COPB2_RAT - dbPTM
COPB2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPB2_RAT
UniProt AC O35142
Protein Name Coatomer subunit beta'
Gene Name Copb2
Organism Rattus norvegicus (Rat).
Sequence Length 905
Subcellular Localization Cytoplasm, cytosol. 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 cytopl
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. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).; This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner..
Protein Sequence MPLRLDIKRKLTAMSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTPEGHAQNVSCATFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSVVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKRFQPSRATAQQEPDGKPASSPVIMASQTTHKEEKSFQELEDDLDTMELEDIDTTDINLDEDILDD
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
8AcetylationMPLRLDIKRKLTAMS
CCCCCHHHHHHHHCH
43.0522902405
350PhosphorylationLAVKDMGSCEIYPQT
EEEEECCCCEEECCE
11.2627097102
354PhosphorylationDMGSCEIYPQTIQHN
ECCCCEEECCEEEEC
2.7227097102
408PhosphorylationSEYAIRESNSVVKIF
CHHHHHHCCHHHHHC
25.2622276854
413AcetylationRESNSVVKIFKNFKE
HHCCHHHHHCCCCCC
40.0222902405
416AcetylationNSVVKIFKNFKEKKS
CHHHHHCCCCCCCCC
66.0222902405
419AcetylationVKIFKNFKEKKSFKP
HHHCCCCCCCCCCCC
77.3822902405
608UbiquitinationRDFSMADKVLPTIPK
CCCCCHHHCCCCCCH
35.81-
627AcetylationRVAHFLEKQGFKQQA
HHHHHHHHCCCCEEE
58.8422902405
828PhosphorylationAKQYPLVTPNEERNV
HHHCCCCCCCHHHHH
28.2522108457
848PhosphorylationRFQPSRATAQQEPDG
HHCCCCCCCCCCCCC
24.7227097102
859PhosphorylationEPDGKPASSPVIMAS
CCCCCCCCCCEEEEE
43.6423712012
860PhosphorylationPDGKPASSPVIMASQ
CCCCCCCCCEEEEEC
25.8727097102
866PhosphorylationSSPVIMASQTTHKEE
CCCEEEEECCCCCCH
15.6427097102
868PhosphorylationPVIMASQTTHKEEKS
CEEEEECCCCCCHHH
28.5127097102
869PhosphorylationVIMASQTTHKEEKSF
EEEEECCCCCCHHHH
24.2627097102

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 COPB2_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPB2_RAT !!

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 COPB2_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of COPB2_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COPB2_RAT

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Related Literatures of Post-Translational Modification

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