PTPRE_HUMAN » Receptor-type tyrosine-protein phosphatase epsilon

PTPRE_HUMAN » Receptor-type tyrosine-protein phosphatase epsilon
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
PTPRE_HUMAN » Receptor-type tyrosine-protein phosphatase epsilon » Protein-tyrosine phosphatase epsilon; R-PTP-epsilon;
Hydrophobic Thickness 33.2 ± 2.0 Å
Tilt Angle 0 ± 0°
ΔGtransfer -50.9 kcal/mol
ΔGfold -29.9 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 47-71 (46-75)
Pathways none
PDB 2jjd (107-697)
OPM none
Complexes none
Interactions

INSR, Complex: INSR:PTPRE, PubMed

PGFRB, Complex: PGFRB:PTPRE

PTPRD, Complex: PTPRE:PTPRD, PubMed

PTPRS, Complex: PTPRS:PTPRE, PubMed

Domains

AA: 159-393, PDBID: 2JJD, Subunit A, Seq Identity:100%, Protein-tyrosine phosphatase

AA: 451-688, PDBID: 2JJD, Subunit D, Seq Identity:100%, Protein-tyrosine phosphatase

UniProt annotation for PTPRE_HUMAN » Receptor-type tyrosine-protein phosphatase epsilon
FUNCTION: Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity).

FUNCTION: Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin- induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake (By similarity).

FUNCTION: Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+).

CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.

SUBUNIT: Monomer. Isoform 2: Homodimer. Can form oligomers. Dimerization is increased by oxidative stress and decreased by EGFR. Isoform 2 interacts with GRB2 (By similarity).

TISSUE SPECIFICITY: Expressed in giant cell tumor (osteoclastoma rich in multinucleated osteoclastic cells).

INDUCTION: Up-regulated by 12-O-tetradecanoylphorbol-13-acetate (TPA) in HL-60 cells.

DOMAIN: The tyrosine-protein phosphatase 2 domain (D2) mediates dimerization. The extreme N- and C- termini of the D2 domain act to inhibit dimerization and removal of these sequences increases dimerization and inhibits enzyme activity (By similarity).

UniProt features for PTPRE_HUMAN » Receptor-type tyrosine-protein phosphatase epsilon
SIGNAL 1 19 Potential.
CHAIN 20 700 Receptor-type tyrosine-protein phosphatase epsilon.
DOMAIN 135 394 Tyrosine-protein phosphatase 1.
DOMAIN 426 689 Tyrosine-protein phosphatase 2.
REGION 335 341 Substrate binding (By similarity).
ACT_SITE 335 335 Phosphocysteine intermediate (By similarity).
ACT_SITE 630 630 Phosphocysteine intermediate (By similarity).
Amino Acid Sequence for PTPRE_HUMAN » Receptor-type tyrosine-protein phosphatase epsilon
MEPLCPLLLV GFSLPLARAL RGNETTADSN ETTTTSGPPD PGASQPLLAW LLLPLLLLLL VLLLAAYFFR FRKQRKAVVS TSDKKMPNGI LEEQEQQRVM LLSRSPSGPK KYFPIPVEHL EEEIRIRSAD DCKQFREEFN SLPSGHIQGT FELANKEENR EKNRYPNILP NDHSRVILSQ LDGIPCSDYI NASYIDGYKE KNKFIAAQGP KQETVNDFWR MVWEQKSATI VMLTNLKERK EEKCHQYWPD QGCWTYGNIR VCVEDCVVLV DYTIRKFCIQ PQLPDGCKAP RLVSQLHFTS WPDFGVPFTP IGMLKFLKKV KTLNPVHAGP IVVHCSAGVG RTGTFIVIDA MMAMMHAEQK VDVFEFVSRI RNQRPQMVQT DMQYTFIYQA LLEYYLYGDT ELDVSSLEKH LQTMHGTTTH FDKIGLEEEF RKLTNVRIMK ENMRTGNLPA NMKKARVIQI IPYDFNRVIL SMKRGQEYTD YINASFIDGY RQKDYFIATQ GPLAHTVEDF WRMIWEWKSH TIVMLTEVQE REQDKCYQYW PTEGSVTHGE ITIEIKNDTL SEAISIRDFL VTLNQPQARQ EEQVRVVRQF HFHGWPEIGI PAEGKGMIDL IAAVQKQQQQ TGNHPITVHC SAGAGRTGTF IALSNILERV KAEGLLDVFQ AVKSLRLQRP HMVQTLEQYE FCYKVVQDFI DIFSDYANFK