TP4A2_HUMAN
ID TP4A2_HUMAN Reviewed; 167 AA.
AC Q12974; A8K9I8; B4DM39; D3DPP0; E9PGJ6; O00649; Q15197; Q15259; Q15260;
AC Q15261; R4GN50;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Protein tyrosine phosphatase type IVA 2;
DE EC=3.1.3.48;
DE AltName: Full=HU-PP-1;
DE AltName: Full=OV-1;
DE AltName: Full=PTP(CAAXII);
DE AltName: Full=Protein-tyrosine phosphatase 4a2;
DE AltName: Full=Protein-tyrosine phosphatase of regenerating liver 2;
DE Short=PRL-2;
DE Flags: Precursor;
GN Name=PTP4A2; Synonyms=PRL2, PTPCAAX2; ORFNames=BM-008;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=8529999; DOI=10.1007/bf00197407;
RA Montagna M., Serova O., Sylla B.S., Feunteun J., Lenoir G.M.;
RT "A 100-kb physical and transcriptional map around the EDH17B2 gene:
RT identification of three novel genes and a pseudogene of a human homologue
RT of the rat PRL-1 tyrosine phosphatase.";
RL Hum. Genet. 96:532-538(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-164, AND
RP ACTIVITY REGULATION.
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 phosphatases.";
RL Cancer Lett. 110:49-55(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Ovary, and Placenta;
RX PubMed=8661118; DOI=10.1006/geno.1996.0336;
RA Zhao Z., Lee C.-C., Monckton D.G., Yazdani A., Coolbaugh M.I., Li X.,
RA Bailey J., Shen Y., Caskey C.T.;
RT "Characterization and genomic mapping of genes and pseudogenes of a new
RT human protein tyrosine phosphatase.";
RL Genomics 35:172-181(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RA Zhao M., Song H., Li N., Peng Y., Han Z., Chen Z.;
RT "A novel gene expressed in human bone marrow.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Thymus;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-167 (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=7490091; DOI=10.1006/geno.1995.1185;
RA Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F., Allen T.,
RA Samson C., Ferri L., Narod S., Morgan K., Simard J.;
RT "Generation of a transcription map at the HSD17B locus centromeric to BRCA1
RT at 17q21.";
RL Genomics 28:530-542(1995).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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., Renedo M.,
RA Oh P., Williams S., Schnitzer J., Mustelin T.;
RT "Subcellular localization of intracellular protein tyrosine phosphatases in
RT T cells.";
RL Eur. J. Immunol. 30:2412-2421(2000).
RN [11]
RP INTERACTION WITH RABGGTB, ISOPRENYLATION AT CYS-164, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF 164-CYS--GLN-167 AND CYS-165.
RX PubMed=11447212; DOI=10.1074/jbc.m010400200;
RA Si X., Zeng Q., Ng C.H., Hong W., Pallen C.J.;
RT "Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with
RT the beta-subunit of geranylgeranyltransferase II.";
RL J. Biol. Chem. 276:32875-32882(2001).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=11734337; DOI=10.1016/s0304-3835(01)00703-0;
RA Wang Q., Holmes D.I.R., Powell S.M., Lu Q.L., Waxman J.;
RT "Analysis of stromal-epithelial interactions in prostate cancer identifies
RT PTPCAAX2 as a potential oncogene.";
RL Cancer Lett. 175:63-69(2002).
RN [13]
RP SUBCELLULAR LOCATION, AND LACK OF INTERACTION WITH TUBULIN.
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 and
RT the mitotic spindle and is required for normal mitosis.";
RL J. Biol. Chem. 277:46659-46668(2002).
RN [14]
RP ACTIVITY 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 [15]
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) by
RT PRL tyrosine phosphatases.";
RL Cancer Lett. 202:201-211(2003).
RN [16]
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., Buerckstuemmer T.,
RA 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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Protein tyrosine phosphatase which stimulates progression
CC from G1 into S phase during mitosis. Promotes tumors. Inhibits
CC geranylgeranyl transferase type II activity by blocking the association
CC between RABGGTA and RABGGTB. {ECO:0000269|PubMed:14643450}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- ACTIVITY REGULATION: Inhibited by sodium orthovanadate and pentamidine.
CC {ECO:0000269|PubMed:12516958, ECO:0000269|PubMed:9018080}.
CC -!- SUBUNIT: In contrast to PTP4A1 and PTP4A3, does not interact with
CC tubulin. Interacts with RABGGTB. {ECO:0000269|PubMed:11447212}.
CC -!- INTERACTION:
CC Q12974; Q9NRU3: CNNM1; NbExp=5; IntAct=EBI-1046324, EBI-11986439;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Early endosome. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Ptp-IV1a, Ptp-IV1b;
CC IsoId=Q12974-1; Sequence=Displayed;
CC Name=2; Synonyms=PTP4Ar;
CC IsoId=Q12974-2; Sequence=VSP_014404, VSP_014405;
CC Name=3;
CC IsoId=Q12974-3; Sequence=VSP_044813;
CC Name=4;
CC IsoId=Q12974-4; Sequence=VSP_055056;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC skeletal muscle, heart and thymus. Overexpressed in prostate tumor
CC tissue. {ECO:0000269|PubMed:10940933, ECO:0000269|PubMed:11734337,
CC ECO:0000269|PubMed:8661118}.
CC -!- PTM: Farnesylated. Farnesylation is required for membrane targeting and
CC for interaction with RABGGTB. Unfarnesylated forms are redirected to
CC the nucleus and cytosol.
CC -!- MISCELLANEOUS: A processed pseudogene with 96% sequence identity was
CC found in the BRCA1 (113705) region of 17q21.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
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DR EMBL; U14603; AAA90979.1; -; mRNA.
DR EMBL; U48297; AAB40598.1; -; mRNA.
DR EMBL; L48722; AAB42169.1; -; Genomic_DNA.
DR EMBL; L48723; AAB42170.1; -; Genomic_DNA.
DR EMBL; L48937; AAB39331.1; -; Genomic_DNA.
DR EMBL; AF208850; AAF64264.1; -; mRNA.
DR EMBL; AK292703; BAF85392.1; -; mRNA.
DR EMBL; AK297280; BAG59751.1; -; mRNA.
DR EMBL; AL136115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07578.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07579.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07582.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07583.1; -; Genomic_DNA.
DR EMBL; BC070182; AAH70182.1; -; mRNA.
DR EMBL; L39000; AAB59575.1; -; mRNA.
DR CCDS; CCDS348.1; -. [Q12974-1]
DR CCDS; CCDS53292.1; -. [Q12974-3]
DR CCDS; CCDS59193.1; -. [Q12974-4]
DR PIR; I68523; I68523.
DR RefSeq; NP_001182029.1; NM_001195100.1. [Q12974-4]
DR RefSeq; NP_001182030.1; NM_001195101.1. [Q12974-3]
DR RefSeq; NP_536316.1; NM_080391.3. [Q12974-1]
DR RefSeq; XP_005271288.1; XM_005271231.3.
DR RefSeq; XP_005271289.1; XM_005271232.3.
DR RefSeq; XP_016857890.1; XM_017002401.1.
DR PDB; 5K22; X-ray; 3.00 A; A=1-163.
DR PDB; 5K23; X-ray; 2.96 A; A=1-167.
DR PDB; 5K25; X-ray; 3.05 A; A=1-167.
DR PDB; 6WUR; X-ray; 2.88 A; A=1-167.
DR PDBsum; 5K22; -.
DR PDBsum; 5K23; -.
DR PDBsum; 5K25; -.
DR PDBsum; 6WUR; -.
DR AlphaFoldDB; Q12974; -.
DR BMRB; Q12974; -.
DR SMR; Q12974; -.
DR BioGRID; 113747; 60.
DR IntAct; Q12974; 20.
DR MINT; Q12974; -.
DR STRING; 9606.ENSP00000344909; -.
DR BindingDB; Q12974; -.
DR ChEMBL; CHEMBL1075105; -.
DR DEPOD; PTP4A2; -.
DR iPTMnet; Q12974; -.
DR PhosphoSitePlus; Q12974; -.
DR BioMuta; PTP4A2; -.
DR DMDM; 68566159; -.
DR EPD; Q12974; -.
DR jPOST; Q12974; -.
DR MassIVE; Q12974; -.
DR MaxQB; Q12974; -.
DR PaxDb; Q12974; -.
DR PeptideAtlas; Q12974; -.
DR PRIDE; Q12974; -.
DR ProteomicsDB; 20332; -.
DR ProteomicsDB; 59070; -. [Q12974-1]
DR ProteomicsDB; 59071; -. [Q12974-2]
DR Antibodypedia; 4406; 214 antibodies from 29 providers.
DR DNASU; 8073; -.
DR Ensembl; ENST00000457805.6; ENSP00000409260.2; ENSG00000184007.22. [Q12974-3]
DR Ensembl; ENST00000602683.5; ENSP00000473490.1; ENSG00000184007.22. [Q12974-4]
DR Ensembl; ENST00000602725.5; ENSP00000473259.1; ENSG00000184007.22. [Q12974-1]
DR Ensembl; ENST00000647444.2; ENSP00000493688.1; ENSG00000184007.22. [Q12974-1]
DR Ensembl; ENST00000649841.1; ENSP00000497092.1; ENSG00000184007.22. [Q12974-1]
DR GeneID; 8073; -.
DR KEGG; hsa:8073; -.
DR MANE-Select; ENST00000647444.2; ENSP00000493688.1; NM_080391.4; NP_536316.1.
DR UCSC; uc001btx.3; human. [Q12974-1]
DR CTD; 8073; -.
DR DisGeNET; 8073; -.
DR GeneCards; PTP4A2; -.
DR HGNC; HGNC:9635; PTP4A2.
DR HPA; ENSG00000184007; Low tissue specificity.
DR MIM; 601584; gene.
DR neXtProt; NX_Q12974; -.
DR OpenTargets; ENSG00000184007; -.
DR PharmGKB; PA33978; -.
DR VEuPathDB; HostDB:ENSG00000184007; -.
DR eggNOG; KOG2836; Eukaryota.
DR GeneTree; ENSGT00940000154383; -.
DR HOGENOM; CLU_099263_2_0_1; -.
DR InParanoid; Q12974; -.
DR OMA; IQVHGWT; -.
DR OrthoDB; 1398550at2759; -.
DR PhylomeDB; Q12974; -.
DR TreeFam; TF313384; -.
DR PathwayCommons; Q12974; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q12974; -.
DR SIGNOR; Q12974; -.
DR BioGRID-ORCS; 8073; 47 hits in 1043 CRISPR screens.
DR ChiTaRS; PTP4A2; human.
DR GeneWiki; PTP4A2; -.
DR GenomeRNAi; 8073; -.
DR Pharos; Q12974; Tchem.
DR PRO; PR:Q12974; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q12974; protein.
DR Bgee; ENSG00000184007; Expressed in corpus callosum and 214 other tissues.
DR ExpressionAtlas; Q12974; baseline and differential.
DR Genevisible; Q12974; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004727; F:prenylated protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00102; Y_phosphatase; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Disulfide bond; Endosome; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Prenylation; Protein phosphatase; Reference proteome.
FT CHAIN 1..164
FT /note="Protein tyrosine phosphatase type IVA 2"
FT /id="PRO_0000094785"
FT PROPEP 165..167
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396731"
FT DOMAIN 5..158
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 69
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 101
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 102..107
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 164
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 164
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:11447212,
FT ECO:0000269|PubMed:9018080"
FT DISULFID 46..101
FT /evidence="ECO:0000250"
FT VAR_SEQ 33..63
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044813"
FT VAR_SEQ 64..82
FT /note="DWPFDDGAPPPNQIVDDWL -> KKKGSVQFQTAALFGEIPT (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014404"
FT VAR_SEQ 83..167
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014405"
FT VAR_SEQ 108..132
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_055056"
FT MUTAGEN 164..167
FT /note="Missing: Locates in the nucleus and cytosol. No
FT interaction with RABGGTB."
FT /evidence="ECO:0000269|PubMed:11447212"
FT MUTAGEN 165
FT /note="C->S: No effect on interaction with RABGGTB."
FT /evidence="ECO:0000269|PubMed:11447212"
FT CONFLICT 13
FT /note="N -> D (in Ref. 3; AAB39331)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="A -> D (in Ref. 9; AAB59575)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="V -> F (in Ref. 5; BAG59751)"
FT /evidence="ECO:0000305"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:6WUR"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:6WUR"
SQ SEQUENCE 167 AA; 19127 MW; E97B88BF87B87943 CRC64;
MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY DKAPVEKEGI
HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH CVAGLGRAPV LVALALIECG
MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR PKMRLRFRDT NGHCCVQ
