UniProt ID | STAU1_HUMAN | |
---|---|---|
UniProt AC | O95793 | |
Protein Name | Double-stranded RNA-binding protein Staufen homolog 1 | |
Gene Name | STAU1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 577 | |
Subcellular Localization | Cytoplasm . Rough endoplasmic reticulum . Localizes exclusively with the rough reticulum endoplasmic (RER). | |
Protein Description | Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.. | |
Protein Sequence | MSQVQVQVQNPSAALSGSQILNKNQSLLSQPLMSIPSTTSSLPSENAGRPIQNSALPSASITSTSAAAESITPTVELNALCMKLGKKPMYKPVDPYSRMQSTYNYNMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKTRQAAKHDAAAKALRILQNEPLPERLEVNGRESEEENLNKSEISQVFEIALKRNLPVNFEVARESGPPHMKNFVTKVSVGEFVGEGEGKSKKISKKNAAIAVLEELKKLPPLPAVERVKPRIKKKTKPIVKPQTSPEYGQGINPISRLAQIQQAKKEKEPEYTLLTERGLPRRREFVMQVKVGNHTAEGTGTNKKVAKRNAAENMLEILGFKVPQAQPTKPALKSEEKTPIKKPGDGRKVTFFEPGSGDENGTSNKEDEFRMPYLSHQQLPAGILPMVPEVAQAVGVSQGHHTKDFTRAAPNPAKATVTAMIARELLYGGTSPTAETILKNNISSGHVPHGPLTRPSEQLDYLSRVQGFQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMAALNILKLLSELDQQSTEMPRTGNGPMSVCGRC | |
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 | ------MSQVQVQVQ ------CCCEEEEEC | 38.77 | 24043423 | |
2 | Acetylation | ------MSQVQVQVQ ------CCCEEEEEC | 38.77 | 19413330 | |
12 | Phosphorylation | QVQVQNPSAALSGSQ EEEECCHHHHHCHHH | 33.45 | 28348404 | |
16 | Phosphorylation | QNPSAALSGSQILNK CCHHHHHCHHHHHCC | 31.50 | 24043423 | |
18 | Phosphorylation | PSAALSGSQILNKNQ HHHHHCHHHHHCCCH | 15.63 | 24043423 | |
54 | Phosphorylation | AGRPIQNSALPSASI CCCCCCCCCCCCCCC | 18.14 | 20068231 | |
58 | Phosphorylation | IQNSALPSASITSTS CCCCCCCCCCCCCCC | 35.18 | 20068231 | |
60 | Phosphorylation | NSALPSASITSTSAA CCCCCCCCCCCCCHH | 30.64 | 20068231 | |
62 | Phosphorylation | ALPSASITSTSAAAE CCCCCCCCCCCHHHH | 24.37 | 20068231 | |
63 | Phosphorylation | LPSASITSTSAAAES CCCCCCCCCCHHHHH | 20.77 | 20068231 | |
64 | Phosphorylation | PSASITSTSAAAESI CCCCCCCCCHHHHHC | 17.46 | 20068231 | |
65 | Phosphorylation | SASITSTSAAAESIT CCCCCCCCHHHHHCC | 18.71 | 20068231 | |
70 | Phosphorylation | STSAAAESITPTVEL CCCHHHHHCCCCHHH | 27.34 | 20068231 | |
72 | Phosphorylation | SAAAESITPTVELNA CHHHHHCCCCHHHHH | 23.37 | 20068231 | |
74 | Phosphorylation | AAESITPTVELNALC HHHHCCCCHHHHHHH | 20.26 | 20068231 | |
98 | Methylation | KPVDPYSRMQSTYNY CCCCHHHCCCCCCCC | 22.70 | 115917917 | |
101 | Phosphorylation | DPYSRMQSTYNYNMR CHHHCCCCCCCCCCC | 24.42 | 28857561 | |
103 | Phosphorylation | YSRMQSTYNYNMRGG HHCCCCCCCCCCCCC | 22.39 | 27642862 | |
108 | Methylation | STYNYNMRGGAYPPR CCCCCCCCCCCCCCC | 36.43 | 24129315 | |
108 | Asymmetric dimethylarginine | STYNYNMRGGAYPPR CCCCCCCCCCCCCCC | 36.43 | - | |
115 | Methylation | RGGAYPPRYFYPFPV CCCCCCCCCCCCCCC | 29.68 | 24129315 | |
115 | Asymmetric dimethylarginine | RGGAYPPRYFYPFPV CCCCCCCCCCCCCCC | 29.68 | - | |
116 | Phosphorylation | GGAYPPRYFYPFPVP CCCCCCCCCCCCCCC | 17.15 | - | |
118 | Phosphorylation | AYPPRYFYPFPVPPL CCCCCCCCCCCCCCE | 8.60 | - | |
155 | Acetylation | AKHDAAAKALRILQN HHHHHHHHHHHHHHC | 43.13 | 25953088 | |
155 | Ubiquitination | AKHDAAAKALRILQN HHHHHHHHHHHHHHC | 43.13 | - | |
176 | Phosphorylation | LEVNGRESEEENLNK EEECCCCCHHHHCCH | 49.28 | 30266825 | |
184 | Phosphorylation | EEENLNKSEISQVFE HHHHCCHHHHHHHHH | 38.80 | 27690223 | |
187 | Phosphorylation | NLNKSEISQVFEIAL HCCHHHHHHHHHHHH | 19.08 | 27690223 | |
189 (in isoform 2) | Acetylation | - | 3.57 | - | |
195 | Acetylation | QVFEIALKRNLPVNF HHHHHHHHCCCCCCH | 30.16 | - | |
195 (in isoform 3) | Acetylation | - | 30.16 | - | |
208 | Phosphorylation | NFEVARESGPPHMKN CHHHHHHHCCCCHHC | 51.55 | 28555341 | |
221 | Phosphorylation | KNFVTKVSVGEFVGE HCCEEEEECHHCCCC | 26.43 | - | |
268 | Ubiquitination | VKPRIKKKTKPIVKP CCCCCCCCCCCCCCC | 57.70 | - | |
269 | Phosphorylation | KPRIKKKTKPIVKPQ CCCCCCCCCCCCCCC | 51.43 | 28464451 | |
270 | Acetylation | PRIKKKTKPIVKPQT CCCCCCCCCCCCCCC | 41.44 | 19608861 | |
274 | Ubiquitination | KKTKPIVKPQTSPEY CCCCCCCCCCCCCCC | 31.93 | - | |
277 | Phosphorylation | KPIVKPQTSPEYGQG CCCCCCCCCCCCCCC | 55.57 | 30278072 | |
278 | Phosphorylation | PIVKPQTSPEYGQGI CCCCCCCCCCCCCCC | 15.53 | 30278072 | |
281 | Phosphorylation | KPQTSPEYGQGINPI CCCCCCCCCCCCCHH | 20.38 | 23927012 | |
289 | Phosphorylation | GQGINPISRLAQIQQ CCCCCHHHHHHHHHH | 23.62 | 28450419 | |
298 | Ubiquitination | LAQIQQAKKEKEPEY HHHHHHHHHHCCCCH | 58.07 | - | |
299 | Ubiquitination | AQIQQAKKEKEPEYT HHHHHHHHHCCCCHH | 76.63 | - | |
299 | 2-Hydroxyisobutyrylation | AQIQQAKKEKEPEYT HHHHHHHHHCCCCHH | 76.63 | - | |
305 | Phosphorylation | KKEKEPEYTLLTERG HHHCCCCHHEEECCC | 17.26 | 29496907 | |
309 | Phosphorylation | EPEYTLLTERGLPRR CCCHHEEECCCCCCC | 27.09 | - | |
309 (in isoform 2) | Phosphorylation | - | 27.09 | - | |
315 (in isoform 3) | Phosphorylation | - | 56.16 | - | |
337 | 2-Hydroxyisobutyrylation | AEGTGTNKKVAKRNA CCCCCCCHHHHHHHH | 48.76 | - | |
341 | Acetylation | GTNKKVAKRNAAENM CCCHHHHHHHHHHHH | 49.53 | 7684505 | |
362 | O-linked_Glycosylation | KVPQAQPTKPALKSE CCCCCCCCCCCCCCC | 37.26 | 55821483 | |
363 | Ubiquitination | VPQAQPTKPALKSEE CCCCCCCCCCCCCCC | 34.67 | - | |
367 | Ubiquitination | QPTKPALKSEEKTPI CCCCCCCCCCCCCCC | 58.91 | - | |
367 | Acetylation | QPTKPALKSEEKTPI CCCCCCCCCCCCCCC | 58.91 | 7684515 | |
368 | Phosphorylation | PTKPALKSEEKTPIK CCCCCCCCCCCCCCC | 52.41 | 23927012 | |
372 | Phosphorylation | ALKSEEKTPIKKPGD CCCCCCCCCCCCCCC | 33.26 | 23927012 | |
382 | Ubiquitination | KKPGDGRKVTFFEPG CCCCCCCEEEEECCC | 51.67 | - | |
384 | Phosphorylation | PGDGRKVTFFEPGSG CCCCCEEEEECCCCC | 26.16 | 28464451 | |
390 | Phosphorylation | VTFFEPGSGDENGTS EEEECCCCCCCCCCC | 54.51 | 29255136 | |
396 | Phosphorylation | GSGDENGTSNKEDEF CCCCCCCCCCCCCCC | 40.48 | 29255136 | |
397 | Phosphorylation | SGDENGTSNKEDEFR CCCCCCCCCCCCCCC | 47.50 | 29255136 | |
399 | Ubiquitination | DENGTSNKEDEFRMP CCCCCCCCCCCCCCC | 67.33 | - | |
407 | Phosphorylation | EDEFRMPYLSHQQLP CCCCCCCCCCCCCCC | 16.11 | 27642862 | |
448 | Ubiquitination | RAAPNPAKATVTAMI CCCCCCHHHHHHHHH | 45.94 | - | |
450 | O-linked_Glycosylation | APNPAKATVTAMIAR CCCCHHHHHHHHHHH | 20.06 | OGP | |
461 | Phosphorylation | MIARELLYGGTSPTA HHHHHHHHCCCCCCH | 26.57 | 28152594 | |
464 | O-linked_Glycosylation | RELLYGGTSPTAETI HHHHHCCCCCCHHHH | 27.46 | OGP | |
464 | Phosphorylation | RELLYGGTSPTAETI HHHHHCCCCCCHHHH | 27.46 | 27251275 | |
465 | Phosphorylation | ELLYGGTSPTAETIL HHHHCCCCCCHHHHH | 24.43 | 25159151 | |
465 | O-linked_Glycosylation | ELLYGGTSPTAETIL HHHHCCCCCCHHHHH | 24.43 | OGP | |
467 | Phosphorylation | LYGGTSPTAETILKN HHCCCCCCHHHHHHC | 36.57 | - | |
467 | O-linked_Glycosylation | LYGGTSPTAETILKN HHCCCCCCHHHHHHC | 36.57 | OGP | |
495 | Phosphorylation | RPSEQLDYLSRVQGF CCHHHHHHHHHHCCC | 18.37 | - | |
506 | Phosphorylation | VQGFQVEYKDFPKNN HCCCEEEECCCCCCC | 19.59 | - | |
507 | Ubiquitination | QGFQVEYKDFPKNNK CCCEEEECCCCCCCC | 39.11 | - | |
554 | Phosphorylation | LNILKLLSELDQQST HHHHHHHHHHHHCCC | 46.69 | - | |
560 | O-linked_Glycosylation | LSELDQQSTEMPRTG HHHHHHCCCCCCCCC | 22.24 | OGP | |
561 | O-linked_Glycosylation | SELDQQSTEMPRTGN HHHHHCCCCCCCCCC | 31.78 | OGP | |
563 | Sulfoxidation | LDQQSTEMPRTGNGP HHHCCCCCCCCCCCC | 2.49 | 21406390 | |
572 | Phosphorylation | RTGNGPMSVCGRC-- CCCCCCCCCCCCC-- | 19.86 | 23917254 |
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 STAU1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STAU1_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 STAU1_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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Phosphorylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND MASSSPECTROMETRY. |