TERA_DROME - dbPTM
TERA_DROME - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MADSKGEDLAT
----CCCCCCHHHHH
32.7819429919
5Acetylation---MADSKGEDLATA
---CCCCCCHHHHHH
67.8621791702
15AcetylationDLATAILKRKDRPNR
HHHHHHHHCCCCCCC
51.8221791702
716PhosphorylationERAENQNSAMDMDED
HHHHHHCCCCCCCCC
18.4010656772
744PhosphorylationAMKFARRSVSDNDIR
HHHHHHHCCCHHHHH
22.0319429919
746PhosphorylationKFARRSVSDNDIRKY
HHHHHCCCHHHHHHH
31.7619429919
782PhosphorylationQTGNTSGSGNNLPVN
CCCCCCCCCCCCCCC
37.8121082442
790PhosphorylationGNNLPVNSPGDNGDD
CCCCCCCCCCCCCCC
30.4119429919
800PhosphorylationDNGDDDLYS------
CCCCCCCCC------
21.2319429919
801PhosphorylationNGDDDLYS-------
CCCCCCCC-------
40.8319429919

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TERA_DROME !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP6A_DROMEHsp67Baphysical
14605208
MFN1_HUMANMFN1physical
23498974
MFN2_HUMANMFN2physical
23498974
MARF_DROMEMarfphysical
23498974
RS27A_DROMERpS27Aphysical
24292889
DERL1_DROMEDer-1genetic
25255315
RB27C_DROMEHrb27Cgenetic
20519548
DIAP1_DROMEthgenetic
21343367
PTPM1_DROMEPlipgenetic
21304887
HRD1_DROMEsip3genetic
25255315
RS10B_DROMERpS10bphysical
22036573
DERL1_DROMEDer-1physical
25255315
TERA_DROMETER94physical
23498974
CLU_DROMEcluphysical
26931463

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TERA_DROME

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

TOP