CEBPZ_HUMAN - dbPTM
CEBPZ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CEBPZ_HUMAN
UniProt AC Q03701
Protein Name CCAAT/enhancer-binding protein zeta
Gene Name CEBPZ
Organism Homo sapiens (Human).
Sequence Length 1054
Subcellular Localization Nucleus.
Protein Description Stimulates transcription from the HSP70 promoter..
Protein Sequence MAAVKEPLEFHAKRPWRPEEAVEDPDEEDEDNTSEAENGFSLEEVLRLGGTKQDYLMLATLDENEEVIDGGKKGAIDDLQQGELEAFIQNLNLAKYTKASLVEEDEPAEKENSSKKEVKIPKINNKNTAESQRTSVNKVKNKNRPEPHSDENGSTTPKVKKDKQNIFEFFERQTLLLRPGGKWYDLEYSNEYSLKPQPQDVVSKYKTLAQKLYQHEINLFKSKTNSQKGASSTWMKAIVSSGTLGDRMAAMILLIQDDAVHTLQFVETLVNLVKKKGSKQQCLMALDTFKELLITDLLPDNRKLRIFSQRPFDKLEQLSSGNKDSRDRRLILWYFEHQLKHLVAEFVQVLETLSHDTLVTTKTRALTVAHELLCNKPEEEKALLVQVVNKLGDPQNRIATKASHLLETLLCKHPNMKGVVSGEVERLLFRSNISSKAQYYAICFLNQMALSHEESELANKLITVYFCFFRTCVKKKDVESKMLSALLTGVNRAYPYSQTGDDKVREQIDTLFKVLHIVNFNTSVQALMLLFQVMNSQQTISDRYYTALYRKMLDPGLMTCSKQAMFLNLVYKSLKADIVLRRVKAFVKRLLQVTCQQMPPFICGALYLVSEILKAKPGLRSQLDDHPESDDEENFIDANDDEDMEKFTDADKETEIVKKLETEETVPETDVETKKPEVASWVHFDNLKGGKQLNKYDPFSRNPLFCGAENTSLWELKKLSVHFHPSVALFAKTILQGNYIQYSGDPLQDFTLMRFLDRFVYRNPKPHKGKENTDSVVMQPKRKHFIKDIRHLPVNSKEFLAKEESQIPVDEVFFHRYYKKVAVKEKQKRDADEESIEDVDDEEFEELIDTFEDDNCFSSGKDDMDFAGNVKKRTKGAKDNTLDEDSEGSDDELGNLDDDEVSLGSMDDEEFAEVDEDGGTFMDVLDDESESVPELEVHSKVSTKKSKRKGTDDFDFAGSFQGPRKKKRNLNDSSLFVSAEEFGHLLDENMGSKFDNIGMNAMANKDNASLKQLRWEAERDDWLHNRDAKSIIKKKKHFKKKRIKTTQKTKKQRK
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
5Acetylation---MAAVKEPLEFHA
---CCCCCCCCCCCC		49.2225953088
33PhosphorylationDEEDEDNTSEAENGF
CCCCCCCCCCHHCCC		40.0230266825
34PhosphorylationEEDEDNTSEAENGFS
CCCCCCCCCHHCCCC		40.8530266825
41PhosphorylationSEAENGFSLEEVLRL
CCHHCCCCHHHHHHC		35.9528176443
52AcetylationVLRLGGTKQDYLMLA
HHHCCCCCCCEEEEE		44.4326051181
72AcetylationEEVIDGGKKGAIDDL
CCEECCCCCCCHHHH		54.2726051181
73UbiquitinationEVIDGGKKGAIDDLQ
CEECCCCCCCHHHHH		57.7729967540
98UbiquitinationLNLAKYTKASLVEED
HCHHHHHHHHHHCCC		32.6521890473
100PhosphorylationLAKYTKASLVEEDEP
HHHHHHHHHHCCCCH		34.2119691289
110AcetylationEEDEPAEKENSSKKE
CCCCHHHCCCCCCCC		65.3926051181
113PhosphorylationEPAEKENSSKKEVKI
CHHHCCCCCCCCEEC		44.6323186163
114PhosphorylationPAEKENSSKKEVKIP
HHHCCCCCCCCEECC		60.37-
126AcetylationKIPKINNKNTAESQR
ECCCCCCCCCHHHHH		51.7125953088
131PhosphorylationNNKNTAESQRTSVNK
CCCCCHHHHHHHHHH		23.6225159151
134PhosphorylationNTAESQRTSVNKVKN
CCHHHHHHHHHHHCC		29.4125627689
135PhosphorylationTAESQRTSVNKVKNK
CHHHHHHHHHHHCCC		26.3625159151
149PhosphorylationKNRPEPHSDENGSTT
CCCCCCCCCCCCCCC		58.2825159151
154PhosphorylationPHSDENGSTTPKVKK
CCCCCCCCCCCCCCC		40.4624732914
155PhosphorylationHSDENGSTTPKVKKD
CCCCCCCCCCCCCCC		48.8224732914
156PhosphorylationSDENGSTTPKVKKDK
CCCCCCCCCCCCCCC		23.8625159151
1632-HydroxyisobutyrylationTPKVKKDKQNIFEFF
CCCCCCCCCCHHHHH		54.87-
174PhosphorylationFEFFERQTLLLRPGG
HHHHHHCEEEECCCC		26.1221406692
184PhosphorylationLRPGGKWYDLEYSNE
ECCCCCEEECCCCCC		17.7118452278
192PhosphorylationDLEYSNEYSLKPQPQ
ECCCCCCCCCCCCCH		24.4522817900
193PhosphorylationLEYSNEYSLKPQPQD
CCCCCCCCCCCCCHH		24.6024719451
195AcetylationYSNEYSLKPQPQDVV
CCCCCCCCCCCHHHH		35.3526051181
203PhosphorylationPQPQDVVSKYKTLAQ
CCCHHHHHHHHHHHH		30.0718452278
204AcetylationQPQDVVSKYKTLAQK
CCHHHHHHHHHHHHH		38.8726051181
211AcetylationKYKTLAQKLYQHEIN
HHHHHHHHHHHHHHH		43.4825953088
213PhosphorylationKTLAQKLYQHEINLF
HHHHHHHHHHHHHHH		18.1724719451
221AcetylationQHEINLFKSKTNSQK
HHHHHHHHCCCCCCC		54.9626051181
224PhosphorylationINLFKSKTNSQKGAS
HHHHHCCCCCCCCCC		47.3924719451
231PhosphorylationTNSQKGASSTWMKAI
CCCCCCCCHHHHHHH		36.6520860994
232PhosphorylationNSQKGASSTWMKAIV
CCCCCCCHHHHHHHH		26.0820860994
233PhosphorylationSQKGASSTWMKAIVS
CCCCCCHHHHHHHHH		27.3829759185
236AcetylationGASSTWMKAIVSSGT
CCCHHHHHHHHHCCC		26.9026051181
240PhosphorylationTWMKAIVSSGTLGDR
HHHHHHHHCCCHHHH		19.5519691289
241PhosphorylationWMKAIVSSGTLGDRM
HHHHHHHCCCHHHHH		25.5419691289
243PhosphorylationKAIVSSGTLGDRMAA
HHHHHCCCHHHHHHH		29.5219691289
279AcetylationLVKKKGSKQQCLMAL
HHHHCCCHHHHHHHH		53.7226051181
314AcetylationFSQRPFDKLEQLSSG
ECCCCCHHHHHHHCC		55.0626051181
314UbiquitinationFSQRPFDKLEQLSSG
ECCCCCHHHHHHHCC		55.0621906983
319PhosphorylationFDKLEQLSSGNKDSR
CHHHHHHHCCCCCHH		35.5720068231
320PhosphorylationDKLEQLSSGNKDSRD
HHHHHHHCCCCCHHH		55.7820068231
323AcetylationEQLSSGNKDSRDRRL
HHHHCCCCCHHHHHH		61.6826051181
376AcetylationAHELLCNKPEEEKAL
HHHHHCCCCHHHHHH		53.4626051181
381AcetylationCNKPEEEKALLVQVV
CCCCHHHHHHHHHHH		47.8426051181
390AcetylationLLVQVVNKLGDPQNR
HHHHHHHHHCCHHHH		42.0926051181
390UbiquitinationLLVQVVNKLGDPQNR
HHHHHHHHHCCHHHH		42.09-
397MethylationKLGDPQNRIATKASH
HHCCHHHHHHHHHHH		18.05-
408PhosphorylationKASHLLETLLCKHPN
HHHHHHHHHHCCCCC		25.6229396449
412AcetylationLLETLLCKHPNMKGV
HHHHHHCCCCCCCCC		63.1625953088
412UbiquitinationLLETLLCKHPNMKGV
HHHHHHCCCCCCCCC		63.1629967540
417UbiquitinationLCKHPNMKGVVSGEV
HCCCCCCCCCCCHHH		56.0129967540
439PhosphorylationNISSKAQYYAICFLN
CCCCHHHHHHHHHHH		10.3426074081
440PhosphorylationISSKAQYYAICFLNQ
CCCHHHHHHHHHHHH		4.2026074081
451PhosphorylationFLNQMALSHEESELA
HHHHHHCCHHHHHHH		21.2226074081
455PhosphorylationMALSHEESELANKLI
HHCCHHHHHHHHHHH		34.6226074081
463PhosphorylationELANKLITVYFCFFR
HHHHHHHHHHHHHHH		21.4227251275
465PhosphorylationANKLITVYFCFFRTC
HHHHHHHHHHHHHHH		5.9827251275
480PhosphorylationVKKKDVESKMLSALL
CCHHHHHHHHHHHHH		24.18-
481UbiquitinationKKKDVESKMLSALLT
CHHHHHHHHHHHHHH		30.29-
496PhosphorylationGVNRAYPYSQTGDDK
CCHHHCCCCCCCCHH		10.7516565220
5032-HydroxyisobutyrylationYSQTGDDKVREQIDT
CCCCCCHHHHHHHHH		48.18-
503AcetylationYSQTGDDKVREQIDT
CCCCCCHHHHHHHHH		48.1826051181
503UbiquitinationYSQTGDDKVREQIDT
CCCCCCHHHHHHHHH		48.1824816145
522PhosphorylationLHIVNFNTSVQALML
HHHCCCCHHHHHHHH		26.5724043423
523PhosphorylationHIVNFNTSVQALMLL
HHCCCCHHHHHHHHH		17.2124043423
536PhosphorylationLLFQVMNSQQTISDR
HHHHHHCCCCCCHHH		12.9324043423
539PhosphorylationQVMNSQQTISDRYYT
HHHCCCCCCHHHHHH		18.1424043423
541PhosphorylationMNSQQTISDRYYTAL
HCCCCCCHHHHHHHH		21.3024043423
571PhosphorylationAMFLNLVYKSLKADI
HHHHHHHHHHHHHHH		9.6820068231
572UbiquitinationMFLNLVYKSLKADIV
HHHHHHHHHHHHHHH		41.66-
621PhosphorylationKAKPGLRSQLDDHPE
HCCCCHHHHCCCCCC		39.8923927012
629PhosphorylationQLDDHPESDDEENFI
HCCCCCCCCCCCCCC		55.6123927012
648PhosphorylationDEDMEKFTDADKETE
HHHHHHHCCCHHHHH		41.1523403867
6522-HydroxyisobutyrylationEKFTDADKETEIVKK
HHHCCCHHHHHHHHH		69.15-
654PhosphorylationFTDADKETEIVKKLE
HCCCHHHHHHHHHHC		36.4323403867
669PhosphorylationTEETVPETDVETKKP
CCCCCCCCCCCCCCC		39.0030576142
675AcetylationETDVETKKPEVASWV
CCCCCCCCCCEEEEE		54.5526051181
675UbiquitinationETDVETKKPEVASWV
CCCCCCCCCCEEEEE		54.5529967540
680PhosphorylationTKKPEVASWVHFDNL
CCCCCEEEEEEEECC		34.5028555341
688UbiquitinationWVHFDNLKGGKQLNK
EEEEECCCCCCCCCC		72.3929967540
695AcetylationKGGKQLNKYDPFSRN
CCCCCCCCCCCCCCC		60.6719608861
717AcetylationNTSLWELKKLSVHFH
CCCHHHHHHHHCCCC		39.9026051181
758MethylationTLMRFLDRFVYRNPK
HHHHHHHHHHHCCCC		25.69-
770UbiquitinationNPKPHKGKENTDSVV
CCCCCCCCCCCCCEE		53.2324816145
773PhosphorylationPHKGKENTDSVVMQP
CCCCCCCCCCEECCC		30.6429083192
775PhosphorylationKGKENTDSVVMQPKR
CCCCCCCCEECCCCH		17.9921815630
778SulfoxidationENTDSVVMQPKRKHF
CCCCCEECCCCHHHC		5.4521406390
787MethylationPKRKHFIKDIRHLPV
CCHHHCCCCCCCCCC		46.27-
787UbiquitinationPKRKHFIKDIRHLPV
CCHHHCCCCCCCCCC		46.2729967540
797UbiquitinationRHLPVNSKEFLAKEE
CCCCCCCHHHHHHCH		47.4833845483
802AcetylationNSKEFLAKEESQIPV
CCHHHHHHCHHCCCC		65.2526051181
805PhosphorylationEFLAKEESQIPVDEV
HHHHHCHHCCCCCHH		34.2027067055
835PhosphorylationKRDADEESIEDVDDE
CCCCCHHHCCCCCHH		29.2716565220
850PhosphorylationEFEELIDTFEDDNCF
HHHHHHHHHCCCCCC		23.1720873877
858PhosphorylationFEDDNCFSSGKDDMD
HCCCCCCCCCCCCCC		40.1420873877
859PhosphorylationEDDNCFSSGKDDMDF
CCCCCCCCCCCCCCC		29.6120873877
949UbiquitinationSTKKSKRKGTDDFDF
CCCCCCCCCCCCCCC		70.6524816145
951PhosphorylationKKSKRKGTDDFDFAG
CCCCCCCCCCCCCCC		35.1225159151
959PhosphorylationDDFDFAGSFQGPRKK
CCCCCCCCCCCCCCC		15.8025159151
973PhosphorylationKKRNLNDSSLFVSAE
CCCCCCCCCEEEEHH		28.0625159151
974PhosphorylationKRNLNDSSLFVSAEE
CCCCCCCCEEEEHHH		28.7925159151
978PhosphorylationNDSSLFVSAEEFGHL
CCCCEEEEHHHHHHH		23.7221712546
992PhosphorylationLLDENMGSKFDNIGM
HHCCCCCCCCCHHHH		21.2724732914
1005AcetylationGMNAMANKDNASLKQ
HHHHHCCCCCHHHHH		42.7026051181
1011MethylationNKDNASLKQLRWEAE
CCCCHHHHHHHHHHH		44.80-
1011UbiquitinationNKDNASLKQLRWEAE
CCCCHHHHHHHHHHH		44.8033845483
1030PhosphorylationLHNRDAKSIIKKKKH
HCCCCHHHHHHHHHH		31.1324719451
1051UbiquitinationKTTQKTKKQRK----
CCCHHHHHHHC----		61.6424816145
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 CEBPZ_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CEBPZ_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 CEBPZ_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFYB_HUMANNFYBphysical
11306579
P53_HUMANTP53physical
12534345
P73_HUMANTP73physical
12534345
EBP2_HUMANEBNA1BP2physical
26344197
PUM3_HUMANKIAA0020physical
26344197
NOLC1_HUMANNOLC1physical
26344197
NOP2_HUMANNOP2physical
26344197
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 CEBPZ_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-695, 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-629 AND SER-973, ANDMASS SPECTROMETRY.
"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-629; SER-973 ANDSER-978, AND MASS 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-629, AND MASSSPECTROMETRY.
"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 SER-34; SER-100 AND SER-241,AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-232 ANDTHR-233, AND MASS SPECTROMETRY.
"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 SER-629 AND SER-835, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-835, AND MASSSPECTROMETRY.

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