Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

Implicated in neuroendocrine secretory processes. May be involved in processes specific for neurosecretory granules, such as their biogenesis, trafficking or regulated exocytosis or may have a general role in neuroendocrine functions. Seems to lack intrinsic enzyme activity. May play a role in the regulation of secretory granules via its interaction with SNTB2.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei448 – 4492CleavageSequence Analysis
Active sitei909 – 9091Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. phosphatase activity Source: InterPro
  2. spectrin binding Source: BHF-UCL

GO - Biological processi

  1. cytokine-mediated signaling pathway Source: Ensembl
  2. dense core granule maturation Source: GO_Central
  3. insulin secretion Source: GO_Central
  4. protein dephosphorylation Source: InterPro
  5. response to cAMP Source: Ensembl
  6. response to estrogen Source: Ensembl
  7. response to glucose Source: Ensembl
  8. response to insulin Source: Ensembl
  9. response to reactive oxygen species Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

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 512
Short name:
ICA 512
Islet cell autoantigen 3
PTP IA-2
Gene namesi
Name:PTPRN
Synonyms:ICA3, ICA512
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9676. PTPRN.

Subcellular locationi

Membrane; Single-pass type I membrane protein
Note: Neuroendocrine secretory granules.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 575541ExtracellularSequence AnalysisAdd
BLAST
Transmembranei576 – 60025HelicalSequence AnalysisAdd
BLAST
Topological domaini601 – 979379CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434By similarityAdd
BLAST
Chaini35 – 979945Receptor-type tyrosine-protein phosphatase-like NPRO_0000025451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi441 – 4411O-linked (GalNAc...)2 Publications
Glycosylationi506 – 5061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi524 – 5241N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

O-glycosylated with core 1 or possibly core 8 glycans.2 Publications
Appears to undergo multiple proteolytic cleavage at consecutive basic residues.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ16849.
PeptideAtlasiQ16849.
PRIDEiQ16849.

PTM databases

DEPODiQ16849.
PhosphoSiteiQ16849.

Miscellaneous databases

PMAP-CutDBQ16849.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ16849.
CleanExiHS_PTPRN.
ExpressionAtlasiQ16849. baseline and differential.
GenevestigatoriQ16849.

Organism-specific databases

HPAiHPA007179.

Interactioni

Subunit structurei

Interacts with phosphorylated SNTB2, protecting it from protein cleavage by CAPN1. Dephosphorylation of SNTB2 upon insulin stimulation disrupts the interaction and results in its cleavage.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111762. 8 interactions.
IntActiQ16849. 11 interactions.
MINTiMINT-1350221.
STRINGi9606.ENSP00000295718.

Structurei

Secondary structure

1
979
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi471 – 4777Combined sources
Helixi483 – 49715Combined sources
Helixi501 – 5033Combined sources
Beta strandi504 – 5107Combined sources
Beta strandi513 – 5186Combined sources
Helixi527 – 53610Combined sources
Helixi538 – 5458Combined sources
Beta strandi549 – 5557Combined sources
Helixi692 – 70413Combined sources
Helixi706 – 71712Combined sources
Helixi727 – 7304Combined sources
Turni732 – 7343Combined sources
Helixi735 – 7373Combined sources
Helixi755 – 7573Combined sources
Beta strandi766 – 7705Combined sources
Beta strandi780 – 7834Combined sources
Helixi788 – 7903Combined sources
Helixi791 – 80111Combined sources
Beta strandi805 – 8084Combined sources
Beta strandi812 – 8143Combined sources
Beta strandi826 – 8327Combined sources
Beta strandi835 – 84410Combined sources
Beta strandi846 – 85813Combined sources
Turni859 – 8613Combined sources
Beta strandi864 – 8729Combined sources
Beta strandi877 – 8804Combined sources
Helixi885 – 89612Combined sources
Beta strandi905 – 9084Combined sources
Beta strandi910 – 9134Combined sources
Helixi914 – 93017Combined sources
Helixi938 – 9469Combined sources
Helixi956 – 97520Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 468-558, 687-976.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16849.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini709 – 969261Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni909 – 9157Substrate bindingBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00780000121961.
HOGENOMiHOG000243992.
HOVERGENiHBG053762.
InParanoidiQ16849.
KOiK07817.
OMAiEVCIQDG.
OrthoDBiEOG7K9K30.
PhylomeDBiQ16849.
TreeFamiTF351976.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR021613. Receptor_IA-2_dom.
IPR029403. RESP18_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF11548. Receptor_IA-2. 1 hit.
PF14948. RESP18. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti673 – 6731S → G in BAG59024 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti419 – 4191S → R.
Corresponds to variant rs35314717 [ dbSNP | Ensembl ].
VAR_051762

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9090Missing in isoform 3. 1 PublicationVSP_045867Add
BLAST
Alternative sequencei479 – 50830KPLSL…FINIS → N in isoform 2. 1 PublicationVSP_043654Add
BLAST

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]
uc002vla.3. human. [Q16849-2]

Polymorphism databases

DMDMi2499754.

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
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. Positions 468-558, 687-976.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111762. 8 interactions.
IntActiQ16849. 11 interactions.
MINTiMINT-1350221.
STRINGi9606.ENSP00000295718.

PTM databases

DEPODiQ16849.
PhosphoSiteiQ16849.

Polymorphism databases

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]
uc002vla.3. human. [Q16849-2]

Organism-specific databases

CTDi5798.
GeneCardsiGC02M220118.
HGNCiHGNC:9676. PTPRN.
HPAiHPA007179.
MIMi601773. gene.
neXtProtiNX_Q16849.
PharmGKBiPA34021.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00780000121961.
HOGENOMiHOG000243992.
HOVERGENiHBG053762.
InParanoidiQ16849.
KOiK07817.
OMAiEVCIQDG.
OrthoDBiEOG7K9K30.
PhylomeDBiQ16849.
TreeFamiTF351976.

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.

Miscellaneous databases

ChiTaRSiPTPRN. human.
EvolutionaryTraceiQ16849.
GeneWikiiPTPRN.
GenomeRNAii5798.
NextBioi22580.
PMAP-CutDBQ16849.
PROiQ16849.
SOURCEiSearch...

Gene expression databases

BgeeiQ16849.
CleanExiHS_PTPRN.
ExpressionAtlasiQ16849. baseline and differential.
GenevestigatoriQ16849.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR021613. Receptor_IA-2_dom.
IPR029403. RESP18_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF11548. Receptor_IA-2. 1 hit.
PF14948. RESP18. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and identification of a receptor-type protein tyrosine phosphatase, IA-2, from human insulinoma."
    Lan M.S., Lu J., Goto Y., Notkins A.L.
    DNA Cell Biol. 13:505-514(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Insulinoma.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Thalamus.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  6. "Islet cell antigen 512 is a diabetes-specific islet autoantigen related to protein tyrosine phosphatases."
    Rabin D.U., Pleasic S.M., Shapiro J.A., Yoo-Warren H., Oles J., Hicks J.M., Goldstein D.E., Rae P.M.
    J. Immunol. 152:3183-3188(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 389-789, ROLE IN DIABETES MELLITUS.
    Tissue: Pancreatic islet.
  7. "ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules."
    Solimena M., Dirkx R. Jr., Hermel J.-M., Pleasic-Williams S., Shapiro J.A., Caron L., Rabin D.U.
    EMBO J. 15:2102-2114(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION, ROLE IN DIABETES MELLITUS.
  8. "Dephosphorylation of beta2-syntrophin and Ca2+/mu-calpain-mediated cleavage of ICA512 upon stimulation of insulin secretion."
    Ort T., Voronov S., Guo J., Zawalich K., Froehner S.C., Zawalich W., Solimena M.
    EMBO J. 20:4013-4023(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNTB2, PROTEOLYTIC PROCESSING, DEPHOSPHORYLATION.
  9. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-441, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
    Halim A., Ruetschi U., Larson G., Nilsson J.
    J. Proteome Res. 12:573-584(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-441, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Structure of the mature ectodomain of the human receptor-type protein-tyrosine phosphatase IA-2."
    Primo M.E., Klinke S., Sica M.P., Goldbaum F.A., Jakoncic J., Poskus E., Ermacora M.R.
    J. Biol. Chem. 283:4674-4681(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 468-558.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 681-979.

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: April 1, 2015
This is version 138 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

Miscellaneous

Autoantigen in insulin-dependent diabetes mellitus (IDDM).

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, 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

External Data

Dasty 3

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 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.