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Q99569

- PKP4_HUMAN

UniProt

Q99569 - PKP4_HUMAN

Protein

Plakophilin-4

Gene

PKP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell-cell junction assembly Source: UniProtKB
    2. cell-cell signaling Source: UniProtKB
    3. positive regulation of cytokinesis Source: UniProtKB
    4. positive regulation of gene expression Source: UniProtKB
    5. positive regulation of Rho GTPase activity Source: UniProtKB
    6. regulation of cell adhesion Source: UniProtKB
    7. single organismal cell-cell adhesion Source: InterPro

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    SignaLinkiQ99569.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Plakophilin-4
    Alternative name(s):
    p0071
    Gene namesi
    Name:PKP4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9026. PKP4.

    Subcellular locationi

    Cell junctiondesmosome 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication. Cytoplasmcytoskeletonspindle pole 1 Publication. Midbody 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
    Note: Associated with the pericentrosomal region in interphase and with spindle poles during mitosis. In anaphase, during chromosome segregation, is recruited to the central microtubule bundle, focussed at the spindle midzone and ultimately localizes to the midbody at cytokinesis. Constituent of the midbody cytoskeletal matrix. Colocalized with desmoplakin at desmosomal junctional plaques in cultured epithelial cells.

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic side of plasma membrane Source: UniProtKB
    4. cytoskeleton Source: UniProtKB
    5. desmosome Source: UniProtKB
    6. midbody Source: UniProtKB
    7. mitotic spindle Source: UniProtKB
    8. perinuclear region of cytoplasm Source: UniProtKB
    9. plasma membrane Source: UniProtKB
    10. spindle midzone Source: UniProtKB
    11. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33359.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11921192Plakophilin-4PRO_0000064289Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei221 – 2211Phosphoserine1 Publication
    Modified residuei231 – 2311Phosphoserine1 Publication
    Modified residuei273 – 2731Phosphoserine1 Publication
    Modified residuei281 – 2811Phosphoserine1 Publication
    Modified residuei314 – 3141Phosphoserine7 Publications
    Modified residuei327 – 3271Phosphoserine1 Publication
    Modified residuei372 – 3721PhosphotyrosineBy similarity
    Modified residuei403 – 4031Phosphoserine1 Publication
    Modified residuei406 – 4061Phosphoserine2 Publications
    Modified residuei415 – 4151Phosphotyrosine2 Publications
    Modified residuei478 – 4781PhosphotyrosineBy similarity
    Cross-linki611 – 611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei776 – 7761Phosphoserine1 Publication
    Modified residuei1135 – 11351PhosphoserineBy similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ99569.
    PaxDbiQ99569.
    PRIDEiQ99569.

    PTM databases

    PhosphoSiteiQ99569.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99569.
    BgeeiQ99569.
    CleanExiHS_PKP4.
    GenevestigatoriQ99569.

    Organism-specific databases

    HPAiCAB037334.

    Interactioni

    Subunit structurei

    Interacts with PDZD2 By similarity. Interacts (via the C-terminus) with FRMPD2 (via the PDZ 2 domain). Interacts with RHOA; the interaction is detected at the midbody. Interacts with ECT2; the interaction is detected at the midbody.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2IPQ96RT13EBI-726447,EBI-993903
    ERBB2IPQ96RT1-23EBI-726447,EBI-8449250

    Protein-protein interaction databases

    BioGridi114074. 16 interactions.
    IntActiQ99569. 12 interactions.
    MINTiMINT-88417.
    STRINGi9606.ENSP00000374409.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99569.
    SMRiQ99569. Positions 525-1011.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati415 – 45541ARM 1Add
    BLAST
    Repeati518 – 55740ARM 2Add
    BLAST
    Repeati560 – 59940ARM 3Add
    BLAST
    Repeati604 – 64441ARM 4Add
    BLAST
    Repeati660 – 70243ARM 5Add
    BLAST
    Repeati706 – 75146ARM 6Add
    BLAST
    Repeati815 – 85541ARM 7Add
    BLAST
    Repeati862 – 90140ARM 8Add
    BLAST
    Repeati950 – 99344ARM 9Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili36 – 7035Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi788 – 7947Poly-Lys

    Sequence similaritiesi

    Belongs to the beta-catenin family.Curated
    Contains 9 ARM repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG276924.
    HOGENOMiHOG000231863.
    HOVERGENiHBG004284.
    InParanoidiQ99569.
    OMAiGIGNLQR.
    OrthoDBiEOG7X6KZB.
    PhylomeDBiQ99569.
    TreeFamiTF321877.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR028443. Plakophilin-4.
    IPR028435. Plakophilin/d_Catenin.
    [Graphical view]
    PANTHERiPTHR10372. PTHR10372. 1 hit.
    PTHR10372:SF8. PTHR10372:SF8. 1 hit.
    PfamiPF00514. Arm. 3 hits.
    [Graphical view]
    SMARTiSM00185. ARM. 6 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50176. ARM_REPEAT. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99569-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MPAPEQASLV EEGQPQTRQE AASTGPGMEP ETTATTILAS VKEQELQFQR     50
    LTRELEVERQ IVASQLERCR LGAESPSIAS TSSTEKSFPW RSTDVPNTGV 100
    SKPRVSDAVQ PNNYLIRTEP EQGTLYSPEQ TSLHESEGSL GNSRSSTQMN 150
    SYSDSGYQEA GSFHNSQNVS KADNRQQHSF IGSTNNHVVR NSRAEGQTLV 200
    QPSVANRAMR RVSSVPSRAQ SPSYVISTGV SPSRGSLRTS LGSGFGSPSV 250
    TDPRPLNPSA YSSTTLPAAR AASPYSQRPA SPTAIRRIGS VTSRQTSNPN 300
    GPTPQYQTTA RVGSPLTLTD AQTRVASPSQ GQVGSSSPKR SGMTAVPQHL 350
    GPSLQRTVHD MEQFGQQQYD IYERMVPPRP DSLTGLRSSY ASQHSQLGQD 400
    LRSAVSPDLH ITPIYEGRTY YSPVYRSPNH GTVELQGSQT ALYRTGSVGI 450
    GNLQRTSSQR STLTYQRNNY ALNTTATYAE PYRPIQYRVQ ECNYNRLQHA 500
    VPADDGTTRS PSIDSIQKDP REFAWRDPEL PEVIHMLQHQ FPSVQANAAA 550
    YLQHLCFGDN KVKMEVCRLG GIKHLVDLLD HRVLEVQKNA CGALRNLVFG 600
    KSTDENKIAM KNVGGIPALL RLLRKSIDAE VRELVTGVLW NLSSCDAVKM 650
    TIIRDALSTL TNTVIVPHSG WNNSSFDDDH KIKFQTSLVL RNTTGCLRNL 700
    SSAGEEARKQ MRSCEGLVDS LLYVIHTCVN TSDYDSKTVE NCVCTLRNLS 750
    YRLELEVPQA RLLGLNELDD LLGKESPSKD SEPSCWGKKK KKKKRTPQED 800
    QWDGVGPIPG LSKSPKGVEM LWHPSVVKPY LTLLAESSNP ATLEGSAGSL 850
    QNLSAGNWKF AAYIRAAVRK EKGLPILVEL LRMDNDRVVS SVATALRNMA 900
    LDVRNKELIG KYAMRDLVNR LPGGNGPSVL SDETMAAICC ALHEVTSKNM 950
    ENAKALADSG GIEKLVNITK GRGDRSSLKV VKAAAQVLNT LWQYRDLRSI 1000
    YKKDGWNQNH FITPVSTLER DRFKSHPSLS TTNQQMSPII QSVGSTSSSP 1050
    ALLGIRDPRS EYDRTQPPMQ YYNSQGDATH KGLYPGSSKP SPIYISSYSS 1100
    PAREQNRRLQ HQQLYYSQDD SNRKNFDAYR LYLQSPHSYE DPYFDDRVHF 1150
    PASTDYSTQY GLKSTTNYVD FYSTKRPSYR AEQYPGSPDS WV 1192
    Length:1,192
    Mass (Da):131,868
    Last modified:November 30, 2010 - v2
    Checksum:i48EA1579E323E019
    GO
    Isoform 2 (identifier: Q99569-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1043-1085: Missing.

    Show »
    Length:1,149
    Mass (Da):127,144
    Checksum:i060914C3E7947CB2
    GO

    Sequence cautioni

    The sequence CAA57478.1 differs from that shown. Reason: Frameshift at positions 334, 337, 864 and 874.
    The sequence CAA57478.1 differs from that shown. Reason: Erroneous termination at position 1193. Translated as stop.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411V → M in AAH50308. (PubMed:15489334)Curated
    Sequence conflicti223 – 2231S → Y in AAH50308. (PubMed:15489334)Curated
    Sequence conflicti235 – 2351G → W in AAH50308. (PubMed:15489334)Curated
    Sequence conflicti335 – 3351S → V in CAA57478. (PubMed:8937994)Curated
    Sequence conflicti336 – 3361S → V in CAA57478. (PubMed:8937994)Curated
    Sequence conflicti447 – 4471S → V in CAA57478. (PubMed:8937994)Curated
    Sequence conflicti448 – 4481V → S in CAA57478. (PubMed:8937994)Curated
    Sequence conflicti538 – 5381Q → E in CAA57478. (PubMed:8937994)Curated
    Sequence conflicti701 – 7011S → T in CAA57478. (PubMed:8937994)Curated
    Sequence conflicti766 – 7661N → D in AAH50308. (PubMed:15489334)Curated
    Sequence conflicti856 – 8561G → S in CAA57478. (PubMed:8937994)Curated
    Sequence conflicti865 – 8651R → G in CAA57478. (PubMed:8937994)Curated
    Sequence conflicti892 – 8921V → G in CAA57478. (PubMed:8937994)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1043 – 108543Missing in isoform 2. 2 PublicationsVSP_006737Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81889 mRNA. Translation: CAA57478.1. Sequence problems.
    AC005042 Genomic DNA. No translation available.
    AC008070 Genomic DNA. No translation available.
    BC050308 mRNA. Translation: AAH50308.1.
    CCDSiCCDS33305.1. [Q99569-1]
    CCDS33306.1. [Q99569-2]
    RefSeqiNP_001005476.1. NM_001005476.1. [Q99569-2]
    NP_003619.2. NM_003628.3. [Q99569-1]
    UniGeneiHs.407580.

    Genome annotation databases

    EnsembliENST00000389757; ENSP00000374407; ENSG00000144283. [Q99569-2]
    ENST00000389759; ENSP00000374409; ENSG00000144283. [Q99569-1]
    GeneIDi8502.
    KEGGihsa:8502.
    UCSCiuc002tzt.1. human. [Q99569-1]
    uc002tzw.3. human. [Q99569-2]

    Polymorphism databases

    DMDMi313104155.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81889 mRNA. Translation: CAA57478.1 . Sequence problems.
    AC005042 Genomic DNA. No translation available.
    AC008070 Genomic DNA. No translation available.
    BC050308 mRNA. Translation: AAH50308.1 .
    CCDSi CCDS33305.1. [Q99569-1 ]
    CCDS33306.1. [Q99569-2 ]
    RefSeqi NP_001005476.1. NM_001005476.1. [Q99569-2 ]
    NP_003619.2. NM_003628.3. [Q99569-1 ]
    UniGenei Hs.407580.

    3D structure databases

    ProteinModelPortali Q99569.
    SMRi Q99569. Positions 525-1011.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114074. 16 interactions.
    IntActi Q99569. 12 interactions.
    MINTi MINT-88417.
    STRINGi 9606.ENSP00000374409.

    PTM databases

    PhosphoSitei Q99569.

    Polymorphism databases

    DMDMi 313104155.

    Proteomic databases

    MaxQBi Q99569.
    PaxDbi Q99569.
    PRIDEi Q99569.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389757 ; ENSP00000374407 ; ENSG00000144283 . [Q99569-2 ]
    ENST00000389759 ; ENSP00000374409 ; ENSG00000144283 . [Q99569-1 ]
    GeneIDi 8502.
    KEGGi hsa:8502.
    UCSCi uc002tzt.1. human. [Q99569-1 ]
    uc002tzw.3. human. [Q99569-2 ]

    Organism-specific databases

    CTDi 8502.
    GeneCardsi GC02P159313.
    H-InvDB HIX0002526.
    HGNCi HGNC:9026. PKP4.
    HPAi CAB037334.
    MIMi 604276. gene.
    neXtProti NX_Q99569.
    PharmGKBi PA33359.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276924.
    HOGENOMi HOG000231863.
    HOVERGENi HBG004284.
    InParanoidi Q99569.
    OMAi GIGNLQR.
    OrthoDBi EOG7X6KZB.
    PhylomeDBi Q99569.
    TreeFami TF321877.

    Enzyme and pathway databases

    SignaLinki Q99569.

    Miscellaneous databases

    ChiTaRSi PKP4. human.
    GeneWikii PKP4.
    GenomeRNAii 8502.
    NextBioi 31815.
    PROi Q99569.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99569.
    Bgeei Q99569.
    CleanExi HS_PKP4.
    Genevestigatori Q99569.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR028443. Plakophilin-4.
    IPR028435. Plakophilin/d_Catenin.
    [Graphical view ]
    PANTHERi PTHR10372. PTHR10372. 1 hit.
    PTHR10372:SF8. PTHR10372:SF8. 1 hit.
    Pfami PF00514. Arm. 3 hits.
    [Graphical view ]
    SMARTi SM00185. ARM. 6 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50176. ARM_REPEAT. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a new armadillo family member, p0071, associated with the junctional plaque: evidence for a subfamily of closely related proteins."
      Hatzfeld M., Nachtsheim C.
      J. Cell Sci. 109:2767-2778(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Frontal cortex.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 2).
      Tissue: Brain.
    4. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-406 AND TYR-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    5. "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-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "The armadillo protein p0071 regulates Rho signalling during cytokinesis."
      Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M., Huttelmaier S., Hatzfeld M.
      Nat. Cell Biol. 8:1432-1440(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ECT2 AND RHOA, SUBCELLULAR LOCATION.
    7. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-611.
      Tissue: Mammary cancer.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-403 AND SER-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-281; SER-314 AND SER-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. "PDZ-domain-directed basolateral targeting of the peripheral membrane protein FRMPD2 in epithelial cells."
      Stenzel N., Fetzer C.P., Heumann R., Erdmann K.S.
      J. Cell Sci. 122:3374-3384(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FRMPD2.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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 TYR-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-221; SER-231 AND SER-776, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPKP4_HUMAN
    AccessioniPrimary (citable) accession number: Q99569
    Secondary accession number(s): Q86W91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 131 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 2
      Human chromosome 2: 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