PTP4A2

Protein-coding gene in the species Homo sapiens
PTP4A2
Identifiers
AliasesPTP4A2, HH13, HH7-2, HU-PP-1, OV-1, PRL-2, PRL2, PTP4A, PTPCAAX2, ptp-IV1a, ptp-IV1b, protein tyrosine phosphatase type IVA, member 2, protein tyrosine phosphatase 4A2
External IDsOMIM: 601584; MGI: 1277117; HomoloGene: 20744; GeneCards: PTP4A2; OMA:PTP4A2 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for PTP4A2
Genomic location for PTP4A2
Band1p35.2Start31,906,421 bp[1]
End31,944,856 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for PTP4A2
Genomic location for PTP4A2
Band4|4 D2.2Start129,705,012 bp[2]
End129,743,796 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • corpus callosum

  • internal globus pallidus

  • inferior ganglion of vagus nerve

  • palpebral conjunctiva

  • middle frontal gyrus

  • optic nerve

  • external globus pallidus

  • parotid gland

  • medulla oblongata

  • ventral tegmental area
Top expressed in
  • tail of embryo

  • extensor digitorum longus muscle

  • triceps brachii muscle

  • genital tubercle

  • vastus lateralis muscle

  • plantaris muscle

  • muscle of thigh

  • gastrocnemius muscle

  • skeletal muscle tissue

  • extraocular muscle
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • prenylated protein tyrosine phosphatase activity
  • protein tyrosine phosphatase activity
  • phosphatase activity
  • phosphoprotein phosphatase activity
  • hydrolase activity
  • protein binding
Cellular component
  • cytoplasm
  • endosome
  • plasma membrane
  • early endosome
  • membrane
  • nucleus
  • cytosol
Biological process
  • protein dephosphorylation
  • dephosphorylation
  • peptidyl-tyrosine dephosphorylation
  • post-translational protein modification
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8073

19244

Ensembl

ENSG00000184007

ENSMUSG00000028788

UniProt

Q12974

O70274

RefSeq (mRNA)
NM_001195100
NM_001195101
NM_003479
NM_080391
NM_080392

NM_001369858
NM_001369859
NM_001369860

NM_001164745
NM_008974

RefSeq (protein)
NP_001182029
NP_001182030
NP_536316
NP_001356787
NP_001356788

NP_001356789

NP_001158217
NP_033000

Location (UCSC)Chr 1: 31.91 – 31.94 MbChr 4: 129.71 – 129.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein tyrosine phosphatase type IVA 2 is an enzyme that in humans is encoded by the PTP4A2 gene.[5][6][7]

The protein encoded by this gene belongs to a small class of the protein tyrosine phosphatase (PTP) family. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. PTPs in this class contain a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif.

This PTP has been shown to primarily associate with plasmic and endosomal membrane through its C-terminal prenylation. This PTP was found to interact with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), and thus may function as a regulator of GGT II activity.

Overexpression of this gene in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis. Alternatively spliced transcript variants that encode two distinct isoforms have been described.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000184007 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028788 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Zhao Z, Lee CC, Monckton DG, Yazdani A, Coolbaugh MI, Li X, Bailey J, Shen Y, Caskey CT (Sep 1996). "Characterization and genomic mapping of genes and pseudogenes of a new human protein tyrosine phosphatase". Genomics. 35 (1): 172–81. doi:10.1006/geno.1996.0336. PMID 8661118.
  6. ^ Zeng Q, Hong W, Tan YH (Apr 1998). "Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1". Biochem Biophys Res Commun. 244 (2): 421–7. doi:10.1006/bbrc.1998.8291. PMID 9514946.
  7. ^ a b "Entrez Gene: PTP4A2 protein tyrosine phosphatase type IVA, member 2".

Further reading

  • Rommens JM, Durocher F, McArthur J, et al. (1996). "Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21". Genomics. 28 (3): 530–42. doi:10.1006/geno.1995.1185. PMID 7490091.
  • Montagna M, Serova O, Sylla BS, et al. (1996). "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 (5): 532–8. doi:10.1007/bf00197407. PMID 8529999. S2CID 24567366.
  • Cates CA, Michael RL, Stayrook KR, et al. (1997). "Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases". Cancer Lett. 110 (1–2): 49–55. doi:10.1016/S0304-3835(96)04459-X. PMID 9018080.
  • Gjörloff-Wingren A, Saxena M, Han S, et al. (2000). "Subcellular localization of intracellular protein tyrosine phosphatases in T cells". Eur. J. Immunol. 30 (8): 2412–21. doi:10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J. PMID 10940933. S2CID 8132613.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Si X, Zeng Q, Ng CH, et al. (2001). "Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II". J. Biol. Chem. 276 (35): 32875–82. doi:10.1074/jbc.M010400200. PMID 11447212.
  • Wang Q, Holmes DI, Powell SM, et al. (2002). "Analysis of stromal-epithelial interactions in prostate cancer identifies PTPCAAX2 as a potential oncogene". Cancer Lett. 175 (1): 63–9. doi:10.1016/S0304-3835(01)00703-0. PMID 11734337.
  • Wang J, Kirby CE, Herbst R (2003). "The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis". J. Biol. Chem. 277 (48): 46659–68. doi:10.1074/jbc.M206407200. PMID 12235145.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Pathak MK, Dhawan D, Lindner DJ, et al. (2003). "Pentamidine is an inhibitor of PRL phosphatases with anticancer activity". Mol. Cancer Ther. 1 (14): 1255–64. PMID 12516958.
  • Werner SR, Lee PA, DeCamp MW, et al. (2004). "Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases". Cancer Lett. 202 (2): 201–11. doi:10.1016/S0304-3835(03)00517-2. PMID 14643450.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
  • Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
  • Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
  • Radke I, Götte M, Kersting C, et al. (2006). "Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer". Br. J. Cancer. 95 (3): 347–54. doi:10.1038/sj.bjc.6603261. PMC 2360632. PMID 16832410.
  • Dumaual CM, Sandusky GE, Crowell PL, Randall SK (2007). "Cellular localization of PRL-1 and PRL-2 gene expression in normal adult human tissues". J. Histochem. Cytochem. 54 (12): 1401–12. doi:10.1369/jhc.6A7019.2006. PMC 3958126. PMID 16957164.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  • v
  • t
  • e
  • 1rxd: Crystal structure of human protein tyrosine phosphatase 4A1
    1rxd: Crystal structure of human protein tyrosine phosphatase 4A1
  • 1x24: Prl-1 (ptp4a)
    1x24: Prl-1 (ptp4a)
  • 1zck: native structure prl-1 (ptp4a1)
    1zck: native structure prl-1 (ptp4a1)
  • v
  • t
  • e
Class I
Classical PTPs
Receptor type PTPs
Non receptor type PTPs
VH1-like or
dual specific
phosphatases
(DSPs)
MAPK phosphatases (MKPs)
Slingshots
PRLs
CDC14s
Atypical DSPs
Phosphatase and tensin
homologs (PTENs)
Myotubularins
Class II
Class III
Class IV


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