KC1A_HUMAN - dbPTM
KC1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KC1A_HUMAN
UniProt AC P48729
Protein Name Casein kinase I isoform alpha
Gene Name CSNK1A1
Organism Homo sapiens (Human).
Sequence Length 337
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Chromosome, centromere, kinetochore . Nucleus speckle . Cytoplasm, cytoskeleton, cilium basal body . Localizes to the centrosome in interphase cells, and to kinetochore
Protein Description Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis. [PubMed: 11955436]
Protein Sequence MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKTKSNMKGF
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
2Acetylation------MASSSGSKA
------CCCCCCCCE		20.3719369195
3Phosphorylation-----MASSSGSKAE
-----CCCCCCCCEE		24.6018691976
4Phosphorylation----MASSSGSKAEF
----CCCCCCCCEEE		29.2222496350
5Phosphorylation---MASSSGSKAEFI
---CCCCCCCCEEEE		44.5923186163
7Phosphorylation-MASSSGSKAEFIVG
-CCCCCCCCEEEEEC		30.5525693802
8UbiquitinationMASSSGSKAEFIVGG
CCCCCCCCEEEEECC		56.3019608861
8SumoylationMASSSGSKAEFIVGG
CCCCCCCCEEEEECC		56.3019608861
8AcetylationMASSSGSKAEFIVGG
CCCCCCCCEEEEECC		56.3019608861
8 (in isoform 2)Ubiquitination-56.30-
16AcetylationAEFIVGGKYKLVRKI
EEEEECCEEEEEEEE		33.0325825284
16UbiquitinationAEFIVGGKYKLVRKI
EEEEECCEEEEEEEE		33.03-
162-HydroxyisobutyrylationAEFIVGGKYKLVRKI
EEEEECCEEEEEEEE		33.03-
17PhosphorylationEFIVGGKYKLVRKIG
EEEECCEEEEEEEEC		16.90-
32PhosphorylationSGSFGDIYLAINITN
CCCCCEEEEEEEECC		8.53-
51UbiquitinationAVKLESQKARHPQLL
EEHHHHHCCCCCHHH		57.58-
59PhosphorylationARHPQLLYESKLYKI
CCCCHHHHHHHHHHH		27.0929759185
62UbiquitinationPQLLYESKLYKILQG
CHHHHHHHHHHHHHC		43.8521890473
62 (in isoform 1)Ubiquitination-43.8521890473
62 (in isoform 2)Ubiquitination-43.8521890473
62UbiquitinationPQLLYESKLYKILQG
CHHHHHHHHHHHHHC		43.8521890473
62AcetylationPQLLYESKLYKILQG
CHHHHHHHHHHHHHC		43.8525953088
64PhosphorylationLLYESKLYKILQGGV
HHHHHHHHHHHHCCC		10.3429759185
65UbiquitinationLYESKLYKILQGGVG
HHHHHHHHHHHCCCC		47.5821890473
65 (in isoform 2)Ubiquitination-47.5821890473
65AcetylationLYESKLYKILQGGVG
HHHHHHHHHHHCCCC		47.5825953088
65UbiquitinationLYESKLYKILQGGVG
HHHHHHHHHHHCCCC		47.5821890473
65 (in isoform 1)Ubiquitination-47.5821890473
85PhosphorylationWYGQEKDYNVLVMDL
EECCCCCCCEEEEEC		20.4519690332
105PhosphorylationEDLFNFCSRRFTMKT
HHHHHHHHHCCCHHH		23.5024719451
109PhosphorylationNFCSRRFTMKTVLML
HHHHHCCCHHHHHHH		18.8822210691
126PhosphorylationQMISRIEYVHTKNFI
HHHHHCEEEHHCCCC		8.6528102081
138 (in isoform 1)Ubiquitination-51.0821890473
138 (in isoform 2)Ubiquitination-51.0821890473
138UbiquitinationNFIHRDIKPDNFLMG
CCCCCCCCCCCCCCC		51.0821906983
152UbiquitinationGIGRHCNKLFLIDFG
CCCHHCCEEEEECHH		46.11-
152AcetylationGIGRHCNKLFLIDFG
CCCHHCCEEEEECHH		46.1125953088
156PhosphorylationHCNKLFLIDFGLAKK
HCCEEEEECHHCCHH		3.0224719451
156 (in isoform 2)Phosphorylation-3.0225159151
162 (in isoform 1)Ubiquitination-56.2121890473
162UbiquitinationLIDFGLAKKYRDNRT
EECHHCCHHHCCCCC		56.2121906983
163UbiquitinationIDFGLAKKYRDNRTR
ECHHCCHHHCCCCCC		39.65-
164PhosphorylationDFGLAKKYRDNRTRQ
CHHCCHHHCCCCCCC		23.6127251275
164 (in isoform 2)Phosphorylation-23.6128348404
179UbiquitinationHIPYREDKNLTGTAR
CCCCCCCCCCCCCCC		49.45-
179AcetylationHIPYREDKNLTGTAR
CCCCCCCCCCCCCCC		49.4526051181
184PhosphorylationEDKNLTGTARYASIN
CCCCCCCCCCHHHHH		11.61-
199PhosphorylationAHLGIEQSRRDDMES
HHCCCCCHHHHHHHH		19.25-
218PhosphorylationLMYFNRTSLPWQGLK
HHHCCCCCCCHHHHH		29.2419860830
225UbiquitinationSLPWQGLKAATKKQK
CCCHHHHHHHHHHHH		42.6821890473
225 (in isoform 1)Ubiquitination-42.6821890473
225UbiquitinationSLPWQGLKAATKKQK
CCCHHHHHHHHHHHH		42.6821890473
229UbiquitinationQGLKAATKKQKYEKI
HHHHHHHHHHHHHHH		48.78-
240UbiquitinationYEKISEKKMSTPVEV
HHHHCCCCCCCCHHH		33.75-
242PhosphorylationKISEKKMSTPVEVLC
HHCCCCCCCCHHHHC		38.1419860830
253 (in isoform 2)Ubiquitination-39.2821890473
253UbiquitinationEVLCKGFPAEFAMYL
HHHCCCCCHHHHHHH		39.2821890473
274PhosphorylationRFEEAPDYMYLRQLF
CCCCCCCHHHHHHHH		6.13-
275SulfoxidationFEEAPDYMYLRQLFR
CCCCCCHHHHHHHHH		3.1130846556
287PhosphorylationLFRILFRTLNHQYDY
HHHHHHHHCCCCCCC		25.2826356563
292PhosphorylationFRTLNHQYDYTFDWT
HHHCCCCCCCCCCHH		11.9026356563
294PhosphorylationTLNHQYDYTFDWTML
HCCCCCCCCCCHHHH		12.3626356563
295PhosphorylationLNHQYDYTFDWTMLK
CCCCCCCCCCHHHHH		16.5426356563
299PhosphorylationYDYTFDWTMLKQKAA
CCCCCCHHHHHHHHH		17.9226356563
302UbiquitinationTFDWTMLKQKAAQQA
CCCHHHHHHHHHHHH		38.6421906983
302 (in isoform 1)Ubiquitination-38.6421890473
304UbiquitinationDWTMLKQKAAQQAAS
CHHHHHHHHHHHHHH		44.0721906983
304 (in isoform 1)Ubiquitination-44.0721890473
311PhosphorylationKAAQQAASSSGQGQQ
HHHHHHHHCCCCCCC		28.2225159151
311 (in isoform 3)Phosphorylation-28.2221955146
312PhosphorylationAAQQAASSSGQGQQA
HHHHHHHCCCCCCCC		33.4925159151
312 (in isoform 3)Phosphorylation-33.4925159151
313 (in isoform 3)Phosphorylation-32.4225159151
313PhosphorylationAQQAASSSGQGQQAQ
HHHHHHCCCCCCCCC		32.4225159151
320PhosphorylationSGQGQQAQTPTGKQT
CCCCCCCCCCCCCCC		43.6127642862
321PhosphorylationGQGQQAQTPTGKQTD
CCCCCCCCCCCCCCC		26.3229255136
321 (in isoform 3)Phosphorylation-26.3225159151
322PhosphorylationQGQQAQTPTGKQTDK
CCCCCCCCCCCCCCC		27.3727251275
323PhosphorylationGQQAQTPTGKQTDKT
CCCCCCCCCCCCCCC		61.4729255136
323 (in isoform 3)Phosphorylation-61.4730206219
325UbiquitinationQAQTPTGKQTDKTKS
CCCCCCCCCCCCCCC		53.132190698
325 (in isoform 1)Ubiquitination-53.1321890473
327PhosphorylationQTPTGKQTDKTKSNM
CCCCCCCCCCCCCCC		42.8417192257
329UbiquitinationPTGKQTDKTKSNMKG
CCCCCCCCCCCCCCC		62.33-
330 (in isoform 2)Ubiquitination-42.3821890473
331UbiquitinationGKQTDKTKSNMKGF-
CCCCCCCCCCCCCC-		45.64-
332PhosphorylationKQTDKTKSNMKGF--
CCCCCCCCCCCCC--		47.6019369195
332 (in isoform 2)Ubiquitination-47.6021890473
335UbiquitinationDKTKSNMKGF-----
CCCCCCCCCC-----		62.51-
339PhosphorylationSNMKGF---------
CCCCCC---------		27251275
340PhosphorylationNMKGF----------
CCCCC----------		-
341PhosphorylationMKGF-----------
CCCC-----------		-
349Phosphorylation-------------------
-------------------		24719451
351Phosphorylation---------------------
---------------------		-
353 (in isoform 2)Ubiquitination-21890473
355Phosphorylation-------------------------
-------------------------		-
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
218SPhosphorylationKinaseAURKAO14965
GPS
218SPhosphorylationKinasePRKACAP17612
GPS
242SPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KC1A_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 KC1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HMGB1_HUMANHMGB1physical
12062430
HMGB2_HUMANHMGB2physical
12062430
RCC1_HUMANRCC1physical
12062430
PP14A_HUMANPPP1R14Aphysical
12062430
SYT9_HUMANSYT9physical
12062430
ERF_HUMANERFphysical
12062430
ADAP1_HUMANADAP1physical
12062430
IMA1_HUMANKPNA2physical
12062430
PP2AA_HUMANPPP2CAphysical
12062430
ACTS_HUMANACTA1physical
12062430
AXIN1_HUMANAXIN1physical
11884395
TNR1B_HUMANTNFRSF1Bphysical
7559483
SHQ1_YEASTSHQ1physical
19426738
APC_HUMANAPCphysical
19426738
PHLP1_HUMANPHLPP1physical
19797085
MDM4_HUMANMDM4physical
16024788
MALT1_HUMANMALT1physical
20551178
BCL10_HUMANBCL10physical
20551178
IKBA_HUMANNFKBIAphysical
20551178
MPIP1_HUMANCDC25Aphysical
20348946
PDE4D_HUMANPDE4Dphysical
20647544
HSP74_HUMANHSPA4physical
22824801
HS90A_HUMANHSP90AA1physical
22824801
MDM2_HUMANMDM2physical
22916255
GLI3_HUMANGLI3physical
16371461
TAU_HUMANMAPTphysical
9771888
SYUA_HUMANSNCAphysical
10617630
SYUA_HUMANSNCAphysical
16959772
PI51A_HUMANPIP5K1Aphysical
22939629
HNRPC_HUMANHNRNPCphysical
15687492
GBB2_HUMANGNB2physical
21988832
SMO_DROMEsmophysical
24244405
FA83G_HUMANFAM83Gphysical
23455922
BACH1_HUMANBACH1physical
23455922
SC16A_HUMANSEC16Aphysical
23455922
HMMR_HUMANHMMRphysical
23455922
KC1D_HUMANCSNK1Dphysical
23455922
KC1E_HUMANCSNK1Ephysical
23455922
SEC13_HUMANSEC13physical
23455922
DYL1_HUMANDYNLL1physical
23455922
ACACA_HUMANACACAphysical
23455922
SC23B_HUMANSEC23Bphysical
23455922
FA83B_HUMANFAM83Bphysical
23455922
ZN618_HUMANZNF618physical
23455922
MZT2B_HUMANMZT2Bphysical
23455922
MZT2A_HUMANMZT2Aphysical
23455922
FA83H_HUMANFAM83Hphysical
23455922
UBP34_HUMANUSP34physical
23455922
EPMIP_HUMANEPM2AIP1physical
23455922
DYL2_HUMANDYNLL2physical
23455922
SNX22_HUMANSNX22physical
23455922
UN45A_HUMANUNC45Aphysical
23455922
FA83D_HUMANFAM83Dphysical
23455922
NGAP_HUMANRASAL2physical
23455922
DBR1_HUMANDBR1physical
23455922
SNX24_HUMANSNX24physical
23455922
TIAM1_HUMANTIAM1physical
25124033
TAU_HUMANMAPTphysical
19014373
TOM20_YEASTTOM20physical
24093680
CAR11_HUMANCARD11physical
25088585
BCL10_HUMANBCL10physical
25088585
MALT1_HUMANMALT1physical
25088585
SQSTM_HUMANSQSTM1physical
27846364
FA83G_HUMANFAM83Gphysical
28514442
ZN618_HUMANZNF618physical
28514442
ZDBF2_HUMANZDBF2physical
28514442
NGAP_HUMANRASAL2physical
28514442
GAPD1_HUMANGAPVD1physical
28514442
HMMR_HUMANHMMRphysical
28514442
FA83D_HUMANFAM83Dphysical
28514442
LRP5_HUMANLRP5physical
28514442
HERC1_HUMANHERC1physical
28514442
UBP34_HUMANUSP34physical
28514442
FA83H_HUMANFAM83Hphysical
28514442
LRP6_HUMANLRP6physical
28514442
TTC9C_HUMANTTC9Cphysical
28514442
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
CING_HUMANCGNphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
CBY1_HUMANCBY1physical
27173435
CAR11_HUMANCARD11physical
19118383
BCL10_HUMANBCL10physical
19118383
MALT1_HUMANMALT1physical
19118383
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 KC1A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, AND MASS SPECTROMETRY.
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-105, 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-3; SER-311; THR-321 ANDSER-332, AND MASS SPECTROMETRY.
"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-313 AND THR-321, 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-311; THR-321 ANDTHR-327, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 (ISOFORM2), AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, AND MASSSPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, AND MASSSPECTROMETRY.

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