SHOC2_HUMAN - dbPTM
SHOC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHOC2_HUMAN
UniProt AC Q9UQ13
Protein Name Leucine-rich repeat protein SHOC-2
Gene Name SHOC2
Organism Homo sapiens (Human).
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..
Protein Sequence MSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKDSSAAQPGVAFSVDNTIKRPNPAPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV
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------MSSSLGKEK
------CCCCCCCCC
28.7421406692
3Phosphorylation-----MSSSLGKEKD
-----CCCCCCCCCC
28.4321406692
4Phosphorylation----MSSSLGKEKDS
----CCCCCCCCCCC
33.5621406692
11PhosphorylationSLGKEKDSKEKDPKV
CCCCCCCCCCCCCCC
54.5021406692
14UbiquitinationKEKDSKEKDPKVPSA
CCCCCCCCCCCCCCH
80.9824816145
57PhosphorylationAKDGKKDSSAAQPGV
CCCCCCCCCCCCCCE
30.6528555341
58PhosphorylationKDGKKDSSAAQPGVA
CCCCCCCCCCCCCEE
37.4428555341
71PhosphorylationVAFSVDNTIKRPNPA
EEEEECCCCCCCCCC
24.3430576142
81PhosphorylationRPNPAPGTRKKSSNA
CCCCCCCCCCCCCCH
37.9528857561
85PhosphorylationAPGTRKKSSNAEVIK
CCCCCCCCCCHHHHH
31.6823403867
86PhosphorylationPGTRKKSSNAEVIKE
CCCCCCCCCHHHHHH
49.2729214152
92UbiquitinationSSNAEVIKELNKCRE
CCCHHHHHHHHHHHH
62.4124816145
102PhosphorylationNKCREENSMRLDLSK
HHHHHHHCCCCCCHH
14.4624719451
111PhosphorylationRLDLSKRSIHILPSS
CCCCHHHHEECCCHH
23.4320068231
117PhosphorylationRSIHILPSSIKELTQ
HHEECCCHHHHHHHH
41.0520068231
118PhosphorylationSIHILPSSIKELTQL
HEECCCHHHHHHHHH
35.4220068231
129PhosphorylationLTQLTELYLYSNKLQ
HHHHHHHHHHCCCCC
9.4322210691
131PhosphorylationQLTELYLYSNKLQSL
HHHHHHHHCCCCCCC
9.1722210691
132PhosphorylationLTELYLYSNKLQSLP
HHHHHHHCCCCCCCC
25.5422210691
212UbiquitinationTTVEKDIKNLSKLSM
CCHHHHHHHHHHHHH
63.0729967540
221PhosphorylationLSKLSMLSIRENKIK
HHHHHHHHHHHHHHH
15.8021712546
297PhosphorylationGLRYNRLSAIPRSLA
CCCHHHHCCCCHHHH
22.4024719451
323UbiquitinationNNNISTLPESLLSSL
CCCCCCCCHHHHHHH
29.2623000965
337UbiquitinationLVKLNSLTLARNCFQ
HHHHCHHHHHHHCEE
20.4229967540
337PhosphorylationLVKLNSLTLARNCFQ
HHHHCHHHHHHHCEE
20.4224719451
369UbiquitinationMEHNRINKIPFGIFS
CCCCCCCCCCCCHHH
49.7623000965
376PhosphorylationKIPFGIFSRAKVLSK
CCCCCHHHHHHHHHH
29.43-
383UbiquitinationSRAKVLSKLNMKDNQ
HHHHHHHHCCCCCCC
39.4529967540
393UbiquitinationMKDNQLTSLPLDFGT
CCCCCCCCCCCCCCC
36.2629967540
413UbiquitinationELNLATNQLTKIPED
HHHHCCCCCCCCCCC
46.2729967540
425UbiquitinationPEDVSGLVSLEVLIL
CCCCCHHCHHHHHHH
7.5729967540
429UbiquitinationSGLVSLEVLILSNNL
CHHCHHHHHHHCCCH
4.9629967540
439UbiquitinationLSNNLLKKLPHGLGN
HCCCHHHHCCCCCCC
68.1929967540
459UbiquitinationELDLEENKLESLPNE
HCCCCCCHHHCCCHH
57.8429967540
471UbiquitinationPNEIAYLKDLQKLVL
CHHHHHHHHHHHHHH
43.6529967540
475UbiquitinationAYLKDLQKLVLTNNQ
HHHHHHHHHHHCCCC
48.1129967540
507PhosphorylationGLGENLLTHLPEEIG
CCCHHHHHCCCHHHC
25.24-
566PhosphorylationQIVAGGPSFIIQFLK
CCCCCCCHHHHHHHH
32.14-
578PhosphorylationFLKMQGPYRAMV---
HHHHCCCCCCCC---
20.1621609022

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
71TPhosphorylationKinasePRKCAP17252
GPS
71TPhosphorylationKinasePRKCDQ05655
GPS
297SPhosphorylationKinasePRKCAP17252
GPS
297SPhosphorylationKinasePRKCDQ05655
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:30865892

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHOC2_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 SHOC2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RASH_HUMANHRASphysical
10783161
RAF1_HUMANRAF1physical
10783161
A4_HUMANAPPphysical
21832049
HUWE1_HUMANHUWE1physical
25022756
PRS8_HUMANPSMC5physical
26519477
RASM_HUMANMRASphysical
26519477
HUWE1_HUMANHUWE1physical
26519477
RAF1_HUMANRAF1physical
26519477

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607721Noonan syndrome-like disorder with loose anagen hair (NSLH)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHOC2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP