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Protein

Speckle-type POZ protein

Gene

SPOP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi6.3.2.19. 2681.
ReactomeiREACT_268718. Hedgehog 'on' state.
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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11254. SPOP.

Subcellular locationi

GO - Cellular componenti

  • Cul3-RING ubiquitin ligase complex Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiSPOP.

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

BgeeiO43791.
CleanExiHS_SPOP.
ExpressionAtlasiO43791. baseline and differential.
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
DUSP7Q168295EBI-743549,EBI-1265847
MYD88Q998366EBI-743549,EBI-447677
NCOA3Q9Y6Q96EBI-743549,EBI-81196
PTENP604844EBI-743549,EBI-696162

Protein-protein interaction databases

BioGridi113993. 35 interactions.
IntActiO43791. 17 interactions.
MINTiMINT-1438409.
STRINGi9606.ENSP00000240327.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000000361.
HOGENOMiHOG000231621.
HOVERGENiHBG001393.
InParanoidiO43791.
KOiK10523.
OMAiTGWKSMV.
OrthoDBiEOG73NG3G.
PhylomeDBiO43791.
TreeFamiTF313419.

Family and domain databases

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

        10         20         30         40         50
MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE
60 70 80 90 100
VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA
110 120 130 140 150
KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL
160 170 180 190 200
PDDKLTLFCE VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT
210 220 230 240 250
DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV
260 270 280 290 300
FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE
310 320 330 340 350
NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA
360 370
EAYRSLASAQ CPFLGPPRKR LKQS
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 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005257723.3.
XP_005257781.1. XM_005257724.3.
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:
EMBLi
GenBanki
DDBJi
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_005257723.3.
XP_005257781.1. XM_005257724.3.
UniGeneiHs.463382.
Hs.740407.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi113993. 35 interactions.
IntActiO43791. 17 interactions.
MINTiMINT-1438409.
STRINGi9606.ENSP00000240327.

PTM databases

PhosphoSiteiO43791.

Polymorphism and mutation databases

BioMutaiSPOP.

Proteomic databases

MaxQBiO43791.
PaxDbiO43791.
PRIDEiO43791.

Protocols and materials databases

DNASUi8405.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8405.
GeneCardsiGC17M047676.
HGNCiHGNC:11254. SPOP.
HPAiHPA046820.
MIMi602650. gene.
neXtProtiNX_O43791.
PharmGKBiPA36084.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG273048.
GeneTreeiENSGT00390000000361.
HOGENOMiHOG000231621.
HOVERGENiHBG001393.
InParanoidiO43791.
KOiK10523.
OMAiTGWKSMV.
OrthoDBiEOG73NG3G.
PhylomeDBiO43791.
TreeFamiTF313419.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 2681.
ReactomeiREACT_268718. Hedgehog 'on' state.
SignaLinkiO43791.

Miscellaneous databases

ChiTaRSiSPOP. human.
EvolutionaryTraceiO43791.
GeneWikiiSPOP.
GenomeRNAii8405.
NextBioi31454.
PROiO43791.
SOURCEiSearch...

Gene expression databases

BgeeiO43791.
CleanExiHS_SPOP.
ExpressionAtlasiO43791. baseline and differential.
GenevestigatoriO43791.

Family and domain databases

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 142 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.