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O43791

- SPOP_HUMAN

UniProt

O43791 - SPOP_HUMAN

Protein

Speckle-type POZ protein

Gene

SPOP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of H2AFY and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL.6 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    2. protein ubiquitination Source: UniProtKB-UniPathway

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    SignaLinkiO43791.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Speckle-type POZ protein
    Alternative name(s):
    HIB homolog 1
    Roadkill homolog 1
    Gene namesi
    Name:SPOP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11254. SPOP.

    Subcellular locationi

    GO - Cellular componenti

    1. Cul3-RING ubiquitin ligase complex Source: UniProtKB
    2. nuclear speck Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi87 – 871Y → A: Strongly reduced affinity for substrate proteins. 1 Publication
    Mutagenesisi123 – 1231Y → A: Strongly reduced affinity for substrate proteins. 1 Publication
    Mutagenesisi130 – 1301D → A: Strongly reduced affinity for substrate proteins. 1 Publication
    Mutagenesisi131 – 1311W → A: Strongly reduced affinity for substrate proteins. 1 Publication
    Mutagenesisi133 – 1331F → A: Strongly reduced affinity for substrate proteins. 1 Publication
    Mutagenesisi186 – 1861L → D: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. 1 Publication
    Mutagenesisi190 – 1901L → D: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. 1 Publication
    Mutagenesisi193 – 1931L → D: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. 1 Publication
    Mutagenesisi217 – 2171I → K: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. 1 Publication

    Organism-specific databases

    PharmGKBiPA36084.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 374374Speckle-type POZ proteinPRO_0000191621Add
    BLAST

    Proteomic databases

    MaxQBiO43791.
    PaxDbiO43791.
    PRIDEiO43791.

    PTM databases

    PhosphoSiteiO43791.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiO43791.
    BgeeiO43791.
    CleanExiHS_SPOP.
    GenevestigatoriO43791.

    Organism-specific databases

    HPAiHPA046820.

    Interactioni

    Subunit structurei

    Interacts with GLI2 and GLI3 By similarity. Homodimer and homooligomer. Heterodimer with SPOPL. Each dimer interacts with two CUL3 molecules. Part of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that contain CUL3 and homodimeric SPOP, or the heterodimer formed by SPOP and SPOPL, plus a target protein, such as H2AFY, PDX1/IPF1, BMI1, BRMS1 and DAXX.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CUL3Q136182EBI-743549,EBI-456129
    DAXXQ9UER75EBI-743549,EBI-77321
    MYD88Q998366EBI-743549,EBI-447677
    NCOA3Q9Y6Q96EBI-743549,EBI-81196

    Protein-protein interaction databases

    BioGridi113993. 29 interactions.
    IntActiO43791. 15 interactions.
    MINTiMINT-1438409.
    STRINGi9606.ENSP00000240327.

    Structurei

    Secondary structure

    1
    374
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 4010
    Helixi41 – 433
    Helixi45 – 484
    Beta strandi57 – 604
    Helixi61 – 633
    Beta strandi65 – 728
    Helixi78 – 803
    Beta strandi83 – 9210
    Beta strandi94 – 10714
    Beta strandi113 – 1186
    Beta strandi123 – 1264
    Beta strandi130 – 1389
    Helixi139 – 1435
    Helixi145 – 1473
    Beta strandi148 – 1503
    Helixi151 – 1533
    Beta strandi155 – 1639
    Helixi186 – 19611
    Beta strandi202 – 2065
    Beta strandi209 – 2135
    Helixi215 – 2217
    Helixi223 – 2308
    Beta strandi231 – 2333
    Helixi234 – 2385
    Beta strandi240 – 2434
    Helixi248 – 26013
    Helixi266 – 2683
    Helixi270 – 27910
    Helixi283 – 2908
    Turni299 – 3013
    Helixi302 – 31110
    Helixi315 – 32713
    Helixi329 – 3324
    Helixi336 – 3449
    Helixi346 – 35712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CR2NMR-A28-173[»]
    3HQHX-ray2.30A28-166[»]
    3HQIX-ray2.62A/B28-329[»]
    3HQLX-ray1.66A/B28-166[»]
    3HQMX-ray1.74A/B28-166[»]
    3HSVX-ray1.43A/B28-166[»]
    3HTMX-ray2.50A/B/C/D172-329[»]
    3HU6X-ray2.70A/B28-329[»]
    3IVBX-ray1.75A28-166[»]
    3IVQX-ray2.10A/B28-166[»]
    3IVVX-ray1.25A28-166[»]
    4EOZX-ray2.40A/C177-319[»]
    4HS2X-ray1.53A270-374[»]
    4J8ZX-ray2.42A/B169-374[»]
    4O1VX-ray2.00A28-166[»]
    ProteinModelPortaliO43791.
    SMRiO43791. Positions 28-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43791.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 161131MATHPROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 297125BTBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni71 – 191121Required for nuclear localizationAdd
    BLAST
    Regioni123 – 13311Important for binding substrate proteinsAdd
    BLAST
    Regioni186 – 21732Important for homodimerizationAdd
    BLAST
    Regioni297 – 35559Important for homodimerizationAdd
    BLAST

    Domaini

    The BTB (POZ) domain mediates dimerization and interaction with CUL3.1 Publication
    The MATH domain mediates interaction with protein-ubiquitin ligase substrates, such as H2AFY and BMI1.1 Publication

    Sequence similaritiesi

    Belongs to the Tdpoz family.Curated
    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 1 MATH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG273048.
    HOGENOMiHOG000231621.
    HOVERGENiHBG001393.
    InParanoidiO43791.
    KOiK10523.
    OMAiSHFGMLL.
    OrthoDBiEOG73NG3G.
    PhylomeDBiO43791.
    TreeFamiTF313419.

    Family and domain databases

    Gene3Di3.30.710.10. 1 hit.
    InterProiIPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR002083. MATH.
    IPR008974. TRAF-like.
    [Graphical view]
    PfamiPF00651. BTB. 1 hit.
    PF00917. MATH. 1 hit.
    [Graphical view]
    SMARTiSM00225. BTB. 1 hit.
    SM00061. MATH. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 1 hit.
    SSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    PS50144. MATH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O43791-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE    50
    VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA 100
    KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL 150
    PDDKLTLFCE VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT 200
    DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV 250
    FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE 300
    NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA 350
    EAYRSLASAQ CPFLGPPRKR LKQS 374
    Length:374
    Mass (Da):42,132
    Last modified:June 1, 1998 - v1
    Checksum:iEE5F4C5CF6FD09DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti239 – 2391N → S in BAD96309. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000644 mRNA. Translation: CAA04199.1.
    AK222589 mRNA. Translation: BAD96309.1.
    AK312691 mRNA. Translation: BAG35570.1.
    CH471109 Genomic DNA. Translation: EAW94671.1.
    CH471109 Genomic DNA. Translation: EAW94672.1.
    CH471109 Genomic DNA. Translation: EAW94673.1.
    CH471109 Genomic DNA. Translation: EAW94674.1.
    CH471109 Genomic DNA. Translation: EAW94675.1.
    BC001269 mRNA. Translation: AAH01269.1.
    BC003385 mRNA. Translation: AAH03385.1.
    CCDSiCCDS11551.1.
    RefSeqiNP_001007227.1. NM_001007226.1.
    NP_001007228.1. NM_001007227.1.
    NP_001007229.1. NM_001007228.1.
    NP_001007230.1. NM_001007229.1.
    NP_001007231.1. NM_001007230.1.
    NP_003554.1. NM_003563.3.
    XP_005257780.1. XM_005257723.2.
    XP_005257781.1. XM_005257724.2.
    UniGeneiHs.463382.
    Hs.740407.

    Genome annotation databases

    EnsembliENST00000347630; ENSP00000240327; ENSG00000121067.
    ENST00000393328; ENSP00000377001; ENSG00000121067.
    ENST00000503676; ENSP00000420908; ENSG00000121067.
    ENST00000504102; ENSP00000425905; ENSG00000121067.
    GeneIDi8405.
    KEGGihsa:8405.
    UCSCiuc002ipb.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000644 mRNA. Translation: CAA04199.1 .
    AK222589 mRNA. Translation: BAD96309.1 .
    AK312691 mRNA. Translation: BAG35570.1 .
    CH471109 Genomic DNA. Translation: EAW94671.1 .
    CH471109 Genomic DNA. Translation: EAW94672.1 .
    CH471109 Genomic DNA. Translation: EAW94673.1 .
    CH471109 Genomic DNA. Translation: EAW94674.1 .
    CH471109 Genomic DNA. Translation: EAW94675.1 .
    BC001269 mRNA. Translation: AAH01269.1 .
    BC003385 mRNA. Translation: AAH03385.1 .
    CCDSi CCDS11551.1.
    RefSeqi NP_001007227.1. NM_001007226.1.
    NP_001007228.1. NM_001007227.1.
    NP_001007229.1. NM_001007228.1.
    NP_001007230.1. NM_001007229.1.
    NP_001007231.1. NM_001007230.1.
    NP_003554.1. NM_003563.3.
    XP_005257780.1. XM_005257723.2.
    XP_005257781.1. XM_005257724.2.
    UniGenei Hs.463382.
    Hs.740407.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CR2 NMR - A 28-173 [» ]
    3HQH X-ray 2.30 A 28-166 [» ]
    3HQI X-ray 2.62 A/B 28-329 [» ]
    3HQL X-ray 1.66 A/B 28-166 [» ]
    3HQM X-ray 1.74 A/B 28-166 [» ]
    3HSV X-ray 1.43 A/B 28-166 [» ]
    3HTM X-ray 2.50 A/B/C/D 172-329 [» ]
    3HU6 X-ray 2.70 A/B 28-329 [» ]
    3IVB X-ray 1.75 A 28-166 [» ]
    3IVQ X-ray 2.10 A/B 28-166 [» ]
    3IVV X-ray 1.25 A 28-166 [» ]
    4EOZ X-ray 2.40 A/C 177-319 [» ]
    4HS2 X-ray 1.53 A 270-374 [» ]
    4J8Z X-ray 2.42 A/B 169-374 [» ]
    4O1V X-ray 2.00 A 28-166 [» ]
    ProteinModelPortali O43791.
    SMRi O43791. Positions 28-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113993. 29 interactions.
    IntActi O43791. 15 interactions.
    MINTi MINT-1438409.
    STRINGi 9606.ENSP00000240327.

    PTM databases

    PhosphoSitei O43791.

    Proteomic databases

    MaxQBi O43791.
    PaxDbi O43791.
    PRIDEi O43791.

    Protocols and materials databases

    DNASUi 8405.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000347630 ; ENSP00000240327 ; ENSG00000121067 .
    ENST00000393328 ; ENSP00000377001 ; ENSG00000121067 .
    ENST00000503676 ; ENSP00000420908 ; ENSG00000121067 .
    ENST00000504102 ; ENSP00000425905 ; ENSG00000121067 .
    GeneIDi 8405.
    KEGGi hsa:8405.
    UCSCi uc002ipb.3. human.

    Organism-specific databases

    CTDi 8405.
    GeneCardsi GC17M047676.
    HGNCi HGNC:11254. SPOP.
    HPAi HPA046820.
    MIMi 602650. gene.
    neXtProti NX_O43791.
    PharmGKBi PA36084.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG273048.
    HOGENOMi HOG000231621.
    HOVERGENi HBG001393.
    InParanoidi O43791.
    KOi K10523.
    OMAi SHFGMLL.
    OrthoDBi EOG73NG3G.
    PhylomeDBi O43791.
    TreeFami TF313419.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    SignaLinki O43791.

    Miscellaneous databases

    ChiTaRSi SPOP. human.
    EvolutionaryTracei O43791.
    GeneWikii SPOP.
    GenomeRNAii 8405.
    NextBioi 31454.
    PROi O43791.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43791.
    Bgeei O43791.
    CleanExi HS_SPOP.
    Genevestigatori O43791.

    Family and domain databases

    Gene3Di 3.30.710.10. 1 hit.
    InterProi IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR002083. MATH.
    IPR008974. TRAF-like.
    [Graphical view ]
    Pfami PF00651. BTB. 1 hit.
    PF00917. MATH. 1 hit.
    [Graphical view ]
    SMARTi SM00225. BTB. 1 hit.
    SM00061. MATH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 1 hit.
    SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    PS50144. MATH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel nuclear speckle-type protein, SPOP."
      Nagai Y., Kojima T., Muro Y., Hachiya T., Nishizawa Y., Wakabayashi T., Hagiwara M.
      FEBS Lett. 418:23-26(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    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].
    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].
      Tissue: Coronary artery.
    4. 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].
      Tissue: Cervix and Placenta.
    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. "Daxx-mediated transcriptional repression of MMP1 gene is reversed by SPOP."
      La M., Kim K., Park J., Won J., Lee J.-H., Fu Y.M., Meadows G.G., Joe C.O.
      Biochem. Biophys. Res. Commun. 320:760-765(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAXX, HOMODIMERIZATION.
    8. "Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase."
      Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I., Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., van Lohuizen M.
      Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BMI1, IDENTIFICATION IN A COMPLEX WITH CUL3 AND BMI1, IDENTIFICATION IN A COMPLEX WITH CUL3 AND H2AFY, SUBCELLULAR LOCATION, FUNCTION.
    9. "Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus."
      Kent D., Bush E.W., Hooper J.E.
      Development 133:2001-2010(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    10. "A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor."
      Zhang Q., Zhang L., Wang B., Ou C.-Y., Chien C.-T., Jiang J.
      Dev. Cell 10:719-729(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    11. "BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase."
      Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H., Chiba T., Tanaka K., Bang O.S., Joe C.O., Chung C.H.
      J. Biol. Chem. 281:12664-12672(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CUL3 AND DAXX, FUNCTION.
    12. "Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex."
      Kim B., Nam H.J., Pyo K.E., Jang M.J., Kim I.S., Kim D., Boo K., Lee S.H., Yoon J.B., Baek S.H., Kim J.H.
      Biochem. Biophys. Res. Commun. 415:720-726(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRMS1, IDENTIFICATION IN A COMPLEX WITH CUL3 AND BRMS1.
    13. "Solution structure of N-terminal domain of speckle-type POZ protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 28-173.
    14. "Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases."
      Zhuang M., Calabrese M.F., Liu J., Waddell M.B., Nourse A., Hammel M., Miller D.J., Walden H., Duda D.M., Seyedin S.N., Hoggard T., Harper J.W., White K.P., Schulman B.A.
      Mol. Cell 36:39-50(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 28-166 IN COMPLEXES WITH H2AFY AND SUBSTRATE PEPTIDES, INTERACTION WITH CUL3; H2AFY AND DAXX, SUBUNIT, FUNCTION, DOMAIN, MUTAGENESIS OF TYR-87; TYR-123; ASP-130; TRP-131; PHE-133; LEU-186; LEU-190; LEU-193 AND ILE-217, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase."
      Errington W.J., Khan M.Q., Bueler S.A., Rubinstein J.L., Chakrabartty A., Prive G.G.
      Structure 20:1141-1153(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 177-319 IN COMPLEX WITH CUL3, FUNCTION, INTERACTION WITH CUL3 AND H2AFY, SUBUNIT.

    Entry informationi

    Entry nameiSPOP_HUMAN
    AccessioniPrimary (citable) accession number: O43791
    Secondary accession number(s): B2R6S3, D3DTW7, Q53HJ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 135 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

    Miscellaneous

    Antigen recognized by serum from scleroderma patient.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3