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Q8IX03

- KIBRA_HUMAN

UniProt

Q8IX03 - KIBRA_HUMAN

Protein

Protein KIBRA

Gene

WWC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ. Plays a role in cognition and memory performance.7 Publications

    GO - Molecular functioni

    1. kinase binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. protein complex scaffold Source: BHF-UCL
    4. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. cell migration Source: UniProtKB
    2. establishment of cell polarity Source: BHF-UCL
    3. hippo signaling Source: Reactome
    4. negative regulation of hippo signaling Source: BHF-UCL
    5. negative regulation of organ growth Source: BHF-UCL
    6. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    7. positive regulation of MAPK cascade Source: UniProtKB
    8. regulation of hippo signaling Source: UniProtKB
    9. regulation of intracellular transport Source: BHF-UCL
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_118607. Signaling by Hippo.
    SignaLinkiQ8IX03.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein KIBRA
    Alternative name(s):
    HBeAg-binding protein 3
    Kidney and brain protein
    Short name:
    KIBRA
    WW domain-containing protein 1
    Gene namesi
    Name:WWC1
    Synonyms:KIAA0869
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:29435. WWC1.

    Subcellular locationi

    Cytoplasm. Cytoplasmperinuclear region. Nucleus. Cell projectionruffle membrane
    Note: Colocalizes with PRKCZ in the perinuclear region.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: BHF-UCL
    3. nucleus Source: UniProtKB
    4. perinuclear region of cytoplasm Source: UniProtKB
    5. protein complex Source: Ensembl
    6. ruffle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    MIMi615602. phenotype.
    PharmGKBiPA143485670.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11131113Protein KIBRAPRO_0000242153Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei542 – 5421Phosphoserine; by CDK11 Publication
    Modified residuei899 – 8991PhosphoserineBy similarity
    Modified residuei912 – 9121Phosphothreonine1 Publication
    Modified residuei929 – 9291Phosphothreonine1 Publication
    Modified residuei931 – 9311Phosphoserine; by CDK12 Publications
    Modified residuei947 – 9471Phosphoserine1 Publication
    Modified residuei975 – 9751Phosphoserine; by PKC/PRKCZ1 Publication
    Modified residuei978 – 9781Phosphoserine; by PKC/PRKCZ1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-542 and Ser-931 by CDK1 in response to spindle damage stress regulates mitotic exit, these two sites are dephosphorylated by CDC14B.6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IX03.
    PaxDbiQ8IX03.
    PRIDEiQ8IX03.

    PTM databases

    PhosphoSiteiQ8IX03.

    Expressioni

    Tissue specificityi

    Expressed in mammary epithelial cells and breast cancer cell lines. Found in the luminal epithelium surrounding the ducts in the normal breast. In the brain, expressed in somatodendritic compartment of neurons in the cortex and hippocampus and in the cerebellum it is found in the Purkinje cells and some granule cells (at protein level). Detected in brain, heart, colon and kidney. In the kidney, expressed in glomerular podocytes, in some tubules and in the collecting duct.4 Publications

    Inductioni

    Strongly up-regulated by progestin treatment.1 Publication

    Gene expression databases

    ArrayExpressiQ8IX03.
    BgeeiQ8IX03.
    CleanExiHS_WWC1.
    GenevestigatoriQ8IX03.

    Organism-specific databases

    HPAiHPA038016.
    HPA038017.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with DDN. Interacts with DYNLL1 and histone H3. The interaction with DYNLL1 is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin and the interaction with histone H3 ensures proper regulatory interaction of WWC1-DYNLL1-ESR1 complexes with target chromatin. Interacts (via WW domains) with DDR1 (via PPxY motif) in a collagen-regulated manner. Interacts with PRKCZ (via the protein kinase domain). Forms a tripartite complex with DDR1 and PRKCZ, but predominantly in the absence of collagen. Interacts (via the ADDV motif) with INADL (via PDZ domain 8). Interacts (via WW domains) with SYNPO (via PPxY motifs). Interacts with NF2 and SNX4.8 Publications

    Protein-protein interaction databases

    BioGridi116884. 15 interactions.
    DIPiDIP-35287N.
    IntActiQ8IX03. 23 interactions.
    MINTiMINT-1405937.
    STRINGi9606.ENSP00000265293.

    Structurei

    Secondary structure

    1
    1113
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi660 – 66910
    Turni670 – 6734
    Beta strandi674 – 68310
    Helixi685 – 6873
    Beta strandi694 – 70411
    Helixi708 – 7114
    Beta strandi712 – 7143
    Beta strandi722 – 73312
    Helixi736 – 7416
    Beta strandi743 – 7519
    Beta strandi757 – 76610
    Beta strandi777 – 7848

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z0UX-ray2.20A/B638-785[»]
    ProteinModelPortaliQ8IX03.
    SMRiQ8IX03. Positions 7-86, 658-785.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IX03.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 3934WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini53 – 8634WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini655 – 783129C2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni839 – 1113275Interaction with histone H3Add
    BLAST
    Regioni953 – 99644Interaction with PRKCZAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili107 – 19387Sequence AnalysisAdd
    BLAST
    Coiled coili293 – 431139Sequence AnalysisAdd
    BLAST
    Coiled coili1001 – 103232Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1111 – 11133ADDV motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi261 – 2655Poly-Ser
    Compositional biasi819 – 87355Glu-richAdd
    BLAST

    Domaini

    The C2-domain mediates homodimerization. It is a calcium-sensitive lipid-binding domain with preference for PI3P.1 Publication

    Sequence similaritiesi

    Belongs to the WWC family. KIBRA subfamily.Curated
    Contains 1 C2 domain.Curated
    Contains 2 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5021.
    HOGENOMiHOG000013211.
    HOVERGENiHBG058082.
    KOiK16685.
    OMAiDPQVGDY.
    OrthoDBiEOG7DJSNR.
    PhylomeDBiQ8IX03.
    TreeFamiTF324040.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00397. WW. 2 hits.
    [Graphical view]
    SMARTiSM00456. WW. 2 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 2 hits.
    PROSITEiPS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IX03-1) [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

    MPRPELPLPE GWEEARDFDG KVYYIDHTNR TTSWIDPRDR YTKPLTFADC     50
    ISDELPLGWE EAYDPQVGDY FIDHNTKTTQ IEDPRVQWRR EQEHMLKDYL 100
    VVAQEALSAQ KEIYQVKQQR LELAQQEYQQ LHAVWEHKLG SQVSLVSGSS 150
    SSSKYDPEIL KAEIATAKSR VNKLKREMVH LQHELQFKER GFQTLKKIDK 200
    KMSDAQGSYK LDEAQAVLRE TKAIKKAITC GEKEKQDLIK SLAMLKDGFR 250
    TDRGSHSDLW SSSSSLESSS FPLPKQYLDV SSQTDISGSF GINSNNQLAE 300
    KVRLRLRYEE AKRRIANLKI QLAKLDSEAW PGVLDSERDR LILINEKEEL 350
    LKEMRFISPR KWTQGEVEQL EMARKRLEKD LQAARDTQSK ALTERLKLNS 400
    KRNQLVRELE EATRQVATLH SQLKSLSSSM QSLSSGSSPG SLTSSRGSLV 450
    ASSLDSSTSA SFTDLYYDPF EQLDSELQSK VEFLLLEGAT GFRPSGCITT 500
    IHEDEVAKTQ KAEGGGRLQA LRSLSGTPKS MTSLSPRSSL SSPSPPCSPL 550
    MADPLLAGDA FLNSLEFEDP ELSATLCELS LGNSAQERYR LEEPGTEGKQ 600
    LGQAVNTAQG CGLKVACVSA AVSDESVAGD SGVYEASVQR LGASEAAAFD 650
    SDESEAVGAT RIQIALKYDE KNKQFAILII QLSNLSALLQ QQDQKVNIRV 700
    AVLPCSESTT CLFRTRPLDA SDTLVFNEVF WVSMSYPALH QKTLRVDVCT 750
    TDRSHLEECL GGAQISLAEV CRSGERSTRW YNLLSYKYLK KQSRELKPVG 800
    VMAPASGPAS TDAVSALLEQ TAVELEKRQE GRSSTQTLED SWRYEETSEN 850
    EAVAEEEEEE VEEEEGEEDV FTEKASPDMD GYPALKVDKE TNTETPAPSP 900
    TVVRPKDRRV GTPSQGPFLR GSTIIRSKTF SPGPQSQYVC RLNRSDSDSS 950
    TLSKKPPFVR NSLERRSVRM KRPSSVKSLR SERLIRTSLD LELDLQATRT 1000
    WHSQLTQEIS VLKELKEQLE QAKSHGEKEL PQWLREDERF RLLLRMLEKR 1050
    QMDRAEHKGE LQTDKMMRAA AKDVHRLRGQ SCKEPPEVQS FREKMAFFTR 1100
    PRMNIPALSA DDV 1113
    Length:1,113
    Mass (Da):125,301
    Last modified:March 1, 2003 - v1
    Checksum:i9010B9C127129165
    GO
    Isoform 2 (identifier: Q8IX03-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         974-974: S → SPPPQPS

    Show »
    Length:1,119
    Mass (Da):125,905
    Checksum:i0AB48E74AB261693
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti561 – 5611F → L in CAE45903. (PubMed:17974005)Curated
    Sequence conflicti759 – 7591C → R in CAE45903. (PubMed:17974005)Curated
    Sequence conflicti811 – 8111T → TVSWDQ in AAO73817. 1 PublicationCurated
    Sequence conflicti834 – 8341S → N in CAE45903. (PubMed:17974005)Curated
    Sequence conflicti865 – 8651Missing in AAO73817. 1 PublicationCurated
    Sequence conflicti1051 – 10511Missing in CAE45903. (PubMed:17974005)Curated
    Sequence conflicti1051 – 10511Missing in BAA74892. (PubMed:10048485)Curated
    Sequence conflicti1064 – 10652DK → AR in AAO73817. 1 PublicationCurated

    Polymorphismi

    Genetic variations in WWC1 define the memory quantitative trait locus (MEMRYQTL) [MIMi:615602].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti250 – 2501R → C.
    Corresponds to variant rs17551608 [ dbSNP | Ensembl ].
    VAR_026844
    Natural varianti734 – 7341M → I Polymorphism; associated with Ala-735; affects KIBRA lipid-binding specificity showing stronger interactions with PI(4)P and PI(5)P. 1 Publication
    Corresponds to variant rs3822660 [ dbSNP | Ensembl ].
    VAR_053449
    Natural varianti735 – 7351S → A Polymorphism; associated with Ile-734; affects KIBRA lipid-binding specificity showing stronger interactions with PI(4)P and PI(5)P. 1 Publication
    Corresponds to variant rs3822659 [ dbSNP | Ensembl ].
    VAR_053450

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei974 – 9741S → SPPPQPS in isoform 2. 3 PublicationsVSP_019448

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF506799 mRNA. Translation: AAO15881.1.
    AK296323 mRNA. Translation: BAG59017.1.
    AC020894 Genomic DNA. No translation available.
    AC026689 Genomic DNA. No translation available.
    BX640827 mRNA. Translation: CAE45903.1.
    AB020676 mRNA. Translation: BAA74892.1.
    AF530058 mRNA. Translation: AAQ09942.1.
    AY189820 mRNA. Translation: AAO73817.1.
    BC004394 mRNA. Translation: AAH04394.1.
    BC017746 mRNA. Translation: AAH17746.1.
    CCDSiCCDS4366.1. [Q8IX03-1]
    CCDS54945.1. [Q8IX03-2]
    RefSeqiNP_001155133.1. NM_001161661.1. [Q8IX03-2]
    NP_001155134.1. NM_001161662.1.
    NP_056053.1. NM_015238.2. [Q8IX03-1]
    UniGeneiHs.484047.

    Genome annotation databases

    EnsembliENST00000265293; ENSP00000265293; ENSG00000113645. [Q8IX03-1]
    ENST00000521089; ENSP00000427772; ENSG00000113645. [Q8IX03-2]
    GeneIDi23286.
    KEGGihsa:23286.
    UCSCiuc003lzu.3. human. [Q8IX03-1]
    uc011den.2. human. [Q8IX03-2]

    Polymorphism databases

    DMDMi74714457.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF506799 mRNA. Translation: AAO15881.1 .
    AK296323 mRNA. Translation: BAG59017.1 .
    AC020894 Genomic DNA. No translation available.
    AC026689 Genomic DNA. No translation available.
    BX640827 mRNA. Translation: CAE45903.1 .
    AB020676 mRNA. Translation: BAA74892.1 .
    AF530058 mRNA. Translation: AAQ09942.1 .
    AY189820 mRNA. Translation: AAO73817.1 .
    BC004394 mRNA. Translation: AAH04394.1 .
    BC017746 mRNA. Translation: AAH17746.1 .
    CCDSi CCDS4366.1. [Q8IX03-1 ]
    CCDS54945.1. [Q8IX03-2 ]
    RefSeqi NP_001155133.1. NM_001161661.1. [Q8IX03-2 ]
    NP_001155134.1. NM_001161662.1.
    NP_056053.1. NM_015238.2. [Q8IX03-1 ]
    UniGenei Hs.484047.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Z0U X-ray 2.20 A/B 638-785 [» ]
    ProteinModelPortali Q8IX03.
    SMRi Q8IX03. Positions 7-86, 658-785.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116884. 15 interactions.
    DIPi DIP-35287N.
    IntActi Q8IX03. 23 interactions.
    MINTi MINT-1405937.
    STRINGi 9606.ENSP00000265293.

    PTM databases

    PhosphoSitei Q8IX03.

    Polymorphism databases

    DMDMi 74714457.

    Proteomic databases

    MaxQBi Q8IX03.
    PaxDbi Q8IX03.
    PRIDEi Q8IX03.

    Protocols and materials databases

    DNASUi 23286.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265293 ; ENSP00000265293 ; ENSG00000113645 . [Q8IX03-1 ]
    ENST00000521089 ; ENSP00000427772 ; ENSG00000113645 . [Q8IX03-2 ]
    GeneIDi 23286.
    KEGGi hsa:23286.
    UCSCi uc003lzu.3. human. [Q8IX03-1 ]
    uc011den.2. human. [Q8IX03-2 ]

    Organism-specific databases

    CTDi 23286.
    GeneCardsi GC05P167652.
    HGNCi HGNC:29435. WWC1.
    HPAi HPA038016.
    HPA038017.
    MIMi 610533. gene.
    615602. phenotype.
    neXtProti NX_Q8IX03.
    PharmGKBi PA143485670.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5021.
    HOGENOMi HOG000013211.
    HOVERGENi HBG058082.
    KOi K16685.
    OMAi DPQVGDY.
    OrthoDBi EOG7DJSNR.
    PhylomeDBi Q8IX03.
    TreeFami TF324040.

    Enzyme and pathway databases

    Reactomei REACT_118607. Signaling by Hippo.
    SignaLinki Q8IX03.

    Miscellaneous databases

    EvolutionaryTracei Q8IX03.
    GeneWikii WWC1.
    GenomeRNAii 23286.
    NextBioi 45094.
    PROi Q8IX03.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IX03.
    Bgeei Q8IX03.
    CleanExi HS_WWC1.
    Genevestigatori Q8IX03.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00397. WW. 2 hits.
    [Graphical view ]
    SMARTi SM00456. WW. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 2 hits.
    PROSITEi PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "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] (ISOFORM 2).
      Tissue: Thalamus.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-1113 (ISOFORM 2).
      Tissue: Fetal brain.
    5. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-1113 (ISOFORM 2).
      Tissue: Brain.
    6. "Screening and cloning of interaction protein 3 of HBeAg."
      Lu Y., Liu Y., Cheng J.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 202-1113 (ISOFORM 1).
      Tissue: Liver.
    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] OF 782-1113 (ISOFORM 1).
      Tissue: Liver and Placenta.
    8. Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PRKCZ, PHOSPHORYLATION AT SER-975 AND SER-978.
    9. "Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells."
      Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C., Peng S., Barnekow A., Kremerskothen J., Kumar R.
      J. Biol. Chem. 281:19092-19099(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH DYNLL1 AND HISTONE H3.
    10. Cited for: POLYMORPHISM, INVOLVEMENT IN MEMRYQTL.
    11. "SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment."
      Traer C.J., Rutherford A.C., Palmer K.J., Wassmer T., Oakley J., Attar N., Carlton J.G., Kremerskothen J., Stephens D.J., Cullen P.J.
      Nat. Cell Biol. 9:1370-1380(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNX4.
    12. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SYNPO AND INADL, TISSUE SPECIFICITY.
    13. "KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling."
      Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W., Daly R.J., Ormandy C.J.
      Biochim. Biophys. Acta 1783:383-393(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INDUCTION, INTERACTION WITH DDR1 AND PRKCZ, TISSUE SPECIFICITY.
    14. "Temporal-spatial expression and novel biochemical properties of the memory-related protein KIBRA."
      Johannsen S., Duning K., Pavenstaedt H., Kremerskothen J., Boeckers T.M.
      Neuroscience 155:1165-1173(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DOMAIN C2.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-912; THR-929 AND SER-931, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Kibra functions as a tumor suppressor protein that regulates Hippo signaling in conjunction with Merlin and Expanded."
      Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D.
      Dev. Cell 18:288-299(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Kibra Is a regulator of the Salvador/Warts/Hippo signaling network."
      Genevet A., Wehr M.C., Brain R., Thompson B.J., Tapon N.
      Dev. Cell 18:300-308(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NF2.
    18. "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-947, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: POLYMORPHISM, INVOLVEMENT IN MEMRYQTL.
    20. "Phospho-regulation of KIBRA by CDK1 and CDC14 phosphatase controls cell-cycle progression."
      Ji M., Yang S., Chen Y., Xiao L., Zhang L., Dong J.
      Biochem. J. 447:93-102(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-542 AND SER-931 BY CDK1, DEPHOSPHORYLATION BY CDC14B.
    21. Cited for: FUNCTION OF C2 DOMAIN, VARIANTS ILE-734 AND ALA-735, CHARACTERIZATION OF VARIANTS ILE-734 AND ALA-735.
    22. "Crystal structure of C2 domain of KIBRA protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 638-785.

    Entry informationi

    Entry nameiKIBRA_HUMAN
    AccessioniPrimary (citable) accession number: Q8IX03
    Secondary accession number(s): B4DK05
    , O94946, Q6MZX4, Q6Y2F8, Q7Z4G8, Q8WVM4, Q9BT29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 94 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3