KC13_YEAST - dbPTM
KC13_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KC13_YEAST
UniProt AC P39962
Protein Name Casein kinase I homolog 3
Gene Name YCK3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 524
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side. Nucleus membrane
Lipid-anchor
Cytoplasmic side. Vacuole membrane
Lipid-anchor
Cytoplasmic side. Targeting to the vacuolar membrane may depend on AP-3 pathway.
Protein Description Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates..
Protein Sequence MSQRSSQHIVGIHYAVGPKIGEGSFGVIFEGENILHSCQAQTGSKRDSSIIMANEPVAIKFEPRHSDAPQLRDEFRAYRILNGCVGIPHAYYFGQEGMHNILIIDLLGPSLEDLFEWCGRKFSVKTTCMVAKQMIDRVRAIHDHDLIYRDIKPDNFLISQYQRISPEGKVIKSCASSSNNDPNLIYMVDFGMAKQYRDPRTKQHIPYRERKSLSGTARYMSINTHFGREQSRRDDLESLGHVFFYFLRGSLPWQGLKAPNNKLKYEKIGMTKQKLNPDDLLLNNAIPYQFATYLKYARSLKFDEDPDYDYLISLMDDALRLNDLKDDGHYDWMDLNGGKGWNIKINRRANLHGYGNPNPRVNGNTARNNVNTNSKTRNTTPVATPKQQAQNSYNKDNSKSRISSNPQSFTKQQHVLKKIEPNSKYIPETHSNLQRPIKSQSQTYDSISHTQNSPFVPYSSSKANPKRSNNEHNLPNHYTNLANKNINYQSQRNYEQENDAYSDDENDTFCSKIYKYCCCCFCCC
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
5Phosphorylation---MSQRSSQHIVGI
---CCCCCCCCEEEE
27.0628889911
6Phosphorylation--MSQRSSQHIVGIH
--CCCCCCCCEEEEE
28.1528889911
48PhosphorylationQTGSKRDSSIIMANE
CCCCCCCCCEEEECC
27.7223749301
49PhosphorylationTGSKRDSSIIMANEP
CCCCCCCCEEEECCC
22.0328889911
214PhosphorylationYRERKSLSGTARYMS
HHHHHCCCCCCEEEE
40.9823749301
325UbiquitinationALRLNDLKDDGHYDW
HHCCCCCCCCCCCCC
57.5523749301
365PhosphorylationNPRVNGNTARNNVNT
CCCCCCCCCCCCCCC
28.5221440633
374PhosphorylationRNNVNTNSKTRNTTP
CCCCCCCCCCCCCCC
33.1127214570
376PhosphorylationNVNTNSKTRNTTPVA
CCCCCCCCCCCCCCC
29.0419684113
379PhosphorylationTNSKTRNTTPVATPK
CCCCCCCCCCCCCHH
29.2319684113
380PhosphorylationNSKTRNTTPVATPKQ
CCCCCCCCCCCCHHH
21.2219684113
384PhosphorylationRNTTPVATPKQQAQN
CCCCCCCCHHHHHHH
31.1123749301
392PhosphorylationPKQQAQNSYNKDNSK
HHHHHHHHCCCCCCC
20.2923749301
398PhosphorylationNSYNKDNSKSRISSN
HHCCCCCCCCCCCCC
41.9921440633
400PhosphorylationYNKDNSKSRISSNPQ
CCCCCCCCCCCCCCC
34.3722369663
403PhosphorylationDNSKSRISSNPQSFT
CCCCCCCCCCCCCHH
23.9720377248
404PhosphorylationNSKSRISSNPQSFTK
CCCCCCCCCCCCHHH
50.5922369663
408PhosphorylationRISSNPQSFTKQQHV
CCCCCCCCHHHHHHH
35.8222369663
410PhosphorylationSSNPQSFTKQQHVLK
CCCCCCHHHHHHHHH
32.9422369663
425PhosphorylationKIEPNSKYIPETHSN
HCCCCCCCCCCCCCC
22.8719823750
429PhosphorylationNSKYIPETHSNLQRP
CCCCCCCCCCCCCCC
25.8319823750
431PhosphorylationKYIPETHSNLQRPIK
CCCCCCCCCCCCCCC
46.8119823750
439PhosphorylationNLQRPIKSQSQTYDS
CCCCCCCCCCCCCCC
35.4723749301
441PhosphorylationQRPIKSQSQTYDSIS
CCCCCCCCCCCCCCC
31.4221440633
443PhosphorylationPIKSQSQTYDSISHT
CCCCCCCCCCCCCCC
34.2522369663
444PhosphorylationIKSQSQTYDSISHTQ
CCCCCCCCCCCCCCC
10.4722369663
446PhosphorylationSQSQTYDSISHTQNS
CCCCCCCCCCCCCCC
18.6423749301
448PhosphorylationSQTYDSISHTQNSPF
CCCCCCCCCCCCCCC
25.1622369663
450PhosphorylationTYDSISHTQNSPFVP
CCCCCCCCCCCCCCC
23.7422369663
459PhosphorylationNSPFVPYSSSKANPK
CCCCCCCCCCCCCCC
23.2819779198
460PhosphorylationSPFVPYSSSKANPKR
CCCCCCCCCCCCCCC
29.9819779198
462UbiquitinationFVPYSSSKANPKRSN
CCCCCCCCCCCCCCC
54.8823749301
490PhosphorylationNKNINYQSQRNYEQE
HCCCCHHHHCCHHHC
22.2823749301
494PhosphorylationNYQSQRNYEQENDAY
CHHHHCCHHHCCCCC
22.6029688323
502PhosphorylationEQENDAYSDDENDTF
HHCCCCCCCCCCCCH
40.0627214570
508PhosphorylationYSDDENDTFCSKIYK
CCCCCCCCHHHHHHH
37.8228889911
517S-palmitoylationCSKIYKYCCCCFCCC
HHHHHHHHCCHHHCC
0.9414668479
518S-palmitoylationSKIYKYCCCCFCCC-
HHHHHHHCCHHHCC-
1.7414668479
519S-palmitoylationKIYKYCCCCFCCC--
HHHHHHCCHHHCC--
1.4514668479
520S-palmitoylationIYKYCCCCFCCC---
HHHHHCCHHHCC---
1.5014668479
522S-palmitoylationKYCCCCFCCC-----
HHHCCHHHCC-----
1.1214668479
523S-palmitoylationYCCCCFCCC------
HHCCHHHCC------
1.2214668479
524S-palmitoylationCCCCFCCC-------
HCCHHHCC-------
7.0414668479

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 KC13_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KC13_YEAST !!

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 KC13_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KFA_YEASTBNA7physical
16319894
DOT6_YEASTDOT6genetic
17314980
NUP53_YEASTNUP53physical
17461799
MPIP_YEASTMIH1physical
18316413
CKS1_YEASTCKS1genetic
19269370
LSM6_YEASTLSM6genetic
19269370
SNF1_YEASTSNF1genetic
19269370
GET2_YEASTGET2genetic
19269370
IES5_YEASTIES5genetic
19269370
RAD51_YEASTRAD51genetic
19269370
UBP3_YEASTUBP3genetic
19269370
MNN11_YEASTMNN11genetic
19269370
IME1_YEASTIME1genetic
19269370
SWI6_YEASTSWI6genetic
19269370
AVO2_YEASTAVO2genetic
19269370
CLA4_YEASTCLA4genetic
19269370
VPS4_YEASTVPS4genetic
19547744
SAC1_YEASTSAC1genetic
19547744
SYUA_HUMANSNCAgenetic
19182805
GAL7_YEASTGAL7physical
20489023
C1TM_YEASTMIS1physical
20489023
SFB2_YEASTSFB2physical
20489023
ATG34_YEASTATG34physical
20489023
YPT31_YEASTYPT31genetic
20526336
EMI2_YEASTEMI2physical
21460040
SYMC_YEASTMES1physical
21460040
HSP72_YEASTSSA2physical
21460040
UBA1_YEASTUBA1physical
21460040
REI1_YEASTREI1genetic
21127252
GLN3_YEASTGLN3genetic
21127252
SUM1_YEASTSUM1genetic
21127252
PP2C2_YEASTPTC2genetic
21127252
KCS1_YEASTKCS1genetic
21127252
PP4C_YEASTPPH3genetic
21127252
DUN1_YEASTDUN1genetic
21127252
VPS41_YEASTVPS41physical
19386605
PEP12_YEASTPEP12genetic
21079247
VPS41_YEASTVPS41physical
21079247
LPE10_YEASTMFM1genetic
22282571
ADP1_YEASTADP1genetic
22282571
RU2A_YEASTLEA1genetic
22282571
SWD3_YEASTSWD3genetic
22282571
SNT1_YEASTSNT1genetic
22282571
COXM1_YEASTCMC1genetic
22282571
EMI1_YEASTEMI1genetic
22282571
BRE5_YEASTBRE5genetic
22282571
TCO89_YEASTTCO89genetic
22282571
PEP5_YEASTPEP5physical
25411340
VPS16_YEASTVPS16physical
25411340
PEP3_YEASTPEP3physical
25411340
VPS33_YEASTVPS33physical
25411340
VAM6_YEASTVAM6physical
25411340
VPS41_YEASTVPS41physical
25411340
VPS41_YEASTVPS41physical
25995379
MGR1_YEASTMGR1genetic
27708008
SNT1_YEASTSNT1genetic
27708008
OMS1_YEASTOMS1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
MRX5_YEASTYJL147Cgenetic
27708008
PTK2_YEASTPTK2genetic
27708008
MRT4_YEASTMRT4genetic
27708008
COXM1_YEASTCMC1genetic
27708008
MSS1_YEASTMSS1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
RU2A_YEASTLEA1genetic
27708008
MON1_YEASTMON1physical
24623720
MEOX2_HUMANMEOX2physical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KC13_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND MASSSPECTROMETRY.

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