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O00743

- PPP6_HUMAN

UniProt

O00743 - PPP6_HUMAN

Protein

Serine/threonine-protein phosphatase 6 catalytic subunit

Gene

PPP6C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Catalytic subunit of protein phosphatase 6 (PP6). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation. N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1. Downregulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7.4 Publications

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi53 – 531Manganese 1By similarity
    Metal bindingi55 – 551Manganese 1By similarity
    Metal bindingi81 – 811Manganese 1By similarity
    Metal bindingi81 – 811Manganese 2By similarity
    Metal bindingi113 – 1131Manganese 2By similarity
    Active sitei114 – 1141Proton donorBy similarity
    Metal bindingi163 – 1631Manganese 2By similarity
    Metal bindingi237 – 2371Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein serine/threonine phosphatase activity Source: MGI

    GO - Biological processi

    1. G1/S transition of mitotic cell cycle Source: ProtInc
    2. protein dephosphorylation Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 6 catalytic subunit (EC:3.1.3.16)
    Short name:
    PP6C
    Cleaved into the following chain:
    Gene namesi
    Name:PPP6C
    Synonyms:PPP6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:9323. PPP6C.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytosol Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33687.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 305305Serine/threonine-protein phosphatase 6 catalytic subunitPRO_0000424504Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 305304Serine/threonine-protein phosphatase 6 catalytic subunit, N-terminally processedPRO_0000058877Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO00743.
    PaxDbiO00743.
    PeptideAtlasiO00743.
    PRIDEiO00743.

    2D gel databases

    OGPiO00743.

    PTM databases

    PhosphoSiteiO00743.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in all tissues tested with highest expression levels in testis, heart, kidney, brain, stomach, liver and skeletal muscle and lowest in placenta, lung colon and spleen.2 Publications

    Inductioni

    Regulated by IL2/interleukin-2 in peripheral blood T cells.1 Publication

    Gene expression databases

    ArrayExpressiO00743.
    BgeeiO00743.
    CleanExiHS_PPP6C.
    GenevestigatoriO00743.

    Organism-specific databases

    HPAiHPA050940.

    Interactioni

    Subunit structurei

    Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with IGBP1, MAP3K7, NFKBIE, PPP6R1, PPP6R2 and PPP6R3.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ANKRD28O150849EBI-359751,EBI-359567
    IGBP1P7831810EBI-359751,EBI-1055954
    MAP3K7O433184EBI-359751,EBI-358684
    PPP6R1Q9UPN711EBI-359751,EBI-359745
    PPP6R2O751708EBI-359751,EBI-359739
    PPP6R3Q5H9R75EBI-359751,EBI-355498
    TIPRLO756634EBI-359751,EBI-1054735

    Protein-protein interaction databases

    BioGridi111529. 32 interactions.
    DIPiDIP-27581N.
    IntActiO00743. 20 interactions.
    MINTiMINT-1139697.
    STRINGi9606.ENSP00000392147.

    Structurei

    3D structure databases

    ProteinModelPortaliO00743.
    SMRiO00743. Positions 5-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172696.
    HOVERGENiHBG000216.
    InParanoidiO00743.
    KOiK15498.
    OMAiVPETSYI.
    OrthoDBiEOG74N5H2.
    PhylomeDBiO00743.
    TreeFamiTF105563.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 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

    Isoform 1 (identifier: O00743-1) [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

    MAPLDLDKYV EIARLCKYLP ENDLKRLCDY VCDLLLEESN VQPVSTPVTV    50
    CGDIHGQFYD LCELFRTGGQ VPDTNYIFMG DFVDRGYYSL ETFTYLLALK 100
    AKWPDRITLL RGNHESRQIT QVYGFYDECQ TKYGNANAWR YCTKVFDMLT 150
    VAALIDEQIL CVHGGLSPDI KTLDQIRTIE RNQEIPHKGA FCDLVWSDPE 200
    DVDTWAISPR GAGWLFGAKV TNEFVHINNL KLICRAHQLV HEGYKFMFDE 250
    KLVTVWSAPN YCYRCGNIAS IMVFKDVNTR EPKLFRAVPD SERVIPPRTT 300
    TPYFL 305
    Length:305
    Mass (Da):35,144
    Last modified:July 1, 1997 - v1
    Checksum:i55E95DB6CEA7CFF4
    GO
    Isoform 2 (identifier: O00743-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         58-79: Missing.

    Show »
    Length:283
    Mass (Da):32,532
    Checksum:iC2334512732059DC
    GO
    Isoform 3 (identifier: O00743-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         25-25: K → KVSPICGLAPSGCGAPAGRPFLSPGPPPVFHFLRFLKE

    Show »
    Length:342
    Mass (Da):38,947
    Checksum:iC26CAD5C8016F112
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 644LCEL → AG in AAD45400. (PubMed:10227379)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei25 – 251K → KVSPICGLAPSGCGAPAGRP FLSPGPPPVFHFLRFLKE in isoform 3. 1 PublicationVSP_041158
    Alternative sequencei58 – 7922Missing in isoform 2. 1 PublicationVSP_038376Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92972 mRNA. Translation: CAA63549.1.
    AF035158 mRNA. Translation: AAD45400.2.
    AK295190 mRNA. Translation: BAH12005.1.
    AK299087 mRNA. Translation: BAH12945.1.
    AK312332 mRNA. Translation: BAG35253.1.
    BT019708 mRNA. Translation: AAV38514.1.
    AL445930 Genomic DNA. Translation: CAI13677.1.
    CH471090 Genomic DNA. Translation: EAW87611.1.
    BC006990 mRNA. Translation: AAH06990.1.
    CCDSiCCDS48018.1. [O00743-3]
    CCDS48019.1. [O00743-2]
    CCDS6861.1. [O00743-1]
    RefSeqiNP_001116827.1. NM_001123355.1. [O00743-3]
    NP_001116841.1. NM_001123369.1. [O00743-2]
    NP_002712.1. NM_002721.4. [O00743-1]
    UniGeneiHs.744091.

    Genome annotation databases

    EnsembliENST00000373547; ENSP00000362648; ENSG00000119414. [O00743-1]
    ENST00000415905; ENSP00000411744; ENSG00000119414. [O00743-2]
    ENST00000451402; ENSP00000392147; ENSG00000119414. [O00743-3]
    GeneIDi5537.
    KEGGihsa:5537.
    UCSCiuc004bpg.4. human. [O00743-1]
    uc010mwv.3. human. [O00743-3]
    uc010mww.3. human. [O00743-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92972 mRNA. Translation: CAA63549.1 .
    AF035158 mRNA. Translation: AAD45400.2 .
    AK295190 mRNA. Translation: BAH12005.1 .
    AK299087 mRNA. Translation: BAH12945.1 .
    AK312332 mRNA. Translation: BAG35253.1 .
    BT019708 mRNA. Translation: AAV38514.1 .
    AL445930 Genomic DNA. Translation: CAI13677.1 .
    CH471090 Genomic DNA. Translation: EAW87611.1 .
    BC006990 mRNA. Translation: AAH06990.1 .
    CCDSi CCDS48018.1. [O00743-3 ]
    CCDS48019.1. [O00743-2 ]
    CCDS6861.1. [O00743-1 ]
    RefSeqi NP_001116827.1. NM_001123355.1. [O00743-3 ]
    NP_001116841.1. NM_001123369.1. [O00743-2 ]
    NP_002712.1. NM_002721.4. [O00743-1 ]
    UniGenei Hs.744091.

    3D structure databases

    ProteinModelPortali O00743.
    SMRi O00743. Positions 5-276.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111529. 32 interactions.
    DIPi DIP-27581N.
    IntActi O00743. 20 interactions.
    MINTi MINT-1139697.
    STRINGi 9606.ENSP00000392147.

    PTM databases

    PhosphoSitei O00743.

    2D gel databases

    OGPi O00743.

    Proteomic databases

    MaxQBi O00743.
    PaxDbi O00743.
    PeptideAtlasi O00743.
    PRIDEi O00743.

    Protocols and materials databases

    DNASUi 5537.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373547 ; ENSP00000362648 ; ENSG00000119414 . [O00743-1 ]
    ENST00000415905 ; ENSP00000411744 ; ENSG00000119414 . [O00743-2 ]
    ENST00000451402 ; ENSP00000392147 ; ENSG00000119414 . [O00743-3 ]
    GeneIDi 5537.
    KEGGi hsa:5537.
    UCSCi uc004bpg.4. human. [O00743-1 ]
    uc010mwv.3. human. [O00743-3 ]
    uc010mww.3. human. [O00743-2 ]

    Organism-specific databases

    CTDi 5537.
    GeneCardsi GC09M127908.
    HGNCi HGNC:9323. PPP6C.
    HPAi HPA050940.
    MIMi 612725. gene.
    neXtProti NX_O00743.
    PharmGKBi PA33687.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172696.
    HOVERGENi HBG000216.
    InParanoidi O00743.
    KOi K15498.
    OMAi VPETSYI.
    OrthoDBi EOG74N5H2.
    PhylomeDBi O00743.
    TreeFami TF105563.

    Miscellaneous databases

    ChiTaRSi PPP6C. human.
    GeneWikii PPP6C.
    GenomeRNAii 5537.
    NextBioi 21450.
    PROi O00743.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00743.
    Bgeei O00743.
    CleanExi HS_PPP6C.
    Genevestigatori O00743.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The novel human protein serine/threonine phosphatase 6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, which are involved in cell cycle regulation."
      Bastians H., Ponstingl H.
      J. Cell Sci. 109:2865-2874(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    2. "Identification of a type 6 protein Ser/Thr phosphatase regulated by interleukin-2 stimulation."
      Filali M., Li S., Kim H.W., Wadzinski B., Kamoun M.
      J. Cell. Biochem. 73:153-163(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION.
      Tissue: Brain.
    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; 2 AND 3).
      Tissue: Cerebellum.
    4. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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] (ISOFORM 1).
      Tissue: Urinary bladder.
    8. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14; 67-100; 118-140; 145-171; 211-231 AND 252-275, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    9. "Alpha 4 associates with protein phosphatases 2A, 4, and 6."
      Chen J., Peterson R.T., Schreiber S.L.
      Biochem. Biophys. Res. Commun. 247:827-832(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGBP1.
    10. "Protein phosphatase 6 subunit with conserved Sit4-associated protein domain targets IkappaBepsilon."
      Stefansson B., Brautigan D.L.
      J. Biol. Chem. 281:22624-22634(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIE; PPP6R1 AND PPP6R2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway."
      Kajino T., Ren H., Iemura S., Natsume T., Stefansson B., Brautigan D.L., Matsumoto K., Ninomiya-Tsuji J.
      J. Biol. Chem. 281:39891-39896(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP3K7.
    12. "Protein phosphatase PP6 N terminal domain restricts G1 to S phase progression in human cancer cells."
      Stefansson B., Brautigan D.L.
      Cell Cycle 6:1386-1392(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Protein phosphatase 6 regulatory subunits composed of ankyrin repeat domains."
      Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.
      Biochemistry 47:1442-1451(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANKRD28; PPP6R1; PPP6R2 AND PPP6R3.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPPP6_HUMAN
    AccessioniPrimary (citable) accession number: O00743
    Secondary accession number(s): B2R5V6
    , B7Z2W9, B7Z5K9, Q5U0A2, Q9UIC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3