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Q9Y2M5

- KLH20_HUMAN

UniProt

Q9Y2M5 - KLH20_HUMAN

Protein

Kelch-like protein 20

Gene

KLHL20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 4 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis (PubMed:20389280). The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination (PubMed:24768539). Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking (PubMed:24768539). Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (PubMed:21670212). In case of tumor, the BCR(KLHL20) E3 ubiquitin ligase complex is involved in tumor hypoxia: following hypoxia, the BCR(KLHL20)complex mediates ubiquitination and degradation of PML, potentiating HIF-1 signaling and cancer progression (PubMed:21840486).6 Publications

    Pathwayi

    GO - Molecular functioni

    1. interferon-gamma binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. cytoskeleton organization Source: ProtInc
    2. Golgi to endosome transport Source: UniProtKB
    3. negative regulation of apoptotic process Source: UniProtKB
    4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    5. protein K33-linked ubiquitination Source: UniProtKB
    6. protein transport Source: UniProtKB-KW
    7. protein ubiquitination Source: UniProtKB
    8. response to interferon-alpha Source: UniProtKB

    Keywords - Biological processi

    Protein transport, Transport, Ubl conjugation pathway

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kelch-like protein 20
    Alternative name(s):
    Kelch-like ECT2-interacting protein
    Kelch-like protein X
    Gene namesi
    Name:KLHL20
    Synonyms:KLEIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25056. KLHL20.

    Subcellular locationi

    Cytoplasmperinuclear region. Nucleus. Golgi apparatustrans-Golgi network. Cell projectionaxon By similarity. Cell projectiondendrite By similarity
    Note: Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN-gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (PubMed:20389280).1 Publication

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. axon Source: UniProtKB-SubCell
    3. Cul3-RING ubiquitin ligase complex Source: UniProtKB
    4. cytoplasm Source: UniProtKB
    5. dendrite Source: UniProtKB-SubCell
    6. Golgi apparatus Source: HPA
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    8. PML body Source: UniProtKB
    9. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Golgi apparatus, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi109 – 1091V → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-111; A-113; A-146; A-148 and A-150. 4 Publications
    Mutagenesisi111 – 1111I → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-113; A-146; A-148 and A-150. 4 Publications
    Mutagenesisi113 – 1131D → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-146; A-148 and A-150. 4 Publications
    Mutagenesisi146 – 1461C → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-148 and A-150. 4 Publications
    Mutagenesisi148 – 1481L → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-146 and A-150. 4 Publications
    Mutagenesisi150 – 1501L → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-146 and A-148. 4 Publications

    Organism-specific databases

    PharmGKBiPA134982126.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 609609Kelch-like protein 20PRO_0000119123Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y2M5.
    PaxDbiQ9Y2M5.
    PRIDEiQ9Y2M5.

    PTM databases

    PhosphoSiteiQ9Y2M5.

    Expressioni

    Inductioni

    By hypoxia.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y2M5.
    BgeeiQ9Y2M5.
    CleanExiHS_KLHL20.
    GenevestigatoriQ9Y2M5.

    Organism-specific databases

    HPAiHPA025034.

    Interactioni

    Subunit structurei

    Component of the BCR(KLHL20) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL20 and RBX1. Interacts with PDZ-RhoGEF/ARHGEF11, DAPK1, PML and CORO7. Interacts with F-actin. Interacts with IFN-gamma (IFNG).6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CUL3Q136182EBI-714379,EBI-456129
    DAPK1P5335511EBI-714379,EBI-358616
    PMLP295909EBI-714379,EBI-295890
    PRMT6Q96LA82EBI-714379,EBI-912440

    Protein-protein interaction databases

    BioGridi118100. 19 interactions.
    IntActiQ9Y2M5. 16 interactions.
    MINTiMINT-6783961.
    STRINGi9606.ENSP00000209884.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2M5.
    SMRiQ9Y2M5. Positions 50-599.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini68 – 13568BTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini170 – 272103BACKAdd
    BLAST
    Repeati319 – 36547Kelch 1Add
    BLAST
    Repeati367 – 41347Kelch 2Add
    BLAST
    Repeati414 – 46047Kelch 3Add
    BLAST
    Repeati462 – 50746Kelch 4Add
    BLAST
    Repeati509 – 55446Kelch 5Add
    BLAST
    Repeati556 – 60146Kelch 6Add
    BLAST

    Sequence similaritiesi

    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 6 Kelch repeats.Curated

    Keywords - Domaini

    Kelch repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG236397.
    HOGENOMiHOG000230814.
    HOVERGENiHBG014286.
    InParanoidiQ9Y2M5.
    KOiK10457.
    OMAiPMSKRRC.
    OrthoDBiEOG7ZWD17.
    PhylomeDBiQ9Y2M5.
    TreeFamiTF329218.

    Family and domain databases

    Gene3Di2.130.10.80. 1 hit.
    3.30.710.10. 1 hit.
    InterProiIPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view]
    PfamiPF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 6 hits.
    [Graphical view]
    PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTiSM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 6 hits.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y2M5-1 [UniParc]FASTAAdd to Basket

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    MEGKPMRRCT NIRPGETGMD VTSRCTLGDP NKLPEGVPQP ARMPYISDKH    50
    PRQTLEVINL LRKHRELCDV VLVVGAKKIY AHRVILSACS PYFRAMFTGE 100
    LAESRQTEVV IRDIDERAME LLIDFAYTSQ ITVEEGNVQT LLPAACLLQL 150
    AEIQEACCEF LKRQLDPSNC LGIRAFADTH SCRELLRIAD KFTQHNFQEV 200
    MESEEFMLLP ANQLIDIISS DELNVRSEEQ VFNAVMAWVK YSIQERRPQL 250
    PQVLQHVRLP LLSPKFLVGT VGSDPLIKSD EECRDLVDEA KNYLLLPQER 300
    PLMQGPRTRP RKPIRCGEVL FAVGGWCSGD AISSVERYDP QTNEWRMVAS 350
    MSKRRCGVGV SVLDDLLYAV GGHDGSSYLN SVERYDPKTN QWSSDVAPTS 400
    TCRTSVGVAV LGGFLYAVGG QDGVSCLNIV ERYDPKENKW TRVASMSTRR 450
    LGVAVAVLGG FLYAVGGSDG TSPLNTVERY NPQENRWHTI APMGTRRKHL 500
    GCAVYQDMIY AVGGRDDTTE LSSAERYNPR TNQWSPVVAM TSRRSGVGLA 550
    VVNGQLMAVG GFDGTTYLKT IEVFDPDANT WRLYGGMNYR RLGGGVGVIK 600
    MTHCESHIW 609
    Length:609
    Mass (Da):67,955
    Last modified:September 1, 2009 - v4
    Checksum:iFA05E3FE8341B422
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711L → Q in BAG50912. (PubMed:14702039)Curated
    Sequence conflicti321 – 3211F → S in BAG50912. (PubMed:14702039)Curated
    Sequence conflicti334 – 3341S → N in BAG50912. (PubMed:14702039)Curated
    Sequence conflicti396 – 3961V → M in BAG50912. (PubMed:14702039)Curated
    Sequence conflicti593 – 5931G → W in BAA77027. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ844466 mRNA. Translation: CAH59617.1.
    AB026190 mRNA. Translation: BAA77027.1.
    AK001430 mRNA. Translation: BAG50912.1.
    AL109921, BX248409 Genomic DNA. Translation: CAI20377.1.
    BX248409, AL109921 Genomic DNA. Translation: CAH73000.1.
    BC063418 mRNA. Translation: AAH63418.1.
    CCDSiCCDS1310.1.
    RefSeqiNP_055273.2. NM_014458.3.
    XP_005245150.1. XM_005245093.1.
    UniGeneiHs.495035.

    Genome annotation databases

    EnsembliENST00000209884; ENSP00000209884; ENSG00000076321.
    GeneIDi27252.
    KEGGihsa:27252.
    UCSCiuc001gjc.3. human.

    Polymorphism databases

    DMDMi257051084.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ844466 mRNA. Translation: CAH59617.1 .
    AB026190 mRNA. Translation: BAA77027.1 .
    AK001430 mRNA. Translation: BAG50912.1 .
    AL109921 , BX248409 Genomic DNA. Translation: CAI20377.1 .
    BX248409 , AL109921 Genomic DNA. Translation: CAH73000.1 .
    BC063418 mRNA. Translation: AAH63418.1 .
    CCDSi CCDS1310.1.
    RefSeqi NP_055273.2. NM_014458.3.
    XP_005245150.1. XM_005245093.1.
    UniGenei Hs.495035.

    3D structure databases

    ProteinModelPortali Q9Y2M5.
    SMRi Q9Y2M5. Positions 50-599.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118100. 19 interactions.
    IntActi Q9Y2M5. 16 interactions.
    MINTi MINT-6783961.
    STRINGi 9606.ENSP00000209884.

    PTM databases

    PhosphoSitei Q9Y2M5.

    Polymorphism databases

    DMDMi 257051084.

    Proteomic databases

    MaxQBi Q9Y2M5.
    PaxDbi Q9Y2M5.
    PRIDEi Q9Y2M5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000209884 ; ENSP00000209884 ; ENSG00000076321 .
    GeneIDi 27252.
    KEGGi hsa:27252.
    UCSCi uc001gjc.3. human.

    Organism-specific databases

    CTDi 27252.
    GeneCardsi GC01P173684.
    HGNCi HGNC:25056. KLHL20.
    HPAi HPA025034.
    neXtProti NX_Q9Y2M5.
    PharmGKBi PA134982126.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236397.
    HOGENOMi HOG000230814.
    HOVERGENi HBG014286.
    InParanoidi Q9Y2M5.
    KOi K10457.
    OMAi PMSKRRC.
    OrthoDBi EOG7ZWD17.
    PhylomeDBi Q9Y2M5.
    TreeFami TF329218.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    GeneWikii KLHL20.
    GenomeRNAii 27252.
    NextBioi 50186.
    PROi Q9Y2M5.

    Gene expression databases

    ArrayExpressi Q9Y2M5.
    Bgeei Q9Y2M5.
    CleanExi HS_KLHL20.
    Genevestigatori Q9Y2M5.

    Family and domain databases

    Gene3Di 2.130.10.80. 1 hit.
    3.30.710.10. 1 hit.
    InterProi IPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view ]
    Pfami PF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 6 hits.
    [Graphical view ]
    PIRSFi PIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTi SM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 6 hits.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Novel kelch-like protein, KLEIP, is involved in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells."
      Hara T., Ishida H., Raziuddin R., Dorkhom S., Kamijo K., Miki T.
      Mol. Biol. Cell 15:1172-1184(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ACTIN.
    2. "Kelch motif containing protein."
      Yoshida K., Sugano S.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      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].
      Tissue: Teratocarcinoma.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
    6. "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases."
      Furukawa M., He Y.J., Borchers C., Xiong Y.
      Nat. Cell Biol. 5:1001-1007(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, INTERACTION WITH CUL3.
    7. "The BTB-Kelch protein KLEIP controls endothelial migration and sprouting angiogenesis."
      Nacak T.G., Alajati A., Leptien K., Fulda C., Weber H., Miki T., Czepluch F.S., Waltenberger J., Wieland T., Augustin H.G., Kroll J.
      Circ. Res. 100:1155-1163(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to control interferon responses."
      Lee Y.R., Yuan W.C., Ho H.C., Chen C.H., Shih H.M., Chen R.H.
      EMBO J. 29:1748-1761(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, INTERACTION WITH DAPK AND IFNG, MUTAGENESIS OF VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
    9. "A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to potentiate HIF-1 signaling and prostate cancer progression."
      Yuan W.C., Lee Y.R., Huang S.F., Lin Y.M., Chen T.Y., Chung H.C., Tsai C.H., Chen H.Y., Chiang C.T., Lai C.K., Lu L.T., Chen C.H., Gu D.L., Pu Y.S., Jou Y.S., Lu K.P., Hsiao P.W., Shih H.M., Chen R.H.
      Cancer Cell 20:214-228(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PML, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, INDUCTION, MUTAGENESIS OF VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
    10. "PDZ-RhoGEF ubiquitination by Cullin3-KLHL20 controls neurotrophin-induced neurite outgrowth."
      Lin M.Y., Lin Y.M., Kao T.C., Chuang H.H., Chen R.H.
      J. Cell Biol. 193:985-994(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARHGEF11, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, MUTAGENESIS OF VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
    11. "K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin E3 ligase regulates protein trafficking."
      Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C., Kuo J.C., Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.
      Mol. Cell 54:586-600(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, INTERACTION WITH CORO7, MUTAGENESIS OF VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.

    Entry informationi

    Entry nameiKLH20_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2M5
    Secondary accession number(s): B3KMA0
    , Q5TZF2, Q5ZF45, Q9H457
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 117 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3