COPB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPB_HUMAN
• UniProt AC: P53618
• Protein Name: Coatomer subunit beta
• Gene Name: COPB1
• Organism: Homo sapiens (Human).
• Sequence Length: 953
• Subcellular Localization: Cytoplasm. Golgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein ; Cytoplasmic side . Cell membrane . Endoplasmic reticulum-Golgi intermediate compartment
• 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. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments..
• Protein Sequence: MTAAENVCYTLINVPMDSEPPSEISLKNDLEKGDVKSKTEALKKVIIMILNGEKLPGLLMTIIRFVLPLQDHTIKKLLLVFWEIVPKTTPDGRLLHEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAELLEPLMPAIRACLEHRHSYVRRNAVLAIYTIYRNFEHLIPDAPELIHDFLVNEKDASCKRNAFMMLIHADQDRALDYLSTCIDQVQTFGDILQLVIVELIYKVCHANPSERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPTAIKAAAQCYIDLIIKESDNNVKLIVLDRLIELKEHPAHERVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSSRNVEELVIVLKKEVIKTNNVSEHEDTDKYRQLLVRTLHSCSVRFPDMAANVIPVLMEFLSDNNEAAAADVLEFVREAIQRFDNLRMLIVEKMLEVFHAIKSVKIYRGALWILGEYCSTKEDIQSVMTEIRRSLGEIPIVESEIKKEAGELKPEEEITVGPVQKLVTEMGTYATQSALSSSRPTKKEEDRPPLRGFLLDGDFFVAASLATTLTKIALRYVALVQEKKKQNSFVAEAMLLMATILHLGKSSLPKKPITDDDVDRISLCLKVLSECSPLMNDIFNKECRQSLSHMLSAKLEEEKLSQKKESEKRNVTVQPDDPISFMQLTAKNEMNCKEDQFQLSLLAAMGNTQRKEAADPLASKLNKVTQLTGFSDPVYAEAYVHVNQYDIVLDVLVVNQTSDTLQNCTLELATLGDLKLVEKPSPLTLAPHDFANIKANVKVASTENGIIFGNIVYDVSGAASDRNCVVLSDIHIDIMDYIQPATCTDAEFRQMWAEFEWENKVTVNTNMVDLNDYLQHILKSTNMKCLTPEKALSGYCGFMAANLYARSIFGEDALANVSIEKPIHQGPDAAVTGHIRIRAKSQGMALSLGDKINLSQKKTSI

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
2	Acetylation	------MTAAENVCY ------CCHHHHHEE	34.28	18491316
2	Phosphorylation	------MTAAENVCY ------CCHHHHHEE	34.28	18491316
9	Phosphorylation	TAAENVCYTLINVPM CHHHHHEEEEECCCC	10.57	27642862
32	Ubiquitination	SLKNDLEKGDVKSKT CCCCCHHCCCCCCHH	68.64	33845483
38	2-Hydroxyisobutyrylation	EKGDVKSKTEALKKV HCCCCCCHHHHHHHH	44.67	-
61	Phosphorylation	KLPGLLMTIIRFVLP CCHHHHHHHHHHHHH	17.14	21406692
75	Ubiquitination	PLQDHTIKKLLLVFW HCCCCHHHHHHHHHH	38.22	33845483
75	2-Hydroxyisobutyrylation	PLQDHTIKKLLLVFW HCCCCHHHHHHHHHH	38.22	-
88	Phosphorylation	FWEIVPKTTPDGRLL HHHCCCCCCCCCCHH	37.17	24719451
105	Phosphorylation	MILVCDAYRKDLQHP HHHHHHHHHCCCCCC	12.63	24719451
107	Ubiquitination	LVCDAYRKDLQHPNE HHHHHHHCCCCCCCH	50.55	23000965
117	Methylation	QHPNEFIRGSTLRFL CCCCHHCCHHHHHHH	38.03	-
126	Ubiquitination	STLRFLCKLKEAELL HHHHHHHHCCHHHHH	65.82	22817900
128	Ubiquitination	LRFLCKLKEAELLEP HHHHHHCCHHHHHHC	40.13	21963094
137	Sulfoxidation	AELLEPLMPAIRACL HHHHHCHHHHHHHHH	2.85	21406390
149	Phosphorylation	ACLEHRHSYVRRNAV HHHHHHCHHHHHHHH	25.86	28348404
160	Phosphorylation	RNAVLAIYTIYRNFE HHHHHHHHHHHHCCH	4.97	28450419
161	Phosphorylation	NAVLAIYTIYRNFEH HHHHHHHHHHHCCHH	12.86	28450419
163	Phosphorylation	VLAIYTIYRNFEHLI HHHHHHHHHCCHHHC	7.54	28450419
185	Ubiquitination	HDFLVNEKDASCKRN HHHHCCCCCCCCCCC	54.08	21963094
190	Ubiquitination	NEKDASCKRNAFMML CCCCCCCCCCEEEEE	46.31	22817900
248	S-nitrosocysteine	ERARFIRCIYNLLQS HHHHHHHHHHHHHHC	3.11	-
248	S-nitrosylation	ERARFIRCIYNLLQS HHHHHHHHHHHHHHC	3.11	19483679
250	Phosphorylation	ARFIRCIYNLLQSSS HHHHHHHHHHHHCCC	11.90	28152594
261	Ubiquitination	QSSSPAVKYEAAGTL HCCCCCCCCEECCEE	39.21	21963094
262	Phosphorylation	SSSPAVKYEAAGTLV CCCCCCCCEECCEEE	12.28	21406692
267	Phosphorylation	VKYEAAGTLVTLSSA CCCEECCEEEEECHH	17.21	20068231
270	Phosphorylation	EAAGTLVTLSSAPTA EECCEEEEECHHHHH	24.84	20068231
272	Phosphorylation	AGTLVTLSSAPTAIK CCEEEEECHHHHHHH	18.32	21406692
273	Phosphorylation	GTLVTLSSAPTAIKA CEEEEECHHHHHHHH	41.18	21406692
276	Phosphorylation	VTLSSAPTAIKAAAQ EEECHHHHHHHHHHH	40.51	20068231
285	Phosphorylation	IKAAAQCYIDLIIKE HHHHHHHHHEEEEEC	5.84	28152594
291	Ubiquitination	CYIDLIIKESDNNVK HHHEEEEECCCCCEE	44.14	32015554
298	Ubiquitination	KESDNNVKLIVLDRL ECCCCCEEEEEEEHH	34.32	32015554
298	2-Hydroxyisobutyrylation	KESDNNVKLIVLDRL ECCCCCEEEEEEEHH	34.32	-
298	Acetylation	KESDNNVKLIVLDRL ECCCCCEEEEEEEHH	34.32	27452117
304	Methylation	VKLIVLDRLIELKEH EEEEEEEHHHHHCCC	33.14	-
309	Ubiquitination	LDRLIELKEHPAHER EEHHHHHCCCHHHHH	40.98	33845483
323	Sulfoxidation	RVLQDLVMDILRVLS HHHHHHHHHHHHHHC	3.27	21406390
339	Ubiquitination	PDLEVRKKTLQLALD CCHHHHHHHHHHHHH	43.85	33845483
340	Phosphorylation	DLEVRKKTLQLALDL CHHHHHHHHHHHHHH	23.83	21406692
349	Phosphorylation	QLALDLVSSRNVEEL HHHHHHHHCCCHHHH	30.77	24719451
350	Phosphorylation	LALDLVSSRNVEELV HHHHHHHCCCHHHHE	22.01	21406692
361	Ubiquitination	EELVIVLKKEVIKTN HHHEEEEEEHHHHCC	35.67	33845483
361	2-Hydroxyisobutyrylation	EELVIVLKKEVIKTN HHHEEEEEEHHHHCC	35.67	-
362	Ubiquitination	ELVIVLKKEVIKTNN HHEEEEEEHHHHCCC	53.72	-
367	Phosphorylation	LKKEVIKTNNVSEHE EEEHHHHCCCCCCCC	22.39	23312004
371	Phosphorylation	VIKTNNVSEHEDTDK HHHCCCCCCCCCHHH	35.05	28985074
376	Phosphorylation	NVSEHEDTDKYRQLL CCCCCCCHHHHHHHH	31.26	23312004
378	Ubiquitination	SEHEDTDKYRQLLVR CCCCCHHHHHHHHHH	44.41	-
378	Acetylation	SEHEDTDKYRQLLVR CCCCCHHHHHHHHHH	44.41	26051181
386	Phosphorylation	YRQLLVRTLHSCSVR HHHHHHHHHHHCCCC	22.73	-
451	Phosphorylation	EVFHAIKSVKIYRGA HHHHHHHCCCCCCHH	23.64	19835603
455	Phosphorylation	AIKSVKIYRGALWIL HHHCCCCCCHHHHHH	9.40	19835603
467	Phosphorylation	WILGEYCSTKEDIQS HHHHHHCCCHHHHHH	41.43	19835603
468	Phosphorylation	ILGEYCSTKEDIQSV HHHHHCCCHHHHHHH	34.59	19835603
476	Sulfoxidation	KEDIQSVMTEIRRSL HHHHHHHHHHHHHHH	3.18	30846556
482	Phosphorylation	VMTEIRRSLGEIPIV HHHHHHHHHCCCCCC	30.77	27499020
491	Phosphorylation	GEIPIVESEIKKEAG CCCCCCHHHHHHHHC	33.45	20068231
494	Acetylation	PIVESEIKKEAGELK CCCHHHHHHHHCCCC	40.27	26051181
494	Ubiquitination	PIVESEIKKEAGELK CCCHHHHHHHHCCCC	40.27	32015554
495	Ubiquitination	IVESEIKKEAGELKP CCHHHHHHHHCCCCC	59.46	29967540
501	Ubiquitination	KKEAGELKPEEEITV HHHHCCCCCHHHEEC	46.19	21906983
507	Phosphorylation	LKPEEEITVGPVQKL CCCHHHEECCHHHHH	23.77	23312004
513	Ubiquitination	ITVGPVQKLVTEMGT EECCHHHHHHHHHHH	45.20	29967540
516	Phosphorylation	GPVQKLVTEMGTYAT CHHHHHHHHHHHHHH	30.59	21945579
518	Sulfoxidation	VQKLVTEMGTYATQS HHHHHHHHHHHHHHH	3.38	30846556
520	Phosphorylation	KLVTEMGTYATQSAL HHHHHHHHHHHHHHH	14.52	21945579
521	Phosphorylation	LVTEMGTYATQSALS HHHHHHHHHHHHHHH	11.26	21945579
523	Phosphorylation	TEMGTYATQSALSSS HHHHHHHHHHHHHCC	16.79	21945579
525	Phosphorylation	MGTYATQSALSSSRP HHHHHHHHHHHCCCC	27.16	21945579
528	Phosphorylation	YATQSALSSSRPTKK HHHHHHHHCCCCCCC	26.45	21945579
529	Phosphorylation	ATQSALSSSRPTKKE HHHHHHHCCCCCCCC	31.08	21945579
530	Phosphorylation	TQSALSSSRPTKKEE HHHHHHCCCCCCCCC	38.61	21945579
533	Phosphorylation	ALSSSRPTKKEEDRP HHHCCCCCCCCCCCC	54.35	21945579
534	Ubiquitination	LSSSRPTKKEEDRPP HHCCCCCCCCCCCCC	61.95	21890473
575	Acetylation	YVALVQEKKKQNSFV HHHHHHHHHHCCCHH	48.45	30587843
575	2-Hydroxyisobutyrylation	YVALVQEKKKQNSFV HHHHHHHHHHCCCHH	48.45	-
575	Malonylation	YVALVQEKKKQNSFV HHHHHHHHHHCCCHH	48.45	26320211
602	Ubiquitination	LGKSSLPKKPITDDD HCCCCCCCCCCCHHC	76.19	29967540
603	Ubiquitination	GKSSLPKKPITDDDV CCCCCCCCCCCHHCH	39.45	33845483
606	Phosphorylation	SLPKKPITDDDVDRI CCCCCCCCHHCHHHH	41.73	20068231
627	Sulfoxidation	LSECSPLMNDIFNKE HHHCCHHHHHHCCHH	4.87	30846556
633	Ubiquitination	LMNDIFNKECRQSLS HHHHHCCHHHHHHHH	47.65	21963094
638	Phosphorylation	FNKECRQSLSHMLSA CCHHHHHHHHHHHHH	16.70	20873877
640	Phosphorylation	KECRQSLSHMLSAKL HHHHHHHHHHHHHHH	16.46	20873877
642	Sulfoxidation	CRQSLSHMLSAKLEE HHHHHHHHHHHHHHH	2.58	30846556
644	Phosphorylation	QSLSHMLSAKLEEEK HHHHHHHHHHHHHHH	18.78	30108239
646	Ubiquitination	LSHMLSAKLEEEKLS HHHHHHHHHHHHHHH	53.72	29967540
651	Ubiquitination	SAKLEEEKLSQKKES HHHHHHHHHHHHHHH	57.63	33845483
651	Acetylation	SAKLEEEKLSQKKES HHHHHHHHHHHHHHH	57.63	25953088
653	Phosphorylation	KLEEEKLSQKKESEK HHHHHHHHHHHHHHH	51.53	25849741
655	Ubiquitination	EEEKLSQKKESEKRN HHHHHHHHHHHHHCC	55.95	-
672	Phosphorylation	VQPDDPISFMQLTAK CCCCCCCCEEEECCC	21.76	28555341
674	Sulfoxidation	PDDPISFMQLTAKNE CCCCCCEEEECCCCC	2.26	21406390
679	Ubiquitination	SFMQLTAKNEMNCKE CEEEECCCCCCCCCC	48.48	32015554
685	Ubiquitination	AKNEMNCKEDQFQLS CCCCCCCCCHHHHHH	60.36	21963094
692	Phosphorylation	KEDQFQLSLLAAMGN CCHHHHHHHHHHCCC	15.56	28555341
703	Ubiquitination	AMGNTQRKEAADPLA HCCCCHHHHHHHHHH	41.72	29967540
711	Phosphorylation	EAADPLASKLNKVTQ HHHHHHHHHHHHHHH	45.41	20068231
712	Ubiquitination	AADPLASKLNKVTQL HHHHHHHHHHHHHHH	50.93	21963094
712	Acetylation	AADPLASKLNKVTQL HHHHHHHHHHHHHHH	50.93	25953088
715	Ubiquitination	PLASKLNKVTQLTGF HHHHHHHHHHHHCCC	58.03	22817900
767	Ubiquitination	LATLGDLKLVEKPSP EEECCCCEEECCCCC	56.05	22817900
771	Ubiquitination	GDLKLVEKPSPLTLA CCCEEECCCCCCCCC	43.23	21906983
771	Acetylation	GDLKLVEKPSPLTLA CCCEEECCCCCCCCC	43.23	25953088
773	Phosphorylation	LKLVEKPSPLTLAPH CEEECCCCCCCCCCC	43.54	25159151
776	Phosphorylation	VEKPSPLTLAPHDFA ECCCCCCCCCCCCCC	25.02	28348404
786	Ubiquitination	PHDFANIKANVKVAS CCCCCCCCCCEEEEE	33.44	21906983
790	Ubiquitination	ANIKANVKVASTENG CCCCCCEEEEECCCC	31.71	22817900
859	Sulfoxidation	KVTVNTNMVDLNDYL CEEEECCEECHHHHH	2.03	30846556
865	Phosphorylation	NMVDLNDYLQHILKS CEECHHHHHHHHHHH	13.74	-
871	Ubiquitination	DYLQHILKSTNMKCL HHHHHHHHHCCCCCC	55.41	21963094
876	Ubiquitination	ILKSTNMKCLTPEKA HHHHCCCCCCCHHHH	28.32	21963094
879	Phosphorylation	STNMKCLTPEKALSG HCCCCCCCHHHHHHH	38.58	24719451
882	Ubiquitination	MKCLTPEKALSGYCG CCCCCHHHHHHHHHH	56.69	21963094
913	Acetylation	LANVSIEKPIHQGPD HHCCEECCCCCCCCC	47.83	25953088
913	Ubiquitination	LANVSIEKPIHQGPD HHCCEECCCCCCCCC	47.83	21890473
924	Phosphorylation	QGPDAAVTGHIRIRA CCCCCEECCEEEEEE	20.51	21406692
933	Phosphorylation	HIRIRAKSQGMALSL EEEEEECCCCCEEHH	30.86	29255136
936	Sulfoxidation	IRAKSQGMALSLGDK EEECCCCCEEHHHCC	2.35	21406390
939	Phosphorylation	KSQGMALSLGDKINL CCCCCEEHHHCCCCH	22.29	21406692
943	Ubiquitination	MALSLGDKINLSQKK CEEHHHCCCCHHHCC	31.53	22817900
949	Ubiquitination	DKINLSQKKTSI--- CCCCHHHCCCCC---	55.43	29967540
949	2-Hydroxyisobutyrylation	DKINLSQKKTSI--- CCCCHHHCCCCC---	55.43	-
949	Acetylation	DKINLSQKKTSI--- CCCCHHHCCCCC---	55.43	25953088
950	Ubiquitination	KINLSQKKTSI---- CCCHHHCCCCC----	39.61	-

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COPG1_HUMAN	COPG1	physical	11056392
COPG2_HUMAN	COPG2	physical	11409905
TRI37_HUMAN	TRIM37	physical	16189514
ARF1_HUMAN	ARF1	physical	10720466
COPB2_HUMAN	COPB2	physical	10921873
COPD_HUMAN	ARCN1	physical	8858162
COPA_HUMAN	COPA	physical	8940050
COPB2_HUMAN	COPB2	physical	8940050
COPD_HUMAN	ARCN1	physical	8940050
COPG1_HUMAN	COPG1	physical	8940050
COPE_HUMAN	COPE	physical	8940050
COPG2_HUMAN	COPG2	physical	11056392
ERD21_HUMAN	KDELR1	physical	11703931
NEF_HV1H2	nef	physical	15202998
ARF1_HUMAN	ARF1	physical	15202998
TMEDA_HUMAN	TMED10	physical	9751720
COPA_HUMAN	COPA	physical	9751720
COPB_HUMAN	COPB1	physical	9751720
COPB2_HUMAN	COPB2	physical	9751720
COPG1_HUMAN	COPG1	physical	9751720
COPD_HUMAN	ARCN1	physical	9751720
COPE_HUMAN	COPE	physical	9751720
COPZ1_HUMAN	COPZ1	physical	9751720
COPA_HUMAN	COPA	physical	9482852
COPB2_HUMAN	COPB2	physical	9482852
COPD_HUMAN	ARCN1	physical	9482852
COPE_HUMAN	COPE	physical	9482852
COPG1_HUMAN	COPG1	physical	9482852
COPZ1_HUMAN	COPZ1	physical	9482852
COPB_HUMAN	COPB1	physical	9482852
A4_HUMAN	APP	physical	21832049
COPD_HUMAN	ARCN1	physical	22939629
COPG1_HUMAN	COPG1	physical	22939629
COPE_HUMAN	COPE	physical	22939629
COPG2_HUMAN	COPG2	physical	22939629
COPZ1_HUMAN	COPZ1	physical	22939629
LZTS2_HUMAN	LZTS2	physical	21988832
DPB1_HUMAN	HLA-DPB1	physical	21988832
XRCC6_HUMAN	XRCC6	physical	21988832
GRB2_HUMAN	GRB2	physical	21988832
ID1_HUMAN	ID1	physical	21988832
TANK_HUMAN	TANK	physical	21988832
IRAK3_HUMAN	IRAK3	physical	21988832
FOXB1_HUMAN	FOXB1	physical	21988832
SRTD1_HUMAN	SERTAD1	physical	21988832
NUB1_HUMAN	NUB1	physical	21988832
VPS18_HUMAN	VPS18	physical	21988832
ACACA_HUMAN	ACACA	physical	22863883
KLC1_HUMAN	KLC1	physical	22863883
ACACA_HUMAN	ACACA	physical	26344197
COPA_HUMAN	COPA	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
UBC_HUMAN	UBC	physical	29058666

Drug and Disease Associations

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