ST17B_HUMAN - dbPTM
ST17B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ST17B_HUMAN
UniProt AC O94768
Protein Name Serine/threonine-protein kinase 17B
Gene Name STK17B
Organism Homo sapiens (Human).
Sequence Length 372
Subcellular Localization Nucleus . Cell membrane. Endoplasmic reticulum-Golgi intermediate compartment. Colocalizes with STK17B at the plasma membrane..
Protein Description Phosphorylates myosin light chains (By similarity). Acts as a positive regulator of apoptosis..
Protein Sequence MSRRRFDCRSISGLLTTTPQIPIKMENFNNFYILTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSCPRVINLHEVYENTSEIILILEYAAGGEIFSLCLPELAEMVSENDVIRLIKQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGIIAYMLLTHTSPFVGEDNQETYLNISQVNVDYSEETFSSVSQLATDFIQSLLVKNPEKRPTAEICLSHSWLQQWDFENLFHPEETSSSSQTQDHSVRSSEDKTSKSSCNGTCGDREDKENIPEDSSMVSKRFRFDDSLPNPHELVSDLLC
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
10PhosphorylationRRRFDCRSISGLLTT
CCCCCCCCCCCCCCC
27.6928102081
12PhosphorylationRFDCRSISGLLTTTP
CCCCCCCCCCCCCCC
25.3228102081
16PhosphorylationRSISGLLTTTPQIPI
CCCCCCCCCCCCCCE
33.4030108239
17PhosphorylationSISGLLTTTPQIPIK
CCCCCCCCCCCCCEE
36.1327080861
18PhosphorylationISGLLTTTPQIPIKM
CCCCCCCCCCCCEEE
14.1427080861
37UbiquitinationNFYILTSKELGRGKF
CEEEEEECCCCCCCC
52.29-
43AcetylationSKELGRGKFAVVRQC
ECCCCCCCCHHHHHH
28.8725953088
43UbiquitinationSKELGRGKFAVVRQC
ECCCCCCCCHHHHHH
28.87-
53UbiquitinationVVRQCISKSTGQEYA
HHHHHHCCCCCHHHH
31.93-
62UbiquitinationTGQEYAAKFLKKRRR
CCHHHHHHHHHHHHC
42.95-
65UbiquitinationEYAAKFLKKRRRGQD
HHHHHHHHHHHCCCC
47.57-
88UbiquitinationIAVLELAKSCPRVIN
HHHHHHHHHCCCEEE
66.28-
185UbiquitinationVDFGMSRKIGHACEL
EECCCCCCCCCHHHH
45.81-
333PhosphorylationSKSSCNGTCGDREDK
CCCCCCCCCCCCCCC
10.18-
347PhosphorylationKENIPEDSSMVSKRF
CCCCCCCCCHHHHHH
20.7628509920
348PhosphorylationENIPEDSSMVSKRFR
CCCCCCCCHHHHHHC
35.2128509920
351PhosphorylationPEDSSMVSKRFRFDD
CCCCCHHHHHHCCCC
14.9628509920
352UbiquitinationEDSSMVSKRFRFDDS
CCCCHHHHHHCCCCC
44.11-
359PhosphorylationKRFRFDDSLPNPHEL
HHHCCCCCCCCHHHH
47.7928348404

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 ST17B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ST17B_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 ST17B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ST17B_HUMANSTK17Bphysical
9786912
A4_HUMANAPPphysical
21832049
KFA_HUMANAFMIDphysical
26186194
KCIP2_HUMANKCNIP2physical
26186194
REV3L_HUMANREV3Lphysical
26496610
GTR1_HUMANSLC2A1physical
26496610
TOX4_HUMANTOX4physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
TRIB1_HUMANTRIB1physical
26496610
ATX2L_HUMANATXN2Lphysical
26496610
MDN1_HUMANMDN1physical
26496610
FAF2_HUMANFAF2physical
26496610
WBP11_HUMANWBP11physical
26496610
UBAC2_HUMANUBAC2physical
26496610
KCIP2_HUMANKCNIP2physical
28514442
TPM2_HUMANTPM2physical
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 ST17B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.
"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-10, AND MASSSPECTROMETRY.

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