UniProt ID | NACA_MOUSE | |
---|---|---|
UniProt AC | Q60817 | |
Protein Name | Nascent polypeptide-associated complex subunit alpha | |
Gene Name | Naca | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 215 | |
Subcellular Localization | Cytoplasm. Nucleus. The heterodimer is located mainly in the cytosol, and the homodimer in the nucleus.. | |
Protein Description | Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity). Isoform 1 and isoform 2 appear to bind DNA and play roles in transcription. Isoform 1 may function as a specific coactivator for JUN, acting to stabilize the interaction of JUN homodimers with promoter elements.. | |
Protein Sequence | MPGEATETVPATEQELPQPQAETGSGTESDSDESVPELEEQDSTQTATQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAMSKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIEDLSQQAQLAAAEKFKVQGEAVSNIQENTQTPTVQEESEEEEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELTM | |
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 |
---|---|---|---|---|---|
31 | Phosphorylation | GSGTESDSDESVPEL CCCCCCCCCCCCCCH | 53.18 | 22802335 | |
34 | Phosphorylation | TESDSDESVPELEEQ CCCCCCCCCCCHHHC | 48.22 | 22802335 | |
43 | Phosphorylation | PELEEQDSTQTATQQ CCHHHCCCHHHHHHH | 23.31 | 15299025 | |
44 | Phosphorylation | ELEEQDSTQTATQQA CHHHCCCHHHHHHHH | 37.92 | 22802335 | |
46 | Phosphorylation | EEQDSTQTATQQAQL HHCCCHHHHHHHHHH | 31.59 | 22802335 | |
99 | Phosphorylation | TRVTIRKSKNILFVI EEEEEECCCCEEEEE | 22.53 | - | |
127 | Sumoylation | YIVFGEAKIEDLSQQ EEEEEEEEHHHHHHH | 42.18 | - | |
132 | Phosphorylation | EAKIEDLSQQAQLAA EEEHHHHHHHHHHHH | 32.35 | - | |
142 | Acetylation | AQLAAAEKFKVQGEA HHHHHHHHHCCCCCH | 45.84 | 23806337 | |
142 | Ubiquitination | AQLAAAEKFKVQGEA HHHHHHHHHCCCCCH | 45.84 | 27667366 | |
159 | Phosphorylation | NIQENTQTPTVQEES CHHHHCCCCCCCCHH | 20.91 | 15005626 | |
161 | Phosphorylation | QENTQTPTVQEESEE HHHCCCCCCCCHHHH | 37.90 | 15345747 | |
166 | Phosphorylation | TPTVQEESEEEEVDE CCCCCCHHHHHCCCC | 49.94 | 15345747 | |
186 | Phosphorylation | KDIELVMSQANVSRA HHHHHHHHHHCCHHH | 20.75 | - | |
191 | Phosphorylation | VMSQANVSRAKAVRA HHHHHCCHHHHHHHH | 26.74 | - | |
203 | Phosphorylation | VRALKNNSNDIVNAI HHHHHCCCHHHHHHH | 45.32 | - | |
2114 | Ubiquitination | ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- | 27667366 |
* 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 NACA_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TBP_MOUSE | Tbp | physical | 9488445 | |
FADD_HUMAN | FADD | physical | 24901053 | |
NSE2_MOUSE | Nsmce2 | physical | 25002400 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASSSPECTROMETRY. | |
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161 AND SER-166, ANDMASS SPECTROMETRY. | |
"Integrin-linked kinase regulates the nuclear entry of the c-Juncoactivator alpha-NAC and its coactivation potency."; Quelo I., Gauthier C., Hannigan G.E., Dedhar S., St-Arnaud R.; J. Biol. Chem. 279:43893-43899(2004). Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ILK, ANDPHOSPHORYLATION AT SER-43. | |
"GSK3 beta-dependent phosphorylation of the alpha NAC coactivatorregulates its nuclear translocation and proteasome-mediateddegradation."; Quelo I., Akhouayri O., Prud'homme J., St Arnaud R.; Biochemistry 43:2906-2914(2004). Cited for: SUBCELLULAR LOCATION, DEGRADATION, AND PHOSPHORYLATION AT THR-159. |