UniProt ID | TSSK1_HUMAN | |
---|---|---|
UniProt AC | Q9BXA7 | |
Protein Name | Testis-specific serine/threonine-protein kinase 1 | |
Gene Name | TSSK1B | |
Organism | Homo sapiens (Human). | |
Sequence Length | 367 | |
Subcellular Localization | Cytoplasm. Cytoplasmic vesicle, secretory vesicle, acrosome. Cell projection, cilium, flagellum. In spermatozoa, present in the sperm head and in the flagellum.. | |
Protein Description | Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-288' of TSKS. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.. | |
Protein Sequence | MDDAAVLKRRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPSVAINKEGESSRGTEPLWTPEPGSDKKSATKLEPEGEAQPQAQPETKPEGTAMQMSRQSEILGFPSKPSTMETEEGPPQQPPETRAQ | |
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 | AVLKRRGYLLGINLG HHHHHCCEEEEEECC | 9.28 | 22817900 | |
31 | Phosphorylation | AKVKSAYSERLKFNV HHHHHHHHHHHCEEE | 18.89 | 30622161 | |
71 | Phosphorylation | LAMLNHCSIIKTYEI HHHHHCCCCCEEEEE | 21.57 | 24719451 | |
75 | Phosphorylation | NHCSIIKTYEIFETS HCCCCCEEEEEEECC | 18.91 | 27794612 | |
76 | Phosphorylation | HCSIIKTYEIFETSH CCCCCEEEEEEECCC | 11.30 | 27794612 | |
156 | Phosphorylation | NIKLSDFSFSKRCLR CEEHHHCCCCCHHHC | 33.33 | 24719451 | |
158 | Phosphorylation | KLSDFSFSKRCLRDD EHHHCCCCCHHHCCC | 20.28 | 30622161 | |
159 | Acetylation | LSDFSFSKRCLRDDS HHHCCCCCHHHCCCC | 45.15 | 19824351 | |
172 | Phosphorylation | DSGRMALSKTFCGSP CCCCEEECCCCCCCC | 21.80 | - | |
174 | Phosphorylation | GRMALSKTFCGSPAY CCEEECCCCCCCCCC | 22.30 | 25693802 | |
178 | Phosphorylation | LSKTFCGSPAYAAPE ECCCCCCCCCCCCHH | 13.92 | 30622161 | |
181 | Phosphorylation | TFCGSPAYAAPEVLQ CCCCCCCCCCHHHHC | 13.49 | 25693802 | |
197 | Phosphorylation | IPYQPKVYDIWSLGV CCCCCCHHHHHHHHH | 14.08 | - | |
207 | Phosphorylation | WSLGVILYIMVCGSM HHHHHHHHHHHHCCC | 3.94 | - | |
216 | Phosphorylation | MVCGSMPYDDSNIKK HHHCCCCCCCCCHHH | 24.60 | - | |
250 | Phosphorylation | GECKDLIYHMLQPDV HHHHHHHHHHHCCCH | 6.62 | 25003641 | |
279 | Phosphorylation | MQPKARGSPSVAINK CCCCCCCCCCEEECC | 14.40 | 23403867 | |
281 | Phosphorylation | PKARGSPSVAINKEG CCCCCCCCEEECCCC | 26.36 | 23403867 | |
290 | Phosphorylation | AINKEGESSRGTEPL EECCCCCCCCCCCCC | 35.87 | - | |
291 | Phosphorylation | INKEGESSRGTEPLW ECCCCCCCCCCCCCC | 30.35 | - | |
308 | Phosphorylation | EPGSDKKSATKLEPE CCCCCCCCCCCCCCC | 47.08 | 25693802 | |
310 | Phosphorylation | GSDKKSATKLEPEGE CCCCCCCCCCCCCCC | 43.16 | 25693802 | |
326 | Phosphorylation | QPQAQPETKPEGTAM CCCCCCCCCCCCCCC | 59.59 | 25693802 | |
331 | Phosphorylation | PETKPEGTAMQMSRQ CCCCCCCCCCHHHCC | 19.79 | 29978859 | |
336 | Phosphorylation | EGTAMQMSRQSEILG CCCCCHHHCCHHHHC | 15.41 | 29978859 | |
339 | Phosphorylation | AMQMSRQSEILGFPS CCHHHCCHHHHCCCC | 26.03 | 29978859 | |
346 | Phosphorylation | SEILGFPSKPSTMET HHHHCCCCCCCCCCC | 55.74 | 29978859 | |
349 | Phosphorylation | LGFPSKPSTMETEEG HCCCCCCCCCCCCCC | 44.09 | 25693802 | |
350 | Phosphorylation | GFPSKPSTMETEEGP CCCCCCCCCCCCCCC | 27.79 | 25693802 | |
353 | Phosphorylation | SKPSTMETEEGPPQQ CCCCCCCCCCCCCCC | 28.63 | 25693802 | |
364 | Phosphorylation | PPQQPPETRAQ---- CCCCCCCCCCC---- | 36.76 | 25693802 |
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 TSSK1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TSSK1_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 TSSK1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HSP7C_HUMAN | HSPA8 | physical | 26186194 | |
HSP76_HUMAN | HSPA6 | physical | 26186194 | |
HSP72_HUMAN | HSPA2 | physical | 26186194 | |
EFTU_HUMAN | TUFM | physical | 26186194 | |
CP131_HUMAN | CEP131 | physical | 26186194 | |
GEPH_HUMAN | GPHN | physical | 26186194 | |
CRBG3_HUMAN | CRYBG3 | physical | 26186194 | |
BORA_HUMAN | BORA | physical | 26186194 | |
GAPD1_HUMAN | GAPVD1 | physical | 26186194 | |
SNX24_HUMAN | SNX24 | physical | 26186194 | |
CRBG3_HUMAN | CRYBG3 | physical | 28514442 | |
CP131_HUMAN | CEP131 | physical | 28514442 | |
GEPH_HUMAN | GPHN | physical | 28514442 | |
SNX24_HUMAN | SNX24 | physical | 28514442 | |
GAPD1_HUMAN | GAPVD1 | physical | 28514442 | |
HSP7C_HUMAN | HSPA8 | physical | 28514442 | |
KI67_HUMAN | MKI67 | physical | 28514442 | |
HSP72_HUMAN | HSPA2 | 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. |
loading...
Phosphorylation | |
Reference | PubMed |
"Identification of the sucrose non-fermenting related kinase SNRK, asa novel LKB1 substrate."; Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A.,Alessi D.R.; FEBS Lett. 579:1417-1423(2005). Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION,AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-174, AND MUTAGENESIS OFTHR-174. |