KLF10_HUMAN - dbPTM
KLF10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLF10_HUMAN
UniProt AC Q13118
Protein Name Krueppel-like factor 10
Gene Name KLF10
Organism Homo sapiens (Human).
Sequence Length 480
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor which binds to the consensus sequence 5'-GGTGTG-3'. Plays a role in the regulation of the circadian clock; binds to the GC box sequence in the promoter of the core clock component ARTNL/BMAL1 and represses its transcriptional activity. Regulates the circadian expression of genes involved in lipogenesis, gluconeogenesis, and glycolysis in the liver. Represses the expression of PCK2, a rate-limiting step enzyme of gluconeogenesis (By similarity). May play a role in the cell cycle regulation..
Protein Sequence MLNFGASLQQTAEERMEMISERPKESMYSWNKTAEKSDFEAVEALMSMSCSWKSDFKKYVENRPVTPVSDLSEEENLLPGTPDFHTIPAFCLTPPYSPSDFEPSQVSNLMAPAPSTVHFKSLSDTAKPHIAAPFKEEEKSPVSAPKLPKAQATSVIRHTADAQLCNHQTCPMKAASILNYQNNSFRRRTHLNVEAARKNIPCAAVSPNRSKCERNTVADVDEKASAALYDFSVPSSETVICRSQPAPVSPQQKSVLVSPPAVSAGGVPPMPVICQMVPLPANNPVVTTVVPSTPPSQPPAVCPPVVFMGTQVPKGAVMFVVPQPVVQSSKPPVVSPNGTRLSPIAPAPGFSPSAAKVTPQIDSSRIRSHICSHPGCGKTYFKSSHLKAHTRTHTGEKPFSCSWKGCERRFARSDELSRHRRTHTGEKKFACPMCDRRFMRSDHLTKHARRHLSAKKLPNWQMEVSKLNDIALPPTPAPTQ
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
21UbiquitinationERMEMISERPKESMY
HHHHHHHHCCHHHHC		63.1829967540
32UbiquitinationESMYSWNKTAEKSDF
HHHCCCCCCCCCCCH		42.7429967540
66PhosphorylationYVENRPVTPVSDLSE
HHHCCCCCCHHHCCH		22.2122468782
93PhosphorylationTIPAFCLTPPYSPSD
CCCHHHCCCCCCHHH		24.33-
97PhosphorylationFCLTPPYSPSDFEPS
HHCCCCCCHHHCCHH		24.57-
135SumoylationPHIAAPFKEEEKSPV
CEEECCCCCCCCCCC		64.26-
135AcetylationPHIAAPFKEEEKSPV
CEEECCCCCCCCCCC		64.2626051181
135SumoylationPHIAAPFKEEEKSPV
CEEECCCCCCCCCCC		64.26-
138UbiquitinationAAPFKEEEKSPVSAP
ECCCCCCCCCCCCCC		60.9829967540
139UbiquitinationAPFKEEEKSPVSAPK
CCCCCCCCCCCCCCC		64.44-
140PhosphorylationPFKEEEKSPVSAPKL
CCCCCCCCCCCCCCC		33.5428985074
143PhosphorylationEEEKSPVSAPKLPKA
CCCCCCCCCCCCCHH		42.0923312004
149SumoylationVSAPKLPKAQATSVI
CCCCCCCHHHHHHHH		64.66-
149UbiquitinationVSAPKLPKAQATSVI
CCCCCCCHHHHHHHH		64.6629967540
149SumoylationVSAPKLPKAQATSVI
CCCCCCCHHHHHHHH		64.66-
184PhosphorylationILNYQNNSFRRRTHL
HHHCCCCCHHHCCCC		27.9028450419
206PhosphorylationNIPCAAVSPNRSKCE
CCCCEEECCCCHHHC		16.2530266825
212UbiquitinationVSPNRSKCERNTVAD
ECCCCHHHCCCCCCC		6.6521963094
223UbiquitinationTVADVDEKASAALYD
CCCCHHHHHHHHHHE		43.0821963094
243PhosphorylationSETVICRSQPAPVSP
CCEEEEECCCCCCCH		35.7830266825
249PhosphorylationRSQPAPVSPQQKSVL
ECCCCCCCHHCCCEE		18.8730266825
328PhosphorylationVPQPVVQSSKPPVVS
EECCCCCCCCCCEEC		28.8128348404
329PhosphorylationPQPVVQSSKPPVVSP
ECCCCCCCCCCEECC		31.9028348404
335PhosphorylationSSKPPVVSPNGTRLS
CCCCCEECCCCCEEE		16.9427251275
339PhosphorylationPVVSPNGTRLSPIAP
CEECCCCCEEECCCC		34.7728348404
342PhosphorylationSPNGTRLSPIAPAPG
CCCCCEEECCCCCCC		15.8028348404
345UbiquitinationGTRLSPIAPAPGFSP
CCEEECCCCCCCCCC		9.5121963094
351PhosphorylationIAPAPGFSPSAAKVT
CCCCCCCCCCCCCCC		24.7028387310
353PhosphorylationPAPGFSPSAAKVTPQ
CCCCCCCCCCCCCCC		39.3928387310
356UbiquitinationGFSPSAAKVTPQIDS
CCCCCCCCCCCCCCH		46.4921906983
358PhosphorylationSPSAAKVTPQIDSSR
CCCCCCCCCCCCHHH		14.5828674419
378UbiquitinationCSHPGCGKTYFKSSH
CCCCCCCCEEEHHHC		44.09-
383PhosphorylationCGKTYFKSSHLKAHT
CCCEEEHHHCCEEEC		17.0628165663
384PhosphorylationGKTYFKSSHLKAHTR
CCEEEHHHCCEEECC		33.1720953893
387UbiquitinationYFKSSHLKAHTRTHT
EEHHHCCEEECCCCC		32.47-
392PhosphorylationHLKAHTRTHTGEKPF
CCEEECCCCCCCCCC		25.58-
393UbiquitinationLKAHTRTHTGEKPFS
CEEECCCCCCCCCCC		28.6921963094
394PhosphorylationKAHTRTHTGEKPFSC
EEECCCCCCCCCCCC		46.5628165663
400PhosphorylationHTGEKPFSCSWKGCE
CCCCCCCCCCCCCHH		18.7728165663
402PhosphorylationGEKPFSCSWKGCERR
CCCCCCCCCCCHHHH		30.5328165663
404UbiquitinationKPFSCSWKGCERRFA
CCCCCCCCCHHHHHH		37.0721963094
422PhosphorylationELSRHRRTHTGEKKF
HHHHHHCCCCCCCCC		24.60-
424PhosphorylationSRHRRTHTGEKKFAC
HHHHCCCCCCCCCCC		46.56-
435UbiquitinationKFACPMCDRRFMRSD
CCCCCCCCCCHHCCH		38.2433845483
441PhosphorylationCDRRFMRSDHLTKHA
CCCCHHCCHHHHHHH		20.0026074081
445PhosphorylationFMRSDHLTKHARRHL
HHCCHHHHHHHHHHH		19.8426074081
446UbiquitinationMRSDHLTKHARRHLS
HCCHHHHHHHHHHHC		41.4422817900
456SumoylationRRHLSAKKLPNWQME
HHHHCCCCCCCCCEE		69.74-
456SumoylationRRHLSAKKLPNWQME
HHHHCCCCCCCCCEE		69.74-
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
93TPhosphorylationKinaseRAF1P04049
PSP
206SPhosphorylationKinaseCDK2P24941
PSP
384SPhosphorylationKinasePKCIP41743
PSP
384SPhosphorylationKinasePKCZQ05513
PSP
445TPhosphorylationKinasePKCIP41743
PSP
445TPhosphorylationKinasePKCZQ05513
PSP
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:12072443
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLF10_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 KLF10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIN3A_HUMANSIN3Aphysical
11438660
SP1_HUMANSP1physical
15087465
PIGC_HUMANPIGCphysical
21900206
TENS1_HUMANTNS1physical
21900206
BOP1_HUMANBOP1physical
21900206
CRIP2_HUMANCRIP2physical
21900206
LENG1_HUMANLENG1physical
21900206
SF3B3_HUMANSF3B3physical
21900206
RL14_HUMANRPL14physical
21900206
TYK2_HUMANTYK2physical
21471442
SIAH1_HUMANSIAH1physical
12072443
ITCH_HUMANITCHphysical
18278048
KAT2B_HUMANKAT2Bphysical
24944246
SIN3A_HUMANSIN3Aphysical
24944246
CDK2_HUMANCDK2physical
25728284
CCNE1_HUMANCCNE1physical
25728284
SIAH1_HUMANSIAH1physical
25728284
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 KLF10_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory