| UniProt ID | STN1_HUMAN | |
|---|---|---|
| UniProt AC | Q9H668 | |
| Protein Name | CST complex subunit STN1 | |
| Gene Name | STN1 {ECO:0000312|HGNC:HGNC:26200} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 368 | |
| Subcellular Localization | Nucleus . Chromosome, telomere . | |
| Protein Description | Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation. [PubMed: 19854130 However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha] | |
| Protein Sequence | MQPGSSRCEEETPSLLWGLDPVFLAFAKLYIRDILDMKESRQVPGVFLYNGHPIKQVDVLGTVIGVRERDAFYSYGVDDSTGVINCICWKKLNTESVSAAPSAARELSLTSQLKKLQETIEQKTKIEIGDTIRVRGSIRTYREEREIHATTYYKVDDPVWNIQIARMLELPTIYRKVYDQPFHSSALEKEEALSNPGALDLPSLTSLLSEKAKEFLMENRVQSFYQQELEMVESLLSLANQPVIHSASSDQVNFKKDTTSKAIHSIFKNAIQLLQEKGLVFQKDDGFDNLYYVTREDKDLHRKIHRIIQQDCQKPNHMEKGCHFLHILACARLSIRPGLSEAVLQQVLELLEDQSDIVSTMEHYYTAF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 38 | Ubiquitination | IRDILDMKESRQVPG HHHHHCCHHHCCCCC | 52.81 | 29967540 | |
| 55 | Ubiquitination | LYNGHPIKQVDVLGT EECCEECCEEEEEEE | 49.04 | - | |
| 90 | Ubiquitination | VINCICWKKLNTESV EEEEEEEEECCCCCC | 42.86 | 22817900 | |
| 91 | Ubiquitination | INCICWKKLNTESVS EEEEEEEECCCCCCC | 23.59 | 21906983 | |
| 114 | Ubiquitination | LSLTSQLKKLQETIE HHHHHHHHHHHHHHH | 43.74 | 29967540 | |
| 115 | Ubiquitination | SLTSQLKKLQETIEQ HHHHHHHHHHHHHHH | 65.09 | - | |
| 119 | Phosphorylation | QLKKLQETIEQKTKI HHHHHHHHHHHHHCC | 19.49 | - | |
| 123 | Ubiquitination | LQETIEQKTKIEIGD HHHHHHHHHCCCCCC | 38.71 | 21906983 | |
| 125 | Ubiquitination | ETIEQKTKIEIGDTI HHHHHHHCCCCCCEE | 45.43 | 22817900 | |
| 131 | Phosphorylation | TKIEIGDTIRVRGSI HCCCCCCEEEECCEE | 12.89 | 23403867 | |
| 176 | Ubiquitination | ELPTIYRKVYDQPFH CCCCCHHHHHCCCCC | 28.33 | 21906983 | |
| 178 | Phosphorylation | PTIYRKVYDQPFHSS CCCHHHHHCCCCCCH | 16.34 | - | |
| 189 | Ubiquitination | FHSSALEKEEALSNP CCCHHHHHHHHHCCC | 62.80 | 21906983 | |
| 194 | Phosphorylation | LEKEEALSNPGALDL HHHHHHHCCCCCCCH | 48.29 | 24719451 | |
| 203 | Phosphorylation | PGALDLPSLTSLLSE CCCCCHHHHHHHHHH | 52.13 | 24719451 | |
| 205 | Phosphorylation | ALDLPSLTSLLSEKA CCCHHHHHHHHHHHH | 22.97 | 26074081 | |
| 206 | Phosphorylation | LDLPSLTSLLSEKAK CCHHHHHHHHHHHHH | 32.38 | 26074081 | |
| 209 | Phosphorylation | PSLTSLLSEKAKEFL HHHHHHHHHHHHHHH | 42.20 | 26074081 | |
| 211 | Ubiquitination | LTSLLSEKAKEFLME HHHHHHHHHHHHHHH | 62.47 | 21906983 | |
| 213 | Ubiquitination | SLLSEKAKEFLMENR HHHHHHHHHHHHHHH | 61.13 | 21906983 | |
| 261 | Ubiquitination | FKKDTTSKAIHSIFK CCCCHHHHHHHHHHH | 49.63 | 29967540 | |
| 265 | Phosphorylation | TTSKAIHSIFKNAIQ HHHHHHHHHHHHHHH | 24.49 | 24719451 | |
| 268 | Ubiquitination | KAIHSIFKNAIQLLQ HHHHHHHHHHHHHHH | 43.74 | 29967540 | |
| 277 | Ubiquitination | AIQLLQEKGLVFQKD HHHHHHHCCCEEECC | 44.58 | 21906983 | |
| 283 | Ubiquitination | EKGLVFQKDDGFDNL HCCCEEECCCCCCCE | 46.45 | 22817900 | |
| 314 | Ubiquitination | IIQQDCQKPNHMEKG HHHHHCCCCCHHHCC | 54.86 | 29967540 |
| 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 STN1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STN1_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 STN1_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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