COPD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPD_HUMAN
• UniProt AC: P48444
• Protein Name: Coatomer subunit delta
• Gene Name: ARCN1
• Organism: Homo sapiens (Human).
• Sequence Length: 511
• 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: Component of the coatomer, 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. The 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)..
• Protein Sequence: MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAAMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGETIMSSSMGKRTSEATKMHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEKSFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDAKNKSGSLEFSIAGQPNDFFPVQVSFVSKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKYEIL

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
9	S-palmitoylation	VLLAAAVCTKAGKAI HHHHHHHHHHHCHHH	2.50	29575903
14	Ubiquitination	AVCTKAGKAIVSRQF HHHHHHCHHHHHHHH	39.54	-
14	Acetylation	AVCTKAGKAIVSRQF HHHHHHCHHHHHHHH	39.54	25953088
18	Phosphorylation	KAGKAIVSRQFVEMT HHCHHHHHHHHHHHH	17.79	26074081
25	Phosphorylation	SRQFVEMTRTRIEGL HHHHHHHHHHHHHHH	18.51	26074081
27	Phosphorylation	QFVEMTRTRIEGLLA HHHHHHHHHHHHHHH	27.17	21406692
38	Ubiquitination	GLLAAFPKLMNTGKQ HHHHHHHHHHCCCCC	54.65	21890473
44	Ubiquitination	PKLMNTGKQHTFVET HHHHCCCCCEEEEEE	36.55	21890473
44	2-Hydroxyisobutyrylation	PKLMNTGKQHTFVET HHHHCCCCCEEEEEE	36.55	-
44	Acetylation	PKLMNTGKQHTFVET HHHHCCCCCEEEEEE	36.55	25953088
53	Phosphorylation	HTFVETESVRYVYQP EEEEEECCEEEEECC	21.22	22468782
54	Ubiquitination	TFVETESVRYVYQPM EEEEECCEEEEECCH	4.10	21890473
56	Phosphorylation	VETESVRYVYQPMEK EEECCEEEEECCHHH	11.01	29759185
58	Phosphorylation	TESVRYVYQPMEKLY ECCEEEEECCHHHEE	9.66	29759185
61	Sulfoxidation	VRYVYQPMEKLYMVL EEEEECCHHHEEEEE	4.13	30846556
63	Ubiquitination	YVYQPMEKLYMVLIT EEECCHHHEEEEEEE	38.37	-
65	Phosphorylation	YQPMEKLYMVLITTK ECCHHHEEEEEEEEC	9.03	22468782
74	Phosphorylation	VLITTKNSNILEDLE EEEEECCCCHHHHHH	27.14	21712546
84	Methylation	LEDLETLRLFSRVIP HHHHHHHHHHHHHHH	40.90	-
93	Phosphorylation	FSRVIPEYCRALEEN HHHHHHHHHHHHHHC	5.06	28152594
132	Phosphorylation	VNLAQIRTFTEMDSH CCHHHEEEEECCCCH	36.22	-
134	Phosphorylation	LAQIRTFTEMDSHEE HHHEEEEECCCCHHH	29.77	-
136	Sulfoxidation	QIRTFTEMDSHEEKV HEEEEECCCCHHHHH	6.10	30846556
138	Phosphorylation	RTFTEMDSHEEKVFR EEEECCCCHHHHHHH	31.33	22617229
142	Ubiquitination	EMDSHEEKVFRAVRE CCCCHHHHHHHHHHH	43.63	-
142	2-Hydroxyisobutyrylation	EMDSHEEKVFRAVRE CCCCHHHHHHHHHHH	43.63	-
142	Acetylation	EMDSHEEKVFRAVRE CCCCHHHHHHHHHHH	43.63	25953088
142	Malonylation	EMDSHEEKVFRAVRE CCCCHHHHHHHHHHH	43.63	26320211
145	Acetylation	SHEEKVFRAVRETQE CHHHHHHHHHHHHHH	34.85	19608861
145	Ubiquitination	SHEEKVFRAVRETQE CHHHHHHHHHHHHHH	34.85	19608861
153	Ubiquitination	AVRETQEREAKAEMR HHHHHHHHHHHHHHH	39.08	21890473
164	Ubiquitination	AEMRRKAKELQQARR HHHHHHHHHHHHHHH	63.09	-
188	Phosphorylation	PGFGGFGSSAVSGGS CCCCCCCCCCCCCCC	16.92	28857561
189	Phosphorylation	GFGGFGSSAVSGGST CCCCCCCCCCCCCCH	32.82	28857561
192	Phosphorylation	GFGSSAVSGGSTAAM CCCCCCCCCCCHHEE	36.83	28857561
195	Phosphorylation	SSAVSGGSTAAMITE CCCCCCCCHHEEEEE	20.56	28857561
196	Phosphorylation	SAVSGGSTAAMITET CCCCCCCHHEEEEEE	23.01	24719451
203	Phosphorylation	TAAMITETIIETDKP HHEEEEEEHHHCCCC	20.71	24400094
203	O-linked_Glycosylation	TAAMITETIIETDKP HHEEEEEEHHHCCCC	20.71	31373491
207	O-linked_Glycosylation	ITETIIETDKPKVAP EEEEHHHCCCCCCCC	38.63	31373491
211	Acetylation	IIETDKPKVAPAPAR HHHCCCCCCCCCCCC	57.69	20167786
220	Phosphorylation	APAPARPSGPSKALK CCCCCCCCCCCCCCC	58.75	25159151
221	Acetylation	PAPARPSGPSKALKL CCCCCCCCCCCCCCC	32.93	19608861
221	Ubiquitination	PAPARPSGPSKALKL CCCCCCCCCCCCCCC	32.93	19608861
223	Phosphorylation	PARPSGPSKALKLGA CCCCCCCCCCCCCCC	33.80	25159151
223	O-linked_Glycosylation	PARPSGPSKALKLGA CCCCCCCCCCCCCCC	33.80	31373491
224	Ubiquitination	ARPSGPSKALKLGAK CCCCCCCCCCCCCCC	61.95	-
224	Acetylation	ARPSGPSKALKLGAK CCCCCCCCCCCCCCC	61.95	25953088
227	Ubiquitination	SGPSKALKLGAKGKE CCCCCCCCCCCCCCC	50.13	-
231	Acetylation	KALKLGAKGKEVDNF CCCCCCCCCCCCHHH	69.58	23954790
233	Acetylation	LKLGAKGKEVDNFVD CCCCCCCCCCHHHHH	54.58	19608861
233	Ubiquitination	LKLGAKGKEVDNFVD CCCCCCCCCCHHHHH	54.58	21906983
241	Acetylation	EVDNFVDKLKSEGET CCHHHHHHHHHCCCC	53.14	26822725
241	Ubiquitination	EVDNFVDKLKSEGET CCHHHHHHHHHCCCC	53.14	21890473
241	2-Hydroxyisobutyrylation	EVDNFVDKLKSEGET CCHHHHHHHHHCCCC	53.14	-
243	Ubiquitination	DNFVDKLKSEGETIM HHHHHHHHHCCCCCH	52.80	21890473
243	2-Hydroxyisobutyrylation	DNFVDKLKSEGETIM HHHHHHHHHCCCCCH	52.80	-
244	Phosphorylation	NFVDKLKSEGETIMS HHHHHHHHCCCCCHH	62.36	23403867
248	Phosphorylation	KLKSEGETIMSSSMG HHHHCCCCCHHCCCC	32.60	27732954
248	Ubiquitination	KLKSEGETIMSSSMG HHHHCCCCCHHCCCC	32.60	21890473
250	Sulfoxidation	KSEGETIMSSSMGKR HHCCCCCHHCCCCCC	4.08	21406390
251	Phosphorylation	SEGETIMSSSMGKRT HCCCCCHHCCCCCCC	18.53	29255136
252	Phosphorylation	EGETIMSSSMGKRTS CCCCCHHCCCCCCCC	13.63	29255136
253	Phosphorylation	GETIMSSSMGKRTSE CCCCHHCCCCCCCCC	25.01	29255136
254	Sulfoxidation	ETIMSSSMGKRTSEA CCCHHCCCCCCCCCC	8.73	30846556
256	Acetylation	IMSSSMGKRTSEATK CHHCCCCCCCCCCHH	43.81	25953088
256	Ubiquitination	IMSSSMGKRTSEATK CHHCCCCCCCCCCHH	43.81	21890473
256	2-Hydroxyisobutyrylation	IMSSSMGKRTSEATK CHHCCCCCCCCCCHH	43.81	-
258	Phosphorylation	SSSMGKRTSEATKMH HCCCCCCCCCCHHCC	34.11	26699800
259	Phosphorylation	SSMGKRTSEATKMHA CCCCCCCCCCHHCCC	29.30	24719451
262	Phosphorylation	GKRTSEATKMHAPPI CCCCCCCHHCCCCCC	25.50	26699800
263	Ubiquitination	KRTSEATKMHAPPIN CCCCCCHHCCCCCCC	35.42	-
263	Ubiquitination	KRTSEATKMHAPPIN CCCCCCHHCCCCCCC	35.42	21890473
273	Phosphorylation	APPINMESVHMKIEE CCCCCHHHHEEEEEE	13.42	22964224
275	Ubiquitination	PINMESVHMKIEEKI CCCHHHHEEEEEEEE	22.54	21890473
309	Acetylation	MLRISDDKYGRIRLH EEEECCCCCCEEEEE	55.37	19608861
309	Ubiquitination	MLRISDDKYGRIRLH EEEECCCCCCEEEEE	55.37	21906983
310	Phosphorylation	LRISDDKYGRIRLHV EEECCCCCCEEEEEE	20.73	28152594
322	Ubiquitination	LHVENEDKKGVQLQT EEEECCCCCCCCCCC	45.29	21890473
323	Ubiquitination	HVENEDKKGVQLQTH EEECCCCCCCCCCCC	76.32	21890473
329	Phosphorylation	KKGVQLQTHPNVDKK CCCCCCCCCCCCCHH	48.14	-
335	Acetylation	QTHPNVDKKLFTAES CCCCCCCHHCEEHHH	47.28	23749302
335	Ubiquitination	QTHPNVDKKLFTAES CCCCCCCHHCEEHHH	47.28	-
335	2-Hydroxyisobutyrylation	QTHPNVDKKLFTAES CCCCCCCHHCEEHHH	47.28	-
336	Ubiquitination	THPNVDKKLFTAESL CCCCCCHHCEEHHHH	44.35	21890473
339	Phosphorylation	NVDKKLFTAESLIGL CCCHHCEEHHHHHCC	39.69	20639409
342	Phosphorylation	KKLFTAESLIGLKNP HHCEEHHHHHCCCCC	23.87	22199227
347	Acetylation	AESLIGLKNPEKSFP HHHHHCCCCCCCCCC	66.30	25953088
347	Ubiquitination	AESLIGLKNPEKSFP HHHHHCCCCCCCCCC	66.30	21890473
351	Acetylation	IGLKNPEKSFPVNSD HCCCCCCCCCCCCCC	59.67	23954790
351	Ubiquitination	IGLKNPEKSFPVNSD HCCCCCCCCCCCCCC	59.67	21890473
363	Acetylation	NSDVGVLKWRLQTTE CCCCCEEEEEEEECC	28.06	25953088
363	Ubiquitination	NSDVGVLKWRLQTTE CCCCCEEEEEEEECC	28.06	21890473
383	O-linked_Glycosylation	LTINCWPSESGNGCD EEEEEECCCCCCCCE	21.64	31373491
385	O-linked_Glycosylation	INCWPSESGNGCDVN EEEECCCCCCCCEEE	41.73	31373491
437	Phosphorylation	RHDSRRNTLEWCLPV CCCCCCCCEEEEEEE	25.01	28450419
441	S-nitrosocysteine	RRNTLEWCLPVIDAK CCCCEEEEEEEEECC	1.94	-
441	Glutathionylation	RRNTLEWCLPVIDAK CCCCEEEEEEEEECC	1.94	22555962
441	S-nitrosylation	RRNTLEWCLPVIDAK CCCCEEEEEEEEECC	1.94	19483679
448	Ubiquitination	CLPVIDAKNKSGSLE EEEEEECCCCCCCEE	62.25	21890473
450	Ubiquitination	PVIDAKNKSGSLEFS EEEECCCCCCCEEEE	56.33	-
476	Ubiquitination	QVSFVSKKNYCNIQV EEEEEECCCEECEEE	45.72	-
478	Phosphorylation	SFVSKKNYCNIQVTK EEEECCCEECEEEEE	8.85	28152594
485	Ubiquitination	YCNIQVTKVTQVDGN EECEEEEEEEEECCC	44.41	21890473
487	Phosphorylation	NIQVTKVTQVDGNSP CEEEEEEEEECCCCC	25.16	30266825
493	Phosphorylation	VTQVDGNSPVRFSTE EEEECCCCCEEEEEE	30.24	30266825
501	Phosphorylation	PVRFSTETTFLVDKY CEEEEEEEEEEEEEE	23.96	28348404

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COPD_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 COPD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COPB_HUMAN	COPB1	physical	10921873
COPB_HUMAN	COPB1	physical	8858162
TMEDA_HUMAN	TMED10	physical	9751720
COPB_HUMAN	COPB1	physical	9482852
COPD_HUMAN	ARCN1	physical	9482852
A4_HUMAN	APP	physical	21832049
COPG1_HUMAN	COPG1	physical	22939629
COPE_HUMAN	COPE	physical	22939629
COPZ1_HUMAN	COPZ1	physical	22939629
COPB_HUMAN	COPB1	physical	22863883
KLC1_HUMAN	KLC1	physical	22863883
P4R3A_HUMAN	SMEK1	physical	22863883
COPA_HUMAN	COPA	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
COPB2_HUMAN	COPB2	physical	26344197
COPE_HUMAN	COPE	physical	26344197
COPG1_HUMAN	COPG1	physical	26344197
COPZ1_HUMAN	COPZ1	physical	26344197
NOB1_HUMAN	NOB1	physical	26344197
SF3B1_HUMAN	SF3B1	physical	26344197

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-309, AND MASSSPECTROMETRY.
PubMed: 19608861