Basic Information

Symbol
PTPN13
RNA class
mRNA
Alias
Protein Tyrosine Phosphatase Non-Receptor Type 13 PTP-BAS PTP1E PTPL1 PTP-BL Protein Tyrosine Phosphatase, Non-Receptor Type 13 (APO-1/CD95 (Fas)-Associated Phosphatase) Tyrosine-Protein Phosphatase Non-Receptor Type 13 Fas-Associated Protein-Tyrosine Phosphatase 1 Protein-Tyrosine Phosphatase PTPL1 Protein-Tyrosine Phosphatase 1E EC 3.1.3.48 HPTPE1 FAP-1 PNP1 APO-1/CD95 (Fas)-Associated Phosphatase HPTP1E PTP-E1 PTPLE
Location (GRCh38)
4:86593944-86815180
UCSC Genome Browser Search in Marker Scope
Forensic tag(s)
-
External database
HGNC NCBI Ensembl OMIM UniProt GTEx

MANE select

Transcript ID
NM_080683.3
Sequence length
8548.0 nt
GC content
0.4347

Transcripts

ID Sequence Length GC content
NM_006264.3 NCBI
GAGUAGCUCCAGCGGCCACGCUGAGGCGAGGGUGACACACCAUGCUCAC… 8491 nt 0.4352
NM_080683.3 NCBI
GAGUAGCUCCAGCGGCCACGCUGAGGCGAGGGUGACACACCAUGCUCAC… 8548 nt 0.4347
NM_080684.3 NCBI
GAGUAGCUCCAGCGGCCACGCUGAGGCGAGGGUGACACACCAUGCUCAC… 7975 nt 0.4345
NM_080685.3 NCBI
GAGUAGCUCCAGCGGCCACGCUGAGGCGAGGGUGACACACCAUGCUCAC… 8563 nt 0.4347
Summary

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP is a large intracellular protein. It has a catalytic PTP domain at its C-terminus and two major structural domains: a region with five PDZ domains and a FERM domain that binds to plasma membrane and cytoskeletal elements. This PTP was found to interact with, and dephosphorylate, Fas receptor and IkappaBalpha through the PDZ domains. This suggests it has a role in Fas mediated programmed cell death. This PTP was also shown to interact with GTPase-activating protein, and thus may function as a regulator of Rho signaling pathways. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported. [provided by RefSeq, Oct 2008]

Forensic Context

No relevant information is available at the moment.