SPSB1_HUMAN - dbPTM
SPSB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPSB1_HUMAN
UniProt AC Q96BD6
Protein Name SPRY domain-containing SOCS box protein 1
Gene Name SPSB1
Organism Homo sapiens (Human).
Sequence Length 273
Subcellular Localization Cytoplasm .
Protein Description Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins..
Protein Sequence MGQKVTGGIKTVDMRDPTYRPLKQELQGLDYCKPTRLDLLLDMPPVSYDVQLLHSWNNNDRSLNVFVKEDDKLIFHRHPVAQSTDAIRGKVGYTRGLHVWQITWAMRQRGTHAVVGVATADAPLHSVGYTTLVGNNHESWGWDLGRNRLYHDGKNQPSKTYPAFLEPDETFIVPDSFLVALDMDDGTLSFIVDGQYMGVAFRGLKGKKLYPVVSAVWGHCEIRMRYLNGLDPEPLPLMDLCRRSVRLALGRERLGEIHTLPLPASLKAYLLYQ
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
4Acetylation----MGQKVTGGIKT
----CCCCCCCCCEE
35.7170841
10AcetylationQKVTGGIKTVDMRDP
CCCCCCCEECCCCCC
45.8570845
10UbiquitinationQKVTGGIKTVDMRDP
CCCCCCCEECCCCCC
45.8521906983
18PhosphorylationTVDMRDPTYRPLKQE
ECCCCCCCCCCHHHH
36.1324719451
19PhosphorylationVDMRDPTYRPLKQEL
CCCCCCCCCCHHHHH
18.6724719451
31PhosphorylationQELQGLDYCKPTRLD
HHHCCCCCCCCCCCC
13.8615601820
68UbiquitinationRSLNVFVKEDDKLIF
CEEEEEEEECCEEEE
43.92-
72UbiquitinationVFVKEDDKLIFHRHP
EEEEECCEEEEECCC
56.66-

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
31YPhosphorylationKinaseMETP08581
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPSB1_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 SPSB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOS2_HUMANNOS2physical
21199876
NOS2_HUMANNOS2physical
21549100
NOS2_HUMANNOS2physical
20603330
PAWR_HUMANPAWRphysical
20561531
DDX4_HUMANDDX4physical
20561531
DDX4_MOUSEDdx4physical
20561531
PAWR_MOUSEPawrphysical
20561531
MET_HUMANMETphysical
15713673
RASA1_HUMANRASA1physical
15713673
CUL5_HUMANCUL5physical
15601820
RBX2_HUMANRNF7physical
15601820
ELOB_HUMANTCEB2physical
15601820
ELOC_HUMANTCEB1physical
15601820
KDM1A_HUMANKDM1Aphysical
23455924
ANM1_HUMANPRMT1physical
23455924
ANM6_HUMANPRMT6physical
23455924
SUV91_HUMANSUV39H1physical
23455924
TGFR2_HUMANTGFBR2physical
26032413
TGFR2_MOUSETgfbr2physical
26032413

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 SPSB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts withMET and enhances the hepatocyte growth factor-induced Erk-Elk-1-serumresponse element pathway.";
Wang D., Li Z., Messing E.M., Wu G.;
J. Biol. Chem. 280:16393-16401(2005).
Cited for: INTERACTION WITH MET AND RASA1, PHOSPHORYLATION AT TYR-31, ANDMUTAGENESIS OF TYR-31.

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