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Q93096

- TP4A1_HUMAN

UniProt

Q93096 - TP4A1_HUMAN

Protein

Protein tyrosine phosphatase type IVA 1

Gene

PTP4A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis.3 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

    Enzyme regulationi

    Inhibited by sodium orthovanadate and pentamidine.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei72 – 721Proton donorCurated
    Active sitei104 – 1041Phosphocysteine intermediate
    Binding sitei110 – 1101Substrate

    GO - Molecular functioni

    1. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. multicellular organismal development Source: UniProtKB-KW
    3. peptidyl-tyrosine dephosphorylation Source: GOC
    4. positive regulation of cell migration Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein tyrosine phosphatase type IVA 1 (EC:3.1.3.48)
    Alternative name(s):
    PTP(CAAXI)
    Protein-tyrosine phosphatase 4a1
    Protein-tyrosine phosphatase of regenerating liver 1
    Short name:
    PRL-1
    Gene namesi
    Name:PTP4A1
    Synonyms:PRL1, PTPCAAX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9634. PTP4A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic side of plasma membrane Source: UniProtKB
    3. early endosome Source: UniProtKB-SubCell
    4. endoplasmic reticulum Source: UniProtKB-SubCell
    5. extracellular vesicular exosome Source: UniProt
    6. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131T → F: Reduces trimerization. 1 Publication
    Mutagenesisi71 – 711D → A: No effect on catalytic activity. 1 Publication
    Mutagenesisi72 – 721D → A: 80% loss of catalytic activity; delay in progression through G2/M. 1 Publication
    Mutagenesisi104 – 1041C → S: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi131 – 1311Q → A: Reduces trimerization. 1 Publication
    Mutagenesisi170 – 1701C → S: Redistributes to the nucleus in resting cells, but still locates to the mitotic spindle in dividing cells. Induces defects in cytokinesis. 1 Publication
    Mutagenesisi171 – 1711C → S: No effect on subcellular location. 1 Publication

    Organism-specific databases

    PharmGKBiPA33977.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 170170Protein tyrosine phosphatase type IVA 1PRO_0000094780Add
    BLAST
    Propeptidei171 – 1733Removed in mature formCuratedPRO_0000396726

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi49 ↔ 1041 Publication
    Modified residuei170 – 1701Cysteine methyl esterCurated
    Lipidationi170 – 1701S-farnesyl cysteine1 Publication

    Post-translational modificationi

    Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus.

    Keywords - PTMi

    Disulfide bond, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiQ93096.
    PaxDbiQ93096.
    PRIDEiQ93096.

    PTM databases

    PhosphoSiteiQ93096.

    Expressioni

    Tissue specificityi

    Expressed in bone marrow, lymph nodes, T lymphocytes, spleen, thymus and tonsil. Overexpressed in tumor cell lines.2 Publications

    Developmental stagei

    Expressed in fetal liver.1 Publication

    Inductioni

    Strongly down-regulated upon tetrodotoxin treatment.1 Publication

    Gene expression databases

    ArrayExpressiQ93096.
    BgeeiQ93096.
    CleanExiHS_PTP4A1.
    GenevestigatoriQ93096.

    Organism-specific databases

    HPAiHPA003281.

    Interactioni

    Subunit structurei

    Homotrimer. Interacts with ATF5 By similarity. Interacts with tubulin.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi113578. 10 interactions.
    IntActiQ93096. 4 interactions.
    MINTiMINT-194351.
    STRINGi9606.ENSP00000359685.

    Structurei

    Secondary structure

    1
    173
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 145
    Beta strandi17 – 215
    Helixi27 – 293
    Helixi30 – 3910
    Beta strandi42 – 476
    Helixi56 – 605
    Beta strandi64 – 674
    Beta strandi72 – 743
    Helixi78 – 9417
    Beta strandi99 – 1035
    Beta strandi105 – 1084
    Turni109 – 1113
    Helixi112 – 12110
    Helixi126 – 1349
    Helixi143 – 1519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RXDX-ray1.90A/B/C2-160[»]
    1XM2X-ray2.70A/B/C/D/E/F1-173[»]
    DisProtiDP00255.
    ProteinModelPortaliQ93096.
    SMRiQ93096. Positions 9-160.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93096.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini82 – 14867Tyrosine-protein phosphataseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 13236Interaction with ATF5By similarityAdd
    BLAST
    Regioni105 – 1106Phosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG265664.
    HOGENOMiHOG000231265.
    HOVERGENiHBG071295.
    InParanoidiQ93096.
    KOiK18041.
    OMAiDKSIAVH.
    OrthoDBiEOG7C8GJD.
    PhylomeDBiQ93096.
    TreeFamiTF313384.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q93096-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE    50
    ATYDTTLVEK EGIHVLDWPF DDGAPPSNQI VDDWLSLVKI KFREEPGCCI 100
    AVHCVAGLGR APVLVALALI EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE 150
    KYRPKMRLRF KDSNGHRNNC CIQ 173
    Length:173
    Mass (Da):19,815
    Last modified:July 5, 2005 - v2
    Checksum:i702008013D3F3835
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48296 mRNA. Translation: AAB40597.1.
    AF051160 Genomic DNA. Translation: AAC39836.1.
    AK312526 mRNA. Translation: BAG35425.1.
    CR749458 mRNA. Translation: CAH18292.1.
    AL135905 Genomic DNA. Translation: CAC12761.1.
    CH471143 Genomic DNA. Translation: EAW88494.1.
    BC023975 mRNA. Translation: AAH23975.1.
    BC045571 mRNA. Translation: AAH45571.1.
    U69701 mRNA. Translation: AAB09080.1.
    CCDSiCCDS4965.1.
    RefSeqiNP_003454.1. NM_003463.4.
    XP_006715626.1. XM_006715563.1.
    UniGeneiHs.227777.
    Hs.706850.

    Genome annotation databases

    EnsembliENST00000370651; ENSP00000359685; ENSG00000112245.
    GeneIDi7803.
    KEGGihsa:7803.
    UCSCiuc003pek.3. human.

    Polymorphism databases

    DMDMi68566217.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48296 mRNA. Translation: AAB40597.1 .
    AF051160 Genomic DNA. Translation: AAC39836.1 .
    AK312526 mRNA. Translation: BAG35425.1 .
    CR749458 mRNA. Translation: CAH18292.1 .
    AL135905 Genomic DNA. Translation: CAC12761.1 .
    CH471143 Genomic DNA. Translation: EAW88494.1 .
    BC023975 mRNA. Translation: AAH23975.1 .
    BC045571 mRNA. Translation: AAH45571.1 .
    U69701 mRNA. Translation: AAB09080.1 .
    CCDSi CCDS4965.1.
    RefSeqi NP_003454.1. NM_003463.4.
    XP_006715626.1. XM_006715563.1.
    UniGenei Hs.227777.
    Hs.706850.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RXD X-ray 1.90 A/B/C 2-160 [» ]
    1XM2 X-ray 2.70 A/B/C/D/E/F 1-173 [» ]
    DisProti DP00255.
    ProteinModelPortali Q93096.
    SMRi Q93096. Positions 9-160.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113578. 10 interactions.
    IntActi Q93096. 4 interactions.
    MINTi MINT-194351.
    STRINGi 9606.ENSP00000359685.

    Chemistry

    BindingDBi Q93096.
    ChEMBLi CHEMBL1075169.

    PTM databases

    PhosphoSitei Q93096.

    Polymorphism databases

    DMDMi 68566217.

    Proteomic databases

    MaxQBi Q93096.
    PaxDbi Q93096.
    PRIDEi Q93096.

    Protocols and materials databases

    DNASUi 7803.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370651 ; ENSP00000359685 ; ENSG00000112245 .
    GeneIDi 7803.
    KEGGi hsa:7803.
    UCSCi uc003pek.3. human.

    Organism-specific databases

    CTDi 7803.
    GeneCardsi GC06P064279.
    HGNCi HGNC:9634. PTP4A1.
    HPAi HPA003281.
    MIMi 601585. gene.
    neXtProti NX_Q93096.
    PharmGKBi PA33977.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265664.
    HOGENOMi HOG000231265.
    HOVERGENi HBG071295.
    InParanoidi Q93096.
    KOi K18041.
    OMAi DKSIAVH.
    OrthoDBi EOG7C8GJD.
    PhylomeDBi Q93096.
    TreeFami TF313384.

    Miscellaneous databases

    EvolutionaryTracei Q93096.
    GeneWikii PTP4A1.
    GenomeRNAii 7803.
    NextBioi 30184.
    PROi Q93096.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q93096.
    Bgeei Q93096.
    CleanExi HS_PTP4A1.
    Genevestigatori Q93096.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases."
      Cates C.A., Michael R.L., Stayrook K.R., Harvey K.A., Burke Y.D., Randall S.K., Crowell P.L., Crowell D.N.
      Cancer Lett. 110:49-55(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, ISOPRENYLATION AT CYS-170.
      Tissue: Mammary carcinoma.
    2. "The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer."
      Peng Y., Genin A., Spinner N.B., Diamond R.H., Taub R.
      J. Biol. Chem. 273:17286-17295(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Regenerating 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: Thalamus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Fetal liver.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 and Testis.
    8. "Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38."
      Dayton M.A., Knobloch T.J.
      Recept. Signal Transduct. 7:241-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-163.
      Tissue: Lung fibroblast.
    9. "Subcellular localization of intracellular protein tyrosine phosphatases in T cells."
      Gjoerloff-Wingren A., Saxena M., Han S., Wang X., Alonso A., Renedo M., Oh P., Williams S., Schnitzer J., Mustelin T.
      Eur. J. Immunol. 30:2412-2421(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    10. "The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis."
      Wang J., Kirby C.E., Herbst R.
      J. Biol. Chem. 277:46659-46668(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-71; ASP-72; CYS-104; CYS-170 AND CYS-171, INTERACTION WITH TUBULIN, FUNCTION.
    11. "Pentamidine is an inhibitor of PRL phosphatases with anticancer activity."
      Pathak M.K., Dhawan D., Lindner D.J., Borden E.C., Farver C., Yi T.
      Mol. Cancer Ther. 1:1255-1264(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    12. "Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases."
      Werner S.R., Lee P.A., DeCamp M.W., Crowell D.N., Randall S.K., Crowell P.L.
      Cancer Lett. 202:201-211(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "PRL-3 and PRL-1 promote cell migration, invasion, and metastasis."
      Zeng Q., Dong J.-M., Guo K., Li J., Tan H.-X., Koh V., Pallen C.J., Manser E., Hong W.
      Cancer Res. 63:2716-2722(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach."
      Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.
      Toxicon 44:597-608(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms."
      Jeong D.G., Kim S.J., Kim J.H., Son J.H., Park M.R., Lim S.M., Yoon T.-S., Ryu S.E.
      J. Mol. Biol. 345:401-413(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF MUTANT SER-104, DISULFIDE BOND, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF THR-13 AND GLN-131, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiTP4A1_HUMAN
    AccessioniPrimary (citable) accession number: Q93096
    Secondary accession number(s): B2R6C8, O00648, Q49A54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 124 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3