Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
CPT2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CPT2 Defects in CPT2 are the cause of carnitine palmitoyltransferase 2 deficiency late-onset (CPT2D); also known as CPT-II deficiency or CPT2 deficiency. CPT2D is an autosomal recessive disorder characterized by recurrent myoglobinuria, episodes of muscle pain, stiffness, and rhabdomyolysis. These symptoms are triggered by prolonged exercise, fasting or viral infection and patients are usually young adults. In addition to this classical, late-onset, muscular type, a hepatic or hepatocardiomuscular form has been reported in infants. Clinical pictures in these children or neonates include hypoketotic hypoglycemia, liver dysfunction, cardiomyopathy and sudden death. Defects in CPT2 are the cause of carnitine palmitoyltransferase 2 deficiency infantile (CPT2DI). A disorder of mitochondrial long-chain fatty acid oxidation characterized by hepatic or hepato-cardio-muscular manifestations with onset in infancy. Clinical features include hypoketotic hypoglycemia, lethargy, seizures, hepatomegaly, liver dysfunction, cardiomegaly and dilated cardiomyopathy. Defects in CPT2 are the cause of carnitine palmitoyltransferase 2 deficiency lethal neonatal (CPT2D-LN); also known as lethal neonatal CPT-II deficiency. It is a lethal neonatal form of CPT2D. This rarely presentation is antenatal with cerebral periventricular cysts and cystic dysplastic kidneys. The clinical variability of the disease is likely attributed to the variable residual enzymatic activity. Defects in CPT2 are a cause of susceptibility to encephalopathy acute infection-induced type 4 (IIAE4). A severe neurologic complication of an infection. It manifests within days in otherwise healthy children after common viral infections, without evidence of viral infection of the brain or inflammatory cell infiltration. In affected children, high- grade fever is accompanied within 12 to 48 hours by febrile convulsions, often leading to coma, multiple-organ failure, brain edema, and high morbidity and mortality. The infections are usually viral, particularly influenza, although other viruses and even mycoplasma have been found to cause the disorder. Polymorphic variants in CPT2 can confer susceptibility to infection-induced encepalopathy. These variants do not cause classical carnitine palmitoyltransferase 2 deficiency, and patients harboring any of them are asymptomatic most of the time. However, they are prone to viral infection (high fever)-related encephalopathy (PubMed:21697855). Belongs to the carnitine/choline acetyltransferase family. Note: This description may include information from UniProtKB.
Protein type: Lipid Metabolism - fatty acid; Mitochondrial; EC 2.3.1.21; Transferase
Chromosomal Location of Human Ortholog: 1p32
Cellular Component: mitochondrion; mitochondrial inner membrane; nucleolus; nucleus
Molecular Function: carnitine O-palmitoyltransferase activity
Biological Process: fatty acid beta-oxidation; cellular lipid metabolic process; carnitine shuttle
Reference #:  P23786 (UniProtKB)
Alt. Names/Synonyms: Carnitine O-palmitoyltransferase 2, mitochondrial; carnitine palmitoyltransferase 2; Carnitine palmitoyltransferase II; CPT II; CPT1; CPT2; CPTASE
Gene Symbols: CPT2
Molecular weight: 73,777 Da
Basal Isoelectric point: 8.38  Predict pI for various phosphorylation states
Select Structure to View Below

CPT2

Protein Structure Not Found.


STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 4 R62 PKLEDTIRRYLSAQk
0 19 K69-ac RRYLSAQkPLLNDGQ
0 1 K69-sc RRYLSAQkPLLNDGQ
0 1 G75 QkPLLNDGQFRKTEQ
0 1 K79 LNDGQFRKTEQFCKS
0 1 K104 EQLVALDKQNKHTSY
0 1 S126-p MYLSARDsVVLNFNP
0 1 K142 MAFNPDPKSEYNDQL
0 1 K142 MAFNPDPKSEYNDQL
0 1 Y217-p YPLDMSQyFRLFNst
0 1 S223-p QyFRLFNstRLPKPS
0 1 T224-p yFRLFNstRLPKPSR
0 6 K239 DELFTDDKARHLLVL
0 1 K239 DELFTDDKARHLLVL
0 1 Y290-p APEFPLAyLTSENRD
0 1 K305 IWAELRQKLMSSGNE
0 2 K305 IWAELRQKLMSSGNE
0 1 K414 DSTVTVQKLNFELTD
0 1 K414 DSTVTVQKLNFELTD
0 1 E418 TVQKLNFELTDALKT
0 2 E418 TVQKLNFELTDALKT
0 1 T420 QKLNFELTDALKTGI
0 2 K424 FELTDALKTGITAAK
0 1 K439 EKFDATMKTLTIDCV
0 1 K453-sc VQFQRGGkEFLKKQK
0 4 K457 RGGkEFLKKQKLSPD
0 1 S490-p VATYESCstAAFKHG
0 1 T491-p ATYESCstAAFKHGR
0 1 Y508-p TIRPASVyTkRCSEA
0 2 K510-ac RPASVyTkRCSEAFV
0 4 K544-ac KYHGQLTkEAAMGQG
0 1 K544-sc KYHGQLTkEAAMGQG
  mouse

 
K62-ac PKLEDTMkRYLSAQk
K69-ac kRYLSAQkPLLNDsQ
K69-sc kRYLSAQkPLLNDsQ
S75-p QkPLLNDsQFRkTEV
K79-sc LNDsQFRkTEVLCKD
K104-ac AHLLAQDkQNKHTSY
S126 MYLTARDSVVLNFNP
K142-ac MAFNPDPkSEYNDQL
K142-sc MAFNPDPkSEYNDQL
Y217 YPLDMSQYFRLFNST
S223 QYFRLFNSTRIPKPS
T224 YFRLFNSTRIPKPSR
K239-ac DELFTDTkARHLLVL
K239-sc DELFTDTkARHLLVL
Y290 VPEFPLAYLTSENRD
K305-ac VWAELRQkLIHGGNE
K305-sc VWAELRQkLIHGGNE
K414-ac DSSVSVQkLSFkLsS
K414-sc DSSVSVQkLSFkLsS
K418-ac SVQkLSFkLsSALkA
K418-sc SVQkLSFkLsSALkA
S420-p QkLSFkLsSALkAGV
K424-sc FkLsSALkAGVTAAK
K439-sc EKFDATMkTLTIDAI
K453 IQFQRGGKEFLkKKK
K457-ac RGGKEFLkKKKLSPD
S490 VATYESCSTAAFKHG
T491 ATYESCSTAAFKHGR
F508 TIRPASIFTKRCSEA
K510 RPASIFTKRCSEAFV
K544-ac KYHGQLTkEAAMGQG
K544-sc KYHGQLTkEAAMGQG
  rat

 
K62 PKLEDTMKRYLNAQK
K69 KRYLNAQKPLLDDSQ
K69 KRYLNAQKPLLDDSQ
S75 QKPLLDDSQFRRTEA
R79 LDDSQFRRTEALCKN
K104 AHLLAQDKQNKHTSY
S126 MYLTARDSIVLNFNP
K142 MAFNPDPKSEYNDQL
K142 MAFNPDPKSEYNDQL
Y217 YPLDMSQYFRLFNST
S223 QYFRLFNSTRIPRPN
T224 YFRLFNSTRIPRPNR
K239 DELFTDTKARHLLVL
K239 DELFTDTKARHLLVL
Y290 VPEFPVAYLTSENRD
K305 VWAELRQKLIFDGNE
K305 VWAELRQKLIFDGNE
T414 NSSASVETLSFNLSG
T414 NSSASVETLSFNLSG
N418 SVETLSFNLSGALKA
N418 SVETLSFNLSGALKA
S420 ETLSFNLSGALKAGI
K424 FNLSGALKAGITAAK
K439 EKFDTTVKTLSIDSI
K453 IQFQRGGKEFLKKKQ
K457 RGGKEFLKKKQLSPD
S490 VATYESCSTAAFKHG
T491 ATYESCSTAAFKHGR
F508 TIRPASIFTKRCSEA
K510 RPASIFTKRCSEAFV
K544 KYHGQLTKEAAMGQG
K544 KYHGQLTKEAAMGQG
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.