MAFK_HUMAN - dbPTM
MAFK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAFK_HUMAN
UniProt AC O60675
Protein Name Transcription factor MafK
Gene Name MAFK
Organism Homo sapiens (Human).
Sequence Length 156
Subcellular Localization Nucleus.
Protein Description Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. [PubMed: 9150357 However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3, and recruiting them to specific DNA-binding sites]
Protein Sequence MTTNPKPNKALKVKKEAGENAPVLSDDELVSMSVRELNQHLRGLTKEEVTRLKQRRRTLKNRGYAASCRIKRVTQKEELERQRVELQQEVEKLARENSSMRLELDALRSKYEALQTFARTVARGPVAPSKVATTSVITIVKSTELSSTSVPFSAAS
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
2Phosphorylation------MTTNPKPNK
------CCCCCCCCC
34.9726699800
3Phosphorylation-----MTTNPKPNKA
-----CCCCCCCCCC
48.5026699800
9UbiquitinationTTNPKPNKALKVKKE
CCCCCCCCCCCCCCC
64.72-
25PhosphorylationGENAPVLSDDELVSM
CCCCCCCCHHHHHHH
43.1629255136
31PhosphorylationLSDDELVSMSVRELN
CCHHHHHHHHHHHHH
20.2629255136
33PhosphorylationDDELVSMSVRELNQH
HHHHHHHHHHHHHHH
15.5429396449
46SumoylationQHLRGLTKEEVTRLK
HHHCCCCHHHHHHHH
57.85-
46UbiquitinationQHLRGLTKEEVTRLK
HHHCCCCHHHHHHHH
57.85-
46SumoylationQHLRGLTKEEVTRLK
HHHCCCCHHHHHHHH
57.85-
71AcetylationYAASCRIKRVTQKEE
HHHHHHEEECCCHHH
22.8220167786
74PhosphorylationSCRIKRVTQKEELER
HHHEEECCCHHHHHH
37.65-
76UbiquitinationRIKRVTQKEELERQR
HEEECCCHHHHHHHH
43.73-
76SumoylationRIKRVTQKEELERQR
HEEECCCHHHHHHHH
43.73-
76SumoylationRIKRVTQKEELERQR
HEEECCCHHHHHHHH
43.73-
92UbiquitinationELQQEVEKLARENSS
HHHHHHHHHHHHCCC
53.26-
98PhosphorylationEKLARENSSMRLELD
HHHHHHCCCHHHHHH
22.2828555341
99PhosphorylationKLARENSSMRLELDA
HHHHHCCCHHHHHHH
21.3625954137
109PhosphorylationLELDALRSKYEALQT
HHHHHHHHHHHHHHH
40.2025954137
110UbiquitinationELDALRSKYEALQTF
HHHHHHHHHHHHHHH
40.4521890473
110UbiquitinationELDALRSKYEALQTF
HHHHHHHHHHHHHHH
40.4521890473
110SumoylationELDALRSKYEALQTF
HHHHHHHHHHHHHHH
40.45-
110SumoylationELDALRSKYEALQTF
HHHHHHHHHHHHHHH
40.45-
111PhosphorylationLDALRSKYEALQTFA
HHHHHHHHHHHHHHH
14.00-
120O-linked_GlycosylationALQTFARTVARGPVA
HHHHHHHHHHCCCCC
18.3220068230
130SumoylationRGPVAPSKVATTSVI
CCCCCCCCCEECEEE
34.5328112733
130UbiquitinationRGPVAPSKVATTSVI
CCCCCCCCCEECEEE
34.53-
133PhosphorylationVAPSKVATTSVITIV
CCCCCCEECEEEEEE
23.69-
133O-linked_GlycosylationVAPSKVATTSVITIV
CCCCCCEECEEEEEE
23.6920068230
134PhosphorylationAPSKVATTSVITIVK
CCCCCEECEEEEEEE
15.9720068230
134O-linked_GlycosylationAPSKVATTSVITIVK
CCCCCEECEEEEEEE
15.9720068230
134O-linked_GlycosylationAPSKVATTSVITIVK
CCCCCEECEEEEEEE
15.9730059200
135O-linked_GlycosylationPSKVATTSVITIVKS
CCCCEECEEEEEEEC
13.7320068230
138O-linked_GlycosylationVATTSVITIVKSTEL
CEECEEEEEEECCCC
19.9820068230
142O-linked_GlycosylationSVITIVKSTELSSTS
EEEEEEECCCCCCCC
19.0720068230
146O-linked_GlycosylationIVKSTELSSTSVPFS
EEECCCCCCCCCCCC
25.9020068230
147O-linked_GlycosylationVKSTELSSTSVPFSA
EECCCCCCCCCCCCC
37.0120068230
153O-linked_GlycosylationSSTSVPFSAAS----
CCCCCCCCCCC----
19.4930059200
153O-linked_GlycosylationSSTSVPFSAAS----
CCCCCCCCCCC----
19.4920068230
156O-linked_GlycosylationSVPFSAAS-------
CCCCCCCC-------
40.2320068230

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 MAFK_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAFK_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 MAFK_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NF2L2_HUMANNFE2L2physical
10747902
KAT6A_HUMANKAT6Aphysical
17083329
BACH1_HUMANBACH1physical
19011633
HDAC1_HUMANHDAC1physical
18241676
HDAC2_HUMANHDAC2physical
18241676
HDAC3_HUMANHDAC3physical
18241676
TF65_HUMANRELAphysical
18241676
NF2L2_HUMANNFE2L2physical
21988832
NF2L2_HUMANNFE2L2physical
23737527

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 MAFK_HUMAN

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Related Literatures of Post-Translational Modification
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-25, AND MASSSPECTROMETRY.
"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-25, AND MASSSPECTROMETRY.
"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-25, AND MASSSPECTROMETRY.

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