CAH3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAH3_MOUSE
• UniProt AC: P16015
• Protein Name: Carbonic anhydrase 3
• Gene Name: Ca3
• Organism: Mus musculus (Mouse).
• Sequence Length: 260
• Subcellular Localization: Cytoplasm.
• Protein Description: Reversible hydration of carbon dioxide..
• Protein Sequence: MAKEWGYASHNGPDHWHELYPIAKGDNQSPIELHTKDIKHDPSLQPWSASYDPGSAKTILNNGKTCRVVFDDTYDRSMLRGGPLSGPYRLRQFHLHWGSSDDHGSEHTVDGVKYAAELHLVHWNPKYNTFGEALKQPDGIAVVGIFLKIGREKGEFQILLDALDKIKTKGKEAPFTHFDPSCLFPACRDYWTYHGSFTTPPCEECIVWLLLKEPMTVSSDQMAKLRSLFSSAENEPPVPLVGNWRPPQPVKGRVVRASFK

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	------MAKEWGYAS ------CCCCCCCCC	20.62	-
3	Malonylation	-----MAKEWGYASH -----CCCCCCCCCC	53.34	26320211
3	Acetylation	-----MAKEWGYASH -----CCCCCCCCCC	53.34	23341599
3	Ubiquitination	-----MAKEWGYASH -----CCCCCCCCCC	53.34	-
7	Phosphorylation	-MAKEWGYASHNGPD -CCCCCCCCCCCCCC	13.15	29899451
9	Phosphorylation	AKEWGYASHNGPDHW CCCCCCCCCCCCCCH	14.70	19060867
24	Ubiquitination	HELYPIAKGDNQSPI HHHEECCCCCCCCCC	68.47	22790023
29	Phosphorylation	IAKGDNQSPIELHTK CCCCCCCCCCEEECC	33.81	27180971
35	Phosphorylation	QSPIELHTKDIKHDP CCCCEEECCCCCCCC	42.93	28464351
36	Acetylation	SPIELHTKDIKHDPS CCCEEECCCCCCCCC	46.86	23864654
36	Ubiquitination	SPIELHTKDIKHDPS CCCEEECCCCCCCCC	46.86	27667366
36	Malonylation	SPIELHTKDIKHDPS CCCEEECCCCCCCCC	46.86	26320211
39	Acetylation	ELHTKDIKHDPSLQP EEECCCCCCCCCCCC	52.68	23864654
39	Ubiquitination	ELHTKDIKHDPSLQP EEECCCCCCCCCCCC	52.68	27667366
39	Malonylation	ELHTKDIKHDPSLQP EEECCCCCCCCCCCC	52.68	26320211
43	Phosphorylation	KDIKHDPSLQPWSAS CCCCCCCCCCCCCCC	45.77	27180971
48	Phosphorylation	DPSLQPWSASYDPGS CCCCCCCCCCCCCCC	17.64	27180971
50	Phosphorylation	SLQPWSASYDPGSAK CCCCCCCCCCCCCCE	25.26	27180971
51	Phosphorylation	LQPWSASYDPGSAKT CCCCCCCCCCCCCEE	26.35	22324799
55	Phosphorylation	SASYDPGSAKTILNN CCCCCCCCCEEHHHC	31.79	22324799
57	Ubiquitination	SYDPGSAKTILNNGK CCCCCCCEEHHHCCC	37.48	27667366
57	Malonylation	SYDPGSAKTILNNGK CCCCCCCEEHHHCCC	37.48	26320211
57	Acetylation	SYDPGSAKTILNNGK CCCCCCCEEHHHCCC	37.48	23864654
64	Ubiquitination	KTILNNGKTCRVVFD EEHHHCCCEEEEEEC	46.72	-
64	Succinylation	KTILNNGKTCRVVFD EEHHHCCCEEEEEEC	46.72	-
64	Phosphoglycerylation	KTILNNGKTCRVVFD EEHHHCCCEEEEEEC	46.72	-
64	Malonylation	KTILNNGKTCRVVFD EEHHHCCCEEEEEEC	46.72	26320211
64	Acetylation	KTILNNGKTCRVVFD EEHHHCCCEEEEEEC	46.72	23806337
65	Phosphorylation	TILNNGKTCRVVFDD EHHHCCCEEEEEECC	13.62	-
66	S-nitrosylation	ILNNGKTCRVVFDDT HHHCCCEEEEEECCC	3.37	22178444
73	Phosphorylation	CRVVFDDTYDRSMLR EEEEECCCCCHHHHC	29.21	27180971
74	Phosphorylation	RVVFDDTYDRSMLRG EEEECCCCCHHHHCC	19.16	17242355
77	Phosphorylation	FDDTYDRSMLRGGPL ECCCCCHHHHCCCCC	21.19	27180971
85	Phosphorylation	MLRGGPLSGPYRLRQ HHCCCCCCCCCEEEE	40.64	28542873
88	Phosphorylation	GGPLSGPYRLRQFHL CCCCCCCCEEEEEEE	26.29	23984901
99	Phosphorylation	QFHLHWGSSDDHGSE EEEEECCCCCCCCCC	25.96	22817900
100	Phosphorylation	FHLHWGSSDDHGSEH EEEECCCCCCCCCCC	43.02	19060867
126	Malonylation	HLVHWNPKYNTFGEA EEEEECCCCCCHHHH	48.17	25418362
126	Acetylation	HLVHWNPKYNTFGEA EEEEECCCCCCHHHH	48.17	22733758
126	Ubiquitination	HLVHWNPKYNTFGEA EEEEECCCCCCHHHH	48.17	-
127	Phosphorylation	LVHWNPKYNTFGEAL EEEECCCCCCHHHHH	22.23	28464351
129	Phosphorylation	HWNPKYNTFGEALKQ EECCCCCCHHHHHCC	29.90	27180971
135	Acetylation	NTFGEALKQPDGIAV CCHHHHHCCCCCEEE	67.82	21728379
135	Ubiquitination	NTFGEALKQPDGIAV CCHHHHHCCCCCEEE	67.82	-
135	Malonylation	NTFGEALKQPDGIAV CCHHHHHCCCCCEEE	67.82	26073543
153	Acetylation	FLKIGREKGEFQILL EEEECCCCCCHHHHH	63.48	22733758
153	Ubiquitination	FLKIGREKGEFQILL EEEECCCCCCHHHHH	63.48	22790023
165	Acetylation	ILLDALDKIKTKGKE HHHHHHHHHHCCCCC	47.13	22733758
165	Ubiquitination	ILLDALDKIKTKGKE HHHHHHHHHHCCCCC	47.13	22790023
171	Ubiquitination	DKIKTKGKEAPFTHF HHHHCCCCCCCCCCC	52.86	-
171	Acetylation	DKIKTKGKEAPFTHF HHHHCCCCCCCCCCC	52.86	23201123
171	Malonylation	DKIKTKGKEAPFTHF HHHHCCCCCCCCCCC	52.86	26320211
176	Phosphorylation	KGKEAPFTHFDPSCL CCCCCCCCCCCHHHC	22.15	22817900
182	S-nitrosylation	FTHFDPSCLFPACRD CCCCCHHHCCHHHCC	5.74	22178444
182	S-palmitoylation	FTHFDPSCLFPACRD CCCCCHHHCCHHHCC	5.74	28526873
182	Glutathionylation	FTHFDPSCLFPACRD CCCCCHHHCCHHHCC	5.74	-
182	S-glutathionyl cysteine	FTHFDPSCLFPACRD CCCCCHHHCCHHHCC	5.74	-
187	S-glutathionyl cysteine	PSCLFPACRDYWTYH HHHCCHHHCCCEEEC	3.28	-
187	S-palmitoylation	PSCLFPACRDYWTYH HHHCCHHHCCCEEEC	3.28	28526873
187	S-nitrosylation	PSCLFPACRDYWTYH HHHCCHHHCCCEEEC	3.28	22178444
187	Glutathionylation	PSCLFPACRDYWTYH HHHCCHHHCCCEEEC	3.28	-
212	Malonylation	CIVWLLLKEPMTVSS HHHHHHHCCCCCCCH	60.79	26073543
212	Acetylation	CIVWLLLKEPMTVSS HHHHHHHCCCCCCCH	60.79	22733758
216	Phosphorylation	LLLKEPMTVSSDQMA HHHCCCCCCCHHHHH	28.14	25521595
218	Phosphorylation	LKEPMTVSSDQMAKL HCCCCCCCHHHHHHH	21.02	23567750
219	Phosphorylation	KEPMTVSSDQMAKLR CCCCCCCHHHHHHHH	27.76	23375375
224	Acetylation	VSSDQMAKLRSLFSS CCHHHHHHHHHHHHC	38.81	23954790
224	Ubiquitination	VSSDQMAKLRSLFSS CCHHHHHHHHHHHHC	38.81	22790023
227	Phosphorylation	DQMAKLRSLFSSAEN HHHHHHHHHHHCCCC	44.17	27180971
230	Phosphorylation	AKLRSLFSSAENEPP HHHHHHHHCCCCCCC	33.65	27180971
251	Malonylation	WRPPQPVKGRVVRAS CCCCCCCCCEEEEEE	47.91	26320211
251	Ubiquitination	WRPPQPVKGRVVRAS CCCCCCCCCEEEEEE	47.91	27667366
258	Phosphorylation	KGRVVRASFK----- CCEEEEEECC-----	24.01	24719451

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

Oops, there are no upstream regulatory protein records of CAH3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CAH3_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 CAH3_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CAH3_MOUSE !!

Drug and Disease Associations

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