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O75365

- TP4A3_HUMAN

UniProt

O75365 - TP4A3_HUMAN

Protein

Protein tyrosine phosphatase type IVA 3

Gene

PTP4A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (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. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II.2 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Enzyme regulationi

    Inhibited by sodium orthovanadate and peroxovanadium compounds, and by pentamidine.2 Publications

    Sites

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

    GO - Molecular functioni

    1. prenylated protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. peptidyl-tyrosine dephosphorylation Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein tyrosine phosphatase type IVA 3 (EC:3.1.3.48)
    Alternative name(s):
    PRL-R
    Protein-tyrosine phosphatase 4a3
    Protein-tyrosine phosphatase of regenerating liver 3
    Short name:
    PRL-3
    Gene namesi
    Name:PTP4A3
    Synonyms:PRL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:9636. PTP4A3.

    Subcellular locationi

    Cell membrane 1 Publication. Early endosome 1 Publication

    GO - Cellular componenti

    1. early endosome Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi49 – 491C → A: No effect on enzymatic activity. 1 Publication
    Mutagenesisi71 – 711D → A: No effect on enzymatic activity. 1 Publication
    Mutagenesisi72 – 721D → A: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi104 – 1041C → A or S: 95% loss of enzymatic activity. 2 Publications
    Mutagenesisi104 – 1041C → S: Reduces migration-promoting activity. 2 Publications
    Mutagenesisi111 – 1111A → S: Enhances catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33979.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 170170Protein tyrosine phosphatase type IVA 3PRO_0000094788Add
    BLAST
    Propeptidei171 – 1733Removed in mature formBy similarityPRO_0000396735

    Amino acid modifications

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

    Post-translational modificationi

    Farnesylated. Farnesylation is required for membrane targeting By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiO75365.
    PaxDbiO75365.
    PRIDEiO75365.

    PTM databases

    PhosphoSiteiO75365.

    Expressioni

    Tissue specificityi

    Mainly expressed in cardiomyocytes and skeletal muscle; also found in pancreas. Consistently overexpressed in colon cancer metastasis.1 Publication

    Gene expression databases

    ArrayExpressiO75365.
    BgeeiO75365.
    CleanExiHS_PTP4A3.
    GenevestigatoriO75365.

    Organism-specific databases

    HPAiHPA003281.

    Interactioni

    Subunit structurei

    Interacts with tubulin.1 Publication

    Protein-protein interaction databases

    BioGridi116327. 37 interactions.
    IntActiO75365. 4 interactions.
    STRINGi9606.ENSP00000332274.

    Structurei

    Secondary structure

    1
    173
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 145
    Beta strandi17 – 226
    Beta strandi23 – 264
    Turni27 – 293
    Helixi30 – 4011
    Beta strandi45 – 495
    Helixi55 – 617
    Beta strandi65 – 684
    Beta strandi69 – 713
    Helixi79 – 9416
    Beta strandi99 – 1035
    Beta strandi107 – 1104
    Helixi111 – 1199
    Helixi120 – 1223
    Helixi125 – 13511
    Beta strandi137 – 1393
    Helixi144 – 1529
    Turni156 – 1583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R6HNMR-A1-169[»]
    1V3ANMR-A1-173[»]
    2MBCNMR-A1-162[»]
    DisProtiDP00254.
    ProteinModelPortaliO75365.
    SMRiO75365. Positions 1-169.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75365.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG265664.
    HOGENOMiHOG000231265.
    HOVERGENiHBG071295.
    InParanoidiO75365.
    KOiK18041.
    OMAiKAKFCDD.
    OrthoDBiEOG7C8GJD.
    PhylomeDBiO75365.
    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]

    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

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: O75365-1) [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

    MARMNRPAPV EVSYKHMRFL ITHNPTNATL STFIEDLKKY GATTVVRVCE    50
    VTYDKTPLEK DGITVVDWPF DDGAPPPGKV VEDWLSLVKA KFCEAPGSCV 100
    AVHCVAGLGR APVLVALALI ESGMKYEDAI QFIRQKRRGA INSKQLTYLE 150
    KYRPKQRLRF KDPHTHKTRC CVM 173
    Length:173
    Mass (Da):19,535
    Last modified:July 5, 2005 - v2
    Checksum:i15DF01999A9A3573
    GO
    Isoform 2 (identifier: O75365-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         111-135: Missing.

    Note: Unstructured and inactive.

    Show »
    Length:148
    Mass (Da):16,777
    Checksum:iE9B7DB82575DF7CD
    GO
    Isoform 3 (identifier: O75365-3) [UniParc]FASTAAdd to Basket

    Also known as: short

    The sequence of this isoform differs from the canonical sequence as follows:
         39-124: Missing.

    Show »
    Length:87
    Mass (Da):10,494
    Checksum:iDE4A4D64102DC8CF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401A → R in AAC29314. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei39 – 12486Missing in isoform 3. 1 PublicationVSP_014406Add
    BLAST
    Alternative sequencei111 – 13525Missing in isoform 2. 2 PublicationsVSP_014407Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF041434 mRNA. Translation: AAC29314.1.
    AJ276554 mRNA. Translation: CAC81757.1.
    BT007303 mRNA. Translation: AAP35967.1.
    BC003105 mRNA. Translation: AAH03105.1.
    U87168 mRNA. Translation: AAB47560.1.
    CCDSiCCDS6382.1. [O75365-2]
    CCDS6383.1. [O75365-1]
    RefSeqiNP_009010.2. NM_007079.3. [O75365-2]
    NP_116000.1. NM_032611.2. [O75365-1]
    XP_005250819.1. XM_005250762.2. [O75365-1]
    XP_005250820.1. XM_005250763.1. [O75365-1]
    XP_005250821.1. XM_005250764.1. [O75365-1]
    XP_005250824.1. XM_005250767.2. [O75365-2]
    XP_006716562.1. XM_006716499.1. [O75365-1]
    XP_006725163.1. XM_006725100.1. [O75365-1]
    XP_006725164.1. XM_006725101.1. [O75365-1]
    XP_006725165.1. XM_006725102.1. [O75365-1]
    XP_006725166.1. XM_006725103.1. [O75365-1]
    UniGeneiHs.43666.
    Hs.744870.

    Genome annotation databases

    EnsembliENST00000329397; ENSP00000332274; ENSG00000184489. [O75365-1]
    ENST00000349124; ENSP00000331730; ENSG00000184489. [O75365-2]
    ENST00000520105; ENSP00000428758; ENSG00000184489. [O75365-2]
    ENST00000521578; ENSP00000428976; ENSG00000184489. [O75365-1]
    GeneIDi11156.
    KEGGihsa:11156.
    UCSCiuc003ywg.1. human. [O75365-1]
    uc003ywh.1. human. [O75365-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF041434 mRNA. Translation: AAC29314.1 .
    AJ276554 mRNA. Translation: CAC81757.1 .
    BT007303 mRNA. Translation: AAP35967.1 .
    BC003105 mRNA. Translation: AAH03105.1 .
    U87168 mRNA. Translation: AAB47560.1 .
    CCDSi CCDS6382.1. [O75365-2 ]
    CCDS6383.1. [O75365-1 ]
    RefSeqi NP_009010.2. NM_007079.3. [O75365-2 ]
    NP_116000.1. NM_032611.2. [O75365-1 ]
    XP_005250819.1. XM_005250762.2. [O75365-1 ]
    XP_005250820.1. XM_005250763.1. [O75365-1 ]
    XP_005250821.1. XM_005250764.1. [O75365-1 ]
    XP_005250824.1. XM_005250767.2. [O75365-2 ]
    XP_006716562.1. XM_006716499.1. [O75365-1 ]
    XP_006725163.1. XM_006725100.1. [O75365-1 ]
    XP_006725164.1. XM_006725101.1. [O75365-1 ]
    XP_006725165.1. XM_006725102.1. [O75365-1 ]
    XP_006725166.1. XM_006725103.1. [O75365-1 ]
    UniGenei Hs.43666.
    Hs.744870.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R6H NMR - A 1-169 [» ]
    1V3A NMR - A 1-173 [» ]
    2MBC NMR - A 1-162 [» ]
    DisProti DP00254.
    ProteinModelPortali O75365.
    SMRi O75365. Positions 1-169.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116327. 37 interactions.
    IntActi O75365. 4 interactions.
    STRINGi 9606.ENSP00000332274.

    Chemistry

    BindingDBi O75365.
    ChEMBLi CHEMBL4162.

    PTM databases

    PhosphoSitei O75365.

    Proteomic databases

    MaxQBi O75365.
    PaxDbi O75365.
    PRIDEi O75365.

    Protocols and materials databases

    DNASUi 11156.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329397 ; ENSP00000332274 ; ENSG00000184489 . [O75365-1 ]
    ENST00000349124 ; ENSP00000331730 ; ENSG00000184489 . [O75365-2 ]
    ENST00000520105 ; ENSP00000428758 ; ENSG00000184489 . [O75365-2 ]
    ENST00000521578 ; ENSP00000428976 ; ENSG00000184489 . [O75365-1 ]
    GeneIDi 11156.
    KEGGi hsa:11156.
    UCSCi uc003ywg.1. human. [O75365-1 ]
    uc003ywh.1. human. [O75365-2 ]

    Organism-specific databases

    CTDi 11156.
    GeneCardsi GC08P142432.
    HGNCi HGNC:9636. PTP4A3.
    HPAi HPA003281.
    MIMi 606449. gene.
    neXtProti NX_O75365.
    PharmGKBi PA33979.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265664.
    HOGENOMi HOG000231265.
    HOVERGENi HBG071295.
    InParanoidi O75365.
    KOi K18041.
    OMAi KAKFCDD.
    OrthoDBi EOG7C8GJD.
    PhylomeDBi O75365.
    TreeFami TF313384.

    Miscellaneous databases

    EvolutionaryTracei O75365.
    GeneWikii PTP4A3.
    GenomeRNAii 11156.
    NextBioi 42423.
    PROi O75365.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75365.
    Bgeei O75365.
    CleanExi HS_PTP4A3.
    Genevestigatori O75365.

    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. Zeng Q., Tan Y.H., Hong W.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Full-length of some muscular transcripts, Telethon (Italy) project B41."
      Ievolella C., Stanchi F., Pacchioni B., Silvia T., Frigimelica E., Scannapieco P., Corso V., Biasio B., Lanfranchi G.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Skeletal muscle.
    3. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Eye.
    5. "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 93-148 (ISOFORM 1).
      Tissue: Lung fibroblast.
    6. Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF CYS-104, ENZYME REGULATION, FUNCTION.
    7. Cited for: OVEREXPRESSION IN COLON CANCER.
    8. "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: INTERACTION WITH TUBULIN.
    9. "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.
    10. "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, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-104.
    11. "Structure of human PRL-3, the phosphatase associated with cancer metastasis."
      Kim K.-A., Song J.-S., Jee J., Sheen M.R., Lee C., Lee T.G., Ro S., Cho J.M., Lee W., Yamazaki T., Jeon Y.H., Cheong C.
      FEBS Lett. 565:181-187(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-173 (ISOFORM 1).
    12. "Structural insights into molecular function of the metastasis-associated phosphatase PRL-3."
      Kozlov G., Cheng J., Ziomek E., Banville D., Gehring K., Ekiel I.
      J. Biol. Chem. 279:11882-11889(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-169 (ISOFORM 1), DISULFIDE BOND, ENZYME ACTIVITY (ISOFORMS 1 AND 2), MUTAGENESIS OF CYS-49; ASP-71; ASP-72 AND ALA-111.

    Entry informationi

    Entry nameiTP4A3_HUMAN
    AccessioniPrimary (citable) accession number: O75365
    Secondary accession number(s): Q8IVN5, Q99849, Q9BTW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 119 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 8
      Human chromosome 8: 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