CPNE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CPNE1_HUMAN
• UniProt AC: Q99829
• Protein Name: Copine-1 {ECO:0000305}
• Gene Name: CPNE1 {ECO:0000312|HGNC:HGNC:2314}
• Organism: Homo sapiens (Human).
• Sequence Length: 537
• Subcellular Localization: Nucleus . Cytoplasm . Cell membrane . Translocates to the cell membrane in a calcium-dependent manner (PubMed:21087455, PubMed:25450385).
• Protein Description: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. [PubMed: 14674885 Involved in the TNF-alpha receptor signaling pathway in a calcium-dependent manner]
• Protein Sequence: MAHCVTLVQLSISCDHLIDKDIGSKSDPLCVLLQDVGGGSWAELGRTERVRNCSSPEFSKTLQLEYRFETVQKLRFGIYDIDNKTPELRDDDFLGGAECSLGQIVSSQVLTLPLMLKPGKPAGRGTITVSAQELKDNRVVTMEVEARNLDKKDFLGKSDPFLEFFRQGDGKWHLVYRSEVIKNNLNPTWKRFSVPVQHFCGGNPSTPIQVQCSDYDSDGSHDLIGTFHTSLAQLQAVPAEFECIHPEKQQKKKSYKNSGTIRVKICRVETEYSFLDYVMGGCQINFTVGVDFTGSNGDPSSPDSLHYLSPTGVNEYLMALWSVGSVVQDYDSDKLFPAFGFGAQVPPDWQVSHEFALNFNPSNPYCAGIQGIVDAYRQALPQVRLYGPTNFAPIINHVARFAAQAAHQGTASQYFMLLLLTDGAVTDVEATREAVVRASNLPMSVIIVGVGGADFEAMEQLDADGGPLHTRSGQAAARDIVQFVPYRRFQNAPREALAQTVLAEVPTQLVSYFRAQGWAPLKPLPPSAKDPAQAPQA

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
20	Ubiquitination	SCDHLIDKDIGSKSD CCCCCCCCCCCCCCC	44.23	-
25	Ubiquitination	IDKDIGSKSDPLCVL CCCCCCCCCCCEEEE	54.38	-
30	Ubiquitination	GSKSDPLCVLLQDVG CCCCCCEEEEEEECC	2.17	-
40	Phosphorylation	LQDVGGGSWAELGRT EEECCCCCHHHCCCC	26.79	22617229
45	Phosphorylation	GGSWAELGRTERVRN CCCHHHCCCCCCCCC	26.43	-
54	Phosphorylation	TERVRNCSSPEFSKT CCCCCCCCCCHHHHE	53.10	22167270
55	Phosphorylation	ERVRNCSSPEFSKTL CCCCCCCCCHHHHEE	30.56	25159151
59	Phosphorylation	NCSSPEFSKTLQLEY CCCCCHHHHEEEEEE	24.06	22167270
60	Ubiquitination	CSSPEFSKTLQLEYR CCCCHHHHEEEEEEE	59.58	21890473
60	Phosphorylation	CSSPEFSKTLQLEYR CCCCHHHHEEEEEEE	59.58	-
65	Ubiquitination	FSKTLQLEYRFETVQ HHHEEEEEEEHHHHH	23.00	-
73	Ubiquitination	YRFETVQKLRFGIYD EEHHHHHHHEEEEEE	36.98	21890473
78	Ubiquitination	VQKLRFGIYDIDNKT HHHHEEEEEECCCCC	2.28	-
84	Ubiquitination	GIYDIDNKTPELRDD EEEECCCCCCCCCCC	62.80	21906983
85	Phosphorylation	IYDIDNKTPELRDDD EEECCCCCCCCCCCC	28.40	24719451
89	Sumoylation	DNKTPELRDDDFLGG CCCCCCCCCCCCCCC	43.58	-
89	Ubiquitination	DNKTPELRDDDFLGG CCCCCCCCCCCCCCC	43.58	-
90	Phosphorylation	NKTPELRDDDFLGGA CCCCCCCCCCCCCCC	72.89	-
117	Ubiquitination	LTLPLMLKPGKPAGR EEEEEEECCCCCCCC	37.45	-
120	Ubiquitination	PLMLKPGKPAGRGTI EEEECCCCCCCCCEE	39.98	-
126	Phosphorylation	GKPAGRGTITVSAQE CCCCCCCEEEEEEHH	16.47	20068231
128	Phosphorylation	PAGRGTITVSAQELK CCCCCEEEEEEHHHH	14.30	-
130	Phosphorylation	GRGTITVSAQELKDN CCCEEEEEEHHHHCC	18.65	21712546
135	Acetylation	TVSAQELKDNRVVTM EEEEHHHHCCCEEEE	52.80	25953088
135	Ubiquitination	TVSAQELKDNRVVTM EEEEHHHHCCCEEEE	52.80	21890473
135	Phosphorylation	TVSAQELKDNRVVTM EEEEHHHHCCCEEEE	52.80	-
140	Sumoylation	ELKDNRVVTMEVEAR HHHCCCEEEEEEEEC	3.68	-
140	Ubiquitination	ELKDNRVVTMEVEAR HHHCCCEEEEEEEEC	3.68	-
140	Acetylation	ELKDNRVVTMEVEAR HHHCCCEEEEEEEEC	3.68	-
142	Sulfoxidation	KDNRVVTMEVEARNL HCCCEEEEEEEECCC	3.52	21406390
151	Ubiquitination	VEARNLDKKDFLGKS EEECCCCHHHHCCCC	58.36	-
152	Ubiquitination	EARNLDKKDFLGKSD EECCCCHHHHCCCCC	54.07	-
152	Sumoylation	EARNLDKKDFLGKSD EECCCCHHHHCCCCC	54.07	-
156	Ubiquitination	LDKKDFLGKSDPFLE CCHHHHCCCCCHHHH	27.67	-
157	Sumoylation	DKKDFLGKSDPFLEF CHHHHCCCCCHHHHH	54.56	-
157	Ubiquitination	DKKDFLGKSDPFLEF CHHHHCCCCCHHHHH	54.56	21890473
158	Phosphorylation	KKDFLGKSDPFLEFF HHHHCCCCCHHHHHH	49.03	21712546
162	Ubiquitination	LGKSDPFLEFFRQGD CCCCCHHHHHHHCCC	7.35	-
163	Phosphorylation	GKSDPFLEFFRQGDG CCCCHHHHHHHCCCC	43.02	-
171	Ubiquitination	FFRQGDGKWHLVYRS HHHCCCCCEEEEEEE	35.86	19608861
171	Acetylation	FFRQGDGKWHLVYRS HHHCCCCCEEEEEEE	35.86	19608861
176	Acetylation	DGKWHLVYRSEVIKN CCCEEEEEEEHHHHC	18.12	19608861
176	Ubiquitination	DGKWHLVYRSEVIKN CCCEEEEEEEHHHHC	18.12	19608861
182	Ubiquitination	VYRSEVIKNNLNPTW EEEEHHHHCCCCCCC	44.98	21890473
187	Ubiquitination	VIKNNLNPTWKRFSV HHHCCCCCCCCCCCC	42.68	-
188	Phosphorylation	IKNNLNPTWKRFSVP HHCCCCCCCCCCCCC	42.41	24961811
190	Ubiquitination	NNLNPTWKRFSVPVQ CCCCCCCCCCCCCCH	46.15	1906983
190	Methylation	NNLNPTWKRFSVPVQ CCCCCCCCCCCCCCH	46.15	-
195	Methylation	TWKRFSVPVQHFCGG CCCCCCCCCHHHCCC	20.89	-
195	Ubiquitination	TWKRFSVPVQHFCGG CCCCCCCCCHHHCCC	20.89	-
253	Ubiquitination	PEKQQKKKSYKNSGT HHHHHCCCCCCCCCC	67.08	-
254	Phosphorylation	EKQQKKKSYKNSGTI HHHHCCCCCCCCCCE	50.66	-
255	Phosphorylation	KQQKKKSYKNSGTIR HHHCCCCCCCCCCEE	24.06	30576142
256	Ubiquitination	QQKKKSYKNSGTIRV HHCCCCCCCCCCEEE	52.29	-
260	Phosphorylation	KSYKNSGTIRVKICR CCCCCCCCEEEEEEE	12.87	25159151
261	Ubiquitination	SYKNSGTIRVKICRV CCCCCCCEEEEEEEE	5.63	-
265	Phosphorylation	SGTIRVKICRVETEY CCCEEEEEEEEEEEE	1.33	-
325	O-linked_Glycosylation	MALWSVGSVVQDYDS HHHHHHCCCCCCCCC	19.57	30379171
332	O-linked_Glycosylation	SVVQDYDSDKLFPAF CCCCCCCCCCCEECC	30.34	30379171
386	Phosphorylation	ALPQVRLYGPTNFAP HCCCCEECCCCCHHH	15.53	28152594
389	Phosphorylation	QVRLYGPTNFAPIIN CCEECCCCCHHHHHH	38.31	28152594
391	Phosphorylation	RLYGPTNFAPIINHV EECCCCCHHHHHHHH	10.60	-
500	Phosphorylation	PREALAQTVLAEVPT CHHHHHHHHHHHCCH	16.33	20860994
505	Phosphorylation	AQTVLAEVPTQLVSY HHHHHHHCCHHHHHH	5.31	-
522	Ubiquitination	AQGWAPLKPLPPSAK HCCCCCCCCCCCCCC	43.37	21890473
527	Ubiquitination	PLKPLPPSAKDPAQA CCCCCCCCCCCHHHC	46.11	-
529	Ubiquitination	KPLPPSAKDPAQAPQ CCCCCCCCCHHHCCC	69.45	2190698
534	Ubiquitination	SAKDPAQAPQA---- CCCCHHHCCCC----	10.57	-

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

Oops, there are no upstream regulatory protein records of CPNE1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CPNE1_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 CPNE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPP5_MOUSE	Ppp5c	physical	12522145
MYCB2_MOUSE	Mycbp2	physical	12522145
UBE2O_MOUSE	Ube2o	physical	12522145
RADI_MOUSE	Rdx	physical	12522145
ACTB_MOUSE	Actb	physical	12522145
TIM13_HUMAN	TIMM13	physical	22939629
F10A1_HUMAN	ST13	physical	22939629
TTL12_HUMAN	TTLL12	physical	22939629
PYGB_HUMAN	PYGB	physical	22939629
STK3_HUMAN	STK3	physical	21988832

Drug and Disease Associations

• Kegg Disease
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• 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-171, AND MASS SPECTROMETRY.
PubMed: 19608861