SPOPL_HUMAN - dbPTM
SPOPL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPOPL_HUMAN
UniProt AC Q6IQ16
Protein Name Speckle-type POZ protein-like
Gene Name SPOPL
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization Nucleus.
Protein Description Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, but with relatively low efficiency. Cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL are less efficient than ubiquitin ligase complexes containing only SPOP. May function to down-regulate the activity of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that contain SPOP..
Protein Sequence MSREPTPPLPGDMSTGPIAESWCYTQVKVVKFSYMWTINNFSFCREEMGEVLKSSTFSSGPSDKMKWCLRVNPKGLDDESKDYLSLYLLLVSCPKSEVRAKFKFSLLNAKREETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGHTNTNTLKVPECRLAEDLGNLWENTRFTDCSFFVRGQEFKAHKSVLAARSPVFNAMFEHEMEESKKNRVEINDLDPEVFKEMMRFIYTGRAPNLDKMADNLLAAADKYALERLKVMCEEALCSNLSVENVADTLVLADLHSAEQLKAQAIDFINRCSVLRQLGCKDGKNWNSNQATDIMETSGWKSMIQSHPHLVAEAFRALASAQCPQFGIPRKRLKQS
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
6Phosphorylation--MSREPTPPLPGDM
--CCCCCCCCCCCCC
32.5528348404
80PhosphorylationPKGLDDESKDYLSLY
CCCCCHHHHHHHHHH
37.5129083192
83PhosphorylationLDDESKDYLSLYLLL
CCHHHHHHHHHHHHH
11.2629083192
85PhosphorylationDESKDYLSLYLLLVS
HHHHHHHHHHHHHHH
14.5629083192
87PhosphorylationSKDYLSLYLLLVSCP
HHHHHHHHHHHHHCC
7.6029083192
92PhosphorylationSLYLLLVSCPKSEVR
HHHHHHHHCCHHHHH
25.3529083192
96PhosphorylationLLVSCPKSEVRAKFK
HHHHCCHHHHHHHHH
26.8529083192
105O-linked_GlycosylationVRAKFKFSLLNAKRE
HHHHHHHHHHHHHHH
32.3230379171
110AcetylationKFSLLNAKREETKAM
HHHHHHHHHHHHHHH
60.3090561
110UbiquitinationKFSLLNAKREETKAM
HHHHHHHHHHHHHHH
60.3029967540
163UbiquitinationTLFCEVSVVQDSVNI
EEEEEEEEEECCEEE
5.6022817900
204UbiquitinationTRFTDCSFFVRGQEF
CCCCCCEEEECCCHH
9.1422817900
215UbiquitinationGQEFKAHKSVLAARS
CCHHHHCHHHHHHHC
47.3129967540
236PhosphorylationFEHEMEESKKNRVEI
HHHHHHHHHHCCCCH
35.3130576142
260PhosphorylationEMMRFIYTGRAPNLD
HHHHHHHHCCCCCHH
18.5124719451
279UbiquitinationNLLAAADKYALERLK
HHHHHHHHHHHHHHH
27.9122817900

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

Oops, there are no upstream regulatory protein records of SPOPL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPOPL_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 SPOPL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPS15_HUMANEPS15physical
27008177

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

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Related Literatures of Post-Translational Modification

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