UniProt ID | SPT17_HUMAN | |
---|---|---|
UniProt AC | Q96L03 | |
Protein Name | Spermatogenesis-associated protein 17 | |
Gene Name | SPATA17 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 361 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | ||
Protein Sequence | MATLARLQARSSTVGNQYYFRNSVVDPFRKKENDAAVKIQSWFRGCQVRAYIRHLNRIVTIIQKWWRSFLGRKQYQLTVQVAYYTMMMNLYNAMAVRIQRRWRGYRVRKYLFNYYYLKEYLKVVSETNDAIRKALEEFAEMKEREEKKANLEREEKKRDYQARKMHYLLSTKQIPGIYNSPFRKEPDPWELQLQKAKPLTHRRPKVKQKDSTSLTDWLACTSARSFPRSEILPPINRKQCQGPFRDITEVLEQRYRPLEPTLRVAEPIDELKLAREELRREEWLQNVNDNMFLPFSSYHKNEKYIPSMHLSSKYGPISYKEQFRSENPKKWICDKDFQTVLPSFELFSKYGKLYSKAGQIV | |
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 |
---|---|---|---|---|---|
12 | Phosphorylation | ARLQARSSTVGNQYY HHHHHHHCCCCCHHH | 22.89 | 22210691 | |
13 | Phosphorylation | RLQARSSTVGNQYYF HHHHHHCCCCCHHHC | 33.41 | 22210691 | |
75 | Phosphorylation | SFLGRKQYQLTVQVA HHCCCCCHHHHHHHH | 14.44 | 24043423 | |
78 | Phosphorylation | GRKQYQLTVQVAYYT CCCCHHHHHHHHHHH | 8.05 | 25262027 | |
83 | Phosphorylation | QLTVQVAYYTMMMNL HHHHHHHHHHHHHHH | 10.70 | 24043423 | |
84 | Phosphorylation | LTVQVAYYTMMMNLY HHHHHHHHHHHHHHH | 4.38 | 24043423 | |
85 | Phosphorylation | TVQVAYYTMMMNLYN HHHHHHHHHHHHHHH | 5.96 | 25262027 | |
91 | Phosphorylation | YTMMMNLYNAMAVRI HHHHHHHHHHHHHHH | 8.89 | 25262027 | |
105 | Phosphorylation | IQRRWRGYRVRKYLF HHHHHCCHHHHHHHH | 9.43 | - | |
115 | Phosphorylation | RKYLFNYYYLKEYLK HHHHHHHHHHHHHHH | 11.92 | - | |
116 | Phosphorylation | KYLFNYYYLKEYLKV HHHHHHHHHHHHHHH | 10.84 | - | |
148 | Ubiquitination | MKEREEKKANLEREE HHHHHHHHHHHHHHH | 45.87 | - | |
167 | Phosphorylation | YQARKMHYLLSTKQI HHHHHHHHHHHHCCC | 13.07 | 29759185 | |
170 | Phosphorylation | RKMHYLLSTKQIPGI HHHHHHHHHCCCCCC | 30.85 | 24719451 | |
171 | Phosphorylation | KMHYLLSTKQIPGIY HHHHHHHHCCCCCCC | 27.26 | 29759185 | |
178 | Phosphorylation | TKQIPGIYNSPFRKE HCCCCCCCCCCCCCC | 18.59 | 29759185 | |
180 | Phosphorylation | QIPGIYNSPFRKEPD CCCCCCCCCCCCCCC | 14.40 | 29759185 | |
211 | Phosphorylation | PKVKQKDSTSLTDWL CCCCCCCCCCHHHHH | 27.25 | 25693802 | |
212 | Phosphorylation | KVKQKDSTSLTDWLA CCCCCCCCCHHHHHH | 37.58 | 25693802 | |
213 | Phosphorylation | VKQKDSTSLTDWLAC CCCCCCCCHHHHHHH | 32.97 | 25693802 | |
215 | Phosphorylation | QKDSTSLTDWLACTS CCCCCCHHHHHHHHC | 25.54 | 25693802 | |
348 | Phosphorylation | LPSFELFSKYGKLYS HHHHHHHHHHCHHHH | 37.28 | 24719451 |
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 SPT17_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPT17_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 SPT17_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KDM1B_HUMAN | KDM1B | physical | 26186194 | |
KDM1B_HUMAN | KDM1B | 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 |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND MASSSPECTROMETRY. |