dbPTM

CPT2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CPT2_MOUSE
UniProt AC	P52825
Protein Name	Carnitine O-palmitoyltransferase 2, mitochondrial
Gene Name	Cpt2
Organism	Mus musculus (Mouse).
Sequence Length	658
Subcellular Localization	Mitochondrion inner membrane Peripheral membrane protein Matrix side.
Protein Description
Protein Sequence	MMPRLLLRDWPRCPSLVLGAPSRPLSAVSGPAEYLQHSIVPTMHYQDSLPRLPIPKLEDTMKRYLSAQKPLLNDSQFRKTEVLCKDFENGIGKELHAHLLAQDKQNKHTSYISGPWFDMYLTARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNLTVSAVRFLKTLRAGLLEPEVFHLNPARSDTDAFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRIPKPSRDELFTDTKARHLLVLRKGHFYVFDVLDQDGNIVNPSEIQAHLKYILSDSSPVPEFPLAYLTSENRDVWAELRQKLIHGGNEETLRKVDSAVFCLCLDDFPMKDLVHLSHTMLHGDGTNRWFDKSFNLIVAKDGTAAVHFEHAWGDGVAVLRFFNEVFRDSTQTPAIAPQSQPAATDSSVSVQKLSFKLSSALKAGVTAAKEKFDATMKTLTIDAIQFQRGGKEFLKKKKLSPDAVAQLAFQMAFLRQYGQTVATYESCSTAAFKHGRTETIRPASIFTKRCSEAFVREPSKHSVGELQHMMAECSKYHGQLTKEAAMGQGFDRHLFALRYLAAARGVTLPELYQDPAYQRINHNILSTSTLSSPAVSLGGFAPVVPDGFGIAYAVHDDWIGCNVSSYSGRNAREFLHCVQKCLEDMFDALEGKAIKT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
62	Acetylation	PKLEDTMKRYLSAQK CCHHHHHHHHHHHCC	39.73	23576753
62	Succinylation	PKLEDTMKRYLSAQK CCHHHHHHHHHHHCC	39.73	26388266
69	Acetylation	KRYLSAQKPLLNDSQ HHHHHHCCCCCCHHH	37.03	23864654
69	Succinylation	KRYLSAQKPLLNDSQ HHHHHHCCCCCCHHH	37.03	-
69	Succinylation	KRYLSAQKPLLNDSQ HHHHHHCCCCCCHHH	37.03	23806337
69	Glutarylation	KRYLSAQKPLLNDSQ HHHHHHCCCCCCHHH	37.03	24703693
75	Phosphorylation	QKPLLNDSQFRKTEV CCCCCCHHHCCHHHH	30.09	23737553
79	Acetylation	LNDSQFRKTEVLCKD CCHHHCCHHHHHHHH	50.77	23576753
79	Succinylation	LNDSQFRKTEVLCKD CCHHHCCHHHHHHHH	50.77	23806337
84	S-nitrosylation	FRKTEVLCKDFENGI CCHHHHHHHHHCCCC	4.86	21278135
84	S-nitrosocysteine	FRKTEVLCKDFENGI CCHHHHHHHHHCCCC	4.86	-
85	Succinylation	RKTEVLCKDFENGIG CHHHHHHHHHCCCCC	62.38	-
85	Acetylation	RKTEVLCKDFENGIG CHHHHHHHHHCCCCC	62.38	23806337
85	Succinylation	RKTEVLCKDFENGIG CHHHHHHHHHCCCCC	62.38	23806337
93	Acetylation	DFENGIGKELHAHLL HHCCCCCHHHHHHHH	56.00	23201123
104	Acetylation	AHLLAQDKQNKHTSY HHHHHHHCCCCCCCC	43.63	23864654
142	Succinylation	MAFNPDPKSEYNDQL CCCCCCCCHHHHHHH	64.40	23954790
142	Acetylation	MAFNPDPKSEYNDQL CCCCCCCCHHHHHHH	64.40	23954790
239	Succinylation	DELFTDTKARHLLVL HHCCCCCCHHEEEEE	46.35	23806337
239	Succinylation	DELFTDTKARHLLVL HHCCCCCCHHEEEEE	46.35	-
239	Acetylation	DELFTDTKARHLLVL HHCCCCCCHHEEEEE	46.35	23576753
239	Glutarylation	DELFTDTKARHLLVL HHCCCCCCHHEEEEE	46.35	24703693
248	Acetylation	RHLLVLRKGHFYVFD HEEEEEECCEEEEEE	53.21	23576753
305	Succinylation	VWAELRQKLIHGGNE HHHHHHHHHHHCCCH	42.87	24315375
305	Malonylation	VWAELRQKLIHGGNE HHHHHHHHHHHCCCH	42.87	26320211
305	Acetylation	VWAELRQKLIHGGNE HHHHHHHHHHHCCCH	42.87	23576753
414	Succinylation	DSSVSVQKLSFKLSS CCCCEEEHHHHHHHH	43.90	23954790
414	Acetylation	DSSVSVQKLSFKLSS CCCCEEEHHHHHHHH	43.90	23864654
418	Succinylation	SVQKLSFKLSSALKA EEEHHHHHHHHHHHH	44.05	23806337
418	Succinylation	SVQKLSFKLSSALKA EEEHHHHHHHHHHHH	44.05	-
418	Acetylation	SVQKLSFKLSSALKA EEEHHHHHHHHHHHH	44.05	23576753
420	Phosphorylation	QKLSFKLSSALKAGV EHHHHHHHHHHHHCC	17.73	23737553
421	Phosphorylation	KLSFKLSSALKAGVT HHHHHHHHHHHHCCH	48.32	23737553
424	Succinylation	FKLSSALKAGVTAAK HHHHHHHHHCCHHHH	42.69	23806337
424	Malonylation	FKLSSALKAGVTAAK HHHHHHHHHCCHHHH	42.69	26320211
424	Acetylation	FKLSSALKAGVTAAK HHHHHHHHHCCHHHH	42.69	23806337
424	Succinylation	FKLSSALKAGVTAAK HHHHHHHHHCCHHHH	42.69	-
424	Glutarylation	FKLSSALKAGVTAAK HHHHHHHHHCCHHHH	42.69	24703693
433	Acetylation	GVTAAKEKFDATMKT CCHHHHHHHHCCCCE	48.08	23864654
439	Acetylation	EKFDATMKTLTIDAI HHHHCCCCEEEEEEE	35.71	23806337
439	Succinylation	EKFDATMKTLTIDAI HHHHCCCCEEEEEEE	35.71	23806337
439	Succinylation	EKFDATMKTLTIDAI HHHHCCCCEEEEEEE	35.71	-
453	Acetylation	IQFQRGGKEFLKKKK EEECCCCHHHHHHCC	48.38	23864654
457	Acetylation	RGGKEFLKKKKLSPD CCCHHHHHHCCCCHH	68.79	23576753
489	S-palmitoylation	TVATYESCSTAAFKH EEEEHHHHCCCHHHC	2.53	28526873
489	S-nitrosylation	TVATYESCSTAAFKH EEEEHHHHCCCHHHC	2.53	21278135
489	S-nitrosocysteine	TVATYESCSTAAFKH EEEEHHHHCCCHHHC	2.53	-
495	Acetylation	SCSTAAFKHGRTETI HHCCCHHHCCCCCCC	40.18	23576753
510	Succinylation	RPASIFTKRCSEAFV CCHHHHHHHHHHHHC	40.43	23806337
510	Acetylation	RPASIFTKRCSEAFV CCHHHHHHHHHHHHC	40.43	23576753
510	Succinylation	RPASIFTKRCSEAFV CCHHHHHHHHHHHHC	40.43	-
512	S-palmitoylation	ASIFTKRCSEAFVRE HHHHHHHHHHHHCCC	4.61	26165157
512	S-nitrosylation	ASIFTKRCSEAFVRE HHHHHHHHHHHHCCC	4.61	21278135
512	S-nitrosocysteine	ASIFTKRCSEAFVRE HHHHHHHHHHHHCCC	4.61	-
535	S-nitrosocysteine	LQHMMAECSKYHGQL HHHHHHHHHHHHCCC	2.86	-
535	S-nitrosylation	LQHMMAECSKYHGQL HHHHHHHHHHHHCCC	2.86	21278135
535	S-palmitoylation	LQHMMAECSKYHGQL HHHHHHHHHHHHCCC	2.86	28526873
537	Acetylation	HMMAECSKYHGQLTK HHHHHHHHHHCCCHH	53.58	23864654
544	Acetylation	KYHGQLTKEAAMGQG HHHCCCHHHHHCCCC	54.68	23576753
544	Succinylation	KYHGQLTKEAAMGQG HHHCCCHHHHHCCCC	54.68	-
544	Glutarylation	KYHGQLTKEAAMGQG HHHCCCHHHHHCCCC	54.68	24703693
544	Succinylation	KYHGQLTKEAAMGQG HHHCCCHHHHHCCCC	54.68	23806337
639	S-nitrosocysteine	NAREFLHCVQKCLED CHHHHHHHHHHHHHH	3.64	-
639	S-nitrosylation	NAREFLHCVQKCLED CHHHHHHHHHHHHHH	3.64	21278135
639	S-palmitoylation	NAREFLHCVQKCLED CHHHHHHHHHHHHHH	3.64	28526873
643	S-nitrosocysteine	FLHCVQKCLEDMFDA HHHHHHHHHHHHHHH	2.55	-
643	S-nitrosylation	FLHCVQKCLEDMFDA HHHHHHHHHHHHHHH	2.55	21278135

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of CPT2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CPT2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CPT2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CPT2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of CPT2_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-544, AND MASS SPECTROMETRY.	16916647 [Abstract]