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UniProtKB - O43791 (SPOP_HUMAN)

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Protein

Speckle-type POZ protein

Gene

SPOP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000121067.17
HGNCiHGNC:11254 SPOP
MIMi602650 gene
neXtProtiNX_O43791

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
ProteomicsDBi49171

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
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi113993, 57 interactors
CORUMiO43791
DIPiDIP-50517N
ELMiO43791
IntActiO43791, 30 interactors
MINTiO43791
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: June 20, 2018
This is version 173 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

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