KLF4_HUMAN - dbPTM
KLF4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLF4_HUMAN
UniProt AC O43474
Protein Name Krueppel-like factor 4
Gene Name KLF4
Organism Homo sapiens (Human).
Sequence Length 513
Subcellular Localization Nucleus.
Protein Description Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription..
Protein Sequence MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRQAGAPNNRWREELSHMKRLPPVLPGRPYDLAAATVATDLESGGAGAACGGSNLAPLPRRETEEFNDLLDLDFILSNSLTHPPESVAATVSSSASASSSSSPSSSGPASAPSTCSFTYPIRAGNDPGVAPGGTGGGLLYGRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLSAPGSEYGSPSVISVSKGSPDGSHPVVVAPYNGGPPRTCPKIKQEAVSSCTHLGAGPPLSNGHRPAAHDFPLGRQLPSRTTPTLGLEEVLSSRDCHPALPLPPGFHPHPGPNYPSFLPDQMQPQVPPLHYQGQSRGFVARAGEPCVCWPHFGTHGMMLTPPSSPLELMPPGSCMPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF
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
13PhosphorylationGESDMAVSDALLPSF
CCCCCHHHHHHCCCH		13.9724532841
19PhosphorylationVSDALLPSFSTFASG
HHHHHCCCHHHCCCC		31.6224532841
21PhosphorylationDALLPSFSTFASGPA
HHHCCCHHHCCCCCC		27.2724532841
25PhosphorylationPSFSTFASGPAGREK
CCHHHCCCCCCCHHH		40.9124719451
32UbiquitinationSGPAGREKTLRQAGA
CCCCCHHHHHHHCCC		52.0418655026
52AcetylationREELSHMKRLPPVLP
HHHHHHHHCCCCCCC		45.4126051181
234PhosphorylationGKFVLKASLSAPGSE
EEEEEEEEECCCCCC		22.6729496963
236PhosphorylationFVLKASLSAPGSEYG
EEEEEEECCCCCCCC		29.8928355574
240PhosphorylationASLSAPGSEYGSPSV
EEECCCCCCCCCCCE		26.9620068231
242PhosphorylationLSAPGSEYGSPSVIS
ECCCCCCCCCCCEEE		25.3020068231
244PhosphorylationAPGSEYGSPSVISVS
CCCCCCCCCCEEEEC		17.0725159151
246PhosphorylationGSEYGSPSVISVSKG
CCCCCCCCEEEECCC		33.5125159151
249PhosphorylationYGSPSVISVSKGSPD
CCCCCEEEECCCCCC		20.4126657352
251PhosphorylationSPSVISVSKGSPDGS
CCCEEEECCCCCCCC		25.2227174698
251O-linked_GlycosylationSPSVISVSKGSPDGS
CCCEEEECCCCCCCC		25.2229237092
252AcetylationPSVISVSKGSPDGSH
CCEEEECCCCCCCCC		62.3426051181
254PhosphorylationVISVSKGSPDGSHPV
EEEECCCCCCCCCCE		24.4525159151
258PhosphorylationSKGSPDGSHPVVVAP
CCCCCCCCCCEEEEE		31.8125159151
278SumoylationPRTCPKIKQEAVSSC
CCCCHHHHHHHHHHC		48.49-
313PhosphorylationPLGRQLPSRTTPTLG
CCCCCCCCCCCCCCC		51.3430624053
315PhosphorylationGRQLPSRTTPTLGLE
CCCCCCCCCCCCCHH		41.2723663014
316PhosphorylationRQLPSRTTPTLGLEE
CCCCCCCCCCCCHHH		17.1121130716
318PhosphorylationLPSRTTPTLGLEEVL
CCCCCCCCCCHHHHH		31.2223663014
327PhosphorylationGLEEVLSSRDCHPAL
CHHHHHHCCCCCCCC		28.1623186163
387PhosphorylationCVCWPHFGTHGMMLT
EEECCCCCCCCEEEC		17.4824719451
421PhosphorylationKPKRGRRSWPRKRTA
CCCCCCCCCCCCCCC		39.8224719451
440PhosphorylationDYAGCGKTYTKSSHL
CCCCCCCCEECCHHH		23.0026074081
441PhosphorylationYAGCGKTYTKSSHLK
CCCCCCCEECCHHHH		18.6926074081
442PhosphorylationAGCGKTYTKSSHLKA
CCCCCCEECCHHHHH		29.6726074081
444PhosphorylationCGKTYTKSSHLKAHL
CCCCEECCHHHHHHH		18.3920166139
445PhosphorylationGKTYTKSSHLKAHLR
CCCEECCHHHHHHHH		34.1020166139
448SumoylationYTKSSHLKAHLRTHT
EECCHHHHHHHHHCC		28.47-
453PhosphorylationHLKAHLRTHTGEKPY
HHHHHHHHCCCCCCC		30.1026074081
455PhosphorylationKAHLRTHTGEKPYHC
HHHHHHCCCCCCCCC		46.5626074081
485PhosphorylationTRHYRKHTGHRPFQC
HHHHHHHHCCCCCCC		37.40-
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
234SPhosphorylationKinasePLK1P53350
PSP
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:21177849
-KUbiquitinationE3 ubiquitin ligaseFBXO32Q969P5
PMID:28068319
-KUbiquitinationE3 ubiquitin ligaseFBXO22Q8NEZ5
PMID:26087183
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLF4_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 KLF4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELK1_HUMANELK1physical
18768922
HDAC5_HUMANHDAC5physical
18768922
HDAC2_HUMANHDAC2physical
19486889
HDAC1_HUMANHDAC1physical
15561714
HDAC2_HUMANHDAC2physical
15561714
KAT5_HUMANKAT5physical
17827213
HDAC7_HUMANHDAC7physical
17827213
EP300_HUMANEP300physical
21252119
HDAC2_HUMANHDAC2physical
21252119
EP300_HUMANEP300physical
20711222
CBP_HUMANCREBBPphysical
21539536
SMCA4_HUMANSMARCA4physical
20305087
PPARG_HUMANPPARGphysical
22282354
SP1_HUMANSP1physical
22282354
TF65_HUMANRELAphysical
22282354
KPCD_HUMANPRKCDphysical
22282354
VHL_HUMANVHLphysical
22284679
CUL2_HUMANCUL2physical
22284679
ELOB_HUMANTCEB2physical
22284679
A4_HUMANAPPphysical
21832049
CTBP1_HUMANCTBP1physical
19751731
CADH1_HUMANCDH1physical
21177849
FBX22_HUMANFBXO22physical
26087183
CUL1_HUMANCUL1physical
26087183
SKP1_HUMANSKP1physical
26087183
FBX32_HUMANFBXO32physical
28068319
BAALC_HUMANBAALCphysical
26050649
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 KLF4_HUMAN

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Proteomic analysis of ubiquitinated proteins in normal hepatocytecell line Chang liver cells.";
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
Proteomics 8:2885-2896(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-32, AND MASSSPECTROMETRY.

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