STK25_HUMAN - dbPTM
STK25_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STK25_HUMAN
UniProt AC O00506
Protein Name Serine/threonine-protein kinase 25
Gene Name STK25
Organism Homo sapiens (Human).
Sequence Length 426
Subcellular Localization Cytoplasm . Golgi apparatus . Localizes to the Golgi apparatus.
Protein Description Oxidant stress-activated serine/threonine kinase that may play a role in the response to environmental stress. Targets to the Golgi apparatus where it appears to regulate protein transport events, cell adhesion, and polarity complexes important for cell migration..
Protein Sequence MAHLRGFANQHSRVDPEELFTKLDRIGKGSFGEVYKGIDNHTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYFGSYLKSTKLWIIMEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFLTELIDRYKRWKSEGHGEESSSEDSDIDGEAEDGEQGPIWTFPPTIRPSPHSKLHKGTALHSSQKPAEPVKRQPRSQCLSTLVRPVFGELKEKHKQSGGSVGALEELENAFSLAEESCPGISDKLMVHLVERVQRFSHNRNHLTSTR
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
12PhosphorylationRGFANQHSRVDPEEL
CCCCCCCCCCCHHHH		25.0028857561
22UbiquitinationDPEELFTKLDRIGKG
CHHHHHHHHHHHCCC		40.84-
28UbiquitinationTKLDRIGKGSFGEVY
HHHHHHCCCCHHHHH		49.35-
30PhosphorylationLDRIGKGSFGEVYKG
HHHHCCCCHHHHHCC		33.30-
35PhosphorylationKGSFGEVYKGIDNHT
CCCHHHHHCCCCCCC		10.13-
36UbiquitinationGSFGEVYKGIDNHTK
CCHHHHHCCCCCCCC		55.34-
43UbiquitinationKGIDNHTKEVVAIKI
CCCCCCCCEEEEEEE		40.75-
48UbiquitinationHTKEVVAIKIIDLEE
CCCEEEEEEEEEHHH		1.9121906983
65UbiquitinationDEIEDIQQEITVLSQ
HHHHHHHHHHHHHHH		44.3821906983
78UbiquitinationSQCDSPYITRYFGSY
HHCCCHHHHHHHHHH		1.69-
94UbiquitinationKSTKLWIIMEYLGGG
HHCCEEEEEEHHCCC		0.86-
97PhosphorylationKLWIIMEYLGGGSAL
CEEEEEEHHCCCCHH		8.02-
126AcetylationTILREILKGLDYLHS
HHHHHHHHHHHHHHH		64.1923236377
142UbiquitinationRKIHRDIKAANVLLS
CHHHHCHHHHHHHHC		45.8221906983
155UbiquitinationLSEQGDVKLADFGVA
HCCCCCCCCCCEECC		42.57-
166PhosphorylationFGVAGQLTDTQIKRN
EECCCCCCCCCHHHC		29.1630266825
168PhosphorylationVAGQLTDTQIKRNTF
CCCCCCCCCHHHCCC		27.2722322096
171UbiquitinationQLTDTQIKRNTFVGT
CCCCCCHHHCCCCCC		29.76-
174PhosphorylationDTQIKRNTFVGTPFW
CCCHHHCCCCCCCCC		24.5922322096
178PhosphorylationKRNTFVGTPFWMAPE
HHCCCCCCCCCCCHH		15.2630266825
199UbiquitinationYDFKADIWSLGITAI
CCCCHHHHHCCEEHH		6.51-
216PhosphorylationAKGEPPNSDLHPMRV
HCCCCCCCCCCCEEE		47.5323879269
231PhosphorylationLFLIPKNSPPTLEGQ
EEEEECCCCCCCCCC		38.0823403867
234PhosphorylationIPKNSPPTLEGQHSK
EECCCCCCCCCCCCC		40.6023186163
240PhosphorylationPTLEGQHSKPFKEFV
CCCCCCCCCCHHHHH		33.8523403867
241UbiquitinationTLEGQHSKPFKEFVE
CCCCCCCCCHHHHHH		52.96-
253UbiquitinationFVEACLNKDPRFRPT
HHHHHHCCCCCCCCC		57.04-
262UbiquitinationPRFRPTAKELLKHKF
CCCCCCHHHHHHCCH		51.91-
276UbiquitinationFITRYTKKTSFLTEL
HHHHCCCHHHHHHHH		41.42-
277PhosphorylationITRYTKKTSFLTELI
HHHCCCHHHHHHHHH		26.6828450419
278PhosphorylationTRYTKKTSFLTELID
HHCCCHHHHHHHHHH		27.4328450419
281PhosphorylationTKKTSFLTELIDRYK
CCHHHHHHHHHHHHH		27.0828450419
335UbiquitinationSPHSKLHKGTALHSS
CCCCCCCCCCCCCCC		69.28-
337PhosphorylationHSKLHKGTALHSSQK
CCCCCCCCCCCCCCC		30.7423312004
341PhosphorylationHKGTALHSSQKPAEP
CCCCCCCCCCCCCCC		35.0028555341
342PhosphorylationKGTALHSSQKPAEPV
CCCCCCCCCCCCCCC		31.3228857561
350AcetylationQKPAEPVKRQPRSQC
CCCCCCCCCCCHHHH		56.9125953088
360PhosphorylationPRSQCLSTLVRPVFG
CHHHHHHHHHHHHHH		19.14-
376PhosphorylationLKEKHKQSGGSVGAL
HHHHHHHCCCCHHHH		50.3428102081
379PhosphorylationKHKQSGGSVGALEEL
HHHHCCCCHHHHHHH		22.3928348404
416PhosphorylationVERVQRFSHNRNHLT
HHHHHHHHHCCCCCC		23.2626074081
423PhosphorylationSHNRNHLTSTR----
HHCCCCCCCCC----		22.0926074081
424PhosphorylationHNRNHLTSTR-----
HCCCCCCCCC-----		28.6626074081
425PhosphorylationNRNHLTSTR------
CCCCCCCCC------		34.8526074081
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
174TPhosphorylationKinaseSTK25O00506
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STK25_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 STK25_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDC10_HUMANPDCD10physical
16189514
2AAA_HUMANPPP2R1Aphysical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
STRN_HUMANSTRNphysical
18782753
STRP1_HUMANSTRIP1physical
18782753
STRN3_HUMANSTRN3physical
18782753
2AAB_HUMANPPP2R1Bphysical
18782753
STRN4_HUMANSTRN4physical
18782753
PHOCN_HUMANMOB4physical
18782753
PDC10_HUMANPDCD10physical
18782753
CT2NL_HUMANCTTNBP2NLphysical
18782753
SIKE1_HUMANSIKE1physical
18782753
STRP2_HUMANSTRIP2physical
18782753
SLMAP_HUMANSLMAPphysical
18782753
TCPA_HUMANTCP1physical
18782753
FGOP2_HUMANFGFR1OP2physical
18782753
A4_HUMANAPPphysical
21832049
STRN_HUMANSTRNphysical
23455922
2AAA_HUMANPPP2R1Aphysical
23455922
2AAB_HUMANPPP2R1Bphysical
23455922
PP2AB_HUMANPPP2CBphysical
23455922
DYL1_HUMANDYNLL1physical
23455922
PP2AA_HUMANPPP2CAphysical
23455922
GOGA2_HUMANGOLGA2physical
23455922
STRN3_HUMANSTRN3physical
23455922
ACACA_HUMANACACAphysical
23455922
SLMAP_HUMANSLMAPphysical
23455922
TAOK1_HUMANTAOK1physical
23455922
CTTB2_HUMANCTTNBP2physical
23455922
SIKE1_HUMANSIKE1physical
23455922
PDC10_HUMANPDCD10physical
23455922
STRN4_HUMANSTRN4physical
23455922
FGOP2_HUMANFGFR1OP2physical
23455922
STK26_HUMANSTK26physical
23455922
CT2NL_HUMANCTTNBP2NLphysical
23455922
STRP2_HUMANSTRIP2physical
23455922
PHOCN_HUMANMOB4physical
23455922
PDC10_HUMANPDCD10physical
25416956
CCDB1_HUMANCCNDBP1physical
25416956
CEP70_HUMANCEP70physical
25416956
IHO1_HUMANCCDC36physical
25416956
ACD11_HUMANACAD11physical
26186194
STK26_HUMANSTK26physical
26186194
STK24_HUMANSTK24physical
26186194
STRN_HUMANSTRNphysical
26186194
STRN3_HUMANSTRN3physical
26186194
PDC10_HUMANPDCD10physical
26186194
GOGA2_HUMANGOLGA2physical
26186194
PAPD1_HUMANMTPAPphysical
26186194
TAOK1_HUMANTAOK1physical
26186194
TAOK2_HUMANTAOK2physical
26186194
ARV1_HUMANARV1physical
26186194
HBS1L_HUMANHBS1Lphysical
26186194
GORS1_HUMANGORASP1physical
26186194
KI20A_HUMANKIF20Aphysical
26186194
CAB39_HUMANCAB39physical
26186194
MTMR6_HUMANMTMR6physical
26186194
STRP1_HUMANSTRIP1physical
26186194
CT2NL_HUMANCTTNBP2NLphysical
26186194
ZN598_HUMANZNF598physical
26186194
PDC10_HUMANPDCD10physical
21516116
STK24_HUMANSTK24physical
28514442
STK26_HUMANSTK26physical
28514442
TAOK1_HUMANTAOK1physical
28514442
CAB39_HUMANCAB39physical
28514442
TAOK2_HUMANTAOK2physical
28514442
GOGA2_HUMANGOLGA2physical
28514442
KI20A_HUMANKIF20Aphysical
28514442
CT2NL_HUMANCTTNBP2NLphysical
28514442
STRP1_HUMANSTRIP1physical
28514442
HBS1L_HUMANHBS1Lphysical
28514442
ZN598_HUMANZNF598physical
28514442
STRN_HUMANSTRNphysical
28514442
STRN3_HUMANSTRN3physical
28514442
GORS1_HUMANGORASP1physical
28514442
MTMR6_HUMANMTMR6physical
28514442
PBX2_HUMANPBX2physical
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 STK25_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168 AND SER-342, ANDMASS SPECTROMETRY.
"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 THR-168 AND THR-174, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168, AND MASSSPECTROMETRY.
"YSK1 is activated by the Golgi matrix protein GM130 and plays a rolein cell migration through its substrate 14-3-3zeta.";
Preisinger C., Short B., De Corte V., Bruyneel E., Haas A.,Kopajtich R., Gettemans J., Barr F.A.;
J. Cell Biol. 164:1009-1020(2004).
Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-174, SUBCELLULARLOCATION, INTERACTION WITH GOLGA2, AND MUTAGENESIS OF LYS-49 ANDASP-158.

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