SHOC2_MOUSE - dbPTM
SHOC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHOC2_MOUSE
UniProt AC O88520
Protein Name Leucine-rich repeat protein SHOC-2
Gene Name Shoc2
Organism Mus musculus (Mouse).
Sequence Length 582
Subcellular Localization Cytoplasm. Nucleus. Translocates from cytoplasm to nucleus upon growth factor stimulation..
Protein Description Regulatory subunit of protein phosphatase 1 (PP1c) that acts as a M-Ras/MRAS effector and participates in MAPK pathway activation. Upon M-Ras/MRAS activation, targets PP1c to specifically dephosphorylate the 'Ser-259' inhibitory site of RAF1 kinase and stimulate RAF1 activity at specialized signaling complexes (By similarity)..
Protein Sequence MSSSLGKEKDSKEKDPKVPSAKEREKESKASGGFGKESKEKEPKAKGKDAKDGKKESSAAQPGVAFSVDNTIKRPNPAPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPPSVKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLPKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNDLLDLPDTIGNLSSLNRLGLRYNRLSAIPRSLAKCSALEELNLENNNISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLSTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV
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
20PhosphorylationEKDPKVPSAKEREKE
CCCCCCCCHHHHHHH
55.7625338131
28PhosphorylationAKEREKESKASGGFG
HHHHHHHHHHCCCCC
44.5920495213
41AcetylationFGKESKEKEPKAKGK
CCHHHHCCCCHHCCC
80.9719849151
67PhosphorylationAQPGVAFSVDNTIKR
CCCCEEEEECCCCCC
20.8722871156
71PhosphorylationVAFSVDNTIKRPNPA
EEEEECCCCCCCCCC
24.3429899451
85PhosphorylationAPGTRKKSSNAEVIK
CCCCCCCCCCHHHHH
31.6827841257
102PhosphorylationNKCREENSMRLDLSK
HHHHHHHCCCCCCHH
14.4624719451
111PhosphorylationRLDLSKRSIHILPPS
CCCCHHCCEECCCCC
23.43-
118PhosphorylationSIHILPPSVKELTQL
CEECCCCCHHHHHHH
43.83-
131PhosphorylationQLTELYLYSNKLQSL
HHHHHHHHCCCCCCC
9.1728576409
205PhosphorylationYLRFNRITTVEKDIK
HHHHHCCCCHHHHHH
22.8820139300
261PhosphorylationPKEIGNCTQITNLDL
CHHHCCCEECCCCCC
27.3125367039
264PhosphorylationIGNCTQITNLDLQHN
HCCCEECCCCCCCCC
21.6625367039
279PhosphorylationDLLDLPDTIGNLSSL
CHHCCCCCCCCHHHH
28.9225367039
284PhosphorylationPDTIGNLSSLNRLGL
CCCCCCHHHHHHHCC
36.4625367039
285PhosphorylationDTIGNLSSLNRLGLR
CCCCCHHHHHHHCCC
32.6025367039
297PhosphorylationGLRYNRLSAIPRSLA
CCCHHHHCCCCHHHH
22.4022942356
369UbiquitinationMEHNRINKIPFGIFS
CCCCCCCCCCCCHHH
49.7622790023
383UbiquitinationSRAKVLSKLNMKDNQ
HHHHHHHHCCCCCCC
39.4527667366
485PhosphorylationLTNNQLSTLPRGIGH
HCCCCCCCCCCCCHH
49.7422067460
578PhosphorylationFLKMQGPYRAMV---
HHHHCCCCCCCC---
20.1629514104

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
-KUbiquitinationE3 ubiquitin ligaseFbxw7Q8VBV4
PMID:30865892

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHOC2_MOUSE !!

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 SHOC2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ROAA_HUMANHNRNPABphysical
20360068
RBMX_HUMANRBMXphysical
20360068
NACAM_HUMANNACAphysical
20360068
NACA_HUMANNACAphysical
20360068
PAIRB_HUMANSERBP1physical
20360068
FUS_HUMANFUSphysical
20360068
TCP4_HUMANSUB1physical
20360068
SGT1_HUMANSUGT1physical
20360068
LAP2A_HUMANTMPOphysical
20360068
LAP2B_HUMANTMPOphysical
20360068
SHOC2_HUMANSHOC2physical
20360068
SCRIB_HUMANSCRIBphysical
20360068
HNRPD_HUMANHNRNPDphysical
20360068
ACACA_HUMANACACAphysical
26496610
CLPT1_HUMANCLPTM1physical
26496610
FOXM1_HUMANFOXM1physical
26496610
GABP1_HUMANGABPB1physical
26496610
GALT2_HUMANGALNT2physical
26496610
GMDS_HUMANGMDSphysical
26496610
PGBM_HUMANHSPG2physical
26496610
I5P2_HUMANINPP5Bphysical
26496610
JAK1_HUMANJAK1physical
26496610
IMA3_HUMANKPNA4physical
26496610
MK07_HUMANMAPK7physical
26496610
PSMD5_HUMANPSMD5physical
26496610
STX3_HUMANSTX3physical
26496610
ICAM5_HUMANICAM5physical
26496610
RBM10_HUMANRBM10physical
26496610
REPS2_HUMANREPS2physical
26496610
RECQ5_HUMANRECQL5physical
26496610
ITM2B_HUMANITM2Bphysical
26496610
1433T_HUMANYWHAQphysical
26496610
PEG10_HUMANPEG10physical
26496610
TNR6B_HUMANTNRC6Bphysical
26496610
PNISR_HUMANPNISRphysical
26496610
LTN1_HUMANLTN1physical
26496610
RM48_HUMANMRPL48physical
26496610
RSF1_HUMANRSF1physical
26496610
WDR60_HUMANWDR60physical
26496610
IMPCT_HUMANIMPACTphysical
26496610
GL8D1_HUMANGLT8D1physical
26496610
HMCES_HUMANHMCESphysical
26496610
TBC24_HUMANTBC1D24physical
26496610
DEFM_HUMANPDFphysical
26496610
NOL10_HUMANNOL10physical
26496610
CDCA3_HUMANCDCA3physical
26496610
AHNK2_HUMANAHNAK2physical
26496610
EME1_HUMANEME1physical
26496610
DAB2P_HUMANDAB2IPphysical
26496610
PLBL2_HUMANPLBD2physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHOC2_MOUSE

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Related Literatures of Post-Translational Modification

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