ZEB1_MOUSE - dbPTM
ZEB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZEB1_MOUSE
UniProt AC Q64318
Protein Name Zinc finger E-box-binding homeobox 1
Gene Name Zeb1
Organism Mus musculus (Mouse).
Sequence Length 1117
Subcellular Localization Nucleus .
Protein Description Acts as a transcriptional repressor. Binds to E-box sequences in the immunoglobulin heavy chain enhancer as well as in the regulatory regions of many other tissue-specific genes. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1 (By similarity). Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting microRNAs..
Protein Sequence MADGPRCKRRKQANPRRNNVTNYNTVVEANSDSDDEDKLHIVEEESITDAADCEGGMPDDELPADQTVLPGGSDRGGGAKNCWQDNVKDNECDSDAENEQNHDPNVEEFLQQQDTAVIYPEAPEEDQRQGTPEASSHDENGTPDAFSQLLTCPYCDRGYKRFTSLKEHIKYRHEKNEDNFSCSLCSYTFAYRTQLERHMTSHKSGREQRHVTQSGGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCISLMPVNGRPRSGLKTSQCSSPSLSTSPGSPTRPQIRQKIENKPLQEPLSVNQIKTEPVDYEFKPIVVASGINCSTPLQNGVFSSGGQLQATSSPQGVVQAVVLPTVGLVSPISINLSDIQNVLKVAVDGNVIRQVLETNQASLASKEQEAVSASPIQQGGHSVISAISLPLVDQDGTTKIIINYSLEQPSQLQVVPQNLKKEIPAPTNSCKSEKLPEDLTVKSETDKSFEGARDDSTCLLCEDCPGDLNALPELKHYDPECPAQPPPPAPATEKPESSASSAGNGDLSPSQPPLKNLLSLLKAYYALNAQPSTEELSKIADSVNLPLDGVKKWFEKMQAGQIPGQSPDPPSPGTGSVNIPTKTDEQPQPADGNEPQEDSTRGQSPVKIRSSPVLPVGSAMNGSRSCTSSPSPLNLCSARNPQGYSCVAEGAQEEPQVEPLDLSLPKQQGELLERSTVSSVYQNSVYSVQEEPLNLSCAKKEPQKDSCVTDSEPVVNVVPPSANPINIAIPTVTAQLPTIVAIADQNSVPCLRALAANKQTILIPQVAYTYSATVSPAVQEPPVKVIQPNGNQDERQDTSSEGVSTVEDQNDSDSTPPKKKTRKTENGMYACDLCDKIFQKSSSLLRHKYEHTGKRPHECGICRKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKRGAEDRDAMEQEDAGPEVLPEVLATEHVGARASPSQADSDERESLTREEDEDSEKEEEEEDKEMEELQEGKECENPQGEEEEEEEEEEEEEEEEEEEVEADEAEHEAAAKTDGTVEVGAAQQAGSLEQKASESEMESESESEQLSEEKTNEA
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
25PhosphorylationNNVTNYNTVVEANSD
CCCCCCCCEEECCCC
18.6328285833
31PhosphorylationNTVVEANSDSDDEDK
CCEEECCCCCCCCCC
45.6027087446
33PhosphorylationVVEANSDSDDEDKLH
EEECCCCCCCCCCEE
46.9427087446
94PhosphorylationVKDNECDSDAENEQN
CCCCCCCCHHHHHHC
50.8325338131
164PhosphorylationRGYKRFTSLKEHIKY
CCCHHHHHHHHHHHH
34.4329176673
200PhosphorylationTQLERHMTSHKSGRE
HHHHHHHHCCCCCCC
22.8924759943
201PhosphorylationQLERHMTSHKSGREQ
HHHHHHHCCCCCCCC
22.7324759943
204PhosphorylationRHMTSHKSGREQRHV
HHHHCCCCCCCCEEE
37.3424759943
212PhosphorylationGREQRHVTQSGGNRK
CCCCEEEECCCCCCE
15.7623737553
214PhosphorylationEQRHVTQSGGNRKFK
CCEEEECCCCCCEEE
39.0223737553
262PhosphorylationKRFSHSGSYSSHISS
CCCCCCCCCCCCCCC
25.5122871156
263PhosphorylationRFSHSGSYSSHISSK
CCCCCCCCCCCCCCC
20.0922871156
264PhosphorylationFSHSGSYSSHISSKK
CCCCCCCCCCCCCCC
19.6922871156
284PhosphorylationPVNGRPRSGLKTSQC
ECCCCCCCCCCCCCC
51.6826160508
288PhosphorylationRPRSGLKTSQCSSPS
CCCCCCCCCCCCCCC
29.1325619855
289PhosphorylationPRSGLKTSQCSSPSL
CCCCCCCCCCCCCCC
27.8325619855
292PhosphorylationGLKTSQCSSPSLSTS
CCCCCCCCCCCCCCC
37.3325619855
293PhosphorylationLKTSQCSSPSLSTSP
CCCCCCCCCCCCCCC
26.5726824392
295PhosphorylationTSQCSSPSLSTSPGS
CCCCCCCCCCCCCCC
36.5825619855
297PhosphorylationQCSSPSLSTSPGSPT
CCCCCCCCCCCCCCC
31.0425619855
298PhosphorylationCSSPSLSTSPGSPTR
CCCCCCCCCCCCCCC
44.2125619855
299PhosphorylationSSPSLSTSPGSPTRP
CCCCCCCCCCCCCCH
24.7221082442
302PhosphorylationSLSTSPGSPTRPQIR
CCCCCCCCCCCHHHH
26.8727087446
304PhosphorylationSTSPGSPTRPQIRQK
CCCCCCCCCHHHHHH
57.5922942356
425PhosphorylationSKEQEAVSASPIQQG
HHCHHHHCCCCCCCC
30.0323984901
427PhosphorylationEQEAVSASPIQQGGH
CHHHHCCCCCCCCCC
18.2825777480
435PhosphorylationPIQQGGHSVISAISL
CCCCCCCEEEEEEEC
25.1523984901
438PhosphorylationQGGHSVISAISLPLV
CCCCEEEEEEECEEE
19.8623984901
441PhosphorylationHSVISAISLPLVDQD
CEEEEEEECEEECCC
24.5323984901
450PhosphorylationPLVDQDGTTKIIINY
EEECCCCCEEEEEEE
32.9525777480
451PhosphorylationLVDQDGTTKIIINYS
EECCCCCEEEEEEEE
26.2725777480
501PhosphorylationVKSETDKSFEGARDD
ECCCCCCCCCCCCCC
31.1927149854
561PhosphorylationSAGNGDLSPSQPPLK
CCCCCCCCCCCCCHH
27.5225266776
619PhosphorylationAGQIPGQSPDPPSPG
CCCCCCCCCCCCCCC
36.8727087446
624PhosphorylationGQSPDPPSPGTGSVN
CCCCCCCCCCCCCCC
41.1525521595
627PhosphorylationPDPPSPGTGSVNIPT
CCCCCCCCCCCCCCC
29.6625619855
629PhosphorylationPPSPGTGSVNIPTKT
CCCCCCCCCCCCCCC
16.3025619855
634PhosphorylationTGSVNIPTKTDEQPQ
CCCCCCCCCCCCCCC
42.6625619855
636PhosphorylationSVNIPTKTDEQPQPA
CCCCCCCCCCCCCCC
47.4427087446
652PhosphorylationGNEPQEDSTRGQSPV
CCCCCCCCCCCCCCC
21.1726643407
653PhosphorylationNEPQEDSTRGQSPVK
CCCCCCCCCCCCCCE
51.6626643407
657PhosphorylationEDSTRGQSPVKIRSS
CCCCCCCCCCEECCC
34.1927087446
663PhosphorylationQSPVKIRSSPVLPVG
CCCCEECCCCEECCC
42.3321082442
664PhosphorylationSPVKIRSSPVLPVGS
CCCEECCCCEECCCC
14.8021082442
671PhosphorylationSPVLPVGSAMNGSRS
CCEECCCCCCCCCCC
25.2826745281
676PhosphorylationVGSAMNGSRSCTSSP
CCCCCCCCCCCCCCC
18.9326160508
678PhosphorylationSAMNGSRSCTSSPSP
CCCCCCCCCCCCCCC
24.3625521595
680PhosphorylationMNGSRSCTSSPSPLN
CCCCCCCCCCCCCCC
33.2221082442
681PhosphorylationNGSRSCTSSPSPLNL
CCCCCCCCCCCCCCC
44.5827149854
682PhosphorylationGSRSCTSSPSPLNLC
CCCCCCCCCCCCCCC
15.9625521595
684PhosphorylationRSCTSSPSPLNLCSA
CCCCCCCCCCCCCCC
43.9222942356
690PhosphorylationPSPLNLCSARNPQGY
CCCCCCCCCCCCCCC
33.1725619855
865PhosphorylationTVEDQNDSDSTPPKK
CCCCCCCCCCCCCCC
40.8025619855
867PhosphorylationEDQNDSDSTPPKKKT
CCCCCCCCCCCCCCC
46.9225619855
868PhosphorylationDQNDSDSTPPKKKTR
CCCCCCCCCCCCCCC
48.9125619855
895PhosphorylationDKIFQKSSSLLRHKY
HHHHHHCHHHHHHHC
31.8524719451
896PhosphorylationKIFQKSSSLLRHKYE
HHHHHCHHHHHHHCC
38.2127149854
933PhosphorylationIEHMRLHSGEKPYQC
HHHHHCCCCCCCCCC
53.9228066266
938PhosphorylationLHSGEKPYQCDKCGK
CCCCCCCCCCCCCCC
32.6128066266
998PhosphorylationEHVGARASPSQADSD
CCCCCCCCHHHCCHH
21.3825263469
1000PhosphorylationVGARASPSQADSDER
CCCCCCHHHCCHHHH
35.1924899341
1004PhosphorylationASPSQADSDERESLT
CCHHHCCHHHHHCCC
44.3725195567
1009PhosphorylationADSDERESLTREEDE
CCHHHHHCCCHHCCC
41.0624899341
1018PhosphorylationTREEDEDSEKEEEEE
CHHCCCCHHHHHHHH
48.8223737553
1090PhosphorylationGAAQQAGSLEQKASE
CHHHHHCCHHHHHCH
31.5827841257
1096PhosphorylationGSLEQKASESEMESE
CCHHHHHCHHHHHCH
49.0025338131
1098PhosphorylationLEQKASESEMESESE
HHHHHCHHHHHCHHH
39.4825338131
1102PhosphorylationASESEMESESESEQL
HCHHHHHCHHHHHHH
45.1529514104

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 ZEB1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZEB1_MOUSE !!

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 ZEB1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTBP1_MOUSECtbp1physical
10567582
CTBP2_MOUSECtbp2physical
10567582
CTBP2_MOUSECtbp2physical
12714599

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZEB1_MOUSE

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Related Literatures of Post-Translational Modification

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