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Q16849

- PTPRN_HUMAN

UniProt

Q16849 - PTPRN_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase-like N

Gene

PTPRN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    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. protein binding Source: IntAct
    2. spectrin binding Source: BHF-UCL
    3. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Ensembl
    2. peptidyl-tyrosine dephosphorylation Source: GOC
    3. response to cAMP Source: Ensembl
    4. response to estrogen Source: Ensembl
    5. response to glucose Source: Ensembl
    6. response to insulin Source: Ensembl
    7. response to reactive oxygen species Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    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: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9676. PTPRN.

    Subcellular locationi

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

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc

    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

    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

    ArrayExpressiQ16849.
    BgeeiQ16849.
    CleanExiHS_PTPRN.
    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. 5 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 – 4777
    Helixi483 – 49715
    Helixi501 – 5033
    Beta strandi504 – 5107
    Beta strandi513 – 5186
    Helixi527 – 53610
    Helixi538 – 5458
    Beta strandi549 – 5557
    Helixi692 – 70413
    Helixi706 – 71712
    Helixi727 – 7304
    Turni732 – 7343
    Helixi735 – 7373
    Helixi755 – 7573
    Beta strandi766 – 7705
    Beta strandi780 – 7834
    Helixi788 – 7903
    Helixi791 – 80111
    Beta strandi805 – 8084
    Beta strandi812 – 8143
    Beta strandi826 – 8327
    Beta strandi835 – 84410
    Beta strandi846 – 85813
    Turni859 – 8613
    Beta strandi864 – 8729
    Beta strandi877 – 8804
    Helixi885 – 89612
    Beta strandi905 – 9084
    Beta strandi910 – 9134
    Helixi914 – 93017
    Helixi938 – 9469
    Helixi956 – 97520

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei576 – 60025HelicalSequence AnalysisAdd
    BLAST

    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.
    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. Align

    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

    MRRPRRPGGL GGSGGLRLLL CLLLLSSRPG GCSAVSAHGC LFDRRLCSHL    50
    EVCIQDGLFG QCQVGVGQAR PLLQVTSPVL QRLQGVLRQL MSQGLSWHDD 100
    LTQYVISQEM ERIPRLRPPE PRPRDRSGLA PKRPGPAGEL LLQDIPTGSA 150
    PAAQHRLPQP PVGKGGAGAS SSLSPLQAEL LPPLLEHLLL PPQPPHPSLS 200
    YEPALLQPYL FHQFGSRDGS RVSEGSPGMV SVGPLPKAEA PALFSRTASK 250
    GIFGDHPGHS YGDLPGPSPA QLFQDSGLLY LAQELPAPSR ARVPRLPEQG 300
    SSSRAEDSPE GYEKEGLGDR GEKPASPAVQ PDAALQRLAA VLAGYGVELR 350
    QLTPEQLSTL LTLLQLLPKG AGRNPGGVVN VGADIKKTME GPVEGRDTAE 400
    LPARTSPMPG HPTASPTSSE VQQVPSPVSS EPPKAARPPV TPVLLEKKSP 450
    LGQSQPTVAG QPSARPAAEE YGYIVTDQKP LSLAAGVKLL EILAEHVHMS 500
    SGSFINISVV GPALTFRIRH NEQNLSLADV TQQAGLVKSE LEAQTGLQIL 550
    QTGVGQREEA AAVLPQTAHS TSPMRSVLLT LVALAGVAGL LVALAVALCV 600
    RQHARQQDKE RLAALGPEGA HGDTTFEYQD LCRQHMATKS LFNRAEGPPE 650
    PSRVSSVSSQ FSDAAQASPS SHSSTPSWCE EPAQANMDIS TGHMILAYME 700
    DHLRNRDRLA KEWQALCAYQ AEPNTCATAQ GEGNIKKNRH PDFLPYDHAR 750
    IKLKVESSPS RSDYINASPI IEHDPRMPAY IATQGPLSHT IADFWQMVWE 800
    SGCTVIVMLT PLVEDGVKQC DRYWPDEGAS LYHVYEVNLV SEHIWCEDFL 850
    VRSFYLKNVQ TQETRTLTQF HFLSWPAEGT PASTRPLLDF RRKVNKCYRG 900
    RSCPIIVHCS DGAGRTGTYI LIDMVLNRMA KGVKEIDIAA TLEHVRDQRP 950
    GLVRSKDQFE FALTAVAEEV NAILKALPQ 979
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2440.1. [Q16849-1 ]
    CCDS56167.1. [Q16849-3 ]
    CCDS56168.1. [Q16849-2 ]
    PIRi I37577.
    RefSeqi NP_001186692.1. NM_001199763.1. [Q16849-2 ]
    NP_001186693.1. NM_001199764.1. [Q16849-3 ]
    NP_002837.1. NM_002846.3. [Q16849-1 ]
    UniGenei Hs.89655.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I1Y X-ray 2.23 A/B 681-979 [» ]
    2QT7 X-ray 1.30 A/B 468-558 [» ]
    3N01 X-ray 1.30 A/B 470-558 [» ]
    3N4W X-ray 1.45 A/B 470-558 [» ]
    3NG8 X-ray 1.35 A/B 470-558 [» ]
    3NP5 X-ray 1.80 A/B/C/D 470-558 [» ]
    ProteinModelPortali Q16849.
    SMRi Q16849. Positions 468-558, 687-976.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111762. 5 interactions.
    IntActi Q16849. 11 interactions.
    MINTi MINT-1350221.
    STRINGi 9606.ENSP00000295718.

    PTM databases

    PhosphoSitei Q16849.

    Polymorphism databases

    DMDMi 2499754.

    Proteomic databases

    PaxDbi Q16849.
    PeptideAtlasi Q16849.
    PRIDEi Q16849.

    Protocols and materials databases

    DNASUi 5798.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295718 ; ENSP00000295718 ; ENSG00000054356 . [Q16849-1 ]
    ENST00000409251 ; ENSP00000386638 ; ENSG00000054356 . [Q16849-2 ]
    ENST00000423636 ; ENSP00000392598 ; ENSG00000054356 . [Q16849-3 ]
    GeneIDi 5798.
    KEGGi hsa:5798.
    UCSCi uc002vkz.3. human. [Q16849-1 ]
    uc002vla.3. human. [Q16849-2 ]

    Organism-specific databases

    CTDi 5798.
    GeneCardsi GC02M220118.
    HGNCi HGNC:9676. PTPRN.
    HPAi HPA007179.
    MIMi 601773. gene.
    neXtProti NX_Q16849.
    PharmGKBi PA34021.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000243992.
    HOVERGENi HBG053762.
    InParanoidi Q16849.
    KOi K07817.
    OMAi EVCIQDG.
    OrthoDBi EOG7K9K30.
    PhylomeDBi Q16849.
    TreeFami TF351976.

    Miscellaneous databases

    EvolutionaryTracei Q16849.
    GeneWikii PTPRN.
    GenomeRNAii 5798.
    NextBioi 22580.
    PMAP-CutDB Q16849.
    PROi Q16849.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16849.
    Bgeei Q16849.
    CleanExi HS_PTPRN.
    Genevestigatori Q16849.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR029021. 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 ]
    Pfami PF11548. Receptor_IA-2. 1 hit.
    PF14948. RESP18. 1 hit.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(1994) [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(2004) [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(2005) [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(2004) [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(1994) [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(1996) [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(2001) [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(2011) [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(2013) [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(2008) [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: October 1, 2014
    This is version 132 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).

    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