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P18433

- PTPRA_HUMAN

UniProt

P18433 - PTPRA_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase alpha

Gene

PTPRA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei410 – 4101SubstrateBy similarity
    Active sitei442 – 4421Phosphocysteine intermediateBy similarity
    Binding sitei486 – 4861SubstrateBy similarity
    Active sitei732 – 7321Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. insulin receptor signaling pathway Source: Ensembl
    3. peptidyl-tyrosine dephosphorylation Source: GOC
    4. protein phosphorylation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_18334. NCAM signaling for neurite out-growth.
    SignaLinkiP18433.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase alpha (EC:3.1.3.48)
    Short name:
    Protein-tyrosine phosphatase alpha
    Short name:
    R-PTP-alpha
    Gene namesi
    Name:PTPRA
    Synonyms:PTPA, PTPRL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:9664. PTPRA.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome
    4. receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34009.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 802783Receptor-type tyrosine-protein phosphatase alphaPRO_0000025433Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi21 – 211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
    Modified residuei211 – 2111PhosphoserineBy similarity
    Modified residuei213 – 2131PhosphoserineBy similarity
    Modified residuei798 – 7981Phosphotyrosine2 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP18433.
    PaxDbiP18433.
    PRIDEiP18433.

    PTM databases

    PhosphoSiteiP18433.

    Expressioni

    Gene expression databases

    ArrayExpressiP18433.
    BgeeiP18433.
    CleanExiHS_PTPRA.
    GenevestigatoriP18433.

    Organism-specific databases

    HPAiHPA029412.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CNTN1P147813EBI-2609645,EBI-2123196From a different organism.
    FynP396882EBI-2609645,EBI-524514From a different organism.
    GRB2P629938EBI-2609645,EBI-401755
    SRCP005234EBI-2609645,EBI-848039From a different organism.
    SRCP129314EBI-2609645,EBI-621482

    Protein-protein interaction databases

    BioGridi111750. 8 interactions.
    IntActiP18433. 9 interactions.
    MINTiMINT-138874.
    STRINGi9606.ENSP00000369756.

    Structurei

    3D structure databases

    ProteinModelPortaliP18433.
    SMRiP18433. Positions 217-794.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 142123ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini166 – 802637CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei143 – 16523HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini241 – 501261Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini533 – 791259Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni442 – 4487Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000231464.
    HOVERGENiHBG053758.
    InParanoidiP18433.
    KOiK18032.
    OrthoDBiEOG7B31M8.
    PhylomeDBiP18433.
    TreeFamiTF351829.

    Family and domain databases

    Gene3Di3.90.190.10. 2 hits.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    IPR016336. Tyr_Pase_rcpt_a/e-type.
    IPR027262. Tyr_Pase_rcpt_alpha.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PIRSFiPIRSF500808. PTPR_alpha. 1 hit.
    PIRSF002006. PTPR_alpha_epsilon. 1 hit.
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 2 hits.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P18433-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MDSWFILVLL GSGLICVSAN NATTVAPSVG ITRLINSSTA EPVKEEAKTS    50
    NPTSSLTSLS VAPTFSPNIT LGPTYLTTVN SSDSDNGTTR TASTNSIGIT 100
    ISPNGTWLPD NQFTDARTEP WEGNSSTAAT TPETFPPSDE TPIIAVMVAL 150
    SSLLVIVFII IVLYMLRFKK YKQAGSHSNS KQAGSHSNSF RLSNGRTEDV 200
    EPQSVPLLAR SPSTNRKYPP LPVDKLEEEI NRRMADDNKL FREEFNALPA 250
    CPIQATCEAA SKEENKEKNR YVNILPYDHS RVHLTPVEGV PDSDYINASF 300
    INGYQEKNKF IAAQGPKEET VNDFWRMIWE QNTATIVMVT NLKERKECKC 350
    AQYWPDQGCW TYGNIRVSVE DVTVLVDYTV RKFCIQQVGD MTNRKPQRLI 400
    TQFHFTSWPD FGVPFTPIGM LKFLKKVKAC NPQYAGAIVV HCSAGVGRTG 450
    TFVVIDAMLD MMHTERKVDV YGFVSRIRAQ RCQMVQTDMQ YVFIYQALLE 500
    HYLYGDTELE VTSLETHLQK IYNKIPGTSN NGLEEEFKKL TSIKIQNDKM 550
    RTGNLPANMK KNRVLQIIPY EFNRVIIPVK RGEENTDYVN ASFIDGYRQK 600
    DSYIASQGPL LHTIEDFWRM IWEWKSCSIV MLTELEERGQ EKCAQYWPSD 650
    GLVSYGDITV ELKKEEECES YTVRDLLVTN TRENKSRQIR QFHFHGWPEV 700
    GIPSDGKGMI SIIAAVQKQQ QQSGNHPITV HCSAGAGRTG TFCALSTVLE 750
    RVKAEGILDV FQTVKSLRLQ RPHMVQTLEQ YEFCYKVVQE YIDAFSDYAN 800
    FK 802
    Length:802
    Mass (Da):90,600
    Last modified:November 1, 1991 - v2
    Checksum:i8E964C3B56B5BE32
    GO
    Isoform 2 (identifier: P18433-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         139-147: Missing.

    Show »
    Length:793
    Mass (Da):89,630
    Checksum:iF49533B2022536E0
    GO
    Isoform 3 (identifier: P18433-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-138: S → SGNSDSKDRR
         179-187: Missing.

    Show »
    Length:802
    Mass (Da):90,719
    Checksum:iD1E6A5E86FE4D3F0
    GO
    Isoform 4 (identifier: P18433-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         179-187: Missing.

    Show »
    Length:793
    Mass (Da):89,703
    Checksum:i487CCC1C06F6E860
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141T → M in CAA38662. (PubMed:2175890)Curated
    Sequence conflicti122 – 1221E → P in CAA37447. (PubMed:2172030)Curated
    Sequence conflicti289 – 2891G → E in CAA38662. (PubMed:2175890)Curated
    Sequence conflicti367 – 3671V → A in CAA38662. (PubMed:2175890)Curated
    Sequence conflicti493 – 4931F → S in CAA38662. (PubMed:2175890)Curated
    Sequence conflicti786 – 7861K → E in CAA38662. (PubMed:2175890)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti109 – 1091P → L.
    Corresponds to variant rs1178027 [ dbSNP | Ensembl ].
    VAR_057134

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei138 – 1381S → SGNSDSKDRR in isoform 3. 1 PublicationVSP_007776
    Alternative sequencei139 – 1479Missing in isoform 2. CuratedVSP_005145
    Alternative sequencei179 – 1879Missing in isoform 3 and isoform 4. 7 PublicationsVSP_007777

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34668 mRNA. Translation: AAA36528.1.
    X54130 mRNA. Translation: CAA38065.1.
    X54890 mRNA. Translation: CAA38662.1.
    X53364 mRNA. Translation: CAA37447.1.
    AK290233 mRNA. Translation: BAF82922.1.
    BX571753 mRNA. Translation: CAE11878.1.
    AL121905 Genomic DNA. Translation: CAC10336.1.
    AL121905 Genomic DNA. Translation: CAC10337.1.
    CH471133 Genomic DNA. Translation: EAX10562.1.
    CH471133 Genomic DNA. Translation: EAX10563.1.
    BC027308 mRNA. Translation: AAH27308.1.
    CCDSiCCDS13038.1. [P18433-3]
    CCDS13039.1. [P18433-4]
    PIRiA36065.
    RefSeqiNP_002827.1. NM_002836.3. [P18433-3]
    NP_543030.1. NM_080840.2. [P18433-4]
    NP_543031.1. NM_080841.2. [P18433-4]
    UniGeneiHs.269577.

    Genome annotation databases

    EnsembliENST00000216877; ENSP00000216877; ENSG00000132670. [P18433-4]
    ENST00000318266; ENSP00000314568; ENSG00000132670. [P18433-4]
    ENST00000356147; ENSP00000348468; ENSG00000132670. [P18433-4]
    ENST00000380393; ENSP00000369756; ENSG00000132670. [P18433-3]
    ENST00000399903; ENSP00000382787; ENSG00000132670. [P18433-3]
    GeneIDi5786.
    KEGGihsa:5786.
    UCSCiuc002whj.3. human. [P18433-3]
    uc002whk.3. human. [P18433-4]
    uc002whm.3. human. [P18433-1]

    Polymorphism databases

    DMDMi126467.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34668 mRNA. Translation: AAA36528.1 .
    X54130 mRNA. Translation: CAA38065.1 .
    X54890 mRNA. Translation: CAA38662.1 .
    X53364 mRNA. Translation: CAA37447.1 .
    AK290233 mRNA. Translation: BAF82922.1 .
    BX571753 mRNA. Translation: CAE11878.1 .
    AL121905 Genomic DNA. Translation: CAC10336.1 .
    AL121905 Genomic DNA. Translation: CAC10337.1 .
    CH471133 Genomic DNA. Translation: EAX10562.1 .
    CH471133 Genomic DNA. Translation: EAX10563.1 .
    BC027308 mRNA. Translation: AAH27308.1 .
    CCDSi CCDS13038.1. [P18433-3 ]
    CCDS13039.1. [P18433-4 ]
    PIRi A36065.
    RefSeqi NP_002827.1. NM_002836.3. [P18433-3 ]
    NP_543030.1. NM_080840.2. [P18433-4 ]
    NP_543031.1. NM_080841.2. [P18433-4 ]
    UniGenei Hs.269577.

    3D structure databases

    ProteinModelPortali P18433.
    SMRi P18433. Positions 217-794.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111750. 8 interactions.
    IntActi P18433. 9 interactions.
    MINTi MINT-138874.
    STRINGi 9606.ENSP00000369756.

    Chemistry

    BindingDBi P18433.
    ChEMBLi CHEMBL3918.

    PTM databases

    PhosphoSitei P18433.

    Polymorphism databases

    DMDMi 126467.

    Proteomic databases

    MaxQBi P18433.
    PaxDbi P18433.
    PRIDEi P18433.

    Protocols and materials databases

    DNASUi 5786.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216877 ; ENSP00000216877 ; ENSG00000132670 . [P18433-4 ]
    ENST00000318266 ; ENSP00000314568 ; ENSG00000132670 . [P18433-4 ]
    ENST00000356147 ; ENSP00000348468 ; ENSG00000132670 . [P18433-4 ]
    ENST00000380393 ; ENSP00000369756 ; ENSG00000132670 . [P18433-3 ]
    ENST00000399903 ; ENSP00000382787 ; ENSG00000132670 . [P18433-3 ]
    GeneIDi 5786.
    KEGGi hsa:5786.
    UCSCi uc002whj.3. human. [P18433-3 ]
    uc002whk.3. human. [P18433-4 ]
    uc002whm.3. human. [P18433-1 ]

    Organism-specific databases

    CTDi 5786.
    GeneCardsi GC20P002844.
    HGNCi HGNC:9664. PTPRA.
    HPAi HPA029412.
    MIMi 176884. gene.
    neXtProti NX_P18433.
    PharmGKBi PA34009.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000231464.
    HOVERGENi HBG053758.
    InParanoidi P18433.
    KOi K18032.
    OrthoDBi EOG7B31M8.
    PhylomeDBi P18433.
    TreeFami TF351829.

    Enzyme and pathway databases

    Reactomei REACT_18334. NCAM signaling for neurite out-growth.
    SignaLinki P18433.

    Miscellaneous databases

    ChiTaRSi PTPRA. human.
    GeneWikii PTPRA.
    GenomeRNAii 5786.
    NextBioi 22506.
    PROi P18433.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18433.
    Bgeei P18433.
    CleanExi HS_PTPRA.
    Genevestigatori P18433.

    Family and domain databases

    Gene3Di 3.90.190.10. 2 hits.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    IPR016336. Tyr_Pase_rcpt_a/e-type.
    IPR027262. Tyr_Pase_rcpt_alpha.
    [Graphical view ]
    Pfami PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF500808. PTPR_alpha. 1 hit.
    PIRSF002006. PTPR_alpha_epsilon. 1 hit.
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 2 hits.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a widely expressed receptor tyrosine phosphatase."
      Sap J., D'Eustachio P., Givol D., Schlessinger J.
      Proc. Natl. Acad. Sci. U.S.A. 87:6112-6116(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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] (ISOFORM 3).
    3. "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] (ISOFORM 4).
    4. "Sequence of a cDNA encoding human LRP (leukocyte common antigen-related peptide)."
      Ohagi S., Nishi M., Steiner D.F.
      Nucleic Acids Res. 18:7159-7159(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      Tissue: Kidney.
    5. "Cloning and chromosomal assignment of a widely expressed human receptor-like protein-tyrosine phosphatase."
      Jirik F.R., Janzen N.M., Melhado I.G., Harder K.W.
      FEBS Lett. 273:239-242(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    6. "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 4).
      Tissue: Thalamus.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Lymph node.
    8. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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 4).
      Tissue: Skin.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 TYR-798, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-798, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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].

    Entry informationi

    Entry nameiPTPRA_HUMAN
    AccessioniPrimary (citable) accession number: P18433
    Secondary accession number(s): A8K2G8
    , D3DVX5, Q14513, Q7Z2I2, Q96TD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 163 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3