UniProt ID | GCP2_DROME | |
---|---|---|
UniProt AC | Q9XYP7 | |
Protein Name | Gamma-tubulin complex component 2 homolog | |
Gene Name | Grip84 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 852 | |
Subcellular Localization | Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . | |
Protein Description | ||
Protein Sequence | MYALLVFVERYSECKPVSESSSSTSLSAMGLPHGNKTSDVNSAAGSVPTTLAIASTSTILTTSQNVSGSTRLSLTQSQDFPTSTPVNCKKATESDTTPVVFVRRGPMDRNRGAGKDERNDLSVIKERVLNAVSDQSLSGYRSVTNKTGNSPKSMPNDLVTLTDVPDEYRTHLLWEYYKVDGDKVPRAEIAAMPLLSQESMLLDELLHCLTGIRESLLVPQKPIISAVGLAKYDTDFDIHTHLDRSLTHQVREILPLASYFMGVQKIIAATDGLGQVMNSLNEALQELTHDFYLIIVQAEQELRHNRLTLQKLLYYLQPTMWVMHEVWSSLVIIQLSDSRDAEVLTYLHERIKRLEGNKDAQQLIIGLVRKAAKPYMRMLQMWIQKGVIVDRHREFLVVDNEVIHRDELPEHYSDDYWERRYTLRDEQIPSFLAKYSDKILRTGKYLNVIRQCGKRVMPTQEMNLEFDPTSERHVSVINDAYYFAARMLLDVLLTENDLMGHLQSVKRYLLLNQGDFTMQFMDACEDELTKNVDHVLPMTLENLLGLTLRISSARNDPYKDDLHCELLPYDLVTQMSKIMKKEENWQAQPRLDLSGLECFAFTYEVKWPCSLVLNHISISKYQMLFRQLFYCKHVERQLCKIWKENSIARQFEPQAASLYRAAFTLRQRMMNAIQNLEYYMMIEIIEPNWHIFIEKMKTVENVDNVLRLHQDFLDSCLKNCMLTESSHLNRSIFKLCKICLKYCEFIQITQRYFQDAELRSMVRDSADSSESEQESLHCPQIETPLDPTDTFSERVRRFDLEFTQLLISFLKQINSMAKKNTADCFMNLVHRINFNAFYTDQMDKMCVEDAIG | |
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 |
---|---|---|---|---|---|
18 | Phosphorylation | YSECKPVSESSSSTS HCCCCCCCCCCCCCC | 40.04 | 21082442 | |
21 | Phosphorylation | CKPVSESSSSTSLSA CCCCCCCCCCCCHHC | 25.02 | 21082442 | |
22 | Phosphorylation | KPVSESSSSTSLSAM CCCCCCCCCCCHHCC | 47.09 | 21082442 | |
24 | Phosphorylation | VSESSSSTSLSAMGL CCCCCCCCCHHCCCC | 35.32 | 22817900 | |
25 | Phosphorylation | SESSSSTSLSAMGLP CCCCCCCCHHCCCCC | 23.44 | 21082442 | |
73 | Phosphorylation | VSGSTRLSLTQSQDF CCCCCEEEEEECCCC | 26.53 | 10037793 | |
75 | Phosphorylation | GSTRLSLTQSQDFPT CCCEEEEEECCCCCC | 23.85 | 22817900 | |
97 | Phosphorylation | KATESDTTPVVFVRR CCCCCCCCCEEEEEC | 21.05 | 28490779 | |
122 | Phosphorylation | KDERNDLSVIKERVL CCCCCCHHHHHHHHH | 25.35 | 22817900 | |
136 | Phosphorylation | LNAVSDQSLSGYRSV HHHCCCCCCCCCCCC | 29.50 | 21082442 | |
150 | Phosphorylation | VTNKTGNSPKSMPND CCCCCCCCCCCCCCC | 34.74 | 30478224 |
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 GCP2_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GCP2_DROME !! |
* 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 GCP2_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SRP68_DROME | Srp68 | physical | 14605208 | |
TBG1_DROME | gammaTub23C | physical | 11134079 | |
GCP3_DROME | Grip91 | physical | 11134079 | |
TBG1_DROME | gammaTub23C | physical | 22729084 | |
GCP4_DROME | Grip75 | physical | 10037793 | |
GCP4_DROME | Grip75 | physical | 22729084 | |
TBG2_DROME | gammaTub37C | physical | 22729084 | |
GCP3_DROME | Grip91 | physical | 10037793 | |
GCP3_DROME | Grip91 | physical | 22729084 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASSSPECTROMETRY. |