1433T_RAT - dbPTM
1433T_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 1433T_RAT
UniProt AC P68255
Protein Name 14-3-3 protein theta
Gene Name Ywhaq
Organism Rattus norvegicus (Rat).
Sequence Length 245
Subcellular Localization Cytoplasm.
Protein Description Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity)..
Protein Sequence MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN
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
1Acetylation-------MEKTELIQ
-------CCHHHHHH
12.29-
3Acetylation-----MEKTELIQKA
-----CCHHHHHHHH
46.1022902405
9UbiquitinationEKTELIQKAKLAEQA
CHHHHHHHHHHHHHH
40.26-
11AcetylationTELIQKAKLAEQAER
HHHHHHHHHHHHHHH
56.0972611869
11UbiquitinationTELIQKAKLAEQAER
HHHHHHHHHHHHHHH
56.09-
45PhosphorylationNEERNLLSVAYKNVV
HHHHHHHHHHHHCHH
14.1027097102
48PhosphorylationRNLLSVAYKNVVGGR
HHHHHHHHHCHHCCC
10.8423984901
49UbiquitinationNLLSVAYKNVVGGRR
HHHHHHHHCHHCCCH
33.26-
49AcetylationNLLSVAYKNVVGGRR
HHHHHHHHCHHCCCH
33.2622902405
63PhosphorylationRSAWRVISSIEQKTD
HHHHHHHHHHHHCCC
23.5425403869
64PhosphorylationSAWRVISSIEQKTDT
HHHHHHHHHHHCCCC
21.0122673903
68AcetylationVISSIEQKTDTSDKK
HHHHHHHCCCCCHHH
35.2622902405
68UbiquitinationVISSIEQKTDTSDKK
HHHHHHHCCCCCHHH
35.26-
74AcetylationQKTDTSDKKLQLIKD
HCCCCCHHHHHHHHH
55.9722902405
82NitrationKLQLIKDYREKVESE
HHHHHHHHHHHHHHH
18.70-
85AcetylationLIKDYREKVESELRS
HHHHHHHHHHHHHHH
42.1622902405
92PhosphorylationKVESELRSICTTVLE
HHHHHHHHHHHHHHH
34.34-
104NitrationVLELLDKYLIANATN
HHHHHHHHHHHCCCC
11.74-
115AcetylationNATNPESKVFYLKMK
CCCCCCCCEEEEEEC
34.4022902405
120UbiquitinationESKVFYLKMKGDYFR
CCCEEEEEECCCHHH
27.47-
120AcetylationESKVFYLKMKGDYFR
CCCEEEEEECCCHHH
27.4713580569
122AcetylationKVFYLKMKGDYFRYL
CEEEEEECCCHHHHH
47.2224623897
139UbiquitinationVACGDDRKQTIENSQ
HHCCCCHHHHHHHCC
59.80-
157AcetylationQEAFDISKKEMQPTH
HHHHHCCHHHCCCCC
53.7622902405
157UbiquitinationQEAFDISKKEMQPTH
HHHHHCCHHHCCCCC
53.76-
210PhosphorylationLDTLNEDSYKDSTLI
HHCCCCCCCCCHHHH
28.0922673903
214PhosphorylationNEDSYKDSTLIMQLL
CCCCCCCHHHHHHHH
22.4422673903
215PhosphorylationEDSYKDSTLIMQLLR
CCCCCCHHHHHHHHH
30.3622673903
226PhosphorylationQLLRDNLTLWTSDSA
HHHHCCCEEEECCCC
26.8928551015
229PhosphorylationRDNLTLWTSDSAGEE
HCCCEEEECCCCCCC
26.2627097102
230PhosphorylationDNLTLWTSDSAGEEC
CCCEEEECCCCCCCC
20.2727097102
232PhosphorylationLTLWTSDSAGEECDA
CEEEECCCCCCCCCH
37.6327097102

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
232SPhosphorylationKinaseCK1-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 1433T_RAT !!

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 1433T_RAT !!

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

Oops, there are no PPI records of 1433T_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 1433T_RAT

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Related Literatures of Post-Translational Modification

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