PTPRO

Protein-coding gene in the species Homo sapiens
PTPRO
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2G59, 2GJT

Identifiers
AliasesPTPRO, GLEPP1, NPHS6, PTP-OC, PTP-U2, PTPROT, PTPU2, R-PTP-O, protein tyrosine phosphatase, receptor type O, protein tyrosine phosphatase receptor type O
External IDsOMIM: 600579; MGI: 1097152; HomoloGene: 21564; GeneCards: PTPRO; OMA:PTPRO - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for PTPRO
Genomic location for PTPRO
Band12p12.3|12p13-p12Start15,322,257 bp[1]
End15,602,175 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for PTPRO
Genomic location for PTPRO
Band6|6 G1Start137,229,317 bp[2]
End137,440,231 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • glomerulus

  • metanephric glomerulus

  • rectum

  • ganglionic eminence

  • middle temporal gyrus

  • human kidney

  • ventricular zone

  • nucleus accumbens

  • prefrontal cortex

  • mucosa of transverse colon
Top expressed in
  • renal corpuscle

  • arcuate nucleus

  • median eminence

  • olfactory bulb

  • barrel cortex

  • ventromedial nucleus

  • piriform cortex

  • mammillary body

  • dorsomedial hypothalamic nucleus

  • substantia nigra
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • phosphoprotein phosphatase activity
  • protein homodimerization activity
  • phosphatase activity
  • Wnt-protein binding
  • protein binding
  • protein tyrosine phosphatase activity
  • transmembrane receptor protein tyrosine phosphatase activity
  • hydrolase activity
Cellular component
  • integral component of membrane
  • lateral plasma membrane
  • membrane
  • growth cone
  • plasma membrane
  • dendritic spine
  • integral component of plasma membrane
  • axon
  • apical plasma membrane
  • neuron projection
  • extracellular exosome
  • lamellipodium
  • glutamatergic synapse
  • GABA-ergic synapse
  • integral component of postsynaptic density membrane
Biological process
  • negative regulation of cell-substrate adhesion
  • negative regulation of neuron projection development
  • monocyte chemotaxis
  • negative regulation of retinal ganglion cell axon guidance
  • regulation of glomerular filtration
  • slit diaphragm assembly
  • protein dephosphorylation
  • glomerulus development
  • axon guidance
  • cell morphogenesis
  • glomerular visceral epithelial cell differentiation
  • peptidyl-tyrosine dephosphorylation
  • negative regulation of glomerular filtration
  • negative regulation of canonical Wnt signaling pathway
  • lamellipodium assembly
  • dephosphorylation
  • regulation of synapse organization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5800

19277

Ensembl

ENSG00000151490

ENSMUSG00000030223

UniProt

Q16827

E9Q612

RefSeq (mRNA)
NM_002848
NM_030667
NM_030668
NM_030669
NM_030670

NM_030671

NM_001164401
NM_001164402
NM_001164403
NM_011216

RefSeq (protein)
NP_002839
NP_109592
NP_109593
NP_109594
NP_109595

NP_109596

NP_001157873
NP_001157874
NP_001157875
NP_035346

Location (UCSC)Chr 12: 15.32 – 15.6 MbChr 6: 137.23 – 137.44 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Receptor-type tyrosine-protein phosphatase O is an enzyme that in humans is encoded by the PTPRO gene.[5][6][7]

This gene encodes a receptor-type protein tyrosine phosphatase containing a single intracellular catalytic domain with a characteristic signature motif. The gene product, which has a transmembrane domain, is an integral membrane protein. Several alternatively spliced transcript variants, some of which encode different isoforms of the protein, have been described. These variants exhibit tissue-specific expression.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000151490 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030223 – 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. ^ Thomas PE, Wharram BL, Goyal M, Wiggins JE, Holzman LB, Wiggins RC (Sep 1994). "GLEPP1, a renal glomerular epithelial cell (podocyte) membrane protein-tyrosine phosphatase. Identification, molecular cloning, and characterization in rabbit". J Biol Chem. 269 (31): 19953–62. doi:10.1016/S0021-9258(17)32113-0. PMID 7519601.
  6. ^ Wiggins RC, Wiggins JE, Goyal M, Wharram BL, Thomas PE (Oct 1995). "Molecular cloning of cDNAs encoding human GLEPP1, a membrane protein tyrosine phosphatase: characterization of the GLEPP1 protein distribution in human kidney and assignment of the GLEPP1 gene to human chromosome 12p12-p13". Genomics. 27 (1): 174–81. doi:10.1006/geno.1995.1021. PMID 7665166.
  7. ^ a b "Entrez Gene: PTPRO protein tyrosine phosphatase, receptor type, O".

Further reading

  • Seimiya H, Sawabe T, Inazawa J, Tsuruo T (1995). "Cloning, expression and chromosomal localization of a novel gene for protein tyrosine phosphatase (PTP-U2) induced by various differentiation-inducing agents". Oncogene. 10 (9): 1731–8. PMID 7753550.
  • Feito MJ, Bragardo M, Buonfiglio D, Bonissoni S, Bottarel F, Malavasi F, Dianzani U (1997). "gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules". Int. Immunol. 9 (8): 1141–7. doi:10.1093/intimm/9.8.1141. PMID 9263011.
  • Avraham S, London R, Tulloch GA, Ellis M, Fu Y, Jiang S, White RA, Painter C, Steinberger A (1998). "Characterization and chromosomal localization of PTPRO, a novel receptor protein tyrosine phosphatase, expressed in hematopoietic stem cells". Gene. 204 (1–2): 5–16. doi:10.1016/S0378-1119(97)00420-4. PMID 9434160.
  • Taniguchi Y, London R, Schinkmann K, Jiang S, Avraham H (1999). "The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and Is associated with the c-Kit receptor". Blood. 94 (2): 539–49. doi:10.1182/blood.V94.2.539. PMID 10397721.
  • Aguiar RC, Yakushijin Y, Kharbanda S, Tiwari S, Freeman GJ, Shipp MA (1999). "PTPROt: an alternatively spliced and developmentally regulated B-lymphoid phosphatase that promotes G0/G1 arrest". Blood. 94 (7): 2403–13. doi:10.1182/blood.V94.7.2403.419k39_2403_2413. PMID 10498613. S2CID 15259010.
  • Wang Z, Bhattacharya N, Meyer MK, Seimiya H, Tsuruo T, Tonani JA, Magnuson NS (2001). "Pim-1 negatively regulates the activity of PTP-U2S phosphatase and influences terminal differentiation and apoptosis of monoblastoid leukemia cells". Arch. Biochem. Biophys. 390 (1): 9–18. doi:10.1006/abbi.2001.2370. PMID 11368509.
  • Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (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.
  • Chen L, Juszczynski P, Takeyama K, Aguiar RC, Shipp MA (2007). "Protein tyrosine phosphatase receptor-type O truncated (PTPROt) regulates SYK phosphorylation, proximal B-cell-receptor signaling, and cellular proliferation". Blood. 108 (10): 3428–33. doi:10.1182/blood-2006-03-013821. PMID 16888096.
  • Motiwala T, Majumder S, Kutay H, Smith DS, Neuberg DS, Lucas DM, Byrd JC, Grever M, Jacob ST (2007). "Methylation and Silencing of Protein Tyrosine Phosphatase Receptor Type O in Chronic Lymphocytic Leukemia". Clin. Cancer Res. 13 (11): 3174–81. doi:10.1158/1078-0432.CCR-06-1720. PMC 3074612. PMID 17545520.
  • Tian J, Wang HP, Mao YY, Jin J, Chen JH (2007). "Reduced glomerular epithelial protein 1 expression and podocyte injury in immunoglobulin A nephropathy". J. Int. Med. Res. 35 (3): 338–45. doi:10.1177/147323000703500308. PMID 17593862. S2CID 24500200.
  • v
  • t
  • e
  • 2g59: Crystal Structure of the Catalytic Domain of Protein Tyrosine Phosphatase from Homo sapiens
    2g59: Crystal Structure of the Catalytic Domain of Protein Tyrosine Phosphatase from Homo sapiens
  • 2gjt: Crystal structure of the human receptor phosphatase PTPRO
    2gjt: Crystal structure of the human receptor phosphatase PTPRO
  • 2pi7: Structure of the catalytic domain of the chick retinal neurite inhibitor-Receptor Protein Tyrosine Phosphatase CRYP-2/cPTPRO
    2pi7: Structure of the catalytic domain of the chick retinal neurite inhibitor-Receptor Protein Tyrosine Phosphatase CRYP-2/cPTPRO
  • 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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