STRAB_HUMAN - dbPTM
STRAB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRAB_HUMAN
UniProt AC Q9C0K7
Protein Name STE20-related kinase adapter protein beta
Gene Name STRADB
Organism Homo sapiens (Human).
Sequence Length 418
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation (By similarity)..
Protein Sequence MSLLDCFCTSRTQVESLRPEKQSETSIHQYLVDEPTLSWSRPSTRASEVLCSTNVSHYELQVEIGRGFDNLTSVHLARHTPTGTLVTIKITNLENCNEERLKALQKAVILSHFFRHPNITTYWTVFTVGSWLWVISPFMAYGSASQLLRTYFPEGMSETLIRNILFGAVRGLNYLHQNGCIHRSIKASHILISGDGLVTLSGLSHLHSLVKHGQRHRAVYDFPQFSTSVQPWLSPELLRQDLHGYNVKSDIYSVGITACELASGQVPFQDMHRTQMLLQKLKGPPYSPLDISIFPQSESRMKNSQSGVDSGIGESVLVSSGTHTVNSDRLHTPSSKTFSPAFFSLVQLCLQQDPEKRPSASSLLSHVFFKQMKEESQDSILSLLPPAYNKPSISLPPVLPWTEPECDFPDEKDSYWEF
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
87PhosphorylationTPTGTLVTIKITNLE
CCCCCEEEEEEECCC
21.4822210691
159PhosphorylationFPEGMSETLIRNILF
CCCCCCHHHHHHHHH
21.8518491316
297PhosphorylationDISIFPQSESRMKNS
CEEECCCCHHHHHCC
37.4629759185
299PhosphorylationSIFPQSESRMKNSQS
EECCCCHHHHHCCCC
42.8129759185
304PhosphorylationSESRMKNSQSGVDSG
CHHHHHCCCCCCCCC
21.8727050516
306PhosphorylationSRMKNSQSGVDSGIG
HHHHCCCCCCCCCCC
40.3721712546
310PhosphorylationNSQSGVDSGIGESVL
CCCCCCCCCCCCEEE
29.88-
315PhosphorylationVDSGIGESVLVSSGT
CCCCCCCEEEEECCC
18.6121712546
319PhosphorylationIGESVLVSSGTHTVN
CCCEEEEECCCCEEC
20.9126471730
320PhosphorylationGESVLVSSGTHTVNS
CCEEEEECCCCEECC
39.9926471730
322PhosphorylationSVLVSSGTHTVNSDR
EEEEECCCCEECCCC
19.1326471730
324PhosphorylationLVSSGTHTVNSDRLH
EEECCCCEECCCCCC
22.6326471730
327PhosphorylationSGTHTVNSDRLHTPS
CCCCEECCCCCCCCC
21.5526471730
370UbiquitinationLLSHVFFKQMKEESQ
HHHHHHHHHHHHHCH
37.7132015554
376PhosphorylationFKQMKEESQDSILSL
HHHHHHHCHHHHHHH
40.1429978859
379PhosphorylationMKEESQDSILSLLPP
HHHHCHHHHHHHCCC
20.1429978859
382PhosphorylationESQDSILSLLPPAYN
HCHHHHHHHCCCCCC
26.6229978859
388PhosphorylationLSLLPPAYNKPSISL
HHHCCCCCCCCCCCC
29.5029978859

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 STRAB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRAB_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 STRAB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STK11_HUMANSTK11physical
28514442
CAB39_HUMANCAB39physical
28514442
NBEA_HUMANNBEAphysical
28514442
KS6A2_HUMANRPS6KA2physical
28514442
KS6A3_HUMANRPS6KA3physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
TCPB_HUMANCCT2physical
28514442
TCPG_HUMANCCT3physical
28514442
TCPH_HUMANCCT7physical
28514442

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 STRAB_HUMAN

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Related Literatures of Post-Translational Modification

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