UniProt ID | PITH1_HUMAN | |
---|---|---|
UniProt AC | Q9GZP4 | |
Protein Name | PITH domain-containing protein 1 | |
Gene Name | PITHD1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 211 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MSHGHSHGGGGCRCAAEREEPPEQRGLAYGLYLRIDLERLQCLNESREGSGRGVFKPWEERTDRSKFVESDADEELLFNIPFTGNVKLKGIIIMGEDDDSHPSEMRLYKNIPQMSFDDTEREPDQTFSLNRDLTGELEYATKISRFSNVYHLSIHISKNFGADTTKVFYIGLRGEWTELRRHEVTICNYEASANPADHRVHQVTPQTHFIS | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSHGHSHGG ------CCCCCCCCC | 37.87 | - | |
6 | Phosphorylation | --MSHGHSHGGGGCR --CCCCCCCCCCCCC | 28.55 | - | |
52 | Methylation | ESREGSGRGVFKPWE CCCCCCCCCCCCCHH | 39.54 | 115487587 | |
56 | Ubiquitination | GSGRGVFKPWEERTD CCCCCCCCCHHHCCC | 46.98 | - | |
65 (in isoform 2) | Ubiquitination | - | 33.00 | 21890473 | |
66 (in isoform 1) | Ubiquitination | - | 55.08 | 21890473 | |
66 | Ubiquitination | EERTDRSKFVESDAD HHCCCHHHCCCCCCC | 55.08 | 21906983 | |
87 | Ubiquitination | IPFTGNVKLKGIIIM CCCCCCEEEEEEEEE | 48.78 | - | |
89 | Acetylation | FTGNVKLKGIIIMGE CCCCEEEEEEEEECC | 42.20 | 26051181 | |
89 | Ubiquitination | FTGNVKLKGIIIMGE CCCCEEEEEEEEECC | 42.20 | - | |
108 (in isoform 2) | Ubiquitination | - | 7.51 | 21890473 | |
109 (in isoform 1) | Ubiquitination | - | 53.65 | 21890473 | |
109 | Ubiquitination | PSEMRLYKNIPQMSF HHHHHHHHCCCCCCC | 53.65 | 21906983 | |
141 (in isoform 2) | Ubiquitination | - | 28.19 | 21890473 | |
142 | Ubiquitination | GELEYATKISRFSNV CCHHHHHEEECCCCE | 30.43 | 21890473 | |
142 (in isoform 1) | Ubiquitination | - | 30.43 | 21890473 | |
150 | Phosphorylation | ISRFSNVYHLSIHIS EECCCCEEEEEEEEE | 10.99 | - | |
169 | Phosphorylation | ADTTKVFYIGLRGEW CCCEEEEEEEECCCC | 9.32 | - | |
185 | Phosphorylation | ELRRHEVTICNYEAS ECEEEEEEEECCCHH | 19.48 | 21945579 | |
189 | Phosphorylation | HEVTICNYEASANPA EEEEEECCCHHCCCC | 14.41 | 21945579 | |
192 | Phosphorylation | TICNYEASANPADHR EEECCCHHCCCCCCC | 19.35 | 21945579 | |
192 | O-linked_Glycosylation | TICNYEASANPADHR EEECCCHHCCCCCCC | 19.35 | OGP | |
204 | Phosphorylation | DHRVHQVTPQTHFIS CCCCEECCCCCCCCC | 11.78 | 26462736 | |
204 | O-linked_Glycosylation | DHRVHQVTPQTHFIS CCCCEECCCCCCCCC | 11.78 | 54901545 | |
207 | Phosphorylation | VHQVTPQTHFIS--- CEECCCCCCCCC--- | 21.69 | 20068231 | |
207 | O-linked_Glycosylation | VHQVTPQTHFIS--- CEECCCCCCCCC--- | 21.69 | 55828789 | |
211 | Phosphorylation | TPQTHFIS------- CCCCCCCC------- | 32.97 | 25159151 | |
211 | O-linked_Glycosylation | TPQTHFIS------- CCCCCCCC------- | 32.97 | 72257159 |
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 PITH1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PITH1_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 PITH1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CDC73_HUMAN | CDC73 | physical | 16169070 | |
CETN2_HUMAN | CETN2 | physical | 26344197 | |
SLK_HUMAN | SLK | physical | 26344197 | |
1433B_HUMAN | YWHAB | physical | 26344197 | |
WDR59_HUMAN | WDR59 | physical | 28514442 | |
DPYL1_HUMAN | CRMP1 | physical | 28514442 | |
EF1A2_HUMAN | EEF1A2 | physical | 28514442 | |
RPR1A_HUMAN | RPRD1A | physical | 28514442 | |
RECQ5_HUMAN | RECQL5 | 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 |
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-189, AND MASSSPECTROMETRY. |