TF3A_HUMAN - dbPTM
TF3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF3A_HUMAN
UniProt AC Q92664
Protein Name Transcription factor IIIA
Gene Name GTF3A
Organism Homo sapiens (Human).
Sequence Length 365
Subcellular Localization Nucleus.
Protein Description Involved in ribosomal large subunit biogenesis. Binds the approximately 50 base pairs internal control region (ICR) of 5S ribosomal RNA genes. It is required for their RNA polymerase III-dependent transcription and may also maintain the transcription of other genes. [PubMed: 24120868 Also binds the transcribed 5S RNA's (By similarity]
Protein Sequence MDPPAVVAESVSSLTIADAFIAAGESSAPTPPRPALPRRFICSFPDCSANYSKAWKLDAHLCKHTGERPFVCDYEGCGKAFIRDYHLSRHILTHTGEKPFVCAANGCDQKFNTKSNLKKHFERKHENQQKQYICSFEDCKKTFKKHQQLKIHQCQHTNEPLFKCTQEGCGKHFASPSKLKRHAKAHEGYVCQKGCSFVAKTWTELLKHVRETHKEEILCEVCRKTFKRKDYLKQHMKTHAPERDVCRCPREGCGRTYTTVFNLQSHILSFHEESRPFVCEHAGCGKTFAMKQSLTRHAVVHDPDKKKMKLKVKKSREKRSLASHLSGYIPPKRKQGQGLSLCQNGESPNCVEDKMLSTVAVLTLG
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
26PhosphorylationAFIAAGESSAPTPPR
HHHHCCCCCCCCCCC
30.7726074081
27PhosphorylationFIAAGESSAPTPPRP
HHHCCCCCCCCCCCC
33.6824719451
30PhosphorylationAGESSAPTPPRPALP
CCCCCCCCCCCCCCC
45.7126074081
51PhosphorylationFPDCSANYSKAWKLD
CCCCCCCHHHHHHCH
15.97-
52PhosphorylationPDCSANYSKAWKLDA
CCCCCCHHHHHHCHH
18.72-
65PhosphorylationDAHLCKHTGERPFVC
HHHHHHHCCCCCEEE
26.6628555341
74PhosphorylationERPFVCDYEGCGKAF
CCCEEECCCCCCHHH
14.75-
85PhosphorylationGKAFIRDYHLSRHIL
CHHHHHHHHHHCCCH
8.5324719451
93PhosphorylationHLSRHILTHTGEKPF
HHHCCCHHCCCCCCE
19.4529214152
95PhosphorylationSRHILTHTGEKPFVC
HCCCHHCCCCCCEEE
41.6328555341
114UbiquitinationCDQKFNTKSNLKKHF
CCCCCCCHHHHHHHH
38.1529967540
150UbiquitinationFKKHQQLKIHQCQHT
HHHHHHHEEEECCCC
33.5329967540
157PhosphorylationKIHQCQHTNEPLFKC
EEEECCCCCCCCCCC
18.5228555341
165PhosphorylationNEPLFKCTQEGCGKH
CCCCCCCCCCCCCCC
30.1926657352
175PhosphorylationGCGKHFASPSKLKRH
CCCCCCCCHHHHHHH
28.8523927012
177PhosphorylationGKHFASPSKLKRHAK
CCCCCCHHHHHHHHH
48.3930576142
193UbiquitinationHEGYVCQKGCSFVAK
CCCCCCCCCCHHHHH
57.6829967540
227AcetylationEVCRKTFKRKDYLKQ
HHHHHHHCCHHHHHH
64.8620167786
233AcetylationFKRKDYLKQHMKTHA
HCCHHHHHHHHHHCC
31.7420167786
340PhosphorylationRKQGQGLSLCQNGES
CCCCCCCCCCCCCCC
33.6428450419
347PhosphorylationSLCQNGESPNCVEDK
CCCCCCCCCCHHHHH
23.8621815630

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 TF3A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TF3A_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 TF3A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TF3A_HUMAN !!

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 TF3A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND MASSSPECTROMETRY.

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