SPOP_HUMAN - dbPTM
SPOP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPOP_HUMAN
UniProt AC O43791
Protein Name Speckle-type POZ protein
Gene Name SPOP
Organism Homo sapiens (Human).
Sequence Length 374
Subcellular Localization Nucleus. Nucleus speckle.
Protein Description 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..
Protein Sequence MSRVPSPPPPAEMSSGPVAESWCYTQIKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVFKEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVENAAEILILADLHSADQLKTQAVDFINYHASDVLETSGWKSMVVSHPHLVAEAYRSLASAQCPFLGPPRKRLKQS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSRVPSPPP
------CCCCCCCCC
41.8226074081
6Phosphorylation--MSRVPSPPPPAEM
--CCCCCCCCCCCHH
47.3730108239
14PhosphorylationPPPPAEMSSGPVAES
CCCCCHHCCCCCCCC
24.5330108239
15PhosphorylationPPPAEMSSGPVAESW
CCCCHHCCCCCCCCH
45.8930108239
54PhosphorylationEMGEVIKSSTFSSGA
HHHHHHHHCCCCCCC
24.40-
64UbiquitinationFSSGANDKLKWCLRV
CCCCCCCCCEEEEEE
52.3432015554
110UbiquitinationKFSILNAKGEETKAM
EEEEECCCCHHHHHH
66.8221906983
115UbiquitinationNAKGEETKAMESQRA
CCCCHHHHHHHHHHH
49.3622817900
215UbiquitinationGQEFQAHKAILAARS
CCHHHHHHHHHHHCC
39.89-
237UbiquitinationEHEMEESKKNRVEIN
HHHHHHHHCCCCCCC
58.3032015554
238UbiquitinationHEMEESKKNRVEIND
HHHHHHHCCCCCCCC
60.3029967540
268UbiquitinationGKAPNLDKMADDLLA
CCCCCHHHHHHHHHH
38.8729901268
279UbiquitinationDLLAAADKYALERLK
HHHHHHHHHHHHHHH
27.9122053931
339AcetylationVLETSGWKSMVVSHP
HHHHCCCCCEECCCH
32.007664267
340PhosphorylationLETSGWKSMVVSHPH
HHHCCCCCEECCCHH
15.4230257219
344PhosphorylationGWKSMVVSHPHLVAE
CCCCEECCCHHHHHH
21.6430257219
353PhosphorylationPHLVAEAYRSLASAQ
HHHHHHHHHHHHHCC
7.7022817900

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
6SPhosphorylationKinaseCDK4P11802
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPOP_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SPOP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPPA2_HUMANDPPA2physical
16189514
RTN3_HUMANRTN3physical
16189514
SIR2_HUMANSIRT2physical
17353931
DOK2_HUMANDOK2physical
17353931
IMA7_HUMANKPNA6physical
17353931
GDIA_HUMANGDI1physical
17353931
PI51B_HUMANPIP5K1Bphysical
17353931
TRAF1_HUMANTRAF1physical
11279055
TRAF6_HUMANTRAF6physical
11279055
BMI1_HUMANBMI1physical
15897469
NCOA3_HUMANNCOA3physical
21577200
CUL3_HUMANCUL3physical
21577200
ESR1_HUMANESR1physical
18414007
SPOP_HUMANSPOPphysical
15240113
PI42B_HUMANPIP4K2Bphysical
18218622
NCOA3_HUMANNCOA3physical
23559371
CUL3_HUMANCUL3physical
16524876
DAXX_HUMANDAXXphysical
16524876
SRRM1_HUMANSRRM1physical
21988832
ANDR_HUMANARphysical
24508459
ATM_HUMANATMphysical
24451148
SPOP_HUMANSPOPphysical
25278611
CUL3_HUMANCUL3physical
25278611
ANDR_HUMANARphysical
25274033
BRMS1_HUMANBRMS1physical
22085717
DEK_HUMANDEKphysical
25278611
ERG_HUMANERGphysical
26344095
ERF_HUMANERFphysical
26344095
PRGR_HUMANPGRphysical
26693071
GLI3_HUMANGLI3physical
26475525
ERG_HUMANERGphysical
26344096
UB2D1_HUMANUBE2D1physical
26344096
UB2D2_HUMANUBE2D2physical
26344096
DDIT3_HUMANDDIT3physical
24990631
ESR1_HUMANESR1physical
25766326
SPOP_HUMANSPOPphysical
27220849
GLI3_HUMANGLI3physical
27220849
EGLN2_HUMANEGLN2physical
28089830
GLI2_HUMANGLI2physical
28032859
CUL3_HUMANCUL3physical
28216678
BRD4_HUMANBRD4physical
28805820
BRD3_HUMANBRD3physical
28805820
BRD2_HUMANBRD2physical
28805820

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPOP_HUMAN

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Related Literatures of Post-Translational Modification

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