PTPRN2

Protein identityUniProt · HPA

UniProt accession

Q92932

Gene

PTPRN2

Ensembl

ENSG00000155093

Chromosome

7

Canonical length

1015 aa

Protein class

Disease related genes, Enzymes, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins, Transporters

Subcellular location

Vesicles

OverviewNCBI Gene

This gene encodes a protein with sequence similarity to receptor-like protein tyrosine phosphatases. However, tyrosine phosphatase activity has not been experimentally validated for this protein. Studies of the rat ortholog suggest that the encoded protein may instead function as a phosphatidylinositol phosphatase with the ability to dephosphorylate phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-diphosphate, and this function may be involved in the regulation of insulin secretion. This protein has been identified as an autoantigen in insulin-dependent diabetes mellitus. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2015]

Canonical amino-acid sequenceUniProt

1015 residues, UniProt reviewed canonical sequence.

>Q92932|PTPRN2
     1  MGPPLPLLLL LLLLLPPRVL PAAPSSVPRG RQLPGRLGCL LEEGLCGASE ACVNDGVFGR
    61  CQKVPAMDFY RYEVSPVALQ RLRVALQKLS GTGFTWQDDY TQYVMDQELA DLPKTYLRRP
   121  EASSPARPSK HSVGSERRYS REGGAALANA LRRHLPFLEA LSQAPASDVL ARTHTAQDRP
   181  PAEGDDRFSE SILTYVAHTS ALTYPPGSRT QLREDLLPRT LGQLQPDELS PKVDSGVDRH
   241  HLMAALSAYA AQRPPAPPGE GSLEPQYLLR APSRMPRPLL APAAPQKWPS PLGDSEDPSS
   301  TGDGARIHTL LKDLQRQPAE VRGLSGLELD GMAELMAGLM QGVDHGVARG SPGRAALGES
   361  GEQADGPKAT LRGDSFPDDG VQDDDDRLYQ EVHRLSATLG GLLQDHGSRL LPGALPFARP
   421  LDMERKKSEH PESSLSSEEE TAGVENVKSQ TYSKDLLGQQ PHSEPGAAAF GELQNQMPGP
   481  SKEEQSLPAG AQEALSDGLQ LEVQPSEEEA RGYIVTDRDP LRPEEGRRLV EDVARLLQVP
   541  SSAFADVEVL GPAVTFKVSA NVQNVTTEDV EKATVDNKDK LEETSGLKIL QTGVGSKSKL
   601  KFLPPQAEQE DSTKFIALTL VSLACILGVL LASGLIYCLR HSSQHRLKEK LSGLGGDPGA
   661  DATAAYQELC RQRMATRPPD RPEGPHTSRI SSVSSQFSDG PIPSPSARSS ASSWSEEPVQ
   721  SNMDISTGHM ILSYMEDHLK NKNRLEKEWE ALCAYQAEPN SSFVAQREEN VPKNRSLAVL
   781  TYDHSRVLLK AENSHSHSDY INASPIMDHD PRNPAYIATQ GPLPATVADF WQMVWESGCV
   841  VIVMLTPLAE NGVRQCYHYW PDEGSNLYHI YEVNLVSEHI WCEDFLVRSF YLKNLQTNET
   901  RTVTQFHFLS WYDRGVPSSS RSLLDFRRKV NKCYRGRSCP IIVHCSDGAG RSGTYVLIDM
   961  VLNKMAKGAK EIDIAATLEH LRDQRPGMVQ TKEQFEFALT AVAEEVNAIL KALPQ

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PTPRN2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Cell surface

Secreted

No

Transmembrane segments

1

Mean surface accessibility (rSASA)

0.48

Highest tissue expression

93 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about PTPRN2.

Disease | ImmuneIEDB

Conditions an epitope on PTPRN2 was assayed in.

• viral infectious disease B cell

Disease | AutoantibodyPubMed

Conditions in which antibodies against PTPRN2 are reported. Each links to that disease's full target list.

• Diabetes Mellitus, Type 1 5

ReferencesPubMed · IEDB

Publications for PTPRN2 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. IEDB — curated epitope assays from the Immune Epitope Database (Vita et al., Nucleic Acids Research 2019). Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.57

gnomAD pLI

0

gnomAD missense Z

0.06

DepMap mean gene effect

0.02

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• insulin secretion involved in cellular response to glucose stimulus
• lipid metabolic process
• neurotransmitter secretion
• protein dephosphorylation
• regulation of secretion

Molecular functions

• transmembrane receptor protein tyrosine phosphatase activity

Cellular components

• ficolin-1-rich granule membrane
• plasma membrane
• receptor complex
• secretory granule
• secretory granule membrane
• synapse
• synaptic vesicle membrane

Protein domainsUniProt · Pfam · InterPro

• Tyrosine-specific protein phosphatase, PTPase domain
• Tyrosine-specific protein phosphatases domain
• Protein-tyrosine phosphatase, catalytic
• Protein-tyrosine phosphatase, active site
• Protein-tyrosine phosphatase receptor IA-2 ectodomain
• Protein-tyrosine phosphatase-like
• RESP18 domain
• Receptor-type tyrosine-protein phosphatase-like N/N2
• Protein-tyrosine phosphatase receptor IA-2, ectodomain superfamily
• Protein-tyrosine phosphatase
• Protein-tyrosine phosphatase receptor IA-2
• RESP18 domain

KeywordsUniProt

• Acetylation
• Cytoplasmic vesicle
• Diabetes mellitus
• Glycoprotein
• Hydrolase
• Lipid metabolism
• Membrane
• Phospholipid metabolism
• Phosphoprotein
• Protein phosphatase
• Receptor
• Signal
• Synapse
• Transmembrane
• Transmembrane helix

InteractionsUniProt · HPA

Protein binding partners of PTPRN2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• AP1G1
• AP2M1
• HAP1
• MYO5A
• PTPRN