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Protein

Receptor-type tyrosine-protein phosphatase-like N

Gene

PTPRN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in vesicle-mediated secretory processes (PubMed:24843546). Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets (By similarity). Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation (PubMed:24843546). Plays a role in insulin secretion in response to glucose stimuli (PubMed:24843546). Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain (By similarity). In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH) (By similarity). Required to maintain normal levels of renin expression and renin release (By similarity). Seems to lack intrinsic enzyme activity (By similarity). May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization (By similarity).By similarity1 Publication
ICA512-transmembrane fragment: ICA512-TMF regulates dynamics and exocytosis of insulin secretory granules (SGs); binding of ICA512-TMF to SNTB2/beta-2-syntrophin is proposed to restrain SGs mobility and exocytosis by tethering them to the actin cytoskeleton depending on UTRN; the function is inhibited by cytoplasmic ICA512-CFF dimerizing with ICA512-TMF and displacing SNTB2.2 Publications
ICA512-cleaved cytosolic fragment: ICA512-CCF translocated to the nucleus promotes expression of insulin and other granule-related genes; the function implicates binding to and regulating activity of STAT5B probably by preventing its dephosphorylation and potentially by inducing its sumoylation by recruiting PIAS4 (PubMed:15596545, PubMed:16622421, PubMed:18178618). Enhances pancreatic beta-cell proliferation by converging with signaling by STAT5B and STAT3 (PubMed:15596545, PubMed:16622421, PubMed:18178618). ICA512-CCF located in the cytoplasm regulates dynamics and exocytosis of insulin secretory granules (SGs) by dimerizing with ICA512-TMF and displacing SNTB2 thus enhancing SGs mobility and exocytosis (PubMed:18824546, PubMed:20886068).5 Publications

GO - Molecular functioni

  • spectrin binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB
  • ubiquitin-like protein ligase binding Source: UniProtKB

GO - Biological processi

  • cytokine-mediated signaling pathway Source: Ensembl
  • dense core granule maturation Source: GO_Central
  • insulin secretion Source: GO_Central
  • insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • luteinization Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of type B pancreatic cell proliferation Source: UniProtKB
  • response to cAMP Source: Ensembl
  • response to estrogen Source: Ensembl
  • response to insulin Source: Ensembl
  • response to reactive oxygen species Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000054356-MONOMER.
BRENDAi3.1.3.48. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase-like N
Short name:
R-PTP-N
Alternative name(s):
Islet cell antigen 5121 Publication
Short name:
ICA 5121 Publication
Islet cell autoantigen 3
PTP IA-2
Cleaved into the following 3 chains:
ICA512-N-terminal fragment
Short name:
ICA512-NTF
ICA512-transmembrane fragment
Short name:
ICA512-TMF
ICA512-cleaved cytosolic fragment
Short name:
ICA512-CCF
Gene namesi
Name:PTPRN
Synonyms:ICA3, ICA512
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9676. PTPRN.

Subcellular locationi

  • Membrane By similarity; Single-pass type I membrane protein By similarity
  • Cytoplasmic vesiclesecretory vesicle membrane 1 Publication; Single-pass type I membrane protein Curated
  • Perikaryon By similarity
  • Cell projectionaxon By similarity
  • Cell junctionsynapse By similarity
  • Cell membrane 1 Publication; Single-pass type I membrane protein By similarity
  • Endosome By similarity

  • Note: Detected on neuronal secretory vesicles, but not on synaptic vesicles. Colocalizes with insulin-containing secretory granules (PubMed:25561468). Primarily detected on secretory vesicle membranes. Transiently found at the cell membrane, when secretory vesicles fuse with the cell membrane to release their cargo. Is then endocytosed and recycled to secretory vesicles via the Golgi apparatus membranes.By similarity1 Publication
ICA512-transmembrane fragment :
ICA512-cleaved cytosolic fragment :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini35 – 575LumenalSequence analysisAdd BLAST541
Transmembranei576 – 600HelicalSequence analysisAdd BLAST25
Topological domaini601 – 979CytoplasmicSequence analysisAdd BLAST379

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, Membrane, Nucleus, Synapse

Pathology & Biotechi

Involvement in diseasei

Autoantigen in insulin-dependent diabetes mellitus (IDDM).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi506N → A: Reduces N-glycosylation. 1 Publication1
Mutagenesisi524N → A: Reduces N-glycosylation. 1 Publication1
Mutagenesisi553G → D: Impairs normal processing and leads to retention in the endoplasmic reticulum and degradation. 1 Publication1

Keywords - Diseasei

Diabetes mellitus

Organism-specific databases

DisGeNETi5798.
OpenTargetsiENSG00000054356.
PharmGKBiPA34021.

Polymorphism and mutation databases

BioMutaiPTPRN.
DMDMi2499754.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34By similarityAdd BLAST34
ChainiPRO_000002545135 – 979Receptor-type tyrosine-protein phosphatase-like NAdd BLAST945
ChainiPRO_000043807935 – 448ICA512-N-terminal fragmentBy similarity1 PublicationAdd BLAST414
ChainiPRO_0000438080449 – 979ICA512-transmembrane fragmentBy similarity1 PublicationAdd BLAST531
ChainiPRO_0000438081659 – 979ICA512-cleaved cytosolic fragment2 PublicationsAdd BLAST321

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40Interchain (in homooligomer)1 Publication
Disulfide bondi47Interchain (in homooligomer)1 Publication
Modified residuei308PhosphoserineBy similarity1
Glycosylationi441O-linked (GalNAc...)2 Publications1
Glycosylationi506N-linked (GlcNAc...)Sequence analysis1 Publication1
Glycosylationi524N-linked (GlcNAc...)Sequence analysis1 Publication1
Cross-linki754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

N-glycosylated.1 Publication
O-glycosylated with core 1 or possibly core 8 glycans.3 Publications
Subject to proteolytic cleavage at multiple sites (PubMed:11483505). Subject to cleavage on a pair of basic residues (By similarity). On exocytosis of secretory granules in pancreatic beta-cells ICA512-TMF is transiently inserted in the plasma-membrane and cleaved by mu-type calpain CPN1 to yield ICA512-CCF (By similarity).By similarity1 Publication1 Publication
Sumoylated at two sites including Lys-754. Sumoylation decreases interaction with STAT5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei448 – 449CleavageBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ16849.
PeptideAtlasiQ16849.
PRIDEiQ16849.

PTM databases

DEPODiQ16849.
iPTMnetiQ16849.
PhosphoSitePlusiQ16849.
UniCarbKBiQ16849.

Miscellaneous databases

PMAP-CutDBQ16849.

Expressioni

Tissue specificityi

Expression is restricted to neuroendocrine cells. Found in pancreas, brain and pituitary.1 Publication

Gene expression databases

BgeeiENSG00000054356.
CleanExiHS_PTPRN.
ExpressionAtlasiQ16849. baseline and differential.
GenevisibleiQ16849. HS.

Organism-specific databases

HPAiHPA007179.

Interactioni

Subunit structurei

Homodimer; shown for the unprocessed protein (proICA512) in the endoplasmic reticulum and resolved during protein maturation as ICA512-TMF seems to be predominantly monomeric in secretory granules; however, ICA512-CCF interacts with ICA512-TMF disrupting the ICA512-TMF:SNTB2 complex. The isolated lumenal RESP18 homology domain has been shown to form disulfide-linked homooligomers (PubMed:25561468, PubMed:18824546, PubMed:26836020). Interacts (via cytoplasmic domain) with phosphorylated SNTB2; this protects PTPRN against cleavage by CAPN1 to produce ICA512-CCF. Dephosphorylation of SNTB2 upon insulin stimulation disrupts the interaction and results in PTPRN cleavage (PubMed:11483505). Interacts with SNX19 (PubMed:16273344). ICA512-CCF interacts with PIAS4; in the nucleus (PubMed:15596545). Interacts with STAT5B (phosphorylated); down-regulated by ICA512-CCF sumoylation; ICA512-CCF prevents STAT5B dephosphorylation; ICA512-CCF mediates interaction of STAT5B with PIAS4 (PubMed:15596545, PubMed:16622421). Interacts (via RESP18 homology domain) with insulin and proinsulin (PubMed:26836020). Interacts with PTPRN2, PTPRA and PTPRE (By similarity).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MADDQ8WXG64EBI-728153,EBI-310528
MALP211453EBI-10200782,EBI-3932027
PLP1P602013EBI-10200782,EBI-8653150
PPIAP629373EBI-728153,EBI-437708
PTPRSQ133325EBI-728153,EBI-711536
PTPRTO145223EBI-728153,EBI-728180
SNX19Q925434EBI-728153,EBI-728232
SPTBN4Q9H2542EBI-728153,EBI-308543

GO - Molecular functioni

  • spectrin binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB
  • ubiquitin-like protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111762. 17 interactors.
IntActiQ16849. 12 interactors.
MINTiMINT-1350221.
STRINGi9606.ENSP00000295718.

Structurei

Secondary structure

1979
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi471 – 477Combined sources7
Helixi483 – 497Combined sources15
Helixi501 – 503Combined sources3
Beta strandi504 – 510Combined sources7
Beta strandi513 – 518Combined sources6
Helixi527 – 536Combined sources10
Helixi538 – 545Combined sources8
Beta strandi549 – 555Combined sources7
Helixi692 – 704Combined sources13
Helixi706 – 717Combined sources12
Helixi727 – 730Combined sources4
Turni732 – 734Combined sources3
Helixi735 – 737Combined sources3
Helixi755 – 757Combined sources3
Beta strandi766 – 770Combined sources5
Beta strandi780 – 783Combined sources4
Helixi788 – 790Combined sources3
Helixi791 – 801Combined sources11
Beta strandi805 – 808Combined sources4
Beta strandi812 – 814Combined sources3
Beta strandi826 – 832Combined sources7
Beta strandi835 – 844Combined sources10
Beta strandi846 – 858Combined sources13
Turni859 – 861Combined sources3
Beta strandi864 – 872Combined sources9
Beta strandi877 – 880Combined sources4
Helixi885 – 896Combined sources12
Beta strandi905 – 908Combined sources4
Beta strandi910 – 913Combined sources4
Helixi914 – 930Combined sources17
Helixi938 – 946Combined sources9
Helixi956 – 975Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I1YX-ray2.23A/B681-979[»]
2QT7X-ray1.30A/B468-558[»]
3N01X-ray1.30A/B470-558[»]
3N4WX-ray1.45A/B470-558[»]
3NG8X-ray1.35A/B470-558[»]
3NP5X-ray1.80A/B/C/D470-558[»]
ProteinModelPortaliQ16849.
SMRiQ16849.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16849.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini709 – 969Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST261

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni35 – 131RESP18 homology domainAdd BLAST97
Regioni449 – 575Sufficient for dimerization of proICA5121 PublicationAdd BLAST127
Regioni601 – 732Sufficient for dimerization of proICA512By similarityAdd BLAST132

Domaini

The RESP18 homology domain is sufficient for targeting proICA512 to secretory granules.1 Publication

Sequence similaritiesi

Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0793. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000243992.
HOVERGENiHBG053762.
InParanoidiQ16849.
KOiK07817.
OMAiFLPYDHA.
OrthoDBiEOG091G0LUR.
PhylomeDBiQ16849.
TreeFamiTF351976.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR033522. PTPRN.
IPR021613. Receptor_IA-2_dom.
IPR029403. RESP18_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PANTHERiPTHR19134:SF2. PTHR19134:SF2. 1 hit.
PfamiPF11548. Receptor_IA-2. 1 hit.
PF14948. RESP18. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16849-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRRPRRPGGL GGSGGLRLLL CLLLLSSRPG GCSAVSAHGC LFDRRLCSHL
60 70 80 90 100
EVCIQDGLFG QCQVGVGQAR PLLQVTSPVL QRLQGVLRQL MSQGLSWHDD
110 120 130 140 150
LTQYVISQEM ERIPRLRPPE PRPRDRSGLA PKRPGPAGEL LLQDIPTGSA
160 170 180 190 200
PAAQHRLPQP PVGKGGAGAS SSLSPLQAEL LPPLLEHLLL PPQPPHPSLS
210 220 230 240 250
YEPALLQPYL FHQFGSRDGS RVSEGSPGMV SVGPLPKAEA PALFSRTASK
260 270 280 290 300
GIFGDHPGHS YGDLPGPSPA QLFQDSGLLY LAQELPAPSR ARVPRLPEQG
310 320 330 340 350
SSSRAEDSPE GYEKEGLGDR GEKPASPAVQ PDAALQRLAA VLAGYGVELR
360 370 380 390 400
QLTPEQLSTL LTLLQLLPKG AGRNPGGVVN VGADIKKTME GPVEGRDTAE
410 420 430 440 450
LPARTSPMPG HPTASPTSSE VQQVPSPVSS EPPKAARPPV TPVLLEKKSP
460 470 480 490 500
LGQSQPTVAG QPSARPAAEE YGYIVTDQKP LSLAAGVKLL EILAEHVHMS
510 520 530 540 550
SGSFINISVV GPALTFRIRH NEQNLSLADV TQQAGLVKSE LEAQTGLQIL
560 570 580 590 600
QTGVGQREEA AAVLPQTAHS TSPMRSVLLT LVALAGVAGL LVALAVALCV
610 620 630 640 650
RQHARQQDKE RLAALGPEGA HGDTTFEYQD LCRQHMATKS LFNRAEGPPE
660 670 680 690 700
PSRVSSVSSQ FSDAAQASPS SHSSTPSWCE EPAQANMDIS TGHMILAYME
710 720 730 740 750
DHLRNRDRLA KEWQALCAYQ AEPNTCATAQ GEGNIKKNRH PDFLPYDHAR
760 770 780 790 800
IKLKVESSPS RSDYINASPI IEHDPRMPAY IATQGPLSHT IADFWQMVWE
810 820 830 840 850
SGCTVIVMLT PLVEDGVKQC DRYWPDEGAS LYHVYEVNLV SEHIWCEDFL
860 870 880 890 900
VRSFYLKNVQ TQETRTLTQF HFLSWPAEGT PASTRPLLDF RRKVNKCYRG
910 920 930 940 950
RSCPIIVHCS DGAGRTGTYI LIDMVLNRMA KGVKEIDIAA TLEHVRDQRP
960 970
GLVRSKDQFE FALTAVAEEV NAILKALPQ
Length:979
Mass (Da):105,848
Last modified:November 1, 1997 - v1
Checksum:iA852B9063D29399D
GO
Isoform 2 (identifier: Q16849-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     479-508: KPLSLAAGVKLLEILAEHVHMSSGSFINIS → N

Note: No experimental confirmation available.
Show »
Length:950
Mass (Da):102,817
Checksum:iAA63FE699D560D7C
GO
Isoform 3 (identifier: Q16849-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.

Note: No experimental confirmation available.
Show »
Length:889
Mass (Da):96,261
Checksum:iBEEAF1F58AF81284
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti673S → G in BAG59024 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051762419S → R.Corresponds to variant rs35314717dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0458671 – 90Missing in isoform 3. 1 PublicationAdd BLAST90
Alternative sequenceiVSP_043654479 – 508KPLSL…FINIS → N in isoform 2. 1 PublicationAdd BLAST30

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18983 mRNA. Translation: AAA90974.1.
AK296335 mRNA. Translation: BAG59024.1.
AC114803 Genomic DNA. Translation: AAY24038.1.
CH471063 Genomic DNA. Translation: EAW70724.1.
CH471063 Genomic DNA. Translation: EAW70726.1.
BC070053 mRNA. Translation: AAH70053.1.
X62899 mRNA. Translation: CAA44688.2.
CCDSiCCDS2440.1. [Q16849-1]
CCDS56167.1. [Q16849-3]
CCDS56168.1. [Q16849-2]
PIRiI37577.
RefSeqiNP_001186692.1. NM_001199763.1. [Q16849-2]
NP_001186693.1. NM_001199764.1. [Q16849-3]
NP_002837.1. NM_002846.3. [Q16849-1]
UniGeneiHs.89655.

Genome annotation databases

EnsembliENST00000295718; ENSP00000295718; ENSG00000054356. [Q16849-1]
ENST00000409251; ENSP00000386638; ENSG00000054356. [Q16849-2]
ENST00000423636; ENSP00000392598; ENSG00000054356. [Q16849-3]
GeneIDi5798.
KEGGihsa:5798.
UCSCiuc002vkz.3. human. [Q16849-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18983 mRNA. Translation: AAA90974.1.
AK296335 mRNA. Translation: BAG59024.1.
AC114803 Genomic DNA. Translation: AAY24038.1.
CH471063 Genomic DNA. Translation: EAW70724.1.
CH471063 Genomic DNA. Translation: EAW70726.1.
BC070053 mRNA. Translation: AAH70053.1.
X62899 mRNA. Translation: CAA44688.2.
CCDSiCCDS2440.1. [Q16849-1]
CCDS56167.1. [Q16849-3]
CCDS56168.1. [Q16849-2]
PIRiI37577.
RefSeqiNP_001186692.1. NM_001199763.1. [Q16849-2]
NP_001186693.1. NM_001199764.1. [Q16849-3]
NP_002837.1. NM_002846.3. [Q16849-1]
UniGeneiHs.89655.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I1YX-ray2.23A/B681-979[»]
2QT7X-ray1.30A/B468-558[»]
3N01X-ray1.30A/B470-558[»]
3N4WX-ray1.45A/B470-558[»]
3NG8X-ray1.35A/B470-558[»]
3NP5X-ray1.80A/B/C/D470-558[»]
ProteinModelPortaliQ16849.
SMRiQ16849.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111762. 17 interactors.
IntActiQ16849. 12 interactors.
MINTiMINT-1350221.
STRINGi9606.ENSP00000295718.

PTM databases

DEPODiQ16849.
iPTMnetiQ16849.
PhosphoSitePlusiQ16849.
UniCarbKBiQ16849.

Polymorphism and mutation databases

BioMutaiPTPRN.
DMDMi2499754.

Proteomic databases

PaxDbiQ16849.
PeptideAtlasiQ16849.
PRIDEiQ16849.

Protocols and materials databases

DNASUi5798.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295718; ENSP00000295718; ENSG00000054356. [Q16849-1]
ENST00000409251; ENSP00000386638; ENSG00000054356. [Q16849-2]
ENST00000423636; ENSP00000392598; ENSG00000054356. [Q16849-3]
GeneIDi5798.
KEGGihsa:5798.
UCSCiuc002vkz.3. human. [Q16849-1]

Organism-specific databases

CTDi5798.
DisGeNETi5798.
GeneCardsiPTPRN.
HGNCiHGNC:9676. PTPRN.
HPAiHPA007179.
MIMi601773. gene.
neXtProtiNX_Q16849.
OpenTargetsiENSG00000054356.
PharmGKBiPA34021.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0793. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000243992.
HOVERGENiHBG053762.
InParanoidiQ16849.
KOiK07817.
OMAiFLPYDHA.
OrthoDBiEOG091G0LUR.
PhylomeDBiQ16849.
TreeFamiTF351976.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000054356-MONOMER.
BRENDAi3.1.3.48. 2681.

Miscellaneous databases

ChiTaRSiPTPRN. human.
EvolutionaryTraceiQ16849.
GeneWikiiPTPRN.
GenomeRNAii5798.
PMAP-CutDBQ16849.
PROiQ16849.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000054356.
CleanExiHS_PTPRN.
ExpressionAtlasiQ16849. baseline and differential.
GenevisibleiQ16849. HS.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR033522. PTPRN.
IPR021613. Receptor_IA-2_dom.
IPR029403. RESP18_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PANTHERiPTHR19134:SF2. PTHR19134:SF2. 1 hit.
PfamiPF11548. Receptor_IA-2. 1 hit.
PF14948. RESP18. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTPRN_HUMAN
AccessioniPrimary (citable) accession number: Q16849
Secondary accession number(s): B4DK12
, F5GZS3, Q08319, Q53QD6, Q6NSL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Does not possess catalytic activity due to replacement of highly conserved residues in tyrosine-protein phosphatase domain.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.