MAZ_HUMAN - dbPTM
MAZ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAZ_HUMAN
UniProt AC P56270
Protein Name Myc-associated zinc finger protein
Gene Name MAZ
Organism Homo sapiens (Human).
Sequence Length 477
Subcellular Localization Nucleus . In brains of Alzheimer disease patients, present in a plaque-like structures.
Protein Description May function as a transcription factor with dual roles in transcription initiation and termination. Binds to two sites, ME1a1 and ME1a2, within the MYC promoter having greater affinity for the former. Also binds to multiple G/C-rich sites within the promoter of the Sp1 family of transcription factors. Regulates inflammation-induced expression of serum amyloid A proteins..
Protein Sequence MFPVFPCTLLAPPFPVLGLDSRGVGGLMNSFPPPQGHAQNPLQVGAELQSRFFASQGCAQSPFQAAPAPPPTPQAPAAEPLQVDLLPVLAAAQESAAAAAAAAAAAAAVAAAPPAPAAASTVDTAALKQPPAPPPPPPPVSAPAAEAAPPASAATIAAAAATAVVAPTSTVAVAPVASALEKKTKSKGPYICALCAKEFKNGYNLRRHEAIHTGAKAGRVPSGAMKMPTMVPLSLLSVPQLSGAGGGGGEAGAGGGAAAVAAGGVVTTTASGKRIRKNHACEMCGKAFRDVYHLNRHKLSHSDEKPYQCPVCQQRFKRKDRMSYHVRSHDGAVHKPYNCSHCGKSFSRPDHLNSHVRQVHSTERPFKCEKCEAAFATKDRLRAHTVRHEEKVPCHVCGKMLSSAYISDHMKVHSQGPHHVCELCNKGTGEVCPMAAAAAAAAAAAAAAVAAPPTAVGSLSGAEGVPVSSQPLPSQPW
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
72PhosphorylationAAPAPPPTPQAPAAE
CCCCCCCCCCCCCCC
33.5311809795
73UbiquitinationAPAPPPTPQAPAAEP
CCCCCCCCCCCCCCC
33.82-
73AcetylationAPAPPPTPQAPAAEP
CCCCCCCCCCCCCCC
33.82-
178PhosphorylationVAVAPVASALEKKTK
HHHHHHHHHHHHHHC
33.3521964256
190PhosphorylationKTKSKGPYICALCAK
HHCCCCCEEHHHHHH
19.8028152594
213PhosphorylationRRHEAIHTGAKAGRV
CCHHHHHHCCCCCCC
32.4924719451
213 (in isoform 2)Phosphorylation-32.4924719451
216UbiquitinationEAIHTGAKAGRVPSG
HHHHHCCCCCCCCCC
53.36-
222PhosphorylationAKAGRVPSGAMKMPT
CCCCCCCCCCCCCCC
36.0124719451
222 (in isoform 2)Phosphorylation-36.0124719451
229PhosphorylationSGAMKMPTMVPLSLL
CCCCCCCCCEEHHHH
27.5724905233
234PhosphorylationMPTMVPLSLLSVPQL
CCCCEEHHHHCCCCC
22.6124905233
237PhosphorylationMVPLSLLSVPQLSGA
CEEHHHHCCCCCCCC
36.7224905233
242PhosphorylationLLSVPQLSGAGGGGG
HHCCCCCCCCCCCCC
22.7324905233
267PhosphorylationVAAGGVVTTTASGKR
HHCCCEEEECCCCCC
18.9424905233
268PhosphorylationAAGGVVTTTASGKRI
HCCCEEEECCCCCCH
14.5724905233
269PhosphorylationAGGVVTTTASGKRIR
CCCEEEECCCCCCHH
14.9524905233
271PhosphorylationGVVTTTASGKRIRKN
CEEEECCCCCCHHHC
42.6324905233
273AcetylationVTTTASGKRIRKNHA
EEECCCCCCHHHCHH
42.0030590295
286UbiquitinationHACEMCGKAFRDVYH
HHHHHCCHHHHHHHH
39.15-
298UbiquitinationVYHLNRHKLSHSDEK
HHHHHCCCCCCCCCC
48.74-
300 (in isoform 2)Phosphorylation-26.2527251275
300PhosphorylationHLNRHKLSHSDEKPY
HHHCCCCCCCCCCCC
26.2523927012
302 (in isoform 2)Phosphorylation-44.0524719451
302PhosphorylationNRHKLSHSDEKPYQC
HCCCCCCCCCCCCCC
44.0525159151
305UbiquitinationKLSHSDEKPYQCPVC
CCCCCCCCCCCCCCH
54.75-
305AcetylationKLSHSDEKPYQCPVC
CCCCCCCCCCCCCCH
54.7526051181
307 (in isoform 2)Phosphorylation-33.5427642862
307PhosphorylationSHSDEKPYQCPVCQQ
CCCCCCCCCCCCHHH
33.5423927012
321MethylationQRFKRKDRMSYHVRS
HHHCCCCCCCEECCC
20.98-
323PhosphorylationFKRKDRMSYHVRSHD
HCCCCCCCEECCCCC
17.0027251275
323 (in isoform 2)Phosphorylation-17.0024719451
324PhosphorylationKRKDRMSYHVRSHDG
CCCCCCCEECCCCCC
8.5927251275
335AcetylationSHDGAVHKPYNCSHC
CCCCCCCCCCCCCCC
42.4726051181
345PhosphorylationNCSHCGKSFSRPDHL
CCCCCCCCCCCCHHH
17.4628555341
347PhosphorylationSHCGKSFSRPDHLNS
CCCCCCCCCCHHHHH
50.4224719451
347 (in isoform 2)Phosphorylation-50.4224719451
354PhosphorylationSRPDHLNSHVRQVHS
CCCHHHHHHHHHHHC
29.7128555341
357MethylationDHLNSHVRQVHSTER
HHHHHHHHHHHCCCC
27.64115482727
361PhosphorylationSHVRQVHSTERPFKC
HHHHHHHCCCCCCCC
32.8625159151
361 (in isoform 2)Phosphorylation-32.8624719451
362PhosphorylationHVRQVHSTERPFKCE
HHHHHHCCCCCCCCC
22.5720068231
370AcetylationERPFKCEKCEAAFAT
CCCCCCCCCCHHEEC
47.0125953088
378UbiquitinationCEAAFATKDRLRAHT
CCHHEECHHHHHHHC
37.10-
378AcetylationCEAAFATKDRLRAHT
CCHHEECHHHHHHHC
37.1023749302
385PhosphorylationKDRLRAHTVRHEEKV
HHHHHHHCCCCCCCC
20.46-
391AcetylationHTVRHEEKVPCHVCG
HCCCCCCCCCHHHCC
48.7925953088
402PhosphorylationHVCGKMLSSAYISDH
HHCCHHHHHHHHHHC
14.9327732954
403PhosphorylationVCGKMLSSAYISDHM
HCCHHHHHHHHHHCC
22.5627732954
405PhosphorylationGKMLSSAYISDHMKV
CHHHHHHHHHHCCCH
11.6927732954
407PhosphorylationMLSSAYISDHMKVHS
HHHHHHHHHCCCHHC
14.5927732954
411AcetylationAYISDHMKVHSQGPH
HHHHHCCCHHCCCCH
33.1225953088
414 (in isoform 2)Phosphorylation-39.5625159151
414PhosphorylationSDHMKVHSQGPHHVC
HHCCCHHCCCCHHHH
39.5628674419
428PhosphorylationCELCNKGTGEVCPMA
HHHCCCCCCCCCHHH
31.6021406692
454PhosphorylationAAVAAPPTAVGSLSG
HHHHCCCCCCCCCCC
32.6823663014
458PhosphorylationAPPTAVGSLSGAEGV
CCCCCCCCCCCCCCC
16.8623663014
460PhosphorylationPTAVGSLSGAEGVPV
CCCCCCCCCCCCCCC
37.3423663014
468PhosphorylationGAEGVPVSSQPLPSQ
CCCCCCCCCCCCCCC
19.7223663014
469PhosphorylationAEGVPVSSQPLPSQP
CCCCCCCCCCCCCCC
35.7323663014
474PhosphorylationVSSQPLPSQPW----
CCCCCCCCCCC----
57.4623663014

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
72TPhosphorylationKinaseMAPK3P27361
GPS
385TPhosphorylationKinaseAKT1P31749
PSP
460SPhosphorylationKinaseCSNK2A1P68400
GPS
469SPhosphorylationKinaseCK2-FAMILY-GPS
469SPhosphorylationKinaseCK2_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAZ_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 MAZ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BPTF_HUMANBPTFphysical
10727212
DCC_HUMANDCCphysical
11527412
FOS_HUMANFOSphysical
19028685
JUN_HUMANJUNphysical
19028685
APOD_HUMANAPODphysical
28514442

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 MAZ_HUMAN

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Related Literatures of Post-Translational Modification

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