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Q5H9R7

- PP6R3_HUMAN

UniProt

Q5H9R7 - PP6R3_HUMAN

Protein

Serine/threonine-protein phosphatase 6 regulatory subunit 3

Gene

PPP6R3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (07 Feb 2006)
      Previous versions | rss
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    Functioni

    Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein phosphatase binding Source: MGI

    GO - Biological processi

    1. regulation of phosphoprotein phosphatase activity Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 6 regulatory subunit 3
    Alternative name(s):
    SAPS domain family member 3
    Sporulation-induced transcript 4-associated protein SAPL
    Gene namesi
    Name:PPP6R3
    Synonyms:C11orf23, KIAA1558, PP6R3, SAPL, SAPS3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1173. PPP6R3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25487.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 873873Serine/threonine-protein phosphatase 6 regulatory subunit 3PRO_0000046100Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei579 – 5791Phosphoserine4 Publications
    Modified residuei617 – 6171Phosphoserine6 Publications
    Modified residuei722 – 7221Phosphoserine1 Publication
    Modified residuei853 – 8531PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5H9R7.
    PaxDbiQ5H9R7.
    PRIDEiQ5H9R7.

    PTM databases

    PhosphoSiteiQ5H9R7.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle, placenta, heart, pancreas, testis, brain, lung, liver, kidney, spleen, thymus, prostate, small intestine, colon and leukocytes.2 Publications

    Gene expression databases

    ArrayExpressiQ5H9R7.
    BgeeiQ5H9R7.
    GenevestigatoriQ5H9R7.

    Organism-specific databases

    HPAiCAB017183.
    HPA038467.
    HPA038468.

    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 PPP6C and ANKRD28.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ANKRD28O150845EBI-355498,EBI-359567
    PPP6CO007435EBI-355498,EBI-359751

    Protein-protein interaction databases

    BioGridi120579. 51 interactions.
    IntActiQ5H9R7. 14 interactions.
    MINTiMINT-5004961.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5H9R7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SAPS family.Curated

    Phylogenomic databases

    eggNOGiNOG303042.
    HOVERGENiHBG069733.
    KOiK15501.
    OrthoDBiEOG7PGDQ3.
    PhylomeDBiQ5H9R7.
    TreeFamiTF313227.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR007587. SAPS.
    [Graphical view]
    PANTHERiPTHR12634. PTHR12634. 1 hit.
    PfamiPF04499. SAPS. 2 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5H9R7-1) [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

    MFWKFDLHSS SHIDTLLERE DVTLKELMDE EDVLQECKAQ NRKLIEFLLK    50
    AECLEDLVSF IIEEPPQDMD EKIRYKYPNI SCELLTSDVS QMNDRLGEDE 100
    SLLMKLYSFL LNDSPLNPLL ASFFSKVLSI LISRKPEQIV DFLKKKHDFV 150
    DLIIKHIGTS AIMDLLLRLL TCIEPPQPRQ DVLNWLNEEK IIQRLVEIVH 200
    PSQEEDRHSN ASQSLCEIVR LSRDQMLQIQ NSTEPDPLLA TLEKQEIIEQ 250
    LLSNIFHKEK NESAIVSAIQ ILLTLLETRR PTFEGHIEIC PPGMSHSACS 300
    VNKSVLEAIR GRLGSFHELL LEPPKKSVMK TTWGVLDPPV GNTRLNVIRL 350
    ISSLLQTNTS SINGDLMELN SIGVILNMFF KYTWNNFLHT QVEICIALIL 400
    ASPFENTENA TITDQDSTGD NLLLKHLFQK CQLIERILEA WEMNEKKQAE 450
    GGRRHGYMGH LTRIANCIVH STDKGPNSAL VQQLIKDLPD EVRERWETFC 500
    TSSLGETNKR NTVDLVTTCH IHSSSDDEID FKETGFSQDS SLQQAFSDYQ 550
    MQQMTSNFID QFGFNDEKFA DQDDIGNVSF DRVSDINFTL NTNESGNIAL 600
    FEACCKERIQ QFDDGGSDEE DIWEEKHIAF TPESQRRSSS GSTDSEESTD 650
    SEEEDGAKQD LFEPSSANTE DKMEVDLSEP PNWSANFDVP METTHGAPLD 700
    SVGSDVWSTE EPMPTKETGW ASFSEFTSSL STKDSLRSNS PVEMETSTEP 750
    MDPLTPSAAA LAVQPEAAGS VAMEASSDGE EDAESTDKVT ETVMNGGMKE 800
    TLSLTVDAKT ETAVFKSEEG KLSTSQDAAC KDAEECPETA EAKCAAPRPP 850
    SSSPEQRTGQ PSAPGDTSVN GPV 873
    Length:873
    Mass (Da):97,669
    Last modified:February 7, 2006 - v2
    Checksum:i5B4C69991E7DE16F
    GO
    Isoform 2 (identifier: Q5H9R7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         544-549: Missing.

    Show »
    Length:867
    Mass (Da):96,957
    Checksum:i9E76BCA0E23EE3DE
    GO
    Isoform 3 (identifier: Q5H9R7-3) [UniParc]FASTAAdd to Basket

    Also known as: B, C11orf23b, SAPLb

    The sequence of this isoform differs from the canonical sequence as follows:
         326-376: Missing.
         516-544: Missing.
         857-873: RTGQPSAPGDTSVNGPV → SGVEIPALPGQWSQQ

    Show »
    Length:791
    Mass (Da):88,909
    Checksum:i1C936F03A484D53D
    GO
    Isoform 4 (identifier: Q5H9R7-4) [UniParc]FASTAAdd to Basket

    Also known as: A, C11orf23a, SAPLa

    The sequence of this isoform differs from the canonical sequence as follows:
         326-376: Missing.
         516-544: Missing.

    Show »
    Length:793
    Mass (Da):88,952
    Checksum:iAC5BEE22285932F4
    GO
    Isoform 5 (identifier: Q5H9R7-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         817-817: S → RVLKSYR

    Show »
    Length:879
    Mass (Da):98,485
    Checksum:iE0AE6571756853C1
    GO
    Isoform 6 (identifier: Q5H9R7-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         516-544: Missing.

    Show »
    Length:844
    Mass (Da):94,445
    Checksum:iADB89AA9C567C580
    GO

    Sequence cautioni

    The sequence AAZ99639.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA91978.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB13384.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAB71396.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti292 – 2921P → S in CAH18675. (PubMed:17974005)Curated
    Sequence conflicti443 – 4431M → V in BAB71396. (PubMed:14702039)Curated
    Sequence conflicti477 – 4771N → S in CAI45957. (PubMed:17974005)Curated
    Sequence conflicti677 – 6771L → P in CAI45957. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti842 – 8421A → V.
    Corresponds to variant rs34009811 [ dbSNP | Ensembl ].
    VAR_057720

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei326 – 37651Missing in isoform 3 and isoform 4. 1 PublicationVSP_017140Add
    BLAST
    Alternative sequencei516 – 54429Missing in isoform 3, isoform 4 and isoform 6. 2 PublicationsVSP_017141Add
    BLAST
    Alternative sequencei544 – 5496Missing in isoform 2. 1 PublicationVSP_017142
    Alternative sequencei817 – 8171S → RVLKSYR in isoform 5. 1 PublicationVSP_017143
    Alternative sequencei857 – 87317RTGQP…VNGPV → SGVEIPALPGQWSQQ in isoform 3. 1 PublicationVSP_017144Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF264779 mRNA. Translation: AAG36934.1.
    AF264780 mRNA. Translation: AAG36935.1.
    DQ111954 mRNA. Translation: AAZ99639.2. Different initiation.
    AB046778 mRNA. Translation: BAB13384.2. Different initiation.
    AL834471 mRNA. Translation: CAD39130.1.
    CR749815 mRNA. Translation: CAH18675.1.
    CR933658 mRNA. Translation: CAI45957.1.
    BC007738 mRNA. Translation: AAH07738.2.
    BC105933 mRNA. Translation: AAI05934.1.
    BC105934 mRNA. Translation: AAI05935.1.
    BC107599 mRNA. Translation: AAI07600.1.
    AK001920 mRNA. Translation: BAA91978.1. Different initiation.
    AK057250 mRNA. Translation: BAB71396.1. Different initiation.
    CCDSiCCDS53671.1. [Q5H9R7-5]
    CCDS53672.1. [Q5H9R7-1]
    CCDS53673.1. [Q5H9R7-2]
    CCDS53674.1. [Q5H9R7-6]
    CCDS53675.1. [Q5H9R7-3]
    CCDS8182.1. [Q5H9R7-4]
    RefSeqiNP_001157632.1. NM_001164160.1. [Q5H9R7-5]
    NP_001157633.1. NM_001164161.1. [Q5H9R7-1]
    NP_001157634.1. NM_001164162.1. [Q5H9R7-2]
    NP_001157635.1. NM_001164163.1. [Q5H9R7-6]
    NP_001157636.1. NM_001164164.1. [Q5H9R7-3]
    NP_060782.2. NM_018312.4. [Q5H9R7-4]
    XP_006718676.1. XM_006718613.1. [Q5H9R7-1]
    XP_006718677.1. XM_006718614.1. [Q5H9R7-2]
    XP_006718681.1. XM_006718618.1. [Q5H9R7-6]
    XP_006718687.1. XM_006718624.1. [Q5H9R7-4]
    UniGeneiHs.503022.

    Genome annotation databases

    EnsembliENST00000265636; ENSP00000265636; ENSG00000110075. [Q5H9R7-4]
    ENST00000393800; ENSP00000377389; ENSG00000110075. [Q5H9R7-1]
    ENST00000393801; ENSP00000377390; ENSG00000110075. [Q5H9R7-5]
    ENST00000524845; ENSP00000431415; ENSG00000110075. [Q5H9R7-6]
    ENST00000524904; ENSP00000433058; ENSG00000110075. [Q5H9R7-2]
    ENST00000529710; ENSP00000437329; ENSG00000110075. [Q5H9R7-3]
    GeneIDi55291.
    KEGGihsa:55291.
    UCSCiuc001onu.3. human. [Q5H9R7-4]
    uc001onv.3. human. [Q5H9R7-5]
    uc001onw.3. human. [Q5H9R7-1]
    uc001onx.3. human. [Q5H9R7-2]
    uc001ony.4. human. [Q5H9R7-6]
    uc009ysh.3. human. [Q5H9R7-3]

    Polymorphism databases

    DMDMi88941982.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF264779 mRNA. Translation: AAG36934.1 .
    AF264780 mRNA. Translation: AAG36935.1 .
    DQ111954 mRNA. Translation: AAZ99639.2 . Different initiation.
    AB046778 mRNA. Translation: BAB13384.2 . Different initiation.
    AL834471 mRNA. Translation: CAD39130.1 .
    CR749815 mRNA. Translation: CAH18675.1 .
    CR933658 mRNA. Translation: CAI45957.1 .
    BC007738 mRNA. Translation: AAH07738.2 .
    BC105933 mRNA. Translation: AAI05934.1 .
    BC105934 mRNA. Translation: AAI05935.1 .
    BC107599 mRNA. Translation: AAI07600.1 .
    AK001920 mRNA. Translation: BAA91978.1 . Different initiation.
    AK057250 mRNA. Translation: BAB71396.1 . Different initiation.
    CCDSi CCDS53671.1. [Q5H9R7-5 ]
    CCDS53672.1. [Q5H9R7-1 ]
    CCDS53673.1. [Q5H9R7-2 ]
    CCDS53674.1. [Q5H9R7-6 ]
    CCDS53675.1. [Q5H9R7-3 ]
    CCDS8182.1. [Q5H9R7-4 ]
    RefSeqi NP_001157632.1. NM_001164160.1. [Q5H9R7-5 ]
    NP_001157633.1. NM_001164161.1. [Q5H9R7-1 ]
    NP_001157634.1. NM_001164162.1. [Q5H9R7-2 ]
    NP_001157635.1. NM_001164163.1. [Q5H9R7-6 ]
    NP_001157636.1. NM_001164164.1. [Q5H9R7-3 ]
    NP_060782.2. NM_018312.4. [Q5H9R7-4 ]
    XP_006718676.1. XM_006718613.1. [Q5H9R7-1 ]
    XP_006718677.1. XM_006718614.1. [Q5H9R7-2 ]
    XP_006718681.1. XM_006718618.1. [Q5H9R7-6 ]
    XP_006718687.1. XM_006718624.1. [Q5H9R7-4 ]
    UniGenei Hs.503022.

    3D structure databases

    ProteinModelPortali Q5H9R7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120579. 51 interactions.
    IntActi Q5H9R7. 14 interactions.
    MINTi MINT-5004961.

    PTM databases

    PhosphoSitei Q5H9R7.

    Polymorphism databases

    DMDMi 88941982.

    Proteomic databases

    MaxQBi Q5H9R7.
    PaxDbi Q5H9R7.
    PRIDEi Q5H9R7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265636 ; ENSP00000265636 ; ENSG00000110075 . [Q5H9R7-4 ]
    ENST00000393800 ; ENSP00000377389 ; ENSG00000110075 . [Q5H9R7-1 ]
    ENST00000393801 ; ENSP00000377390 ; ENSG00000110075 . [Q5H9R7-5 ]
    ENST00000524845 ; ENSP00000431415 ; ENSG00000110075 . [Q5H9R7-6 ]
    ENST00000524904 ; ENSP00000433058 ; ENSG00000110075 . [Q5H9R7-2 ]
    ENST00000529710 ; ENSP00000437329 ; ENSG00000110075 . [Q5H9R7-3 ]
    GeneIDi 55291.
    KEGGi hsa:55291.
    UCSCi uc001onu.3. human. [Q5H9R7-4 ]
    uc001onv.3. human. [Q5H9R7-5 ]
    uc001onw.3. human. [Q5H9R7-1 ]
    uc001onx.3. human. [Q5H9R7-2 ]
    uc001ony.4. human. [Q5H9R7-6 ]
    uc009ysh.3. human. [Q5H9R7-3 ]

    Organism-specific databases

    CTDi 55291.
    GeneCardsi GC11P068229.
    HGNCi HGNC:1173. PPP6R3.
    HPAi CAB017183.
    HPA038467.
    HPA038468.
    MIMi 610879. gene.
    neXtProti NX_Q5H9R7.
    PharmGKBi PA25487.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG303042.
    HOVERGENi HBG069733.
    KOi K15501.
    OrthoDBi EOG7PGDQ3.
    PhylomeDBi Q5H9R7.
    TreeFami TF313227.

    Miscellaneous databases

    ChiTaRSi PPP6R3. human.
    GenomeRNAii 55291.
    NextBioi 59478.
    PROi Q5H9R7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5H9R7.
    Bgeei Q5H9R7.
    Genevestigatori Q5H9R7.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR007587. SAPS.
    [Graphical view ]
    PANTHERi PTHR12634. PTHR12634. 1 hit.
    Pfami PF04499. SAPS. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The sequence and gene characterization of a 400-kb candidate region for IDDM4 on chromosome 11q13."
      Twells R.C.J., Metzker M.L., Brown S.D., Cox R., Garey C., Hammond H., Hey P.J., Levy E., Nakagawa Y., Philips M.S., Todd J.A., Hess J.F.
      Genomics 72:231-242(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, TISSUE SPECIFICITY.
    2. Guergnon J., Stefansson B., Brautigan D.L.
      Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION.
    3. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 226-873 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
      DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 620-873 (ISOFORMS 1/2/4/6).
      Tissue: Colon carcinoma, Melanoma and Seminal plasma.
    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 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 650-873 (ISOFORMS 1/2/4/6).
      Tissue: Muscle.
    7. "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] OF 221-873 (ISOFORM 1).
      Tissue: Placenta and Testis.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: SUBCELLULAR LOCATION, INTERACTION WITH PPP6C AND ANKRD28.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPP6R3_HUMAN
    AccessioniPrimary (citable) accession number: Q5H9R7
    Secondary accession number(s): Q3B7I1
    , Q3I4Y0, Q3KR35, Q68CR3, Q7L4R8, Q8N3B2, Q96MB2, Q9H2K5, Q9H2K6, Q9HCL4, Q9NUY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 95 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 11
      Human chromosome 11: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3