TF3C2_MOUSE - dbPTM
TF3C2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF3C2_MOUSE
UniProt AC Q8BL74
Protein Name General transcription factor 3C polypeptide 2
Gene Name Gtf3c2
Organism Mus musculus (Mouse).
Sequence Length 907
Subcellular Localization Nucleus.
Protein Description Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. May play a direct role in stabilizing interactions of TFIIIC2 with TFIIIC1 (By similarity)..
Protein Sequence MDTCGVGYVALGEADPVGSMIVVDSPGQEELSQLDVKASETSGVEASIEMSLPPPLPGFEDSSDRRLPPDQESLTRLEQQDLSSEMSKVSNTRASKPSGRRGGRTARGAKRPQQRKPPSTPLVPGLLDQSNPLSTPMPKKRSQKSKGDLLLLKLSKGLDQPESPHPKRPPEDFETPSGERPRRRAAQVALLYLQELAEELSTALPAPPLSGPKSPKVSSPTKPKKTRQASSQGEEDGSARDEDFVLQVEGEDEEESEAPSENSSDPEPVAPRSTPRGPAAGKQKPHCRGMAPNGLPNYIMAPVWKCLHLTKDLREQHHSFWEFAEWIPVAWKWQLLSELEAAPYLPQEEKSPLFSVQREGIPEDGTIYRINRFSSITAHPERWDVSFFTGGPLWALDWCPVPEGSAASQYVALFSSPDMNETHPLSQLHSGPGLLQLWGLGTLQQESCPGNRAHFVYGIACDSGCIWDLKFCPSGAWEHPETLRKAPLLPRLGLLALACSDGKVLLFSLPHPEALLAQQPPDAMKPAIYKVQCLATLQVGSVQASDPSECGQCLSLAWMPTRPHHHLAAGYYNGMVVFWNLPTNSPLQRIRLSDGSLKLYPFQCFLAHDQAVRTIQWCKANSHFLVSAGSDRKIKFWDLRRPYEPINCIKRFLSTELSWLLPYNGVTVAQDNCYASYGLCGIHYIDAGYLGFKAYFTAPRKGTVWSLSGSDWLGTVAAGDISGELIAAILPDMASNPINVKKPAERRFPIYKADLIPYQDSPEDQDYSSTSSETPNPPKARTYTETINHHYLLFQDTDLSSFHNLLRREPMLRMQEGEGHSQLCLDRLQLEAIHKVRFSPNLDSYGWLVSGGQSGLVRIHFVRGLTSPLAHRVQLESRANFNAMFQPSFPTEGPGFSPSSHCLLPNP
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
25PhosphorylationGSMIVVDSPGQEELS
CCEEEECCCCCHHHH		21.2230352176
62PhosphorylationPLPGFEDSSDRRLPP
CCCCCCCCCCCCCCC		27.26-
83PhosphorylationRLEQQDLSSEMSKVS
HHHHHHHHHHHHHHH		32.3227841257
84PhosphorylationLEQQDLSSEMSKVSN
HHHHHHHHHHHHHHC		44.6127841257
90PhosphorylationSSEMSKVSNTRASKP
HHHHHHHHCCCCCCC		35.9030387612
96MethylationVSNTRASKPSGRRGG
HHCCCCCCCCCCCCC		42.07-
130PhosphorylationVPGLLDQSNPLSTPM
CCCCCCCCCCCCCCC		39.8326643407
134PhosphorylationLDQSNPLSTPMPKKR
CCCCCCCCCCCCCCC		31.5526643407
135PhosphorylationDQSNPLSTPMPKKRS
CCCCCCCCCCCCCCC		31.1526643407
153AcetylationKGDLLLLKLSKGLDQ
CCCHHHHHHHCCCCC		51.1619849111
163PhosphorylationKGLDQPESPHPKRPP
CCCCCCCCCCCCCCC		34.8825521595
192PhosphorylationAAQVALLYLQELAEE
HHHHHHHHHHHHHHH		13.7423984901
201PhosphorylationQELAEELSTALPAPP
HHHHHHHHHCCCCCC		18.2123984901
202PhosphorylationELAEELSTALPAPPL
HHHHHHHHCCCCCCC		44.8523984901
210PhosphorylationALPAPPLSGPKSPKV
CCCCCCCCCCCCCCC		59.8426239621
214PhosphorylationPPLSGPKSPKVSSPT
CCCCCCCCCCCCCCC		32.8426239621
216AcetylationLSGPKSPKVSSPTKP
CCCCCCCCCCCCCCC		62.9419856619
218PhosphorylationGPKSPKVSSPTKPKK
CCCCCCCCCCCCCCC		36.4026745281
219PhosphorylationPKSPKVSSPTKPKKT
CCCCCCCCCCCCCCC		39.3126824392
221PhosphorylationSPKVSSPTKPKKTRQ
CCCCCCCCCCCCCCC		63.0226745281
230PhosphorylationPKKTRQASSQGEEDG
CCCCCCCCCCCCCCC		18.1723684622
231PhosphorylationKKTRQASSQGEEDGS
CCCCCCCCCCCCCCC		45.2623684622
256PhosphorylationEGEDEEESEAPSENS
ECCCHHHCCCCCCCC		42.19-
593PhosphorylationPLQRIRLSDGSLKLY
CCCEEECCCCCEEEE		30.0325338131
650UbiquitinationYEPINCIKRFLSTEL
CCCCCHHHHHHCCCC		39.02-
695PhosphorylationGYLGFKAYFTAPRKG
CCCCEEEEEECCCCC		11.3123970565
758PhosphorylationYKADLIPYQDSPEDQ
EECCCCCCCCCCCCC		20.2624759943
761PhosphorylationDLIPYQDSPEDQDYS
CCCCCCCCCCCCCCC		18.0519060867
767PhosphorylationDSPEDQDYSSTSSET
CCCCCCCCCCCCCCC		10.0121183079
768PhosphorylationSPEDQDYSSTSSETP
CCCCCCCCCCCCCCC		35.1130635358
769PhosphorylationPEDQDYSSTSSETPN
CCCCCCCCCCCCCCC		26.5319060867
770PhosphorylationEDQDYSSTSSETPNP
CCCCCCCCCCCCCCC		30.2630635358
771PhosphorylationDQDYSSTSSETPNPP
CCCCCCCCCCCCCCC		28.2930635358
772PhosphorylationQDYSSTSSETPNPPK
CCCCCCCCCCCCCCC		45.6519060867
774PhosphorylationYSSTSSETPNPPKAR
CCCCCCCCCCCCCCC		30.2519060867
867PhosphorylationHFVRGLTSPLAHRVQ
EEECCCCCCCHHHHH		23.98-
888PhosphorylationFNAMFQPSFPTEGPG
CCCCCCCCCCCCCCC		32.8325777480
891PhosphorylationMFQPSFPTEGPGFSP
CCCCCCCCCCCCCCC		52.1126643407
897PhosphorylationPTEGPGFSPSSHCLL
CCCCCCCCCCCCCCC		29.7726643407
899PhosphorylationEGPGFSPSSHCLLPN
CCCCCCCCCCCCCCC		31.3626643407
900PhosphorylationGPGFSPSSHCLLPNP
CCCCCCCCCCCCCCC		22.9226643407
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 TF3C2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TF3C2_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 TF3C2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3C1_HUMANGTF3C1physical
26496610
MBP_HUMANMBPphysical
26496610
RL28_HUMANRPL28physical
26496610
TAF10_HUMANTAF10physical
26496610
ZMYM2_HUMANZMYM2physical
26496610
TF3C5_HUMANGTF3C5physical
26496610
TF3C4_HUMANGTF3C4physical
26496610
TF3C3_HUMANGTF3C3physical
26496610
ADNP_HUMANADNPphysical
26496610
S39AA_HUMANSLC39A10physical
26496610
PAPD5_HUMANPAPD5physical
26496610
ZMAT3_HUMANZMAT3physical
26496610
CA131_HUMANC1orf131physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TF3C2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND MASSSPECTROMETRY.

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