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O43791

- SPOP_HUMAN

UniProt

O43791 - SPOP_HUMAN

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Protein

Speckle-type POZ protein

Gene
SPOP
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  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
Complete GO annotation...

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

Nucleus. Nucleus speckle 3 Publications

GO - Cellular componenti

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

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.7 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.

Miscellaneous databases

EvolutionaryTraceiO43791.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 161131MATHAdd
BLAST
Domaini173 – 297125BTBAdd
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.
Contains 1 BTB (POZ) domain.
Contains 1 MATH domain.

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

Sequence conflict

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

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.
ENST00000393331; ENSP00000377004; 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 .
ENST00000393331 ; ENSP00000377004 ; 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

« 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: September 3, 2014
This is version 134 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

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