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Protein Page:
MMAA (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
MMAA Probable GTPase. May function as chaperone. May be involved in the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis. Defects in MMAA are the cause of methylmalonic aciduria type cblA (MMAA); also known as methylmalonic aciduria type A or vitamin B12-responsive methylmalonicaciduria of cblA complementation type. MMAA is a disorder of methylmalonate and cobalamin metabolism due to defective synthesis of adenosylcobalamin. Inheritance is autosomal recessive. Belongs to the ArgK family. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.-.-; Chaperone
Chromosomal Location of Human Ortholog: 4q31.21
Cellular Component: mitochondrial matrix
Molecular Function: GTP binding; GTPase activity
Biological Process: cellular lipid metabolic process; cobalamin biosynthetic process; cobalamin metabolic process; fatty acid beta-oxidation; short-chain fatty acid catabolic process; vitamin metabolic process; water-soluble vitamin metabolic process
Disease: Methylmalonic Aciduria, Cbla Type
Reference #:  Q8IVH4 (UniProtKB)
Alt. Names/Synonyms: cblA; methylmalonic aciduria (cobalamin deficiency) cblA type; methylmalonic aciduria type A; Methylmalonic aciduria type A protein, mitochondrial; MGC120010; MGC120011; MGC120012; MGC120013; MMAA
Gene Symbols: MMAA
Molecular weight: 46,538 Da
Basal Isoelectric point: 9.37  Predict pI for various phosphorylation states
Select Structure to View Below

MMAA

Protein Structure Not Found.


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Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 S110‑p EAITLVEstHsRKKE
0 1 T111‑p AITLVEstHsRKKEL
0 1 S113‑p TLVEstHsRKKELAQ
0 4 K140 QEQSNKGKPLAFRVG
0 2 K165 TFIEYFGKMLTERGH
0 1 S189‑p SSCTSGGsLLGDKTR
0 2 Y207 LSRDMNAYIRPSPTR
0 1 K323 RSQVWKPKVIRISAR
0 1 S331‑p VIRISARsGEGIsEM
0 1 S336‑p ARsGEGIsEMWDKMK
0 1 S352‑p FQDLMLAsGELTAKR
  mouse

 
S107 EAITLVESTHTRKRE
T108 AITLVESTHTRKREL
T110 TLVESTHTRKRELAQ
K137‑ac QELRNQGkPLTFRVG
K162‑ac TFIECFGkMLTEQGH
S186 SSCTSGGSLLGDKTR
Y204 LSRDMNAYIRPSPTS
K320 RSEVWRPKVIRISAR
S328 VIRISARSGEGITEM
T333 ARSGEGITEMWDTMR
S349 FQHQMLASGELAAKR
  rat

 
S107 EAITLVESTHTRKKE
T108 AITLVESTHTRKKEL
T110 TLVESTHTRKKELAQ
K137‑ac RELQNHGkPFTFRVG
K162 TFIECFGKMLTERGH
S186 SSCTSGGSLLGDKTR
Y204‑p LSRDMNAyIRPSPTS
K320‑ac RSEVWRPkVIRISAR
S328 VIRISARSGEGITEM
T333 ARSGEGITEMWDIMR
S349 FQHRMLASGELAAKR
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