COPB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPB2_MOUSE
• UniProt AC: O55029
• Protein Name: Coatomer subunit beta'
• Gene Name: Copb2
• Organism: Mus musculus (Mouse).
• 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 cytoplas
• 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: MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKGFQPSRPTAQQEPDGKPASSPVIMASQTTHKEEKSLLELEVDLDNLELEDIDTTDINLDEDILDD

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
15	Phosphorylation	KRKLTARSDRVKSVD HHHHHCCCCCEEEEE	27.57	-
20	Phosphorylation	ARSDRVKSVDLHPTE CCCCCEEEEECCCCC	20.29	-
26	Phosphorylation	KSVDLHPTEPWMLAS EEEECCCCCHHHHHH	43.88	-
56	S-palmitoylation	LVKTFEVCDLPVRAA EEEEEEECCCCHHHH	3.33	28526873
64	Acetylation	DLPVRAAKFVARKNW CCCHHHHHHHHCCCE	39.11	22826441
190	Glutathionylation	GHEKGVNCIDYYSGG CCCCCCCEEEECCCC	2.02	24333276
194	Phosphorylation	GVNCIDYYSGGDKPY CCCEEEECCCCCCCE	9.33	22817900
212	Acetylation	GADDRLVKIWDYQNK CCCCCEEEEEECCCC	42.54	22826441
212	Ubiquitination	GADDRLVKIWDYQNK CCCCCEEEEEECCCC	42.54	22790023
276	S-palmitoylation	YGMERVWCVASLRGS CCCCEEEEEEEECCC	1.35	28526873
318	Ubiquitination	NGKIIWAKHSEVQQA CCCEEEECCHHHHHH	32.44	22790023
318	Acetylation	NGKIIWAKHSEVQQA CCCEEEECCHHHHHH	32.44	22826441
328	Ubiquitination	EVQQANLKAMGDTEI HHHHHCHHHHCCCCC	35.81	22790023
336	Ubiquitination	AMGDTEIKDGERLPL HHCCCCCCCCCCCCE	54.14	27667366
350	Phosphorylation	LAVKDMGSCEIYPQT EEEEECCCCEEECCE	11.26	26370283
354	Phosphorylation	DMGSCEIYPQTIQHN ECCCCEEECCEEEEC	2.72	-
386	Acetylation	TAMALRNKSFGSAQE EEEHHCCCCCCCHHH	40.50	23236377
386	Malonylation	TAMALRNKSFGSAQE EEEHHCCCCCCCHHH	40.50	26320211
419	Acetylation	VKIFKNFKEKKSFKP HHHHHCHHCCCCCCC	77.38	19854969
421	Acetylation	IFKNFKEKKSFKPDF HHHCHHCCCCCCCCC	55.07	19854977
560	Phosphorylation	TIAHLDRTMYLLGYI EEEECCCCCHHEEEE	15.16	29472430
562	Phosphorylation	AHLDRTMYLLGYIPK EECCCCCHHEEEECC	9.73	29472430
569	Acetylation	YLLGYIPKDNRLYLG HHEEEECCCCEEECC	59.06	22826441
608	Ubiquitination	RDFSMADKVLPTIPK CCCCCHHHCCCCCCH	35.81	22790023
627	Ubiquitination	RVAHFLEKQGFKQQA HHHHHHHHCCCCEEE	58.84	22790023
627	Acetylation	RVAHFLEKQGFKQQA HHHHHHHHCCCCEEE	58.84	22826441
767	Phosphorylation	TYLPSQVSRVVKLWR HCCHHHHHHHHHHHH	16.24	29514104
778	Phosphorylation	KLWRENLSKVNQKAA HHHHHHHHHHHHHHH	46.25	27841257
783	Ubiquitination	NLSKVNQKAAESLAD HHHHHHHHHHHHHCC	44.34	22790023
787	Phosphorylation	VNQKAAESLADPTEY HHHHHHHHHCCCHHH	24.91	-
822	Ubiquitination	HADLWPAKQYPLVTP CCCCCCHHHCCCCCC	46.41	22790023
828	Phosphorylation	AKQYPLVTPNEERNV HHHCCCCCCCHHHHH	28.25	-
845	Phosphorylation	EAKGFQPSRPTAQQE HHCCCCCCCCCCCCC	39.86	25159016
848	Phosphorylation	GFQPSRPTAQQEPDG CCCCCCCCCCCCCCC	35.67	25777480
859	Phosphorylation	EPDGKPASSPVIMAS CCCCCCCCCCEEEEE	43.64	26824392
860	Phosphorylation	PDGKPASSPVIMASQ CCCCCCCCCEEEEEC	25.87	27087446
866	Phosphorylation	SSPVIMASQTTHKEE CCCEEEEECCCCHHH	15.64	25159016
868	Phosphorylation	PVIMASQTTHKEEKS CEEEEECCCCHHHHH	28.51	25159016
869	Phosphorylation	VIMASQTTHKEEKSL EEEEECCCCHHHHHH	24.26	25159016
871	Ubiquitination	MASQTTHKEEKSLLE EEECCCCHHHHHHEE	66.53	22790023

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

Oops, there are no upstream regulatory protein records of COPB2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COPB2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of COPB2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of COPB2_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.