; Michael, R. L.; Stayrook, K. R.; Harvey, K. A.; Burke,
Y. D.; Randall, S. K.; Crowell, P. L.; Crowell, D. N.: Prenylation
of oncogenic human PTP(CAAX) protein tyrosine phosphatases. Cancer
Lett. 110: 49-55, 1996.
2. Diamond, R. H.; Cressman, D. E.; Laz, T. M.; Abrams, C. S.; Taub,
R.: PRL-1, a unique nuclear protein tyrosine phosphatase, affects
cell growth. Cell. Biol. 14: 3752-3762, 1994.
3. Montagna, M.; Serova, O.; Sylla, B. S.; Feunteun, J.; Lenoir, G.
M.: A 100-kb physical and transcriptional map around the EDH17B2
gene: identification of three novel genes and a pseudogene of a human
homologue of the rat PRL-1 tyrosine phosphatase. Hum. Genet. 96:
532-538, 1995.
4. Peng, Y.; Genin, A.; Spinner, N. B.; Diamond, R. H.; Taub, R.:
The gene encoding human nuclear protein tyrosine phosphatase, PRL-1:
cloning, chromosomal localization, and identification of an intron
enhancer. J. Biol. Chem. 273: 17286-17295, 1998.
5. Zeng, Q.; Hong, W.; Tan, Y. H.: Mouse PRL-2 and PRL-3, two potentially
prenylated protein tyrosine phosphatases homologous to PRL-1. Biochem.
Biophys. Res. Commun. 244: 421-427, 1998.
*FIELD* CN
Rebekah S. Rasooly - updated: 8/6/1999
*FIELD* CD
Alan F. Scott: 12/18/1996
*FIELD* ED
mgross: 08/06/1999
mgross: 8/6/1999
alopez: 12/2/1998
mark: 12/19/1996
*RECORD*
*FIELD* NO
601585
*FIELD* TI
*601585 PROTEIN-TYROSINE PHOSPHATASE, TYPE 4A, 1; PTP4A1
;;PHOPHATASE OF REGENERATING LIVER 1; PRL1;;
read morePTP(CAAX1)
*FIELD* TX
Cellular processes involving growth, differentiation, and metabolism are
often regulated in part by protein phosphorylation and
dephosphorylation. The protein tyrosine phosphatases (PTPs), which
hydrolyze the phosphate monoesters of tyrosine residues, all share a
common active site motif and are classified into 3 groups. These include
the receptor-like PTPs, the intracellular PTPs, and the dual-specificity
PTPs, which can dephosphorylate at serine and threonine residues as well
as at tyrosines. Diamond et al. (1994) described a PTP from regenerating
rat liver that is a member of a fourth class. The gene, which they
designated Prl1, was one of many immediate-early genes and expressed
mainly in the nucleus. Overexpression of Prl1 in stably transfected
cells resulted in a transformed phenotype, which suggested that it may
play some role in tumorigenesis. By using an in vitro prenylation
screen, Cates et al. (1996) isolated 2 human cDNAs encoding PRL1
homologs, designated PTP(CAAX1) and PTP(CAAX2) (PRL2; 601584), that are
farnesylated in vitro by mammalian farnesyl:protein transferase.
Overexpression of these PTPs in epithelial cells caused a transformed
phenotype in cultured cells and tumor growth in nude mice. The authors
concluded that PTP(CAAX1) and PTP(CAAX2) represent a novel class of
isoprenylated, oncogenic PTPs. Peng et al. (1998) reported that the
human PTP(CAAX1) gene, or PRL1, is composed of 6 exons and contains 2
promoters. The predicted mouse, rat, and human PRL1 proteins are
identical. Zeng et al. (1998) determined that the human PRL1 and PRL2
proteins share 87% amino acid sequence identity.
By FISH, Peng et al. (1998) mapped the PRL1 gene to 6q12.
*FIELD* SA
Montagna et al. (1995)
*FIELD* RF
1. Cates, C. A.; Michael, R. L.; Stayrook, K. R.; Harvey, K. A.; Burke,
Y. D.; Randall, S. K.; Crowell, P. L.; Crowell, D. N.: Prenylation
of oncogenic human PTP(CAAX) protein tyrosine phosphatases. Cancer
Lett. 110: 49-55, 1996.
2. Diamond, R. H.; Cressman, D. E.; Laz, T. M.; Abrams, C. S.; Taub,
R.: PRL-1, a unique nuclear protein tyrosine phosphatase, affects
cell growth. Cell. Biol. 14: 3752-3762, 1994.
3. Montagna, M.; Serova, O.; Sylla, B. S.; Feunteun, J.; Lenoir, G.
M.: A 100-kb physical and transcriptional map around the EDH17B2
gene: identification of three novel genes and a pseudogene of a human
homologue of the rat PRL-1 tyrosine phosphatase. Hum. Genet. 96:
532-538, 1995.
4. Peng, Y.; Genin, A.; Spinner, N. B.; Diamond, R. H.; Taub, R.:
The gene encoding human nuclear protein tyrosine phosphatase, PRL-1:
cloning, chromosomal localization, and identification of an intron
enhancer. J. Biol. Chem. 273: 17286-17295, 1998.
5. Zeng, Q.; Hong, W.; Tan, Y. H.: Mouse PRL-2 and PRL-3, two potentially
prenylated protein tyrosine phosphatases homologous to PRL-1. Biochem.
Biophys. Res. Commun. 244: 421-427, 1998.
*FIELD* CN
Rebekah S. Rasooly - updated: 8/6/1999
*FIELD* CD
Alan F. Scott: 12/18/1996
*FIELD* ED
mgross: 08/06/1999
mgross: 8/6/1999
alopez: 12/2/1998
mark: 12/19/1996