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 02-OCT-2024, entry version 206. 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=6; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 121. DR IntAct; Q12974; 22. DR MINT; Q12974; -. DR STRING; 9606.ENSP00000493688; -. DR BindingDB; Q12974; -. DR ChEMBL; CHEMBL1075105; -. DR DrugCentral; Q12974; -. DR DEPOD; PTP4A2; -. DR iPTMnet; Q12974; -. DR PhosphoSitePlus; Q12974; -. DR BioMuta; PTP4A2; -. DR DMDM; 68566159; -. DR jPOST; Q12974; -. DR MassIVE; Q12974; -. DR PaxDb; 9606-ENSP00000344909; -. DR PeptideAtlas; Q12974; -. DR ProteomicsDB; 20332; -. DR ProteomicsDB; 59070; -. [Q12974-1] DR ProteomicsDB; 59071; -. [Q12974-2] DR Pumba; Q12974; -. DR Antibodypedia; 4406; 226 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 AGR; HGNC:9635; -. 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; GIEVHSW; -. DR OrthoDB; 117411at2759; -. 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; 69 hits in 1123 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 216 other cell types or tissues. DR ExpressionAtlas; Q12974; baseline and differential. 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 CDD; cd18536; PTP-IVa2; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR050561; PTP. 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 PANTHER; PTHR23339:SF65; PROTEIN TYROSINE PHOSPHATASE TYPE IVA 2; 1. DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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; Proteomics identification; KW 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 //