STAP1_HUMAN - dbPTM
STAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAP1_HUMAN
UniProt AC Q9ULZ2
Protein Name Signal-transducing adaptor protein 1
Gene Name STAP1
Organism Homo sapiens (Human).
Sequence Length 295
Subcellular Localization Nucleus . Cytoplasm . Mitochondrion .
Protein Description In BCR signaling, appears to function as a docking protein acting downstream of TEC and participates in a positive feedback loop by increasing the activity of TEC..
Protein Sequence MMAKKPPKPAPRRIFQERLKITALPLYFEGFLLIKRSGYREYEHYWTELRGTTLFFYTDKKSIIYVDKLDIVDLTCLTEQNSTEKNCAKFTLVLPKEEVQLKTENTESGEEWRGFILTVTELSVPQNVSLLPGQVIKLHEVLEREKKRRIETEQSTSVEKEKEPTEDYVDVLNPMPACFYTVSRKEATEMLQKNPSLGNMILRPGSDSRNYSITIRQEIDIPRIKHYKVMSVGQNYTIELEKPVTLPNLFSVIDYFVKETRGNLRPFICSTDENTGQEPSMEGRSEKLKKNPHIA
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
22PhosphorylationFQERLKITALPLYFE
HHHHHCEEEECCEEE
22.13-
27PhosphorylationKITALPLYFEGFLLI
CEEEECCEEEEEEEE
9.54-
42PhosphorylationKRSGYREYEHYWTEL
ECCCCCCEEEEEEEE
10.06-
45PhosphorylationGYREYEHYWTELRGT
CCCCEEEEEEEECCC
11.33-
57PhosphorylationRGTTLFFYTDKKSII
CCCEEEEEECCCEEE
13.49-
65PhosphorylationTDKKSIIYVDKLDIV
ECCCEEEEEECCCEE
10.8328064214
82PhosphorylationTCLTEQNSTEKNCAK
EEECCCCCCCCCEEE
37.3225627689
83PhosphorylationCLTEQNSTEKNCAKF
EECCCCCCCCCEEEE
59.5325627689
152PhosphorylationEKKRRIETEQSTSVE
HHHHCCCCCCCCCCC
36.6328634120
155PhosphorylationRRIETEQSTSVEKEK
HCCCCCCCCCCCCCC
19.2028634120
156PhosphorylationRIETEQSTSVEKEKE
CCCCCCCCCCCCCCC
36.1629449344
157PhosphorylationIETEQSTSVEKEKEP
CCCCCCCCCCCCCCC
33.2629449344
165PhosphorylationVEKEKEPTEDYVDVL
CCCCCCCCCCHHHHH
42.4527155012
168PhosphorylationEKEPTEDYVDVLNPM
CCCCCCCHHHHHCCC
7.7227155012
181PhosphorylationPMPACFYTVSRKEAT
CCCCEEEEEEHHHHH
7.5527762562
196PhosphorylationEMLQKNPSLGNMILR
HHHHHCCCCCCCEEC
59.3016964243
206PhosphorylationNMILRPGSDSRNYSI
CCEECCCCCCCCEEE
34.7930108239
208PhosphorylationILRPGSDSRNYSITI
EECCCCCCCCEEEEE
24.9130108239

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 STAP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAP1_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 STAP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH3K1_HUMANSH3KBP1physical
25416956
RETR3_HUMANFAM134Cphysical
25416956
CD2AP_HUMANCD2APphysical
26186194
ST1A1_HUMANSULT1A1physical
26186194
SH3K1_HUMANSH3KBP1physical
26186194
CAZA2_HUMANCAPZA2physical
26186194
CAPZB_HUMANCAPZBphysical
26186194
SH3K1_HUMANSH3KBP1physical
21516116
SH3K1_HUMANSH3KBP1physical
28514442
CD2AP_HUMANCD2APphysical
28514442
ST1A1_HUMANSULT1A1physical
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 STAP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND MASSSPECTROMETRY.

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