Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O70274

- TP4A2_MOUSE

UniProt

O70274 - TP4A2_MOUSE

Protein

Protein tyrosine phosphatase type IVA 2

Gene

Ptp4a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB By similarity.By similarity

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Enzyme regulationi

    Inhibited by sodium orthovanadate and pentamidine.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691Proton donorBy similarity
    Active sitei101 – 1011Phosphocysteine intermediateBy similarity
    Binding sitei107 – 1071SubstrateBy similarity

    GO - Molecular functioni

    1. protein tyrosine phosphatase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein tyrosine phosphatase type IVA 2 (EC:3.1.3.48)
    Alternative name(s):
    Protein-tyrosine phosphatase 4a2
    Protein-tyrosine phosphatase of regenerating liver 2
    Short name:
    PRL-2
    Gene namesi
    Name:Ptp4a2
    Synonyms:Prl2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1277117. Ptp4a2.

    Subcellular locationi

    Cell membrane 1 Publication. Early endosome 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi164 – 1674Missing: Locates in the nucleus. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 164164Protein tyrosine phosphatase type IVA 2PRO_0000094786Add
    BLAST
    Propeptidei165 – 1673Removed in mature formCuratedPRO_0000396732

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 101By similarity
    Modified residuei164 – 1641Cysteine methyl esterCurated
    Lipidationi164 – 1641S-farnesyl cysteine1 Publication

    Post-translational modificationi

    Farnesylated. Farnesylation is required for membrane targeting and for interaction with RABGGTB By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiO70274.
    PaxDbiO70274.
    PRIDEiO70274.

    PTM databases

    PhosphoSiteiO70274.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle, and at lower levels in liver, lung, heart, kidney, brain, testis and spleen.1 Publication

    Gene expression databases

    ArrayExpressiO70274.
    BgeeiO70274.
    CleanExiMM_PTP4A2.
    GenevestigatoriO70274.

    Interactioni

    Subunit structurei

    In contrast to PTP4A1 and PTP4A3, does not interact with tubulin. Interacts with RABGGTB By similarity.By similarity

    Protein-protein interaction databases

    IntActiO70274. 1 interaction.
    MINTiMINT-4105284.

    Structurei

    3D structure databases

    ProteinModelPortaliO70274.
    SMRiO70274. Positions 6-157.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini79 – 14567Tyrosine-protein phosphataseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni102 – 1076Phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG316886.
    GeneTreeiENSGT00390000009788.
    HOGENOMiHOG000231265.
    HOVERGENiHBG071295.
    InParanoidiO70274.
    KOiK18041.
    OMAiNGHNCCV.
    OrthoDBiEOG7C8GJD.
    PhylomeDBiO70274.
    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.

    O70274-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY    50
    DKAPVEKEGI HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH 100
    CVAGLGRAPV LVALALIECG MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR 150
    PKMRLRFRDT NGHCCVQ 167
    Length:167
    Mass (Da):19,127
    Last modified:August 1, 1998 - v1
    Checksum:iE97B88BF87B87943
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035644 mRNA. Translation: AAC15874.1.
    AK033092 mRNA. Translation: BAC28149.1.
    AK045093 mRNA. Translation: BAC32217.1.
    AK155895 mRNA. Translation: BAE33489.1.
    BC086794 mRNA. Translation: AAH86794.1.
    BC087551 mRNA. Translation: AAH87551.1.
    CCDSiCCDS18704.1.
    PIRiJC5981.
    RefSeqiNP_001158217.1. NM_001164745.1.
    NP_033000.1. NM_008974.4.
    UniGeneiMm.193688.

    Genome annotation databases

    EnsembliENSMUST00000030578; ENSMUSP00000030578; ENSMUSG00000028788.
    ENSMUST00000165853; ENSMUSP00000125901; ENSMUSG00000028788.
    GeneIDi19244.
    KEGGimmu:19244.
    UCSCiuc008uyf.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035644 mRNA. Translation: AAC15874.1 .
    AK033092 mRNA. Translation: BAC28149.1 .
    AK045093 mRNA. Translation: BAC32217.1 .
    AK155895 mRNA. Translation: BAE33489.1 .
    BC086794 mRNA. Translation: AAH86794.1 .
    BC087551 mRNA. Translation: AAH87551.1 .
    CCDSi CCDS18704.1.
    PIRi JC5981.
    RefSeqi NP_001158217.1. NM_001164745.1.
    NP_033000.1. NM_008974.4.
    UniGenei Mm.193688.

    3D structure databases

    ProteinModelPortali O70274.
    SMRi O70274. Positions 6-157.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O70274. 1 interaction.
    MINTi MINT-4105284.

    Chemistry

    BindingDBi O70274.

    PTM databases

    PhosphoSitei O70274.

    Proteomic databases

    MaxQBi O70274.
    PaxDbi O70274.
    PRIDEi O70274.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030578 ; ENSMUSP00000030578 ; ENSMUSG00000028788 .
    ENSMUST00000165853 ; ENSMUSP00000125901 ; ENSMUSG00000028788 .
    GeneIDi 19244.
    KEGGi mmu:19244.
    UCSCi uc008uyf.2. mouse.

    Organism-specific databases

    CTDi 8073.
    MGIi MGI:1277117. Ptp4a2.

    Phylogenomic databases

    eggNOGi NOG316886.
    GeneTreei ENSGT00390000009788.
    HOGENOMi HOG000231265.
    HOVERGENi HBG071295.
    InParanoidi O70274.
    KOi K18041.
    OMAi NGHNCCV.
    OrthoDBi EOG7C8GJD.
    PhylomeDBi O70274.
    TreeFami TF313384.

    Miscellaneous databases

    ChiTaRSi PTP4A2. mouse.
    NextBioi 296062.
    PROi O70274.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O70274.
    Bgeei O70274.
    CleanExi MM_PTP4A2.
    Genevestigatori O70274.

    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. "Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1."
      Zeng Q., Hong W., Tan Y.H.
      Biochem. Biophys. Res. Commun. 244:421-427(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Testis.
    3. "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].
      Strain: C57BL/6.
      Tissue: Brain and Embryo.
    4. "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome."
      Zeng Q., Si X., Horstmann H., Xu Y., Hong W., Pallen C.J.
      J. Biol. Chem. 275:21444-21452(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-164, SUBCELLULAR LOCATION, MUTAGENESIS OF 164-CYS--GLN-167.

    Entry informationi

    Entry nameiTP4A2_MOUSE
    AccessioniPrimary (citable) accession number: O70274
    Secondary accession number(s): Q3U1K7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3