UniProt ID | TCF19_HUMAN | |
---|---|---|
UniProt AC | Q9Y242 | |
Protein Name | Transcription factor 19 | |
Gene Name | TCF19 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 345 | |
Subcellular Localization | Nucleus . | |
Protein Description | Potential trans-activating factor that could play an important role in the transcription of genes required for the later stages of cell cycle progression.. | |
Protein Sequence | MLPCFQLLRIGGGRGGDLYTFHPPAGAGCTYRLGHRADLCDVALRPQQEPGLISGIHAELHAEPRGDDWRVSLEDHSSQGTLVNNVRLPRGHRLELSDGDLLTFGPEGPPGTSPSEFYFMFQQVRVKPQDFAAITIPRSRGEARVGAGFRPMLPSQGAPQRPLSTFSPAPKATLILNSIGSLSKLRPQPLTFSPSWGGPKSLPVPAPPGEMGTTPSAPPQRNRRKSVHRVLAELDDESEPPENPPPVLMEPRKKLRVDKAPLTPTGNRRGRPRKYPVSAPMAPPAVGGGEPCAAPCCCLPQEETVAWVQCDGCDVWFHVACVGCSIQAAREADFRCPGCRAGIQT | |
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 |
---|---|---|---|---|---|
14 | Methylation | LLRIGGGRGGDLYTF EEEECCCCCCCCEEE | 49.55 | 30761345 | |
19 | Phosphorylation | GGRGGDLYTFHPPAG CCCCCCCEEECCCCC | 16.46 | - | |
20 | Phosphorylation | GRGGDLYTFHPPAGA CCCCCCEEECCCCCC | 23.82 | - | |
30 | Phosphorylation | PPAGAGCTYRLGHRA CCCCCCCCEECCCCC | 15.68 | - | |
31 | Phosphorylation | PAGAGCTYRLGHRAD CCCCCCCEECCCCCC | 14.12 | - | |
78 | Phosphorylation | VSLEDHSSQGTLVNN EEEECCCCCCEEEEC | 29.25 | 17525332 | |
135 | Phosphorylation | PQDFAAITIPRSRGE CCCEEEEEEECCCCC | 21.87 | 24719451 | |
138 | Methylation | FAAITIPRSRGEARV EEEEEEECCCCCCCC | 34.83 | 115918329 | |
155 | Phosphorylation | GFRPMLPSQGAPQRP CCCCCCCCCCCCCCC | 36.97 | - | |
181 | Phosphorylation | LILNSIGSLSKLRPQ EEECCCCCHHHCCCC | 28.00 | 25627689 | |
183 | Phosphorylation | LNSIGSLSKLRPQPL ECCCCCHHHCCCCCC | 31.20 | 25627689 | |
191 | Phosphorylation | KLRPQPLTFSPSWGG HCCCCCCCCCCCCCC | 28.84 | 25159151 | |
193 | Phosphorylation | RPQPLTFSPSWGGPK CCCCCCCCCCCCCCC | 16.88 | 22199227 | |
195 | Phosphorylation | QPLTFSPSWGGPKSL CCCCCCCCCCCCCCC | 36.84 | 29514088 | |
263 | Phosphorylation | RVDKAPLTPTGNRRG CCCCCCCCCCCCCCC | 20.11 | 27732954 | |
265 | Phosphorylation | DKAPLTPTGNRRGRP CCCCCCCCCCCCCCC | 41.68 | 27732954 |
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 TCF19_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TCF19_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 TCF19_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TNR16_HUMAN | NGFR | physical | 10485890 | |
LZTR1_HUMAN | LZTR1 | physical | 20211142 | |
A4_HUMAN | APP | physical | 21832049 | |
DNJA3_HUMAN | DNAJA3 | physical | 25416956 | |
E2F6_HUMAN | E2F6 | physical | 28514442 | |
MBD3_HUMAN | MBD3 | physical | 28514442 | |
MTA3_HUMAN | MTA3 | physical | 28514442 | |
MTA2_HUMAN | MTA2 | physical | 28514442 | |
LIN9_HUMAN | LIN9 | physical | 28514442 | |
P66B_HUMAN | GATAD2B | physical | 28514442 | |
MTA1_HUMAN | MTA1 | physical | 28514442 |
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 |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASSSPECTROMETRY. |