STRAA_HUMAN - dbPTM
STRAA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRAA_HUMAN
UniProt AC Q7RTN6
Protein Name STE20-related kinase adapter protein alpha
Gene Name STRADA
Organism Homo sapiens (Human).
Sequence Length 431
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..
Protein Sequence MSFLVSKPERIRRWVSEKFIVEGLRDLELFGEQPPGDTRRKTNDASSESIASFSKQEVMSSFLPEGGCYELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEELTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLRPVTPITNFEGSQSQDHSGIFGLVTNLEELEVDDWEF
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
2 (in isoform 2)Phosphorylation-27.5625693802
2 (in isoform 3)Phosphorylation-27.5625693802
2Phosphorylation------MSFLVSKPE
------CCCCCCCHH
27.5625850435
5 (in isoform 2)Phosphorylation-6.9625693802
5 (in isoform 3)Phosphorylation-6.9625693802
9 (in isoform 3)Phosphorylation-65.5628348404
9 (in isoform 2)Phosphorylation-65.5628348404
9PhosphorylationSFLVSKPERIRRWVS
CCCCCCHHHHHHHHC
65.5627251275
10 (in isoform 2)Phosphorylation-35.9228348404
10 (in isoform 3)Phosphorylation-35.9228348404
12 (in isoform 2)Phosphorylation-32.4125693802
12 (in isoform 3)Phosphorylation-32.4125693802
13 (in isoform 6)Phosphorylation-35.4629523821
15 (in isoform 2)Phosphorylation-5.1325693802
15 (in isoform 3)Phosphorylation-5.1325693802
17 (in isoform 2)Phosphorylation-42.2225693802
17 (in isoform 6)Phosphorylation-42.2225849741
17 (in isoform 3)Phosphorylation-42.2225693802
18 (in isoform 6)Phosphorylation-32.6525849741
20 (in isoform 6)Phosphorylation-4.0025849741
23 (in isoform 6)Phosphorylation-18.3425849741
25 (in isoform 6)Phosphorylation-58.2729523821
42PhosphorylationPGDTRRKTNDASSES
CCCCCCCCCCCCHHH
36.2023927012
46PhosphorylationRRKTNDASSESIASF
CCCCCCCCHHHHHHC
37.1923927012
47PhosphorylationRKTNDASSESIASFS
CCCCCCCHHHHHHCC
36.7628985074
49PhosphorylationTNDASSESIASFSKQ
CCCCCHHHHHHCCHH
25.9620363803
52PhosphorylationASSESIASFSKQEVM
CCHHHHHHCCHHHHH
28.5123927012
54PhosphorylationSESIASFSKQEVMSS
HHHHHHCCHHHHHHH
30.8223927012
69PhosphorylationFLPEGGCYELLTVIG
CCCCCCHHHHEEHHC
16.9427050516
91UbiquitinationTVNLARYKPTGEYVT
EEEECCCCCCCCEEE
30.46-
202 (in isoform 3)Ubiquitination-1.6821906983
202 (in isoform 2)Ubiquitination-1.6821906983
212PhosphorylationVDGKVYLSGLRSNLS
ECCEEEEHHHHHCCC
20.3524719451
222PhosphorylationRSNLSMISHGQRQRV
HHCCCEECCCCCCCE
16.9622210691
239UbiquitinationDFPKYSVKVLPWLSP
CCCCCCEEEHHCCCH
31.922190698
239 (in isoform 1)Ubiquitination-31.9221906983
302PhosphorylationTVPCLLDTSTIPAEE
CCCEEEECCCCCHHH
27.9528102081
303PhosphorylationVPCLLDTSTIPAEEL
CCEEEECCCCCHHHC
24.8128348404
304PhosphorylationPCLLDTSTIPAEELT
CEEEECCCCCHHHCC
32.8328348404
311PhosphorylationTIPAEELTMSPSRSV
CCCHHHCCCCCCHHH
20.9122199227
313PhosphorylationPAEELTMSPSRSVAN
CHHHCCCCCCHHHHC
17.9422199227
315PhosphorylationEELTMSPSRSVANSG
HHCCCCCCHHHHCCC
29.8528102081
324PhosphorylationSVANSGLSDSLTTST
HHHCCCCCCCCCCCC
28.7826471730
326PhosphorylationANSGLSDSLTTSTPR
HCCCCCCCCCCCCCC
25.0026657352
328PhosphorylationSGLSDSLTTSTPRPS
CCCCCCCCCCCCCCC
23.7425850435
329PhosphorylationGLSDSLTTSTPRPSN
CCCCCCCCCCCCCCC
35.5822817900
330PhosphorylationLSDSLTTSTPRPSNG
CCCCCCCCCCCCCCC
31.0426471730
387PhosphorylationKQIKRRASEALPELL
HHHHHHHHHHHHHHH
22.9128111955
398PhosphorylationPELLRPVTPITNFEG
HHHHCCCCCCCCCCC
16.2024275569
419PhosphorylationSGIFGLVTNLEELEV
CCEEEEECCHHHCCC
38.8514702039

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
329TPhosphorylationKinaseSTK11Q15831
GPS
419TPhosphorylationKinaseSTK11Q15831
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRAA_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 STRAA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
21860411
STK11_HUMANSTK11physical
21860411

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 STRAA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.
"Activation of the tumour suppressor kinase LKB1 by the STE20-likepseudokinase STRAD.";
Baas A.F., Boudeau J., Sapkota G.P., Smit L., Medema R., Morrice N.A.,Alessi D.R., Clevers H.C.;
EMBO J. 22:3062-3072(2003).
Cited for: IDENTIFICATION (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,INTERACTION WITH STK11/LKB1, MUTAGENESIS OF THR-329 AND THR-419, ANDPHOSPHORYLATION AT THR-329 AND THR-419.

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