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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
26 | Phosphorylation | AFIAAGESSAPTPPR HHHHCCCCCCCCCCC | 30.77 | 26074081 | |
27 | Phosphorylation | FIAAGESSAPTPPRP HHHCCCCCCCCCCCC | 33.68 | 24719451 | |
30 | Phosphorylation | AGESSAPTPPRPALP CCCCCCCCCCCCCCC | 45.71 | 26074081 | |
51 | Phosphorylation | FPDCSANYSKAWKLD CCCCCCCHHHHHHCH | 15.97 | - | |
52 | Phosphorylation | PDCSANYSKAWKLDA CCCCCCHHHHHHCHH | 18.72 | - | |
65 | Phosphorylation | DAHLCKHTGERPFVC HHHHHHHCCCCCEEE | 26.66 | 28555341 | |
74 | Phosphorylation | ERPFVCDYEGCGKAF CCCEEECCCCCCHHH | 14.75 | - | |
85 | Phosphorylation | GKAFIRDYHLSRHIL CHHHHHHHHHHCCCH | 8.53 | 24719451 | |
93 | Phosphorylation | HLSRHILTHTGEKPF HHHCCCHHCCCCCCE | 19.45 | 29214152 | |
95 | Phosphorylation | SRHILTHTGEKPFVC HCCCHHCCCCCCEEE | 41.63 | 28555341 | |
114 | Ubiquitination | CDQKFNTKSNLKKHF CCCCCCCHHHHHHHH | 38.15 | 29967540 | |
150 | Ubiquitination | FKKHQQLKIHQCQHT HHHHHHHEEEECCCC | 33.53 | 29967540 | |
157 | Phosphorylation | KIHQCQHTNEPLFKC EEEECCCCCCCCCCC | 18.52 | 28555341 | |
165 | Phosphorylation | NEPLFKCTQEGCGKH CCCCCCCCCCCCCCC | 30.19 | 26657352 | |
175 | Phosphorylation | GCGKHFASPSKLKRH CCCCCCCCHHHHHHH | 28.85 | 23927012 | |
177 | Phosphorylation | GKHFASPSKLKRHAK CCCCCCHHHHHHHHH | 48.39 | 30576142 | |
193 | Ubiquitination | HEGYVCQKGCSFVAK CCCCCCCCCCHHHHH | 57.68 | 29967540 | |
227 | Acetylation | EVCRKTFKRKDYLKQ HHHHHHHCCHHHHHH | 64.86 | 20167786 | |
233 | Acetylation | FKRKDYLKQHMKTHA HCCHHHHHHHHHHCC | 31.74 | 20167786 | |
340 | Phosphorylation | RKQGQGLSLCQNGES CCCCCCCCCCCCCCC | 33.64 | 28450419 | |
347 | Phosphorylation | SLCQNGESPNCVEDK CCCCCCCCCCHHHHH | 23.86 | 21815630 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TF3A_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of TF3A_HUMAN !! |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |