MAF1_HUMAN - dbPTM
MAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAF1_HUMAN
UniProt AC Q9H063
Protein Name Repressor of RNA polymerase III transcription MAF1 homolog
Gene Name MAF1
Organism Homo sapiens (Human).
Sequence Length 256
Subcellular Localization Nucleus. Cytoplasm.
Protein Description Element of the mTORC1 signaling pathway that acts as a mediator of diverse signals and that represses RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA..
Protein Sequence MKLLENSSFEAINSQLTVETGDAHIIGRIESYSCKMAGDDKHMFKQFCQEGQPHVLEALSPPQTSGLSPSRLSKSQGGEEEGPLSDKCSRKTLFYLIATLNESFRPDYDFSTARSHEFSREPSLSWVVNAVNCSLFSAVREDFKDLKPQLWNAVDEEICLAECDIYSYNPDLDSDPFGEDGSLWSFNYFFYNKRLKRIVFFSCRSISGSTYTPSEAGNELDMELGEEEVEEESRSGGSGAEETSTMEEDRVPVICI
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
35SumoylationRIESYSCKMAGDDKH
EEEEECCEECCCCHH
26.33-
35SumoylationRIESYSCKMAGDDKH
EEEEECCEECCCCHH
26.33-
60PhosphorylationPHVLEALSPPQTSGL
CCHHHHCCCCCCCCC
41.4030266825
64PhosphorylationEALSPPQTSGLSPSR
HHCCCCCCCCCCHHH
30.4523401153
65PhosphorylationALSPPQTSGLSPSRL
HCCCCCCCCCCHHHH
32.2723401153
68PhosphorylationPPQTSGLSPSRLSKS
CCCCCCCCHHHHCCC
25.1022167270
70PhosphorylationQTSGLSPSRLSKSQG
CCCCCCHHHHCCCCC
42.3430266825
73PhosphorylationGLSPSRLSKSQGGEE
CCCHHHHCCCCCCCC
29.2030266825
74UbiquitinationLSPSRLSKSQGGEEE
CCHHHHCCCCCCCCC
51.9327667366
75PhosphorylationSPSRLSKSQGGEEEG
CHHHHCCCCCCCCCC
30.5929255136
85PhosphorylationGEEEGPLSDKCSRKT
CCCCCCCCHHHCHHH
37.8523403867
87UbiquitinationEEGPLSDKCSRKTLF
CCCCCCHHHCHHHHH
30.63-
89PhosphorylationGPLSDKCSRKTLFYL
CCCCHHHCHHHHHHH
42.4223312004
205PhosphorylationIVFFSCRSISGSTYT
EEEEEEEECCCCCCC
25.9829978859
207PhosphorylationFFSCRSISGSTYTPS
EEEEEECCCCCCCCC
28.1229978859
209PhosphorylationSCRSISGSTYTPSEA
EEEECCCCCCCCCHH
16.0829978859
210PhosphorylationCRSISGSTYTPSEAG
EEECCCCCCCCCHHC
34.6329978859
211PhosphorylationRSISGSTYTPSEAGN
EECCCCCCCCCHHCC
20.5329978859
212PhosphorylationSISGSTYTPSEAGNE
ECCCCCCCCCHHCCC
22.0429978859
214PhosphorylationSGSTYTPSEAGNELD
CCCCCCCCHHCCCCC
32.0711230166
235PhosphorylationEVEEESRSGGSGAEE
HHHHHHHCCCCCCCC
57.7024719451
238PhosphorylationEESRSGGSGAEETST
HHHHCCCCCCCCCCC
38.0528348404
243PhosphorylationGGSGAEETSTMEEDR
CCCCCCCCCCCCCCC
22.4728787133
244PhosphorylationGSGAEETSTMEEDRV
CCCCCCCCCCCCCCC
29.0928348404
245PhosphorylationSGAEETSTMEEDRVP
CCCCCCCCCCCCCCC
35.7028348404

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
60SPhosphorylationKinaseMTORP42345
Uniprot
68SPhosphorylationKinaseMTORP42345
Uniprot
75SPhosphorylationKinaseMTORP42345
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
35KSumoylation

23673667
60SPhosphorylation

18669648
68SPhosphorylation

20233713
75SPhosphorylation

17081983

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 MAF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAF1_HUMANMAF1physical
20817737
RAD50_HUMANRAD50physical
26186194
TSR3_HUMANTSR3physical
26186194
KC1D_HUMANCSNK1Dphysical
26186194
VCIP1_HUMANVCPIP1physical
26186194
ARMX3_HUMANARMCX3physical
26186194
RPC1_HUMANPOLR3Aphysical
26186194
RPC6_HUMANPOLR3Fphysical
26186194
RPC2_HUMANPOLR3Bphysical
26186194
RPC6_HUMANPOLR3Fphysical
28514442
VCIP1_HUMANVCPIP1physical
28514442
TSR3_HUMANTSR3physical
28514442
ARMX3_HUMANARMCX3physical
28514442
FSBP_HUMANRAD54Bphysical
28514442
RA54B_HUMANRAD54Bphysical
28514442
RAD50_HUMANRAD50physical
28514442
KC1D_HUMANCSNK1Dphysical
28514442
RPC1_HUMANPOLR3Aphysical
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 MAF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, andtargets their repressor Maf1.";
Kantidakis T., Ramsbottom B.A., Birch J.L., Dowding S.N., White R.J.;
Proc. Natl. Acad. Sci. U.S.A. 107:11823-11828(2010).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-75, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-75.
"mTORC1 directly phosphorylates and regulates human MAF1.";
Michels A.A., Robitaille A.M., Buczynski-Ruchonnet D., Hodroj W.,Reina J.H., Hall M.N., Hernandez N.;
Mol. Cell. Biol. 30:3749-3757(2010).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-60; SER-68 AND SER-75 BY MTOR,PHOSPHORYLATION AT THR-64; SER-65; SER-70; THR-212 AND SER-214, ANDMUTAGENESIS OF SER-60; SER-68 AND SER-75.
"Requirement of the mTOR kinase for the regulation of Maf1phosphorylation and control of RNA polymerase III-dependenttranscription in cancer cells.";
Shor B., Wu J., Shakey Q., Toral-Barza L., Shi C., Follettie M.,Yu K.;
J. Biol. Chem. 285:15380-15392(2010).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-60; THR-64; SER-68 AND SER-75,SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-60; THR-64; SER-68 ANDSER-75.
"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-75, 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-60; SER-68 AND SER-75,AND MASS 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-75, AND MASSSPECTROMETRY.

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