UniProt ID | TERA_DROME | |
---|---|---|
UniProt AC | Q7KN62 | |
Protein Name | Transitional endoplasmic reticulum ATPase TER94 | |
Gene Name | TER94 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 801 | |
Subcellular Localization | Cytoplasm . Nucleus . Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:18590813). | |
Protein Description | Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. Involved in the ubiquitin-proteasome system. Important for oskar mRNA localization and/or anchoring during oogenesis. Involved in germ cell formation.. | |
Protein Sequence | MADSKGEDLATAILKRKDRPNRLIVEEAQNDDNSVVSLSQAKMDELQLFRGDTVILKGKRRKETVCIVLSDDTCPDEKIRMNRVVRNNLCVHLSDVVSVQSCPDVKYGKRVRILPIDESTEGVTGNLFEIYLKPYFLEAYRPIHMGDNFIVRAAMRPIEFKVVLTDPEPYCIVAPETVIFCDGDPIKREEEEESLNAVGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDLIDLEDDKIDAEVLASLAVTMENFRYAMTKSSPSALRETVVEVPNTTWTDIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIRQAIEAEIRREKERAENQNSAMDMDEDDPVPEITSAHFEEAMKFARRSVSDNDIRKYEMFAQTLQQSRGFGQNFRFPGQTGNTSGSGNNLPVNSPGDNGDDDLYS | |
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 |
---|---|---|---|---|---|
4 | Phosphorylation | ----MADSKGEDLAT ----CCCCCCHHHHH | 32.78 | 19429919 | |
5 | Acetylation | ---MADSKGEDLATA ---CCCCCCHHHHHH | 67.86 | 21791702 | |
15 | Acetylation | DLATAILKRKDRPNR HHHHHHHHCCCCCCC | 51.82 | 21791702 | |
716 | Phosphorylation | ERAENQNSAMDMDED HHHHHHCCCCCCCCC | 18.40 | 10656772 | |
744 | Phosphorylation | AMKFARRSVSDNDIR HHHHHHHCCCHHHHH | 22.03 | 19429919 | |
746 | Phosphorylation | KFARRSVSDNDIRKY HHHHHCCCHHHHHHH | 31.76 | 19429919 | |
782 | Phosphorylation | QTGNTSGSGNNLPVN CCCCCCCCCCCCCCC | 37.81 | 21082442 | |
790 | Phosphorylation | GNNLPVNSPGDNGDD CCCCCCCCCCCCCCC | 30.41 | 19429919 | |
800 | Phosphorylation | DNGDDDLYS------ CCCCCCCCC------ | 21.23 | 19429919 | |
801 | Phosphorylation | NGDDDLYS------- CCCCCCCC------- | 40.83 | 19429919 |
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 TERA_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TERA_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 TERA_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HSP6A_DROME | Hsp67Ba | physical | 14605208 | |
MFN1_HUMAN | MFN1 | physical | 23498974 | |
MFN2_HUMAN | MFN2 | physical | 23498974 | |
MARF_DROME | Marf | physical | 23498974 | |
RS27A_DROME | RpS27A | physical | 24292889 | |
DERL1_DROME | Der-1 | genetic | 25255315 | |
RB27C_DROME | Hrb27C | genetic | 20519548 | |
DIAP1_DROME | th | genetic | 21343367 | |
PTPM1_DROME | Plip | genetic | 21304887 | |
HRD1_DROME | sip3 | genetic | 25255315 | |
RS10B_DROME | RpS10b | physical | 22036573 | |
DERL1_DROME | Der-1 | physical | 25255315 | |
TERA_DROME | TER94 | physical | 23498974 | |
CLU_DROME | clu | physical | 26931463 |
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-716, AND MASSSPECTROMETRY. |