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Protein Page:
SLC25A13 (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
SLC25A13 Catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle. Defects in SLC25A13 are the cause of citrullinemia type 2 (CTLN2). Citrullinemia belongs to the urea cycle disorders. It is an autosomal recessive disease characterized primarily by elevated serum and urine citrulline levels. Ammonia intoxication is another manifestation. CTLN2 is characterized by neuropsychiatric symptoms including abnormal behaviors, loss of memory, seizures and coma. Death can result from brain edema. Onset is sudden and usually between the ages of 20 and 50 years. Defects in SLC25A13 are the cause of neonatal intrahepatic cholestasis due to citrin deficiency (NICCD). NICCD is a form of citrullinemia type 2 with neonatal onset. NICCD is characterized by suppression of the bile flow, hepatic fibrosis, low birth weight, growth retardation, hypoproteinemia, variable liver dysfunction. NICCD is generally not severe and symptoms disappear by one year of age with an appropriate diet. Years or even decades later, however, some individuals develop the characteristic features of citrullinemia type 2 with neuropsychiatric symptoms. Belongs to the mitochondrial carrier family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Transporter; Mitochondrial; Membrane protein, integral; Transporter, SLC family; Membrane protein, multi-pass
Cellular Component: mitochondrion; integral to plasma membrane; mitochondrial inner membrane
Molecular Function: L-aspartate transmembrane transporter activity; transporter activity; calcium ion binding; L-glutamate transmembrane transporter activity
Biological Process: L-glutamate transport; transport; ATP biosynthetic process; cellular respiration; carbohydrate metabolic process; glucose metabolic process; aspartate transport; response to calcium ion; malate-aspartate shuttle; transmembrane transport; gluconeogenesis
Reference #:  Q9UJS0 (UniProtKB)
Alt. Names/Synonyms: ARALAR2; Calcium-binding mitochondrial carrier protein Aralar2; Citrin; CMC2; CTLN2; Mitochondrial aspartate glutamate carrier 2; SLC25A13; Solute carrier family 25 member 13; solute carrier family 25, member 13; solute carrier family 25, member 13 (citrin)
Gene Symbols: SLC25A13
Molecular weight: 74,176 Da
Basal Isoelectric point: 8.79  Predict pI for various phosphorylation states
Select Structure to View Below

SLC25A13

Protein Structure Not Found.


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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 2 R18 RADPAELRTIFLKYA
0 1 R18 RADPAELRTIFLKYA
0 1 R18 RADPAELRTIFLKYA
0 1 K23 ELRTIFLKYASIEKN
0 1 K29 LKYASIEKNGEFFMS
0 1 K29 LKYASIEKNGEFFMS
0 1 S51-p YLNIFGEsQPNPKTV
0 1 K56 GEsQPNPKTVELLSG
0 1 K56 GEsQPNPKTVELLSG
0 1 K104 QLFDKAGKGEVTFED
0 1 K113 EVTFEDVKQVFGQTT
0 2 R177 RDNARTGRVTAIDFR
0 1 S218-p TSHQVSFsyFNGFNS
0 1 Y219-p SHQVSFsyFNGFNSL
0 1 K251 RKDVEVTKEEFVLAA
0 1 K251 RKDVEVTKEEFVLAA
0 1 K251 RKDVEVTKEEFVLAA
0 1 K353 VYPIDLVKTRMQNQR
0 2 K353-ub VYPIDLVkTRMQNQR
0 1 K353 VYPIDLVKTRMQNQR
0 1 K372 FVGELMYKNSFDCFk
0 9 K379-ac KNSFDCFkKVLRYEG
0 2 K379-sc KNSFDCFkKVLRYEG
0 1 K405-ac LLGVAPEkAIkLTVN
0 1 K405 LLGVAPEKAIkLTVN
0 1 K405 LLGVAPEKAIkLTVN
0 2 K408-ub VAPEkAIkLTVNDFV
0 1 K453-m1 TNPLEIVkIRLQVAG
0 5 K484-ac LGFFGIYkGAKACFL
0 2 K484-ub LGFFGIYkGAKACFL
0 2 K484-sc LGFFGIYkGAKACFL
0 1 K576-sc ILREEGPkALWKGAG
0 2 K580 EGPkALWKGAGARVF
0 1 K580 EGPkALWKGAGARVF
0 2 Y657-p IENKFGLyLPLFKPS
0 8 K662 GLyLPLFKPSVstSK
0 2 S664 yLPLFKPSVstSKAI
0 2 S666-p PLFKPSVstSKAIGG
0 1 T667-p LFKPSVstSKAIGGG
  mouse

 
K18-ac RADPAELkAIFLkYA
K18-ub RADPAELkAIFLkYA
K18-sc RADPAELkAIFLkYA
K23-ac ELkAIFLkYASIEkN
K29-ac LkYASIEkNGEFFMS
K29-ub LkYASIEkNGEFFMS
S51-p YLNIFGEsQPNPkTV
K56-ac GEsQPNPkTVELLSG
K56-sc GEsQPNPkTVELLSG
K104-sc QLFDKAGkGEVTFED
K113-ac EVTFEDVkQIFGQTT
K177-sc RDNAKTGkVSAIDFR
S218 RSHQVSFSYFNGFNS
Y219 SHQVSFSYFNGFNSL
K251-ac RKDVEVTkEEFALAA
K251-ub RKDVEVTkEEFALAA
K251-sc RKDVEVTkEEFALAA
K354-ac VYPIDLVkTRMQNQR
K354-ub VYPIDLVkTRMQNQR
K354-sc VYPIDLVkTRMQNQR
K373-sc FVGELMYkNSFDCFk
K380-ac kNSFDCFkKVLRYEG
K380-sc kNSFDCFkKVLRYEG
K406-ac LLGVAPEkAIkLTVN
K406-ub LLGVAPEkAIkLTVN
K406-sc LLGVAPEkAIkLTVN
K409-ub VAPEkAIkLTVNDFV
K454 TNPLEIVKIRLQVAG
K485-ac LGFFGIYkGAKACFL
K485-ub LGFFGIYkGAKACFL
K485-sc LGFFGIYkGAKACFL
K577 ILREEGPKALWkGVA
K581-ac EGPKALWkGVAARVF
K581-sc EGPKALWkGVAARVF
Y658 IENKFGLYLPLFkPs
K663-ac GLYLPLFkPsAsTSK
S665-p YLPLFkPsAsTSKVT
S667-p PLFkPsAsTSKVTAG
T668 LFkPsAsTSKVTAGD
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