STK33_HUMAN - dbPTM
STK33_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STK33_HUMAN
UniProt AC Q9BYT3
Protein Name Serine/threonine-protein kinase 33
Gene Name STK33
Organism Homo sapiens (Human).
Sequence Length 514
Subcellular Localization Cytoplasm, perinuclear region.
Protein Description Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME (By similarity). Not essential for the survival of KRAS-dependent AML cell lines..
Protein Sequence MADSGLDKKSTKCPDCSSASQKDVLCVCSSKTRVPPVLVVEMSQTSSIGSAESLISLERKKEKNINRDITSRKDLPSRTSNVERKASQQQWGRGNFTEGKVPHIRIENGAAIEEIYTFGRILGKGSFGIVIEATDKETETKWAIKKVNKEKAGSSAVKLLEREVNILKSVKHEHIIHLEQVFETPKKMYLVMELCEDGELKEILDRKGHFSENETRWIIQSLASAIAYLHNNDIVHRDLKLENIMVKSSLIDDNNEINLNIKVTDFGLAVKKQSRSEAMLQATCGTPIYMAPEVISAHDYSQQCDIWSIGVVMYMLLRGEPPFLASSEEKLFELIRKGELHFENAVWNSISDCAKSVLKQLMKVDPAHRITAKELLDNQWLTGNKLSSVRPTNVLEMMKEWKNNPESVEENTTEEKNKPSTEEKLKSYQPWGNVPDANYTSDEEEEKQSTAYEKQFPATSKDNFDMCSSSFTSSKLLPAEIKGEMEKTPVTPSQGTATKYPAKSGALSRTKKKL
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
10PhosphorylationDSGLDKKSTKCPDCS
CCCCCCCCCCCCCCC
38.5526670566
11PhosphorylationSGLDKKSTKCPDCSS
CCCCCCCCCCCCCCC
45.6126670566
20PhosphorylationCPDCSSASQKDVLCV
CCCCCCCCCCCEEEE
39.4528961369
29PhosphorylationKDVLCVCSSKTRVPP
CCEEEEECCCCCCCC
17.9330622161
30PhosphorylationDVLCVCSSKTRVPPV
CEEEEECCCCCCCCE
32.6830622161
31UbiquitinationVLCVCSSKTRVPPVL
EEEEECCCCCCCCEE
24.85-
43PhosphorylationPVLVVEMSQTSSIGS
CEEEEECCCCCCCCC
19.4627732954
45PhosphorylationLVVEMSQTSSIGSAE
EEEECCCCCCCCCHH
19.6927732954
46PhosphorylationVVEMSQTSSIGSAES
EEECCCCCCCCCHHH
16.6027732954
47PhosphorylationVEMSQTSSIGSAESL
EECCCCCCCCCHHHH
34.0627732954
50PhosphorylationSQTSSIGSAESLISL
CCCCCCCCHHHHHHH
27.4822199227
53PhosphorylationSSIGSAESLISLERK
CCCCCHHHHHHHHHH
30.6227732954
56PhosphorylationGSAESLISLERKKEK
CCHHHHHHHHHHHHH
29.4829523821
73AcetylationNRDITSRKDLPSRTS
CCCCCCCCCCCCCCC
64.487825429
79PhosphorylationRKDLPSRTSNVERKA
CCCCCCCCCCHHHHH
29.0528555341
85UbiquitinationRTSNVERKASQQQWG
CCCCHHHHHHHHHHC
38.59-
87PhosphorylationSNVERKASQQQWGRG
CCHHHHHHHHHHCCC
31.40-
100UbiquitinationRGNFTEGKVPHIRIE
CCCCCCCCCCEEEEE
46.49-
116PhosphorylationGAAIEEIYTFGRILG
CCCEEEEEEHHHHHC
10.17-
141UbiquitinationTDKETETKWAIKKVN
CCCHHHHHHHHHHHC
28.53-
154PhosphorylationVNKEKAGSSAVKLLE
HCHHHCCHHHHHHHH
21.7121406692
155PhosphorylationNKEKAGSSAVKLLER
CHHHCCHHHHHHHHH
35.8421406692
158UbiquitinationKAGSSAVKLLEREVN
HCCHHHHHHHHHHHH
47.25-
168UbiquitinationEREVNILKSVKHEHI
HHHHHHHHHCCHHCE
49.78-
240UbiquitinationDIVHRDLKLENIMVK
CCCCCCCCHHCEEEE
59.03-
271UbiquitinationTDFGLAVKKQSRSEA
EECCEEEECCCCCHH
39.22-
301PhosphorylationVISAHDYSQQCDIWS
HHCCCCCHHHCCHHH
21.6027251275
356PhosphorylationSISDCAKSVLKQLMK
HHHHHHHHHHHHHHC
17.7321406692
359UbiquitinationDCAKSVLKQLMKVDP
HHHHHHHHHHHCCCH
38.95-
373UbiquitinationPAHRITAKELLDNQW
HHHCCCHHHHHHCCC
40.00-
382PhosphorylationLLDNQWLTGNKLSSV
HHHCCCCCCCCCCCC
35.43-
385AcetylationNQWLTGNKLSSVRPT
CCCCCCCCCCCCCCC
51.6025953088
385UbiquitinationNQWLTGNKLSSVRPT
CCCCCCCCCCCCCCC
51.60-
387PhosphorylationWLTGNKLSSVRPTNV
CCCCCCCCCCCCCCH
28.5324719451
388PhosphorylationLTGNKLSSVRPTNVL
CCCCCCCCCCCCCHH
32.3628796482
392PhosphorylationKLSSVRPTNVLEMMK
CCCCCCCCCHHHHHH
27.6528796482
402UbiquitinationLEMMKEWKNNPESVE
HHHHHHHHCCHHHHH
48.19-
407PhosphorylationEWKNNPESVEENTTE
HHHCCHHHHHHCCCC
35.77-
420PhosphorylationTEEKNKPSTEEKLKS
CCCCCCCCHHHHHHH
50.49-
421PhosphorylationEEKNKPSTEEKLKSY
CCCCCCCHHHHHHHC
57.60-
427PhosphorylationSTEEKLKSYQPWGNV
CHHHHHHHCCCCCCC
39.1626074081
428PhosphorylationTEEKLKSYQPWGNVP
HHHHHHHCCCCCCCC
19.6026074081
439PhosphorylationGNVPDANYTSDEEEE
CCCCCCCCCCHHHHH
14.8930576142
440PhosphorylationNVPDANYTSDEEEEK
CCCCCCCCCHHHHHH
29.5222617229
441PhosphorylationVPDANYTSDEEEEKQ
CCCCCCCCHHHHHHH
32.4422617229
449PhosphorylationDEEEEKQSTAYEKQF
HHHHHHHCHHHHHHC
26.5226852163
450PhosphorylationEEEEKQSTAYEKQFP
HHHHHHCHHHHHHCC
30.6626852163
452PhosphorylationEEKQSTAYEKQFPAT
HHHHCHHHHHHCCCC
24.6126852163
454UbiquitinationKQSTAYEKQFPATSK
HHCHHHHHHCCCCCC
44.56-
468PhosphorylationKDNFDMCSSSFTSSK
CCCCCCCCCCCCCCC
23.5218691976
469PhosphorylationDNFDMCSSSFTSSKL
CCCCCCCCCCCCCCC
25.2521712546
470PhosphorylationNFDMCSSSFTSSKLL
CCCCCCCCCCCCCCC
19.0921712546
472PhosphorylationDMCSSSFTSSKLLPA
CCCCCCCCCCCCCCC
33.7629116813
473PhosphorylationMCSSSFTSSKLLPAE
CCCCCCCCCCCCCCC
24.3829514088
474PhosphorylationCSSSFTSSKLLPAEI
CCCCCCCCCCCCCCC
25.0229514088
488PhosphorylationIKGEMEKTPVTPSQG
CCCEEEECCCCCCCC
15.0824505115
491PhosphorylationEMEKTPVTPSQGTAT
EEEECCCCCCCCCCC
20.5821815630
493PhosphorylationEKTPVTPSQGTATKY
EECCCCCCCCCCCCC
31.6922817900
496PhosphorylationPVTPSQGTATKYPAK
CCCCCCCCCCCCCCC
24.4222817900
498PhosphorylationTPSQGTATKYPAKSG
CCCCCCCCCCCCCCC
30.8324505115
500PhosphorylationSQGTATKYPAKSGAL
CCCCCCCCCCCCCCC
12.22-
504PhosphorylationATKYPAKSGALSRTK
CCCCCCCCCCCCCCC
31.25-
508PhosphorylationPAKSGALSRTKKKL-
CCCCCCCCCCCCCC-
37.0524505115
510PhosphorylationKSGALSRTKKKL---
CCCCCCCCCCCC---
43.79-

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
382TPhosphorylationKinaseSTK33Q9BYT3
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STK33_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 STK33_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90B_HUMANHSP90AB1physical
22451720
HS90A_HUMANHSP90AA1physical
22451720
CDC37_HUMANCDC37physical
22451720
HERC2_HUMANHERC2physical
22451720
BAG2_HUMANBAG2physical
22451720
UBP5_HUMANUSP5physical
22451720
UBP15_HUMANUSP15physical
22451720
A4_HUMANAPPphysical
21832049

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 STK33_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441 AND THR-491, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469 AND SER-470, ANDMASS SPECTROMETRY.

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