PTPRZ1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
3JXF, 3S97, 5AWX

Identifiers

Aliases

PTPRZ1, HPTPZ, HPTPzeta, PTP-ZETA, PTP18, PTPRZ, PTPZ, R-PTP-zeta-2, RPTPB, RPTPbeta, phosphacan, protein tyrosine phosphatase, receptor type Z1, protein tyrosine phosphatase receptor type Z1

External IDs

OMIM: 176891 MGI: 97816 HomoloGene: 2136 GeneCards: PTPRZ1

Gene location (Human)

Chr.	Chromosome 7 (human)^[1]

Band	7q31.32	Start	121,873,089 bp^[1]
Band	7q31.32	End	122,062,036 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 6 (mouse)^[2]

Band	6\|6 A3.1	Start	22,875,501 bp^[2]
Band	6\|6 A3.1	End	23,052,915 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

ganglionic eminence

endothelial cell

amygdala

Region I of hippocampus proper

optic nerve

caudate nucleus

nucleus accumbens

corpus callosum

external globus pallidus

substantia nigra

Top expressed in

mammillary body

median eminence

ventromedial nucleus

arcuate nucleus

cerebellar vermis

dorsomedial hypothalamic nucleus

substantia nigra

lateral hypothalamus

suprachiasmatic nucleus

olfactory bulb

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	phosphoprotein phosphatase activity phosphatase activity protein binding protein tyrosine phosphatase activity transmembrane receptor protein tyrosine phosphatase activity hydrolase activity integrin binding
Cellular component	integral component of membrane membrane integral component of plasma membrane extracellular region perineuronal net intrinsic component of plasma membrane plasma membrane extracellular matrix synapse
Biological process	axonogenesis protein dephosphorylation oligodendrocyte differentiation regulation of oligodendrocyte progenitor proliferation central nervous system development hematopoietic progenitor cell differentiation learning or memory peptidyl-tyrosine dephosphorylation dephosphorylation cytokine-mediated signaling pathway regulation of myelination negative regulation of neuron apoptotic process positive regulation of oligodendrocyte differentiation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


5803


19283

Ensembl


ENSG00000106278


ENSMUSG00000068748

UniProt


P23471


B9EKR1

RefSeq (mRNA)


NM_001206838 NM_001206839 NM_002851 NM_001369395 NM_001369396


NM_001081306 NM_011219 NM_178180 NM_001311064 NM_001361349

RefSeq (protein)


NP_001193767 NP_001193768 NP_002842

NP_001074775 NP_001297993 NP_001348278 NP_035349 NP_001389981
NP_001389982 NP_001389983

Location (UCSC)

Chr 7: 121.87 – 122.06 Mb

Chr 6: 22.88 – 23.05 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Receptor-type tyrosine-protein phosphatase zeta also known as phosphacan is an enzyme that in humans is encoded by the PTPRZ1 gene.^[5]^[6]^[7]

Function

This gene is a member of the receptor tyrosine phosphatase family and encodes a single-pass type I membrane protein with two cytoplasmic tyrosine-protein phosphatase domains, an alpha-carbonic anhydrase domain and a fibronectin type III domain. Alternative splice variants that encode different protein isoforms have been described but their full-length nature has not been determined.^[7]

Clinical significance

Expression of this gene is induced in gastric cancer cells, in the remyelinating oligodendrocytes of multiple sclerosis lesions, and in human embryonic kidney cells under hypoxic conditions. Both the protein and transcript are overexpressed in glioblastoma cells, promoting their haptotactic migration.^[7]

References

Krueger NX, Saito H (1992). "A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases". Proc. Natl. Acad. Sci. U.S.A. 89 (16): 7417–21. Bibcode:1992PNAS...89.7417K. doi:10.1073/pnas.89.16.7417. PMC 49721. PMID 1323835.
Kaplan R, Morse B, Huebner K, Croce C, Howk R, Ravera M, Ricca G, Jaye M, Schlessinger J (1990). "Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain". Proc. Natl. Acad. Sci. U.S.A. 87 (18): 7000–4. Bibcode:1990PNAS...87.7000K. doi:10.1073/pnas.87.18.7000. PMC 54670. PMID 2169617.
Krueger NX, Streuli M, Saito H (1990). "Structural diversity and evolution of human receptor-like protein tyrosine phosphatases". EMBO J. 9 (10): 3241–52. doi:10.1002/j.1460-2075.1990.tb07523.x. PMC 552056. PMID 2170109.
Morton SM, Veile RA, Helms C, Lee M, Kuo WL, Gray J, Donis-Keller H (1998). "Subregional localization of 21 chromosome 7-specific expressed sequence tags (ESTs) by FISH using newly identified YACs and P1s". Genomics. 46 (3): 491–4. doi:10.1006/geno.1997.5051. PMID 9441757.
Onyango P, Lubyova B, Gardellin P, Kurzbauer R, Weith A (1998). "Molecular cloning and expression analysis of five novel genes in chromosome 1p36". Genomics. 50 (2): 187–98. doi:10.1006/geno.1997.5186. PMID 9653645.
Sanger Centre T, Washington University Genome Sequencing Cente T (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
Maeda N, Ichihara-Tanaka K, Kimura T, Kadomatsu K, Muramatsu T, Noda M (1999). "A receptor-like protein-tyrosine phosphatase PTPzeta/RPTPbeta binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to PTPzeta". J. Biol. Chem. 274 (18): 12474–9. doi:10.1074/jbc.274.18.12474. PMID 10212223.
Kawachi H, Tamura H, Watakabe I, Shintani T, Maeda N, Noda M (1999). "Protein tyrosine phosphatase zeta/RPTPbeta interacts with PSD-95/SAP90 family". Brain Res. Mol. Brain Res. 72 (1): 47–54. doi:10.1016/S0169-328X(99)00204-1. PMID 10521598.
Meng K, Rodriguez-Peña A, Dimitrov T, Chen W, Yamin M, Noda M, Deuel TF (2000). "Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2603–8. Bibcode:2000PNAS...97.2603M. doi:10.1073/pnas.020487997. PMC 15975. PMID 10706604.
Kawachi H, Fujikawa A, Maeda N, Noda M (2001). "Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase zeta /beta by the yeast substrate-trapping system". Proc. Natl. Acad. Sci. U.S.A. 98 (12): 6593–8. Bibcode:2001PNAS...98.6593K. doi:10.1073/pnas.041608698. PMC 34398. PMID 11381105.
Thomaidou D, Coquillat D, Meintanis S, Noda M, Rougon G, Matsas R (2001). "Soluble forms of NCAM and F3 neuronal cell adhesion molecules promote Schwann cell migration: identification of protein tyrosine phosphatases zeta/beta as the putative F3 receptors on Schwann cells". J. Neurochem. 78 (4): 767–78. doi:10.1046/j.1471-4159.2001.00454.x. PMID 11520897. S2CID 24682985.
Harroch S, Furtado GC, Brueck W, Rosenbluth J, Lafaille J, Chao M, Buxbaum JD, Schlessinger J (2002). "A critical role for the protein tyrosine phosphatase receptor type Z in functional recovery from demyelinating lesions". Nat. Genet. 32 (3): 411–4. doi:10.1038/ng1004. PMID 12355066. S2CID 19800079.
Müller S, Kunkel P, Lamszus K, Ulbricht U, Lorente GA, Nelson AM, von Schack D, Chin DJ, Lohr SC, Westphal M, Melcher T (2003). "A role for receptor tyrosine phosphatase zeta in glioma cell migration". Oncogene. 22 (43): 6661–8. doi:10.1038/sj.onc.1206763. PMID 14555979.
Bonora E, Lamb JA, Barnby G, Sykes N, Moberly T, Beyer KS, Klauck SM, Poustka F, Bacchelli E, Blasi F, Maestrini E, Battaglia A, Haracopos D, Pedersen L, Isager T, Eriksen G, Viskum B, Sorensen EU, Brondum-Nielsen K, Cotterill R, van Engeland H, de Jonge M, Kemner C, Steggehuis K, Scherpenisse M, Rutter M, Bolton PF, Parr JR, Poustka A, Bailey AJ, Monaco AP (2005). "Mutation screening and association analysis of six candidate genes for autism on chromosome 7q". Eur. J. Hum. Genet. 13 (2): 198–207. doi:10.1038/sj.ejhg.5201315. PMID 15523497.
Polykratis A, Katsoris P, Courty J, Papadimitriou E (2005). "Characterization of heparin affin regulatory peptide signaling in human endothelial cells". J. Biol. Chem. 280 (23): 22454–61. doi:10.1074/jbc.M414407200. PMID 15797857.
Wang V, Davis DA, Haque M, Huang LE, Yarchoan R (2005). "Differential gene up-regulation by hypoxia-inducible factor-1alpha and hypoxia-inducible factor-2alpha in HEK293T cells". Cancer Res. 65 (8): 3299–306. doi:10.1158/0008-5472.CAN-04-4130. PMID 15833863.
Lu KV, Jong KA, Kim GY, Singh J, Dia EQ, Yoshimoto K, Wang MY, Cloughesy TF, Nelson SF, Mischel PS (2005). "Differential induction of glioblastoma migration and growth by two forms of pleiotrophin". J. Biol. Chem. 280 (29): 26953–64. doi:10.1074/jbc.M502614200. PMID 15908427.

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs

Receptor type PTPs	PTPRA PTPRB PTPRC PTPRD PTPRE PTPRF PTPRG PTPRH PTPRJ PTPRK PTPRM PTPRN PTPRN2 PTPRO PTPRQ PTPRR PTPRS PTPRT PTPRU PTPRZ1 PTPRZ2
Non receptor type PTPs	PTPN1 PTPN2 PTPN3 PTPN4 PTPN5 PTPN6 PTPN7 PTPN9 PTPN11 PTPN12 PTPN13 PTPN14 PTPN18 PTPN20 PTPN21 PTPN22 PTPN23

VH1-like or
dual specific
phosphatases
(DSPs)

MAPK phosphatases (MKPs)	DUSP1 DUSP2 DUSP4 DUSP5 DUSP6 DUSP7 DUSP8 DUSP9 DUSP10 DUSP16 MK-STYX
Slingshots	SSH1 SSH2 SSH3
PRLs	PTP4A1 PTP4A2 PTP4A3
CDC14s	CDC14A CDC14B CDKN3 PTP9Q22
Atypical DSPs	DUSP3 DUSP11 DUSP12 DUSP13A DUSP13B DUSP14 DUSP15 DUSP18 DUSP19 DUSP21 DUSP22 DUSP23 DUSP24 DUSP25 DUSP26 DUSP27 EMP2A RNGTT STYX
Phosphatase and tensin homologs (PTENs)	PTEN TPIP TPTE TNS TENC1
Myotubularins	MTM1 MTMR2 MTMR3 MTMR4 MTMR5 MTMR6 MTMR7 MTMR8 MTMR9 MTMR10 MTMR11 MTMR12 MTMR13 MTMR14 MTMR15

Class II

ACP1

Class III

Cdc25
- CDC25A
- CDC25B
- CDC25C

Class IV

EYA1
EYA2
EYA3
EYA4

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)

3.1.11-16:
Exonuclease

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

3.1.21-31:
Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme;see ((Restriction enzyme)) UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Function

Clinical significance

References

Further reading