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Q9H3S7

- PTN23_HUMAN

UniProt

Q9H3S7 - PTN23_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 23

Gene

PTPN23

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis.3 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1392 – 13921Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cilium morphogenesis Source: UniProtKB
    2. protein transport Source: UniProtKB-KW
    3. regulation of cell migration Source: InterPro
    4. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cilium biogenesis/degradation, Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 23 (EC:3.1.3.48)
    Alternative name(s):
    His domain-containing protein tyrosine phosphatase
    Short name:
    HD-PTP
    Protein tyrosine phosphatase TD14
    Short name:
    PTP-TD14
    Gene namesi
    Name:PTPN23
    Synonyms:KIAA1471
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:14406. PTPN23.

    Subcellular locationi

    GO - Cellular componenti

    1. ciliary basal body Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    4. early endosome Source: UniProtKB
    5. endosome Source: UniProtKB
    6. extracellular vesicular exosome Source: UniProt
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi202 – 2021L → D: Nearly abolishes interaction with CHMP4B. Abolishes interaction with CHMP4B; when associated with D-206. 1 Publication
    Mutagenesisi206 – 2061I → D: Abolishes interaction with CHMP4B; when associated with D-202. 1 Publication
    Mutagenesisi678 – 6781F → D: Abolishes interaction with UBAP1. 1 Publication

    Organism-specific databases

    PharmGKBiPA33996.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16361636Tyrosine-protein phosphatase non-receptor type 23PRO_0000094777Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1123 – 11231Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H3S7.
    PaxDbiQ9H3S7.
    PeptideAtlasiQ9H3S7.
    PRIDEiQ9H3S7.

    PTM databases

    PhosphoSiteiQ9H3S7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H3S7.
    BgeeiQ9H3S7.
    CleanExiHS_PTPN23.
    GenevestigatoriQ9H3S7.

    Organism-specific databases

    HPAiHPA016845.

    Interactioni

    Subunit structurei

    Interacts with GRAP2 and GRB2. Interacts with UBAP1 and CHMP4B.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CHMP4BQ9H4442EBI-724478,EBI-749627
    GRAP2O757918EBI-724478,EBI-740418
    Grap2O891002EBI-724478,EBI-642151From a different organism.
    GRB2P629936EBI-724478,EBI-401755
    PDCD6O753403EBI-724478,EBI-352915
    PTK2Q053974EBI-724478,EBI-702142
    SH3GL2Q999622EBI-724478,EBI-77938
    TSG101Q998162EBI-724478,EBI-346882

    Protein-protein interaction databases

    BioGridi117430. 26 interactions.
    DIPiDIP-29923N.
    IntActiQ9H3S7. 14 interactions.
    MINTiMINT-1425077.
    STRINGi9606.ENSP00000265562.

    Structurei

    Secondary structure

    1
    1636
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 204
    Helixi23 – 3210
    Turni38 – 414
    Helixi42 – 5615
    Helixi62 – 8120
    Beta strandi94 – 974
    Turni99 – 1013
    Beta strandi104 – 1085
    Helixi110 – 13122
    Helixi137 – 16024
    Helixi167 – 1693
    Helixi171 – 19525
    Helixi200 – 22122
    Helixi224 – 2307
    Helixi233 – 26230
    Helixi266 – 28621
    Turni287 – 2893
    Helixi292 – 31827
    Helixi327 – 3293
    Helixi349 – 3524
    Turni356 – 3594

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RAUX-ray1.95A/B2-361[»]
    ProteinModelPortaliQ9H3S7.
    SMRiQ9H3S7. Positions 4-697, 1142-1459.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H3S7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 394387BRO1PROSITE-ProRule annotationAdd
    BLAST
    Repeati250 – 28334TPR 1Add
    BLAST
    Repeati374 – 40734TPR 2Add
    BLAST
    Repeati953 – 95421
    Repeati955 – 95622
    Repeati957 – 95823
    Repeati959 – 96024
    Repeati961 – 96225
    Repeati963 – 96426
    Domaini1192 – 1452261Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni770 – 1130361HisAdd
    BLAST
    Regioni953 – 964126 X 2 AA approximate tandem repeats of P-QAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili550 – 62374Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi716 – 1108393Pro-richAdd
    BLAST
    Compositional biasi1509 – 157365Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BRO1 domain.PROSITE-ProRule annotation
    Contains 2 TPR repeats.Curated
    Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG5599.
    HOVERGENiHBG082231.
    InParanoidiQ9H3S7.
    KOiK18040.
    OMAiIARCYTM.
    OrthoDBiEOG72C4ZH.
    PhylomeDBiQ9H3S7.
    TreeFamiTF323502.

    Family and domain databases

    Gene3Di1.25.40.280. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR025304. ALIX_V_dom.
    IPR004328. BRO1_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR028770. PTPN23.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PANTHERiPTHR19134:SF27. PTHR19134:SF27. 1 hit.
    PfamiPF13949. ALIX_LYPXL_bnd. 1 hit.
    PF03097. BRO1. 1 hit.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM01041. BRO1. 1 hit.
    SM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS51180. BRO1. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9H3S7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAVPRMPMI WLDLKEAGDF HFQPAVKKFV LKNYGENPEA YNEELKKLEL     50
    LRQNAVRVPR DFEGCSVLRK YLGQLHYLQS RVPMGSGQEA AVPVTWTEIF 100
    SGKSVAHEDI KYEQACILYN LGALHSMLGA MDKRVSEEGM KVSCTHFQCA 150
    AGAFAYLREH FPQAYSVDMS RQILTLNVNL MLGQAQECLL EKSMLDNRKS 200
    FLVARISAQV VDYYKEACRA LENPDTASLL GRIQKDWKKL VQMKIYYFAA 250
    VAHLHMGKQA EEQQKFGERV AYFQSALDKL NEAIKLAKGQ PDTVQDALRF 300
    TMDVIGGKYN SAKKDNDFIY HEAVPALDTL QPVKGAPLVK PLPVNPTDPA 350
    VTGPDIFAKL VPMAAHEASS LYSEEKAKLL REMMAKIEDK NEVLDQFMDS 400
    MQLDPETVDN LDAYSHIPPQ LMEKCAALSV RPDTVRNLVQ SMQVLSGVFT 450
    DVEASLKDIR DLLEEDELLE QKFQEAVGQA GAISITSKAE LAEVRREWAK 500
    YMEVHEKASF TNSELHRAMN LHVGNLRLLS GPLDQVRAAL PTPALSPEDK 550
    AVLQNLKRIL AKVQEMRDQR VSLEQQLREL IQKDDITASL VTTDHSEMKK 600
    LFEEQLKKYD QLKVYLEQNL AAQDRVLCAL TEANVQYAAV RRVLSDLDQK 650
    WNSTLQTLVA SYEAYEDLMK KSQEGRDFYA DLESKVAALL ERTQSTCQAR 700
    EAARQQLLDR ELKKKPPPRP TAPKPLLPRR EESEAVEAGD PPEELRSLPP 750
    DMVAGPRLPD TFLGSATPLH FPPSPFPSST GPGPHYLSGP LPPGTYSGPT 800
    QLIQPRAPGP HAMPVAPGPA LYPAPAYTPE LGLVPRSSPQ HGVVSSPYVG 850
    VGPAPPVAGL PSAPPPQFSG PELAMAVRPA TTTVDSIQAP IPSHTAPRPN 900
    PTPAPPPPCF PVPPPQPLPT PYTYPAGAKQ PIPAQHHFSS GIPAGFPAPR 950
    IGPQPQPHPQ PHPSQAFGPQ PPQQPLPLQH PHLFPPQAPG LLPPQSPYPY 1000
    APQPGVLGQP PPPLHTQLYP GPAQDPLPAH SGALPFPSPG PPQPPHPPLA 1050
    YGPAPSTRPM GPQAAPLTIR GPSSAGQSTP SPHLVPSPAP SPGPGPVPPR 1100
    PPAAEPPPCL RRGAAAADLL SSSPESQHGG TQSPGGGQPL LQPTKVDAAE 1150
    GRRPQALRLI ERDPYEHPER LRQLQQELEA FRGQLGDVGA LDTVWRELQD 1200
    AQEHDARGRS IAIARCYSLK NRHQDVMPYD SNRVVLRSGK DDYINASCVE 1250
    GLSPYCPPLV ATQAPLPGTA ADFWLMVHEQ KVSVIVMLVS EAEMEKQKVA 1300
    RYFPTERGQP MVHGALSLAL SSVRSTETHV ERVLSLQFRD QSLKRSLVHL 1350
    HFPTWPELGL PDSPSNLLRF IQEVHAHYLH QRPLHTPIIV HCSSGVGRTG 1400
    AFALLYAAVQ EVEAGNGIPE LPQLVRRMRQ QRKHMLQEKL HLRFCYEAVV 1450
    RHVEQVLQRH GVPPPCKPLA SASISQKNHL PQDSQDLVLG GDVPISSIQA 1500
    TIAKLSIRPP GGLESPVASL PGPAEPPGLP PASLPESTPI PSSSPPPLSS 1550
    PLPEAPQPKE EPPVPEAPSS GPPSSSLELL ASLTPEAFSL DSSLRGKQRM 1600
    SKHNFLQAHN GQGLRATRPS DDPLSLLDPL WTLNKT 1636
    Length:1,636
    Mass (Da):178,974
    Last modified:March 1, 2001 - v1
    Checksum:i536BDDF9D3DC95C0
    GO

    Sequence cautioni

    The sequence BAA95995.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti647 – 6471L → G in CAB53676. (PubMed:17974005)Curated
    Sequence conflicti1087 – 10871S → P in CAB53676. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti944 – 9441A → T.2 Publications
    Corresponds to variant rs6780013 [ dbSNP | Ensembl ].
    VAR_022682
    Natural varianti1099 – 10991P → S in a lung cancer cell line; may be a common polymorphism. 1 Publication
    Corresponds to variant rs149563514 [ dbSNP | Ensembl ].
    VAR_022683

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025194 mRNA. Translation: BAB19280.1.
    AF290614 mRNA. Translation: AAK28025.1.
    AK289502 mRNA. Translation: BAF82191.1.
    CH471055 Genomic DNA. Translation: EAW64823.1.
    BC004881 mRNA. Translation: AAH04881.2.
    BC027711 mRNA. Translation: AAH27711.2.
    BC089042 mRNA. Translation: AAH89042.1.
    AB040904 mRNA. Translation: BAA95995.2. Different initiation.
    AL110210 mRNA. Translation: CAB53676.1.
    BT009758 mRNA. Translation: AAP88760.1.
    AF169350 mRNA. Translation: AAD50276.1.
    CCDSiCCDS2754.1.
    PIRiT14756.
    RefSeqiNP_056281.1. NM_015466.2.
    UniGeneiHs.25524.

    Genome annotation databases

    EnsembliENST00000265562; ENSP00000265562; ENSG00000076201.
    GeneIDi25930.
    KEGGihsa:25930.
    UCSCiuc003crf.1. human.

    Polymorphism databases

    DMDMi68053318.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025194 mRNA. Translation: BAB19280.1 .
    AF290614 mRNA. Translation: AAK28025.1 .
    AK289502 mRNA. Translation: BAF82191.1 .
    CH471055 Genomic DNA. Translation: EAW64823.1 .
    BC004881 mRNA. Translation: AAH04881.2 .
    BC027711 mRNA. Translation: AAH27711.2 .
    BC089042 mRNA. Translation: AAH89042.1 .
    AB040904 mRNA. Translation: BAA95995.2 . Different initiation.
    AL110210 mRNA. Translation: CAB53676.1 .
    BT009758 mRNA. Translation: AAP88760.1 .
    AF169350 mRNA. Translation: AAD50276.1 .
    CCDSi CCDS2754.1.
    PIRi T14756.
    RefSeqi NP_056281.1. NM_015466.2.
    UniGenei Hs.25524.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RAU X-ray 1.95 A/B 2-361 [» ]
    ProteinModelPortali Q9H3S7.
    SMRi Q9H3S7. Positions 4-697, 1142-1459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117430. 26 interactions.
    DIPi DIP-29923N.
    IntActi Q9H3S7. 14 interactions.
    MINTi MINT-1425077.
    STRINGi 9606.ENSP00000265562.

    PTM databases

    PhosphoSitei Q9H3S7.

    Polymorphism databases

    DMDMi 68053318.

    Proteomic databases

    MaxQBi Q9H3S7.
    PaxDbi Q9H3S7.
    PeptideAtlasi Q9H3S7.
    PRIDEi Q9H3S7.

    Protocols and materials databases

    DNASUi 25930.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265562 ; ENSP00000265562 ; ENSG00000076201 .
    GeneIDi 25930.
    KEGGi hsa:25930.
    UCSCi uc003crf.1. human.

    Organism-specific databases

    CTDi 25930.
    GeneCardsi GC03P047397.
    HGNCi HGNC:14406. PTPN23.
    HPAi HPA016845.
    MIMi 606584. gene.
    neXtProti NX_Q9H3S7.
    PharmGKBi PA33996.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOVERGENi HBG082231.
    InParanoidi Q9H3S7.
    KOi K18040.
    OMAi IARCYTM.
    OrthoDBi EOG72C4ZH.
    PhylomeDBi Q9H3S7.
    TreeFami TF323502.

    Miscellaneous databases

    ChiTaRSi PTPN23. human.
    EvolutionaryTracei Q9H3S7.
    GeneWikii PTPN23.
    GenomeRNAii 25930.
    NextBioi 47476.
    PROi Q9H3S7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H3S7.
    Bgeei Q9H3S7.
    CleanExi HS_PTPN23.
    Genevestigatori Q9H3S7.

    Family and domain databases

    Gene3Di 1.25.40.280. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR025304. ALIX_V_dom.
    IPR004328. BRO1_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR028770. PTPN23.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    PANTHERi PTHR19134:SF27. PTHR19134:SF27. 1 hit.
    Pfami PF13949. ALIX_LYPXL_bnd. 1 hit.
    PF03097. BRO1. 1 hit.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM01041. BRO1. 1 hit.
    SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS51180. BRO1. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "HD-PTP: a novel protein tyrosine phosphatase gene on human chromosome 3p21.3."
      Toyooka S., Ouchida M., Jitsumori Y., Tsukuda K., Sakai A., Nakamura A., Shimizu N., Shimizu K.
      Biochem. Biophys. Res. Commun. 278:671-678(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-1099, SUBCELLULAR LOCATION.
      Tissue: Stomach cancer.
    2. "Cloning, chromosomal assignment and tissue expression of a novel human protein tyrosine phosphatase (PTP-TD14) gene."
      Qu X., Zhai Y., Wei H., Zhang C., Xing G., Lu C., Wang M., He F.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "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].
      Tissue: Cerebellum.
    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].
      Tissue: Muscle, Ovary and Skin.
    6. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1383, VARIANT THR-944.
      Tissue: Brain.
    7. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-1636, VARIANT THR-944.
      Tissue: Brain.
    9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1060-1636.
    10. "Differential expression of PTPase RNAs resulting from K562 differentiation induced by PMA."
      Dayton M.A., Blanchard K.L.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1351-1493.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "The Bro1-related protein HD-PTP/PTPN23 is required for endosomal cargo sorting and multivesicular body morphogenesis."
      Doyotte A., Mironov A., McKenzie E., Woodman P.
      Proc. Natl. Acad. Sci. U.S.A. 105:6308-6313(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHMP4B, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-202 AND ILE-206.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Functional genomic screen for modulators of ciliogenesis and cilium length."
      Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
      Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL."
      Tanase C.A.
      PLoS ONE 5:E14339-E14339(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRAP2 AND GRB2, SUBCELLULAR LOCATION.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "UBAP1 is a component of an endosome-specific ESCRT-I complex that is essential for MVB sorting."
      Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A., Brownhill K., Bennion J., Pickering-Brown S., Woodman P.
      Curr. Biol. 21:1245-1250(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UBAP1, SUBCELLULAR LOCTION, MUTAGENESIS OF PHE-678.
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release."
      Sette P., Mu R., Dussupt V., Jiang J., Snyder G., Smith P., Xiao T.S., Bouamr F.
      Structure 19:1485-1495(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-361.

    Entry informationi

    Entry nameiPTN23_HUMAN
    AccessioniPrimary (citable) accession number: Q9H3S7
    Secondary accession number(s): A8K0D7
    , Q7KZF8, Q8N6Z5, Q9BSR5, Q9P257, Q9UG03, Q9UMZ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 117 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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