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Q6TDP4

- KLH17_HUMAN

UniProt

Q6TDP4 - KLH17_HUMAN

Protein

Kelch-like protein 17

Gene

KLHL17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(KLHL17) mediates the ubiquitination and subsequenct degradation of GLUR6. May play a role in the actin-based neuronal function By similarity.By similarity

    Pathwayi

    GO - Molecular functioni

    1. protein complex scaffold Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. brain development Source: Ensembl
    3. protein ubiquitination Source: UniProtKB-UniPathway

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kelch-like protein 17
    Alternative name(s):
    Actinfilin
    Gene namesi
    Name:KLHL17
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24023. KLHL17.

    Subcellular locationi

    Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell junctionsynapse By similarity
    Note: Postsynaptic density.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. dendrite cytoplasm Source: Ensembl
    4. extracellular space Source: UniProt
    5. neuronal cell body Source: Ensembl
    6. postsynaptic density Source: UniProtKB-SubCell
    7. postsynaptic membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134887396.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 642642Kelch-like protein 17PRO_0000119119Add
    BLAST

    Proteomic databases

    MaxQBiQ6TDP4.
    PaxDbiQ6TDP4.
    PRIDEiQ6TDP4.

    PTM databases

    PhosphoSiteiQ6TDP4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6TDP4.
    BgeeiQ6TDP4.
    CleanExiHS_KLHL17.
    GenevestigatoriQ6TDP4.

    Organism-specific databases

    HPAiHPA031251.

    Interactioni

    Subunit structurei

    Interacts with F-actin; the interaction disruptes the F-actin structures and leads to marked changes of neuronal morphology. Component of a complex, composed of PDZK1, SYNGAP1, KLHL17 and NMDA receptors. Interacts directly with PDZK1 (via PDZ1 domain); the interaction is important for integrity of actin cytoskeleton structures in neurons. Interacts with DLG4 and SYNGAP1. Interacts (via kelch repeats) with GRIK2 (via C-terminus); the interaction targets GRIK2 for degradation via ubiquitin-proteasome pathway. Interacts with GRIK1. Interacts with (via BTB domain) CUL3; the interaction regulates surface GRIK2 expression By similarity.By similarity

    Protein-protein interaction databases

    BioGridi130885. 1 interaction.
    STRINGi9606.ENSP00000343930.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6TDP4.
    SMRiQ6TDP4. Positions 74-320, 343-622.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini92 – 15968BTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini194 – 296103BACKAdd
    BLAST
    Repeati343 – 38947Kelch 1Add
    BLAST
    Repeati390 – 43647Kelch 2Add
    BLAST
    Repeati438 – 48346Kelch 3Add
    BLAST
    Repeati484 – 53047Kelch 4Add
    BLAST
    Repeati532 – 57746Kelch 5Add
    BLAST
    Repeati578 – 62447Kelch 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni289 – 641353Interaction with F-actinBy similarityAdd
    BLAST
    Regioni640 – 6423Interaction with PDZK1By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi15 – 5238Pro-richAdd
    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.
    InParanoidiQ6TDP4.
    KOiK10454.
    OMAiMQLLNRD.
    OrthoDBiEOG7ZWD17.
    PhylomeDBiQ6TDP4.
    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.
    IPR011043. Gal_Oxase/kelch_b-propeller.
    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. 5 hits.
    [Graphical view]
    PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTiSM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 6 hits.
    [Graphical view]
    SUPFAMiSSF50965. SSF50965. 1 hit.
    SSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6TDP4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPRSERPAG RTQSPEHGSP GPGPEAPPPP PPQPPAPEAE RTRPRQARPA    50
    APMEGAVQLL SREGHSVAHN SKRHYHDAFV AMSRMRQRGL LCDIVLHVAA 100
    KEIRAHKVVL ASCSPYFHAM FTNEMSESRQ THVTLHDIDP QALDQLVQFA 150
    YTAEIVVGEG NVQTLLPAAS LLQLNGVRDA CCKFLLSQLD PSNCLGIRGF 200
    ADAHSCSDLL KAAHRYVLQH FVDVAKTEEF MLLPLKQVLE LVSSDSLNVP 250
    SEEEVYRAVL SWVKHDVDAR RQHVPRLMKC VRLPLLSRDF LLGHVDAESL 300
    VRHHPDCKDL LIEALKFHLL PEQRGVLGTS RTRPRRCEGA GPVLFAVGGG 350
    SLFAIHGDCE AYDTRTDRWH VVASMSTRRA RVGVAAVGNR LYAVGGYDGT 400
    SDLATVESYD PVTNTWQPEV SMGTRRSCLG VAALHGLLYS AGGYDGASCL 450
    NSAERYDPLT GTWTSVAAMS TRRRYVRVAT LDGNLYAVGG YDSSSHLATV 500
    EKYEPQVNVW SPVASMLSRR SSAGVAVLEG ALYVAGGNDG TSCLNSVERY 550
    SPKAGAWESV APMNIRRSTH DLVAMDGWLY AVGGNDGSSS LNSIEKYNPR 600
    TNKWVAASCM FTRRSSVGVA VLELLNFPPP SSPTLSVSST SL 642
    Length:642
    Mass (Da):69,874
    Last modified:July 5, 2004 - v1
    Checksum:iFE37BBCCD32131BF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY423763 mRNA. Translation: AAR03710.1.
    AL645608 Genomic DNA. Translation: CAI15569.1.
    CCDSiCCDS30550.1.
    RefSeqiNP_938073.1. NM_198317.2.
    UniGeneiHs.109212.

    Genome annotation databases

    EnsembliENST00000338591; ENSP00000343930; ENSG00000187961.
    GeneIDi339451.
    KEGGihsa:339451.
    UCSCiuc001aca.2. human.

    Polymorphism databases

    DMDMi52783052.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY423763 mRNA. Translation: AAR03710.1 .
    AL645608 Genomic DNA. Translation: CAI15569.1 .
    CCDSi CCDS30550.1.
    RefSeqi NP_938073.1. NM_198317.2.
    UniGenei Hs.109212.

    3D structure databases

    ProteinModelPortali Q6TDP4.
    SMRi Q6TDP4. Positions 74-320, 343-622.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 130885. 1 interaction.
    STRINGi 9606.ENSP00000343930.

    PTM databases

    PhosphoSitei Q6TDP4.

    Polymorphism databases

    DMDMi 52783052.

    Proteomic databases

    MaxQBi Q6TDP4.
    PaxDbi Q6TDP4.
    PRIDEi Q6TDP4.

    Protocols and materials databases

    DNASUi 339451.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338591 ; ENSP00000343930 ; ENSG00000187961 .
    GeneIDi 339451.
    KEGGi hsa:339451.
    UCSCi uc001aca.2. human.

    Organism-specific databases

    CTDi 339451.
    GeneCardsi GC01P000885.
    HGNCi HGNC:24023. KLHL17.
    HPAi HPA031251.
    neXtProti NX_Q6TDP4.
    PharmGKBi PA134887396.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236397.
    HOGENOMi HOG000230814.
    HOVERGENi HBG014286.
    InParanoidi Q6TDP4.
    KOi K10454.
    OMAi MQLLNRD.
    OrthoDBi EOG7ZWD17.
    PhylomeDBi Q6TDP4.
    TreeFami TF329218.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi KLHL17. human.
    GenomeRNAii 339451.
    NextBioi 97399.
    PROi Q6TDP4.

    Gene expression databases

    ArrayExpressi Q6TDP4.
    Bgeei Q6TDP4.
    CleanExi HS_KLHL17.
    Genevestigatori Q6TDP4.

    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.
    IPR011043. Gal_Oxase/kelch_b-propeller.
    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. 5 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 SSF50965. SSF50965. 1 hit.
    SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Huang C.Q., Wu S.L., Shan Y.X.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].

    Entry informationi

    Entry nameiKLH17_HUMAN
    AccessioniPrimary (citable) accession number: Q6TDP4
    Secondary accession number(s): Q5SV94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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