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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

Miscellaneous

Antigen recognized by serum from scleroderma patient.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • RNA polymerase II transcription factor binding Source: Ensembl
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processUbl conjugation pathway

Enzyme and pathway databases

BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-5632684. Hedgehog 'on' state.
SignaLinkiO43791.
SIGNORiO43791.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000121067.17.
HGNCiHGNC:11254. SPOP.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi87Y → A: Strongly reduced affinity for substrate proteins. 1 Publication1
Mutagenesisi123Y → A: Strongly reduced affinity for substrate proteins. 1 Publication1
Mutagenesisi130D → A: Strongly reduced affinity for substrate proteins. 1 Publication1
Mutagenesisi131W → A: Strongly reduced affinity for substrate proteins. 1 Publication1
Mutagenesisi133F → A: Strongly reduced affinity for substrate proteins. 1 Publication1
Mutagenesisi186L → D: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. 1 Publication1
Mutagenesisi190L → D: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. 1 Publication1
Mutagenesisi193L → D: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. 1 Publication1
Mutagenesisi217I → K: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. 1 Publication1

Organism-specific databases

DisGeNETi8405.
OpenTargetsiENSG00000121067.
PharmGKBiPA36084.

Polymorphism and mutation databases

BioMutaiSPOP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001916211 – 374Speckle-type POZ proteinAdd BLAST374

Proteomic databases

EPDiO43791.
MaxQBiO43791.
PaxDbiO43791.
PeptideAtlasiO43791.
PRIDEiO43791.

PTM databases

iPTMnetiO43791.
PhosphoSitePlusiO43791.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000121067.
CleanExiHS_SPOP.
ExpressionAtlasiO43791. baseline and differential.
GenevisibleiO43791. HS.

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

Show more details

GO - Molecular functioni

  • RNA polymerase II transcription factor binding Source: Ensembl
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113993. 48 interactors.
CORUMiO43791.
DIPiDIP-50517N.
ELMiO43791.
IntActiO43791. 30 interactors.
MINTiMINT-1438409.
STRINGi9606.ENSP00000240327.

Structurei

Secondary structure

1374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 40Combined sources10
Helixi41 – 43Combined sources3
Helixi45 – 48Combined sources4
Beta strandi57 – 60Combined sources4
Helixi61 – 63Combined sources3
Beta strandi65 – 72Combined sources8
Helixi78 – 80Combined sources3
Beta strandi83 – 92Combined sources10
Beta strandi94 – 107Combined sources14
Beta strandi113 – 118Combined sources6
Beta strandi123 – 126Combined sources4
Beta strandi130 – 138Combined sources9
Helixi139 – 143Combined sources5
Helixi145 – 147Combined sources3
Beta strandi148 – 150Combined sources3
Helixi151 – 153Combined sources3
Beta strandi155 – 163Combined sources9
Helixi186 – 196Combined sources11
Beta strandi202 – 206Combined sources5
Beta strandi209 – 213Combined sources5
Helixi215 – 221Combined sources7
Helixi223 – 230Combined sources8
Beta strandi231 – 233Combined sources3
Helixi234 – 238Combined sources5
Beta strandi240 – 243Combined sources4
Helixi248 – 260Combined sources13
Helixi266 – 268Combined sources3
Helixi270 – 279Combined sources10
Helixi283 – 290Combined sources8
Turni299 – 301Combined sources3
Helixi302 – 311Combined sources10
Helixi315 – 327Combined sources13
Helixi329 – 332Combined sources4
Helixi336 – 344Combined sources9
Helixi346 – 357Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43791.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 161MATHPROSITE-ProRule annotationAdd BLAST131
Domaini173 – 297BTBPROSITE-ProRule annotationAdd BLAST125

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni71 – 191Required for nuclear localizationAdd BLAST121
Regioni123 – 133Important for binding substrate proteinsAdd BLAST11
Regioni186 – 217Important for homodimerizationAdd BLAST32
Regioni297 – 355Important for homodimerizationAdd BLAST59

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

Phylogenomic databases

eggNOGiKOG1987. Eukaryota.
ENOG410XQV8. LUCA.
GeneTreeiENSGT00390000000361.
HOGENOMiHOG000231621.
HOVERGENiHBG001393.
InParanoidiO43791.
KOiK10523.
OMAiFNYMWTI.
OrthoDBiEOG091G07ZM.
PhylomeDBiO43791.
TreeFamiTF313419.

Family and domain databases

CDDicd14734. SPOP_C. 1 hit.
Gene3Di2.60.210.10. 1 hit.
InterProiView protein in InterPro
IPR000210. BTB/POZ_dom.
IPR002083. MATH/TRAF_dom.
IPR011333. SKP1/BTB/POZ_sf.
IPR034089. SPOP_C.
IPR008974. TRAF-like.
PfamiView protein in Pfam
PF00651. BTB. 1 hit.
PF00917. MATH. 1 hit.
SMARTiView protein in SMART
SM00225. BTB. 1 hit.
SM00061. MATH. 1 hit.
SUPFAMiSSF49599. SSF49599. 1 hit.
SSF54695. SSF54695. 1 hit.
PROSITEiView protein in PROSITE
PS50097. BTB. 1 hit.
PS50144. MATH. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti239N → S in BAD96309 (Ref. 3) Curated1

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_005257723.4.
XP_005257781.1. XM_005257724.4.
XP_016880693.1. XM_017025204.1.
UniGeneiHs.463382.
Hs.740407.

Genome annotation databases

EnsembliENST00000347630; ENSP00000240327; ENSG00000121067.
ENST00000393328; ENSP00000377001; ENSG00000121067.
ENST00000503676; ENSP00000420908; ENSG00000121067.
ENST00000504102; ENSP00000425905; ENSG00000121067.
GeneIDi8405.
KEGGihsa:8405.
UCSCiuc002ipd.4. human.

Similar proteinsi

Entry informationi

Entry nameiSPOP_HUMAN
AccessioniPrimary (citable) accession number: O43791
Secondary accession number(s): B2R6S3, D3DTW7, Q53HJ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: November 22, 2017
This is version 167 of the entry and version 1 of the sequence. See 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 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