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)

Q86TP1

- PRUNE_HUMAN

UniProt

Q86TP1 - PRUNE_HUMAN

Protein

Protein prune homolog

Gene

PRUNE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP, as substrate. Plays a role in cell proliferation, is able to induce cell motility and acts as a negative regulator of NME1.5 Publications

    Catalytic activityi

    Diphosphate + H2O = 2 phosphate.

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Activated by magnesium ions and inhibited by manganese ions. Inhibited by dipyridamole, moderately sensitive to IBMX and inhibited by vinpocetine.1 Publication

    Kineticsi

    1. KM=0.91 µM for cAMP2 Publications
    2. KM=2.3 µM for cGMP2 Publications

    Vmax=12.8 pmol/min/µg enzyme with cAMP as substrate2 Publications

    Vmax=0.8 pmol/min/µg enzyme with cGMP as substrate2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi28 – 281Manganese 1By similarity
    Metal bindingi30 – 301Manganese 2By similarity
    Metal bindingi106 – 1061Manganese 1By similarity
    Metal bindingi106 – 1061Manganese 2By similarity
    Metal bindingi179 – 1791Manganese 2By similarity

    GO - Molecular functioni

    1. inorganic diphosphatase activity Source: UniProtKB-EC
    2. manganese ion binding Source: InterPro
    3. protein binding Source: IntAct

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein prune homolog (EC:3.6.1.1)
    Short name:
    hPrune
    Alternative name(s):
    Drosophila-related expressed sequence 17
    Short name:
    DRES-17
    Short name:
    DRES17
    HTcD37
    Gene namesi
    Name:PRUNE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:13420. PRUNE.

    Subcellular locationi

    Cytoplasm. Nucleus. Cell junctionfocal adhesion
    Note: In some transfected cells a nuclear staining is also observed.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. focal adhesion Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi28 – 281D → A: Partial loss of cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-106. Partial loss of cAMP PDE activity; when associated with D-106 and D-179. 1 Publication
    Mutagenesisi106 – 1061D → A: No change in cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-28. Partial loss of cAMP PDE activity; when associated with D-28 and D-179. 1 Publication
    Mutagenesisi126 – 1294DHRP → AAAA: Partial loss of cAMP PDE activity.
    Mutagenesisi179 – 1791D → A: Partial loss of cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-28 and D-106. 1 Publication

    Organism-specific databases

    PharmGKBiPA134939749.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453Protein prune homologPRO_0000337987Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ86TP1.
    PaxDbiQ86TP1.
    PRIDEiQ86TP1.

    PTM databases

    PhosphoSiteiQ86TP1.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Seems to be overexpressed in aggressive sarcoma subtypes, such as leiomyosarcomas and malignant fibrous histiocytomas (MFH) as well as in the less malignant liposarcomas.3 Publications

    Gene expression databases

    ArrayExpressiQ86TP1.
    BgeeiQ86TP1.
    CleanExiHS_PRUNE.
    GenevestigatoriQ86TP1.

    Organism-specific databases

    HPAiHPA028411.

    Interactioni

    Subunit structurei

    Homooligomer. Able to homodimerize via its C-terminal domain. Interacts with NME1. Interacts with GSK3; at focal adhesion complexes where paxillin and vinculin are colocalized.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NME1P155312EBI-2127112,EBI-741141

    Protein-protein interaction databases

    BioGridi121827. 4 interactions.
    IntActiQ86TP1. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86TP1.
    SMRiQ86TP1. Positions 18-360.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni393 – 42028Essential for homodimerizationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi106 – 1083DHH motif

    Sequence similaritiesi

    Belongs to the PPase class C family. Prune subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG1227.
    HOVERGENiHBG058142.
    InParanoidiQ86TP1.
    KOiK01514.
    OMAiIYMDLEA.
    PhylomeDBiQ86TP1.
    TreeFamiTF323914.

    Family and domain databases

    InterProiIPR001667. DDH_dom.
    IPR004097. DHHA2.
    [Graphical view]
    PfamiPF01368. DHH. 1 hit.
    PF02833. DHHA2. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86TP1-1) [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

    MEDYLQGCRA ALQESRPLHV VLGNEACDLD STVSALALAF YLAKTTEAEE    50
    VFVPVLNIKR SELPLRGDIV FFLQKVHIPE SILIFRDEID LHALYQAGQL 100
    TLILVDHHIL SKSDTALEEA VAEVLDHRPI EPKHCPPCHV SVELVGSCAT 150
    LVTERILQGA PEILDRQTAA LLHGTIILDC VNMDLKIGKA TPKDSKYVEK 200
    LEALFPDLPK RNDIFDSLQK AKFDVSGLTT EQMLRKDQKT IYRQGVKVAI 250
    SAIYMDLEAF LQRSNLLADL HAFCQAHSYD VLVAMTIFFN THNEPVRQLA 300
    IFCPHVALQT TICEVLERSH SPPLKLTPAS STHPNLHAYL QGNTQVSRKK 350
    LLPLLQEALS AYFDSMKIPS GQPETADVSR EQVDKELDRA SNSLISGLSQ 400
    DEEDPPLPPT PMNSLVDECP LDQGLPKLSA EAVFEKCSQI SLSQSTTASL 450
    SKK 453
    Length:453
    Mass (Da):50,200
    Last modified:May 5, 2009 - v2
    Checksum:i34BE1909AB89DBD5
    GO
    Isoform 2 (identifier: Q86TP1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         45-112: TTEAEEVFVPVLNIKRSELPLRGDIVFFLQKVHIPESILIFRDEIDLHALYQAGQLTLILVDHHILSK → A

    Note: No experimental confirmation available.

    Show »
    Length:386
    Mass (Da):42,456
    Checksum:i6E3355352353B0A5
    GO
    Isoform 3 (identifier: Q86TP1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-182: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:271
    Mass (Da):30,127
    Checksum:iEADC5693A59D308F
    GO
    Isoform 4 (identifier: Q86TP1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         15-174: Missing.
         259-311: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:240
    Mass (Da):26,611
    Checksum:i7D8897402A2B3136
    GO
    Isoform 5 (identifier: Q86TP1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-182: Missing.
         259-311: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:218
    Mass (Da):24,131
    Checksum:iDC0632A96FDD07EE
    GO
    Isoform 6 (identifier: Q86TP1-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-232: Missing.
         259-311: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:168
    Mass (Da):18,478
    Checksum:i54405F7EA079B5C2
    GO
    Isoform 7 (identifier: Q86TP1-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-232: Missing.

    Show »
    Length:221
    Mass (Da):24,475
    Checksum:i108DE09A66C5F957
    GO

    Sequence cautioni

    The sequence BAB55423.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAG60534.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141E → A in AAK00592. 1 PublicationCurated
    Sequence conflicti19 – 224HVVL → AWHE in AAF04914. (PubMed:10524757)Curated
    Sequence conflicti221 – 2211A → V in AAC95290. (PubMed:10602478)Curated
    Sequence conflicti221 – 2211A → V in AAF04914. (PubMed:10524757)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti397 – 3971G → R.
    Corresponds to variant rs3738477 [ dbSNP | Ensembl ].
    VAR_059559
    Natural varianti397 – 3971G → S.
    Corresponds to variant rs3738477 [ dbSNP | Ensembl ].
    VAR_043728

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 232232Missing in isoform 6 and isoform 7. 2 PublicationsVSP_034013Add
    BLAST
    Alternative sequencei1 – 182182Missing in isoform 3 and isoform 5. 2 PublicationsVSP_034014Add
    BLAST
    Alternative sequencei15 – 174160Missing in isoform 4. 1 PublicationVSP_034015Add
    BLAST
    Alternative sequencei45 – 11268TTEAE…HILSK → A in isoform 2. 1 PublicationVSP_034016Add
    BLAST
    Alternative sequencei259 – 31153Missing in isoform 4, isoform 5 and isoform 6. 3 PublicationsVSP_034017Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051907 mRNA. Translation: AAC95290.1.
    AF123538 mRNA. Translation: AAK00592.1.
    AF123539 mRNA. Translation: AAK00593.1.
    AK027875 mRNA. Translation: BAB55423.1. Different initiation.
    AK294154 mRNA. Translation: BAG57478.1.
    AK298273 mRNA. Translation: BAG60534.1. Different initiation.
    AK315120 mRNA. Translation: BAG37575.1.
    AL590133 Genomic DNA. Translation: CAI13338.1.
    AL590133 Genomic DNA. Translation: CAI13341.1.
    AL590133 Genomic DNA. Translation: CAI13342.1.
    AL590133 Genomic DNA. Translation: CAI13343.1.
    CH471121 Genomic DNA. Translation: EAW53486.1.
    CH471121 Genomic DNA. Translation: EAW53488.1.
    CH471121 Genomic DNA. Translation: EAW53489.1.
    BC014886 mRNA. Translation: AAH14886.1.
    BC025304 mRNA. Translation: AAH25304.1.
    BC063481 mRNA. Translation: AAH63481.1.
    U67085 mRNA. Translation: AAF04914.1.
    AL122054 mRNA. Translation: CAH56396.1.
    CCDSiCCDS977.1. [Q86TP1-1]
    RefSeqiNP_067045.1. NM_021222.1. [Q86TP1-1]
    XP_005245453.1. XM_005245396.1. [Q86TP1-3]
    XP_005245454.1. XM_005245397.2. [Q86TP1-3]
    UniGeneiHs.78524.

    Genome annotation databases

    EnsembliENST00000271620; ENSP00000271620; ENSG00000143363. [Q86TP1-1]
    ENST00000368934; ENSP00000357930; ENSG00000143363. [Q86TP1-5]
    ENST00000368935; ENSP00000357931; ENSG00000143363. [Q86TP1-6]
    ENST00000368936; ENSP00000357932; ENSG00000143363. [Q86TP1-3]
    ENST00000368937; ENSP00000357933; ENSG00000143363. [Q86TP1-5]
    GeneIDi58497.
    KEGGihsa:58497.
    UCSCiuc001ewh.1. human. [Q86TP1-1]
    uc001ewj.1. human. [Q86TP1-6]
    uc001ewk.1. human. [Q86TP1-5]
    uc010pco.1. human. [Q86TP1-7]

    Polymorphism databases

    DMDMi229462737.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051907 mRNA. Translation: AAC95290.1 .
    AF123538 mRNA. Translation: AAK00592.1 .
    AF123539 mRNA. Translation: AAK00593.1 .
    AK027875 mRNA. Translation: BAB55423.1 . Different initiation.
    AK294154 mRNA. Translation: BAG57478.1 .
    AK298273 mRNA. Translation: BAG60534.1 . Different initiation.
    AK315120 mRNA. Translation: BAG37575.1 .
    AL590133 Genomic DNA. Translation: CAI13338.1 .
    AL590133 Genomic DNA. Translation: CAI13341.1 .
    AL590133 Genomic DNA. Translation: CAI13342.1 .
    AL590133 Genomic DNA. Translation: CAI13343.1 .
    CH471121 Genomic DNA. Translation: EAW53486.1 .
    CH471121 Genomic DNA. Translation: EAW53488.1 .
    CH471121 Genomic DNA. Translation: EAW53489.1 .
    BC014886 mRNA. Translation: AAH14886.1 .
    BC025304 mRNA. Translation: AAH25304.1 .
    BC063481 mRNA. Translation: AAH63481.1 .
    U67085 mRNA. Translation: AAF04914.1 .
    AL122054 mRNA. Translation: CAH56396.1 .
    CCDSi CCDS977.1. [Q86TP1-1 ]
    RefSeqi NP_067045.1. NM_021222.1. [Q86TP1-1 ]
    XP_005245453.1. XM_005245396.1. [Q86TP1-3 ]
    XP_005245454.1. XM_005245397.2. [Q86TP1-3 ]
    UniGenei Hs.78524.

    3D structure databases

    ProteinModelPortali Q86TP1.
    SMRi Q86TP1. Positions 18-360.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121827. 4 interactions.
    IntActi Q86TP1. 2 interactions.

    Chemistry

    ChEMBLi CHEMBL2079850.

    PTM databases

    PhosphoSitei Q86TP1.

    Polymorphism databases

    DMDMi 229462737.

    Proteomic databases

    MaxQBi Q86TP1.
    PaxDbi Q86TP1.
    PRIDEi Q86TP1.

    Protocols and materials databases

    DNASUi 58497.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000271620 ; ENSP00000271620 ; ENSG00000143363 . [Q86TP1-1 ]
    ENST00000368934 ; ENSP00000357930 ; ENSG00000143363 . [Q86TP1-5 ]
    ENST00000368935 ; ENSP00000357931 ; ENSG00000143363 . [Q86TP1-6 ]
    ENST00000368936 ; ENSP00000357932 ; ENSG00000143363 . [Q86TP1-3 ]
    ENST00000368937 ; ENSP00000357933 ; ENSG00000143363 . [Q86TP1-5 ]
    GeneIDi 58497.
    KEGGi hsa:58497.
    UCSCi uc001ewh.1. human. [Q86TP1-1 ]
    uc001ewj.1. human. [Q86TP1-6 ]
    uc001ewk.1. human. [Q86TP1-5 ]
    uc010pco.1. human. [Q86TP1-7 ]

    Organism-specific databases

    CTDi 58497.
    GeneCardsi GC01P150980.
    H-InvDB HIX0001042.
    HGNCi HGNC:13420. PRUNE.
    HPAi HPA028411.
    neXtProti NX_Q86TP1.
    PharmGKBi PA134939749.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1227.
    HOVERGENi HBG058142.
    InParanoidi Q86TP1.
    KOi K01514.
    OMAi IYMDLEA.
    PhylomeDBi Q86TP1.
    TreeFami TF323914.

    Miscellaneous databases

    GenomeRNAii 58497.
    NextBioi 64992.
    PROi Q86TP1.

    Gene expression databases

    ArrayExpressi Q86TP1.
    Bgeei Q86TP1.
    CleanExi HS_PRUNE.
    Genevestigatori Q86TP1.

    Family and domain databases

    InterProi IPR001667. DDH_dom.
    IPR004097. DHHA2.
    [Graphical view ]
    Pfami PF01368. DHH. 1 hit.
    PF02833. DHHA2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evidence for interaction between human PRUNE and nm23-H1 NDPKinase."
      Reymond A., Volorio S., Merla G., Al-Maghtheh M., Zuffardi O., Bulfone A., Ballabio A., Zollo M.
      Oncogene 18:7244-7252(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH NME1, SUBCELLULAR LOCATION, FUNCTION.
    2. "Human Prune homolog."
      Zollo M., Volorio S.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
    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] (ISOFORMS 1; 5 AND 7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-453 (ISOFORMS 1/3).
      Tissue: Brain cortex, Kidney and Thyroid.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1; 3 AND 6).
      Tissue: Blood and Brain.
    7. "Sequencing analysis of forty-eight human image cDNA clones similar to Drosophila mutant protein."
      Volorio S., Simon G., Repetto M., Cucciardi M., Banfi S., Borsani G., Ballabio A., Zollo M.
      DNA Seq. 9:307-315(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-453 (ISOFORM 1).
      Tissue: Brain.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-453 (ISOFORMS 1/2/3/4/5/6/7).
      Tissue: Testis.
    9. Cited for: TISSUE SPECIFICITY, FUNCTION.
    10. Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH NME1, ENZYME REGULATION, MUTAGENESIS OF ASP-28; ASP-106; 126-ASP--PRO-129 AND ASP-179.
    11. "Overexpression of h-prune in breast cancer is correlated with advanced disease status."
      Zollo M., Andre A., Cossu A., Sini M.C., D'Angelo A., Marino N., Budroni M., Tanda F., Arrigoni G., Palmieri G.
      Clin. Cancer Res. 11:199-205(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    12. "Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions."
      Kobayashi T., Hino S., Oue N., Asahara T., Zollo M., Yasui W., Kikuchi A.
      Mol. Cell. Biol. 26:898-911(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GSK3B, SUBCELLULAR LOCATION, FUNCTION.
    13. "Domain mapping on the human metastasis regulator protein h-Prune reveals a C-terminal dimerization domain."
      Middelhaufe S., Garzia L., Ohndorf U.M., Kachholz B., Zollo M., Steegborn C.
      Biochem. J. 407:199-205(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NME1, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    14. "Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility."
      Garzia L., D'Angelo A., Amoresano A., Knauer S.K., Cirulli C., Campanella C., Stauber R.H., Steegborn C., Iolascon A., Zollo M.
      Oncogene 27:1853-1864(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NME1, FUNCTION.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPRUNE_HUMAN
    AccessioniPrimary (citable) accession number: Q86TP1
    Secondary accession number(s): B2RCH8
    , B4DFL7, Q5SZF9, Q659E5, Q6P4E0, Q8N654, Q96JU5, Q9C071, Q9C072, Q9UIV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 89 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 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3