COPB_DROME - dbPTM
COPB_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPB_DROME
UniProt AC P45437
Protein Name Coatomer subunit beta
Gene Name betaCOP {ECO:0000312|FlyBase:FBgn0008635}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 964
Subcellular Localization Cytoplasm. Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. The coatomer is cytoplasmic or polymerized on the cytoplasmic side o
Protein Description The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Required for limiting lipid storage in lipid droplets..
Protein Sequence MTSQVPCYTIINSPDLEVTNEMQLKRDLEKGDTNVKIETLKRVIKLLLNGERYPGLIMTIIRFVLPVQNHTIKKLLLIFWEIVPKTSADGKLLQEMILVCDAYRKDLQHPNEFLRGSTLRFLCKLKEPELLEPLMPAIRACLDHRHSYVRRNAVLAIFTIYKNFDWLVPDGPELIASFLDTQQDMSCKRNAFLMLLHADQERALNYLASCIDQVHTFGDILQLVIVELIYKVCHANPAERSRFIRCIYNLLNSSSNAVRYESAGTLITLSLAPTAIKAAASCYIELVVKESDNNVKLIVLDRLVAMKEHEGMEKVMQDLVMDVLRVLAAPDIEVRRKTLALALDLVYSRNIGEMVLVLKKEVAKTHNVEHEDTGKYRQLLVRTLHTCSIKFPDVAANVIPVLVEFLSDTNELAAADVLIFIREAIQKFPALRALIIEHLIEAFPQIKSSKIHRAAVWILGEYVEGSQILEVIAVIQQTLGEVPMVEAEQRRLAGDQTEEQKQQQGSAGGNAAGSAAEGSGSGNASNKVTSDGTYATQSAYSLAPVAKAEKRPPLRQYLMDGDFFIGAALSATLTKLALRYAELETEARAQNRLTTQVMLIMSSILHLGKSGFPSKPITNDDTDRIFVCLRTLSERTPEAISVFTLYCREALGKMLDAQHDEDQRMLKEKQKATAKVQPDDPVLFAQLSNGRDNQLGENVFESSLNQALAGSKNAQLSDVASPNSKLNKVTQLTGFSDPVYAEAYVNVNQYDIVLDVLIVNQTNDTLQNCTLELATLGDLKLVERPHPVVLAPHDFCNIKANVKVSSTENGIIFGNIVYETALNTNVVVLNTIHIDIMDYIIPASCTDTEFRQMWQDFEWENKVTVNTSFTDLHEYLKHLLKSTNMKCLTPEKALSGQCGFMAANMYAKSIFGENALANLSIEKPVDDPDSKVTGHIRIRAKSQGMALSLGDKISSSQKQSVQAA
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
541PhosphorylationYATQSAYSLAPVAKA
EECCCCCCCCCCCCH
20.1221082442
711PhosphorylationLNQALAGSKNAQLSD
HHHHHHCCCCCCHHC
19.6829892262
721PhosphorylationAQLSDVASPNSKLNK
CCHHCCCCCCCHHCH
25.1819429919
724PhosphorylationSDVASPNSKLNKVTQ
HCCCCCCCHHCHHHH
41.7419429919
867PhosphorylationENKVTVNTSFTDLHE
CCCEEEECCCHHHHH
22.3819429919
868PhosphorylationNKVTVNTSFTDLHEY
CCEEEECCCHHHHHH
22.4219429919
877AcetylationTDLHEYLKHLLKSTN
HHHHHHHHHHHHHCC
31.1621791702
942PhosphorylationHIRIRAKSQGMALSL
EEEEEECCCCCEEHH
30.8622817900

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 COPB_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPB_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 COPB_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFS1_DROMECG12264physical
22036573
TCPG_DROMECctgammaphysical
22036573
2AAA_DROMEPp2A-29Bphysical
22036573
CCD1P_DROMECyp12d1-pphysical
22036573
IDH3A_DROMEl(1)G0156physical
22036573

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

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Related Literatures of Post-Translational Modification

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