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Q53G59

- KLH12_HUMAN

UniProt

Q53G59 - KLH12_HUMAN

Protein

Kelch-like protein 12

Gene

KLHL12

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 2 (16 May 2006)
      Previous versions | rss
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    Functioni

    Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport. The BCR(KLHL12) complex is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). As part of the BCR(KLHL12) complex, also acts as a negative regulator of the Wnt signaling pathway by mediating ubiquitination and subsequent proteolysis of DVL3. The BCR(KLHL12) complex also mediates polyubiquitination of DRD4, without leading to degradation of DRD4.4 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. COPII vesicle coating Source: UniProtKB
    2. ER to Golgi vesicle-mediated transport Source: UniProtKB
    3. protein monoubiquitination Source: UniProtKB
    4. Wnt signaling pathway Source: UniProtKB

    Keywords - Biological processi

    ER-Golgi transport, Transport, Ubl conjugation pathway, Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_200841. degradation of DVL.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kelch-like protein 12
    Alternative name(s):
    CUL3-interacting protein 1
    DKIR homolog
    Short name:
    hDKIR
    Gene namesi
    Name:KLHL12
    Synonyms:C3IP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19360. KLHL12.

    Subcellular locationi

    Cytoplasmic vesicleCOPII-coated vesicle 1 Publication

    GO - Cellular componenti

    1. Cul3-RING ubiquitin ligase complex Source: UniProtKB
    2. ER to Golgi transport vesicle Source: UniProtKB
    3. Golgi membrane Source: GOC

    Keywords - Cellular componenti

    Cytoplasmic vesicle

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi289 – 2902FG → AA: Abolishes interaction with SEC31A and subsequent monoubiquitination of SEC31A. 1 Publication

    Organism-specific databases

    PharmGKBiPA134952416.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 568568Kelch-like protein 12PRO_0000234349Add
    BLAST

    Proteomic databases

    MaxQBiQ53G59.
    PaxDbiQ53G59.
    PRIDEiQ53G59.

    PTM databases

    PhosphoSiteiQ53G59.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Highly expressed in testis and at lower levels in the submandibular salivary gland.2 Publications

    Gene expression databases

    ArrayExpressiQ53G59.
    BgeeiQ53G59.
    CleanExiHS_KLHL12.
    GenevestigatoriQ53G59.

    Interactioni

    Subunit structurei

    Component of the BCR(KLHL12) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL12 and RBX1. This complex interacts with DVL3 upon activation of the Wnt signaling pathway by WNT3A. Interacts with DRD4, KLHL12 and SEC31A.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN1P542532EBI-740929,EBI-930964
    PEF1Q9UBV82EBI-740929,EBI-724639

    Protein-protein interaction databases

    BioGridi121890. 28 interactions.
    IntActiQ53G59. 20 interactions.
    MINTiMINT-1434520.
    STRINGi9606.ENSP00000356230.

    Structurei

    Secondary structure

    1
    568
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi281 – 2866
    Turni291 – 2933
    Beta strandi299 – 3035
    Turni304 – 3074
    Beta strandi308 – 3114
    Beta strandi323 – 3275
    Beta strandi330 – 3345
    Beta strandi346 – 3505
    Beta strandi360 – 3623
    Beta strandi373 – 3775
    Beta strandi380 – 3845
    Beta strandi395 – 4006
    Turni401 – 4044
    Beta strandi405 – 4117
    Beta strandi420 – 4245
    Beta strandi427 – 4315
    Beta strandi443 – 4464
    Turni448 – 4503
    Beta strandi453 – 4564
    Beta strandi467 – 4715
    Beta strandi474 – 4785
    Beta strandi483 – 4864
    Beta strandi490 – 4945
    Turni495 – 4984
    Beta strandi499 – 5035
    Beta strandi514 – 5185
    Beta strandi521 – 5255
    Beta strandi530 – 54112
    Turni542 – 5454
    Beta strandi546 – 55914
    Beta strandi561 – 5666

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VPJX-ray1.85A268-567[»]
    ProteinModelPortaliQ53G59.
    SMRiQ53G59. Positions 5-567.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53G59.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 10068BTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini135 – 236102BACKAdd
    BLAST
    Repeati282 – 32948Kelch 1Add
    BLAST
    Repeati331 – 37949Kelch 2Add
    BLAST
    Repeati380 – 42647Kelch 3Add
    BLAST
    Repeati427 – 47347Kelch 4Add
    BLAST
    Repeati475 – 52046Kelch 5Add
    BLAST
    Repeati522 – 56746Kelch 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni405 – 568164Interaction with DVL3Add
    BLAST

    Domaini

    The BTB domain is required for interaction with CUL3.

    Sequence similaritiesi

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

    Keywords - Domaini

    Kelch repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG73120.
    HOGENOMiHOG000230814.
    HOVERGENiHBG014286.
    InParanoidiQ53G59.
    KOiK10450.
    OMAiRYDPHTG.
    OrthoDBiEOG7HTHGF.
    PhylomeDBiQ53G59.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q53G59-1) [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

    MGGIMAPKDI MTNTHAKSIL NSMNSLRKSN TLCDVTLRVE QKDFPAHRIV    50
    LAACSDYFCA MFTSELSEKG KPYVDIQGLT ASTMEILLDF VYTETVHVTV 100
    ENVQELLPAA CLLQLKGVKQ ACCEFLESQL DPSNCLGIRD FAETHNCVDL 150
    MQAAEVFSQK HFPEVVQHEE FILLSQGEVE KLIKCDEIQV DSEEPVFEAV 200
    INWVKHAKKE REESLPNLLQ YVRMPLLTPR YITDVIDAEP FIRCSLQCRD 250
    LVDEAKKFHL RPELRSQMQG PRTRARLGAN EVLLVVGGFG SQQSPIDVVE 300
    KYDPKTQEWS FLPSITRKRR YVASVSLHDR IYVIGGYDGR SRLSSVECLD 350
    YTADEDGVWY SVAPMNVRRG LAGATTLGDM IYVSGGFDGS RRHTSMERYD 400
    PNIDQWSMLG DMQTAREGAG LVVASGVIYC LGGYDGLNIL NSVEKYDPHT 450
    GHWTNVTPMA TKRSGAGVAL LNDHIYVVGG FDGTAHLSSV EAYNIRTDSW 500
    TTVTSMTTPR CYVGATVLRG RLYAIAGYDG NSLLSSIECY DPIIDSWEVV 550
    TSMGTQRCDA GVCVLREK 568
    Length:568
    Mass (Da):63,277
    Last modified:May 16, 2006 - v2
    Checksum:i4EB1BC33B6351B5D
    GO
    Isoform 2 (identifier: Q53G59-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MDVNKFEASVGFLDVKKFLSTWKLQNPRTHFVLSPHCFM

    Show »
    Length:606
    Mass (Da):67,727
    Checksum:i47F91BE5B8ED7C33
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti122 – 1221C → R in BAD96792. 1 PublicationCurated
    Sequence conflicti197 – 1982FE → LG in BAD96792. 1 PublicationCurated
    Sequence conflicti394 – 3941T → A in BAD96792. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721P → L.
    Corresponds to variant rs12569087 [ dbSNP | Ensembl ].
    VAR_050049

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MDVNKFEASVGFLDVKKFLS TWKLQNPRTHFVLSPHCFM in isoform 2. 1 PublicationVSP_042975

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190900 mRNA. Translation: AAG17175.1.
    AK027656 mRNA. Translation: BAB55271.1.
    AK301791 mRNA. Translation: BAH13554.1.
    AK223072 mRNA. Translation: BAD96792.1.
    AC096632 Genomic DNA. No translation available.
    BC003183 mRNA. Translation: AAH03183.1.
    BC004175 mRNA. Translation: AAH04175.1.
    CCDSiCCDS1429.1. [Q53G59-1]
    RefSeqiNP_067646.1. NM_021633.2. [Q53G59-1]
    XP_005245460.1. XM_005245403.1. [Q53G59-2]
    UniGeneiHs.706793.

    Genome annotation databases

    EnsembliENST00000367261; ENSP00000356230; ENSG00000117153. [Q53G59-1]
    GeneIDi59349.
    KEGGihsa:59349.
    UCSCiuc001gyn.1. human. [Q53G59-1]
    uc010pqc.1. human. [Q53G59-2]

    Polymorphism databases

    DMDMi97054498.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190900 mRNA. Translation: AAG17175.1 .
    AK027656 mRNA. Translation: BAB55271.1 .
    AK301791 mRNA. Translation: BAH13554.1 .
    AK223072 mRNA. Translation: BAD96792.1 .
    AC096632 Genomic DNA. No translation available.
    BC003183 mRNA. Translation: AAH03183.1 .
    BC004175 mRNA. Translation: AAH04175.1 .
    CCDSi CCDS1429.1. [Q53G59-1 ]
    RefSeqi NP_067646.1. NM_021633.2. [Q53G59-1 ]
    XP_005245460.1. XM_005245403.1. [Q53G59-2 ]
    UniGenei Hs.706793.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VPJ X-ray 1.85 A 268-567 [» ]
    ProteinModelPortali Q53G59.
    SMRi Q53G59. Positions 5-567.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121890. 28 interactions.
    IntActi Q53G59. 20 interactions.
    MINTi MINT-1434520.
    STRINGi 9606.ENSP00000356230.

    PTM databases

    PhosphoSitei Q53G59.

    Polymorphism databases

    DMDMi 97054498.

    Proteomic databases

    MaxQBi Q53G59.
    PaxDbi Q53G59.
    PRIDEi Q53G59.

    Protocols and materials databases

    DNASUi 59349.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367261 ; ENSP00000356230 ; ENSG00000117153 . [Q53G59-1 ]
    GeneIDi 59349.
    KEGGi hsa:59349.
    UCSCi uc001gyn.1. human. [Q53G59-1 ]
    uc010pqc.1. human. [Q53G59-2 ]

    Organism-specific databases

    CTDi 59349.
    GeneCardsi GC01M202860.
    HGNCi HGNC:19360. KLHL12.
    MIMi 614522. gene.
    neXtProti NX_Q53G59.
    PharmGKBi PA134952416.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG73120.
    HOGENOMi HOG000230814.
    HOVERGENi HBG014286.
    InParanoidi Q53G59.
    KOi K10450.
    OMAi RYDPHTG.
    OrthoDBi EOG7HTHGF.
    PhylomeDBi Q53G59.
    TreeFami TF329218.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_200841. degradation of DVL.

    Miscellaneous databases

    ChiTaRSi KLHL12. human.
    EvolutionaryTracei Q53G59.
    GeneWikii KLHL12.
    GenomeRNAii 59349.
    NextBioi 65257.
    PROi Q53G59.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q53G59.
    Bgeei Q53G59.
    CleanExi HS_KLHL12.
    Genevestigatori Q53G59.

    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. "Sequence of a novel kelch-like protein, C3IP1."
      Du M., Zu Z., Liou J.-Y., Chu K.-Y., Sansores Garcia L., Yeh E., Wu K.K.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Teratocarcinoma, Testis and Thyroid.
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
      Tissue: Kidney adenocarcinoma.
    6. "hDKIR, a human homologue of the Drosophila kelch protein, involved in a ring-like structure."
      Mai A., Jung S.K., Yonehara S.
      Exp. Cell Res. 300:72-83(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH KLHL2.
    7. Cited for: TISSUE SPECIFICITY.
    8. "The KLHL12-cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation."
      Angers S., Thorpe C.J., Biechele T.L., Goldenberg S.J., Zheng N., Maccoss M.J., Moon R.T.
      Nat. Cell Biol. 8:348-357(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CUL3 AND DVL3.
    9. "BTB Protein KLHL12 targets the dopamine D4 receptor for ubiquitination by a Cul3-based E3 ligase."
      Rondou P., Haegeman G., Vanhoenacker P., Van Craenenbroeck K.
      J. Biol. Chem. 283:11083-11096(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DRD4.
    10. "KLHL12-mediated ubiquitination of the dopamine D4 receptor does not target the receptor for degradation."
      Rondou P., Skieterska K., Packeu A., Lintermans B., Vanhoenacker P., Vauquelin G., Haegeman G., Van Craenenbroeck K.
      Cell. Signal. 22:900-913(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Ubiquitin-dependent regulation of COPII coat size and function."
      Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., Rape M.
      Nature 482:495-500(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BCR(KLHL12) COMPLEX, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SEC31A, MUTAGENESIS OF 289-PHE-GLY-290.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 268-567.

    Entry informationi

    Entry nameiKLH12_HUMAN
    AccessioniPrimary (citable) accession number: Q53G59
    Secondary accession number(s): A6NEN8, B7Z7B8, Q9HBX5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 94 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3