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P23471

- PTPRZ_HUMAN

UniProt

P23471 - PTPRZ_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase zeta

Gene

PTPRZ1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 4 (24 Mar 2009)
      Previous versions | rss
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    Functioni

    Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1901 – 19011SubstrateBy similarity
    Active sitei1933 – 19331Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei1977 – 19771SubstrateBy similarity
    Sitei2223 – 22231Ancestral active site

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein tyrosine phosphatase activity Source: UniProtKB
    3. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. axonogenesis Source: Ensembl
    2. central nervous system development Source: ProtInc
    3. learning or memory Source: UniProtKB
    4. oligodendrocyte differentiation Source: UniProtKB
    5. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    6. protein dephosphorylation Source: ProtInc
    7. regulation of oligodendrocyte progenitor proliferation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SignaLinkiP23471.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase zeta (EC:3.1.3.48)
    Short name:
    R-PTP-zeta
    Alternative name(s):
    Protein-tyrosine phosphatase receptor type Z polypeptide 1
    Protein-tyrosine phosphatase receptor type Z polypeptide 2
    R-PTP-zeta-2
    Gene namesi
    Name:PTPRZ1
    Synonyms:HTPZP2, PTPRZ, PTPRZ2, PTPZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9685. PTPRZ1.

    Subcellular locationi

    Isoform 1 : Cell membrane; Single-pass type I membrane protein. Secreted By similarity
    Note: A secreted form is apparently generated by shedding of the extracellular domain.By similarity

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc
    2. perineuronal net Source: Ensembl
    3. proteinaceous extracellular matrix Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34029.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424By similarityAdd
    BLAST
    Chaini25 – 23152291Receptor-type tyrosine-protein phosphatase zetaPRO_0000025468Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi56 ↔ 2401 Publication
    Glycosylationi105 – 1051N-linked (GlcNAc...)1 Publication
    Disulfide bondi133 ↔ 2641 Publication
    Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi587 – 5871O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi602 – 6021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi629 – 6291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi637 – 6371O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi997 – 9971O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi1017 – 10171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1050 – 10501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1082 – 10821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1122 – 11221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1457 – 14571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1549 – 15491O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi1551 – 15511O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi1562 – 15621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1618 – 16181N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2055 – 20551Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP23471.
    PRIDEiP23471.

    PTM databases

    PhosphoSiteiP23471.

    Expressioni

    Tissue specificityi

    Specifically expressed in the central nervous system, where it is localized in the Purkinje cell layer of the cerebellum, the dentate gyrus, and the subependymal layer of the anterior horn of the lateral ventricle. Developmentally regulated in the brain.1 Publication

    Gene expression databases

    ArrayExpressiP23471.
    BgeeiP23471.
    CleanExiHS_PTPRZ1.
    GenevestigatoriP23471.

    Organism-specific databases

    HPAiCAB025106.
    HPA015103.

    Interactioni

    Subunit structurei

    The carbonic-anhydrase like domain interacts with CNTN1 (contactin).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALKQ9UM732EBI-2263175,EBI-357361

    Protein-protein interaction databases

    BioGridi111767. 8 interactions.
    DIPiDIP-42063N.
    IntActiP23471. 9 interactions.
    MINTiMINT-1350337.
    STRINGi9606.ENSP00000377047.

    Structurei

    Secondary structure

    1
    2315
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 423
    Helixi46 – 483
    Helixi49 – 524
    Helixi54 – 574
    Beta strandi58 – 603
    Helixi68 – 703
    Beta strandi71 – 733
    Beta strandi78 – 847
    Beta strandi94 – 974
    Beta strandi102 – 1054
    Beta strandi111 – 1166
    Beta strandi121 – 13414
    Beta strandi141 – 1444
    Beta strandi150 – 1589
    Turni160 – 1623
    Helixi166 – 1716
    Beta strandi176 – 18510
    Helixi191 – 1933
    Helixi194 – 2029
    Beta strandi209 – 2113
    Helixi217 – 2204
    Beta strandi226 – 2338
    Beta strandi244 – 2518
    Beta strandi253 – 2553
    Helixi257 – 2615
    Helixi262 – 2654
    Beta strandi267 – 2726
    Beta strandi275 – 2806

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JXFX-ray2.00A/B34-302[»]
    3S97X-ray2.30A/B34-302[»]
    ProteinModelPortaliP23471.
    SMRiP23471. Positions 34-301, 313-409, 1698-2284.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23471.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 16361612ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1663 – 2315653CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1637 – 166226HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 300265Alpha-carbonic anhydraseAdd
    BLAST
    Domaini314 – 413100Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1717 – 1992276Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2023 – 2282260Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1933 – 19397Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000090262.
    HOVERGENiHBG053760.
    InParanoidiP23471.
    KOiK08114.
    OMAiVMNDSDT.
    OrthoDBiEOG7K6PT4.
    PhylomeDBiP23471.
    TreeFamiTF351978.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.10.200.10. 1 hit.
    3.90.190.10. 2 hits.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00194. Carb_anhydrase. 1 hit.
    PF00041. fn3. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    SM00060. FN3. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF51069. SSF51069. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEiPS51144. ALPHA_CA_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [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: P23471-1) [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

    MRILKRFLAC IQLLCVCRLD WANGYYRQQR KLVEEIGWSY TGALNQKNWG     50
    KKYPTCNSPK QSPINIDEDL TQVNVNLKKL KFQGWDKTSL ENTFIHNTGK 100
    TVEINLTNDY RVSGGVSEMV FKASKITFHW GKCNMSSDGS EHSLEGQKFP 150
    LEMQIYCFDA DRFSSFEEAV KGKGKLRALS ILFEVGTEEN LDFKAIIDGV 200
    ESVSRFGKQA ALDPFILLNL LPNSTDKYYI YNGSLTSPPC TDTVDWIVFK 250
    DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY 300
    TGKEEIHEAV CSSEPENVQA DPENYTSLLV TWERPRVVYD TMIEKFAVLY 350
    QQLDGEDQTK HEFLTDGYQD LGAILNNLLP NMSYVLQIVA ICTNGLYGKY 400
    SDQLIVDMPT DNPELDLFPE LIGTEEIIKE EEEGKDIEEG AIVNPGRDSA 450
    TNQIRKKEPQ ISTTTHYNRI GTKYNEAKTN RSPTRGSEFS GKGDVPNTSL 500
    NSTSQPVTKL ATEKDISLTS QTVTELPPHT VEGTSASLND GSKTVLRSPH 550
    MNLSGTAESL NTVSITEYEE ESLLTSFKLD TGAEDSSGSS PATSAIPFIS 600
    ENISQGYIFS SENPETITYD VLIPESARNA SEDSTSSGSE ESLKDPSMEG 650
    NVWFPSSTDI TAQPDVGSGR ESFLQTNYTE IRVDESEKTT KSFSAGPVMS 700
    QGPSVTDLEM PHYSTFAYFP TEVTPHAFTP SSRQQDLVST VNVVYSQTTQ 750
    PVYNGETPLQ PSYSSEVFPL VTPLLLDNQI LNTTPAASSS DSALHATPVF 800
    PSVDVSFESI LSSYDGAPLL PFSSASFSSE LFRHLHTVSQ ILPQVTSATE 850
    SDKVPLHASL PVAGGDLLLE PSLAQYSDVL STTHAASETL EFGSESGVLY 900
    KTLMFSQVEP PSSDAMMHAR SSGPEPSYAL SDNEGSQHIF TVSYSSAIPV 950
    HDSVGVTYQG SLFSGPSHIP IPKSSLITPT ASLLQPTHAL SGDGEWSGAS 1000
    SDSEFLLPDT DGLTALNISS PVSVAEFTYT TSVFGDDNKA LSKSEIIYGN 1050
    ETELQIPSFN EMVYPSESTV MPNMYDNVNK LNASLQETSV SISSTKGMFP 1100
    GSLAHTTTKV FDHEISQVPE NNFSVQPTHT VSQASGDTSL KPVLSANSEP 1150
    ASSDPASSEM LSPSTQLLFY ETSASFSTEV LLQPSFQASD VDTLLKTVLP 1200
    AVPSDPILVE TPKVDKISST MLHLIVSNSA SSENMLHSTS VPVFDVSPTS 1250
    HMHSASLQGL TISYASEKYE PVLLKSESSH QVVPSLYSND ELFQTANLEI 1300
    NQAHPPKGRH VFATPVLSID EPLNTLINKL IHSDEILTST KSSVTGKVFA 1350
    GIPTVASDTF VSTDHSVPIG NGHVAITAVS PHRDGSVTST KLLFPSKATS 1400
    ELSHSAKSDA GLVGGGEDGD TDDDGDDDDD DRGSDGLSIH KCMSCSSYRE 1450
    SQEKVMNDSD THENSLMDQN NPISYSLSEN SEEDNRVTSV SSDSQTGMDR 1500
    SPGKSPSANG LSQKHNDGKE ENDIQTGSAL LPLSPESKAW AVLTSDEESG 1550
    SGQGTSDSLN ENETSTDFSF ADTNEKDADG ILAAGDSEIT PGFPQSPTSS 1600
    VTSENSEVFH VSEAEASNSS HESRIGLAEG LESEKKAVIP LVIVSALTFI 1650
    CLVVLVGILI YWRKCFQTAH FYLEDSTSPR VISTPPTPIF PISDDVGAIP 1700
    IKHFPKHVAD LHASSGFTEE FETLKEFYQE VQSCTVDLGI TADSSNHPDN 1750
    KHKNRYINIV AYDHSRVKLA QLAEKDGKLT DYINANYVDG YNRPKAYIAA 1800
    QGPLKSTAED FWRMIWEHNV EVIVMITNLV EKGRRKCDQY WPADGSEEYG 1850
    NFLVTQKSVQ VLAYYTVRNF TLRNTKIKKG SQKGRPSGRV VTQYHYTQWP 1900
    DMGVPEYSLP VLTFVRKAAY AKRHAVGPVV VHCSAGVGRT GTYIVLDSML 1950
    QQIQHEGTVN IFGFLKHIRS QRNYLVQTEE QYVFIHDTLV EAILSKETEV 2000
    LDSHIHAYVN ALLIPGPAGK TKLEKQFQLL SQSNIQQSDY SAALKQCNRE 2050
    KNRTSSIIPV ERSRVGISSL SGEGTDYINA SYIMGYYQSN EFIITQHPLL 2100
    HTIKDFWRMI WDHNAQLVVM IPDGQNMAED EFVYWPNKDE PINCESFKVT 2150
    LMAEEHKCLS NEEKLIIQDF ILEATQDDYV LEVRHFQCPK WPNPDSPISK 2200
    TFELISVIKE EAANRDGPMI VHDEHGGVTA GTFCALTTLM HQLEKENSVD 2250
    VYQVAKMINL MRPGVFADIE QYQFLYKVIL SLVSTRQEEN PSTSLDSNGA 2300
    ALPDGNIAES LESLV 2315
    Length:2,315
    Mass (Da):254,587
    Last modified:March 24, 2009 - v4
    Checksum:iED9DD98D4CCA2883
    GO
    Isoform 2 (identifier: P23471-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1723-1729: Missing.

    Show »
    Length:2,308
    Mass (Da):253,677
    Checksum:iB18D669E478E9239
    GO
    Isoform 3 (identifier: P23471-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         755-1614: Missing.
         1723-1729: Missing.

    Show »
    Length:1,448
    Mass (Da):162,663
    Checksum:i07434438564290C4
    GO

    Sequence cautioni

    The sequence AAC39934.1 differs from that shown. Reason: Contaminating sequence. The N-terminus may be contaminated with vector sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti310 – 3101V → A in AAC39934. (PubMed:9653645)Curated
    Sequence conflicti312 – 3121S → R in AAC39934. (PubMed:9653645)Curated
    Sequence conflicti1426 – 14261Missing in AAA60225. (PubMed:1323835)Curated
    Sequence conflicti1426 – 14261Missing(PubMed:8387522)Curated
    Sequence conflicti1426 – 14261Missing in EAL24344. (PubMed:12690205)Curated
    Sequence conflicti1426 – 14261Missing in EAW83561. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31I → S.
    Corresponds to variant rs740965 [ dbSNP | Ensembl ].
    VAR_038942
    Natural varianti6 – 61R → L.
    Corresponds to variant rs11980387 [ dbSNP | Ensembl ].
    VAR_038943
    Natural varianti1433 – 14331G → D.3 Publications
    Corresponds to variant rs1147504 [ dbSNP | Ensembl ].
    VAR_038944

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei755 – 1614860Missing in isoform 3. 1 PublicationVSP_054061Add
    BLAST
    Alternative sequencei1723 – 17297Missing in isoform 2 and isoform 3. 1 PublicationVSP_054062

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93426 mRNA. Translation: AAA60225.1.
    AC006020 Genomic DNA. Translation: AAF03527.1.
    AC006353 Genomic DNA. No translation available.
    AC073095 Genomic DNA. No translation available.
    CH236947 Genomic DNA. Translation: EAL24344.1.
    CH471070 Genomic DNA. Translation: EAW83561.1.
    U88967 mRNA. Translation: AAC39934.1. Sequence problems.
    X54135 mRNA. Translation: CAA38070.1.
    CCDSiCCDS34740.1. [P23471-1]
    CCDS56505.1. [P23471-3]
    PIRiA46151.
    RefSeqiNP_001193767.1. NM_001206838.1.
    NP_001193768.1. NM_001206839.1. [P23471-3]
    NP_002842.2. NM_002851.2. [P23471-1]
    XP_005250576.1. XM_005250519.1. [P23471-2]
    UniGeneiHs.489824.

    Genome annotation databases

    EnsembliENST00000393386; ENSP00000377047; ENSG00000106278. [P23471-1]
    ENST00000449182; ENSP00000410000; ENSG00000106278. [P23471-3]
    GeneIDi5803.
    KEGGihsa:5803.
    UCSCiuc003vjy.3. human. [P23471-1]

    Polymorphism databases

    DMDMi229485537.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93426 mRNA. Translation: AAA60225.1 .
    AC006020 Genomic DNA. Translation: AAF03527.1 .
    AC006353 Genomic DNA. No translation available.
    AC073095 Genomic DNA. No translation available.
    CH236947 Genomic DNA. Translation: EAL24344.1 .
    CH471070 Genomic DNA. Translation: EAW83561.1 .
    U88967 mRNA. Translation: AAC39934.1 . Sequence problems.
    X54135 mRNA. Translation: CAA38070.1 .
    CCDSi CCDS34740.1. [P23471-1 ]
    CCDS56505.1. [P23471-3 ]
    PIRi A46151.
    RefSeqi NP_001193767.1. NM_001206838.1.
    NP_001193768.1. NM_001206839.1. [P23471-3 ]
    NP_002842.2. NM_002851.2. [P23471-1 ]
    XP_005250576.1. XM_005250519.1. [P23471-2 ]
    UniGenei Hs.489824.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3JXF X-ray 2.00 A/B 34-302 [» ]
    3S97 X-ray 2.30 A/B 34-302 [» ]
    ProteinModelPortali P23471.
    SMRi P23471. Positions 34-301, 313-409, 1698-2284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111767. 8 interactions.
    DIPi DIP-42063N.
    IntActi P23471. 9 interactions.
    MINTi MINT-1350337.
    STRINGi 9606.ENSP00000377047.

    PTM databases

    PhosphoSitei P23471.

    Polymorphism databases

    DMDMi 229485537.

    Proteomic databases

    PaxDbi P23471.
    PRIDEi P23471.

    Protocols and materials databases

    DNASUi 5803.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393386 ; ENSP00000377047 ; ENSG00000106278 . [P23471-1 ]
    ENST00000449182 ; ENSP00000410000 ; ENSG00000106278 . [P23471-3 ]
    GeneIDi 5803.
    KEGGi hsa:5803.
    UCSCi uc003vjy.3. human. [P23471-1 ]

    Organism-specific databases

    CTDi 5803.
    GeneCardsi GC07P121513.
    HGNCi HGNC:9685. PTPRZ1.
    HPAi CAB025106.
    HPA015103.
    MIMi 176891. gene.
    604008. gene.
    neXtProti NX_P23471.
    PharmGKBi PA34029.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000090262.
    HOVERGENi HBG053760.
    InParanoidi P23471.
    KOi K08114.
    OMAi VMNDSDT.
    OrthoDBi EOG7K6PT4.
    PhylomeDBi P23471.
    TreeFami TF351978.

    Enzyme and pathway databases

    SignaLinki P23471.

    Miscellaneous databases

    ChiTaRSi PTPRZ1. human.
    EvolutionaryTracei P23471.
    GeneWikii PTPRZ1.
    GenomeRNAii 5803.
    NextBioi 22622.
    PROi P23471.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23471.
    Bgeei P23471.
    CleanExi HS_PTPRZ1.
    Genevestigatori P23471.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.10.200.10. 1 hit.
    3.90.190.10. 2 hits.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00194. Carb_anhydrase. 1 hit.
    PF00041. fn3. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    SM00060. FN3. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF51069. SSF51069. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEi PS51144. ALPHA_CA_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases."
      Krueger N.X., Saito H.
      Proc. Natl. Acad. Sci. U.S.A. 89:7417-7421(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-1433.
      Tissue: Brain.
    2. "The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system."
      Levy J.B., Canoll P.D., Silvennoinen O., Barnea G., Morse B., Honegger A.M., Huang J.-T., Cannizzaro L.A., Park S.-H., Druck T., Huebner K., Sap J., Ehrlich M., Musacchio J.M., Schlessinger J.
      J. Biol. Chem. 268:10573-10581(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
      Tissue: Brain stem.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-1433.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-1433.
    6. "Molecular cloning and expression analysis of five novel genes in chromosome 1p36."
      Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.
      Genomics 50:187-198(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-999 (ISOFORM 1), TISSUE SPECIFICITY.
    7. "Structural diversity and evolution of human receptor-like protein tyrosine phosphatases."
      Krueger N.X., Streuli M., Saito H.
      EMBO J. 9:3241-3252(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1480-2092 (ISOFORM 1).
      Tissue: Liver.
    8. "Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain."
      Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M., Ricca G., Jaye M., Schlessinger J.
      Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1750-1991 AND 2048-2281 (ISOFORM 1).
      Tissue: Brain stem.
    9. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
      Tissue: Plasma.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2055, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules."
      Bouyain S., Watkins D.J.
      Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-302, INTERACTION WITH CNTN1, DISULFIDE BONDS.

    Entry informationi

    Entry nameiPTPRZ_HUMAN
    AccessioniPrimary (citable) accession number: P23471
    Secondary accession number(s): A4D0W5
    , C9JFM0, O76043, Q9UDR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 165 of the entry and version 4 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

    Was termed (PubMed:8387522 and PubMed:2170109) RPTPase beta.Curated
    The human genome was initially thought to contain 2 genes for PTPRZ: PTPRZ1 (on chr 7) and PTPRZ2 (on chr 1). However, PTPRZ2 probably does not exist and corresponds to PTPRZ1.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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