UniProtKB/Swiss-Prot P22033: Variant p.Arg532His

Methylmalonyl-CoA mutase, mitochondrial
Gene: MMUT
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Variant information Variant position:

532 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Arginine (R) to Histidine (H) at position 532 (R532H, p.Arg532His). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Change from large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Other resources:

Links to websites of interest for the variant.

Variant rs1141321 [ dbSNP | Ensembl ]

Sequence information Variant position:

532 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

750 The length of the canonical sequence.
Location on the sequence:

NRQIEKLKKIKSSRDQALAE R CLAALTECAASGDGNILALA The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         NRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALA

Mouse                         KKQIEKLKKIKSSRDQALAEQCLSALTQCAASGDGNILALA

Pig                           NKQIEKLKKVNPAGIKLWLERCLTALTACAASGDGNILALA

Bovine                        NKQIEKLKKVKSSRDQALAERCLDALTACAASGDGNILALA

Caenorhabditis elegans        EEQCAKLNHIRATRDAEKAQKALDAITEGAR-GNGNLMELA

Sequence annotation in neighborhood:

The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:

Type: the type of sequence feature.
Positions: endpoints of the sequence feature.
Description: contains additional information about the feature.

Type	Positions	Description
Chain	33 – 750	Methylmalonyl-CoA mutase, mitochondrial
Helix	527 – 543

Literature citations
Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction.
Jansen R.; Kalousek F.; Fenton W.A.; Rosenberg L.E.; Ledley F.D.;
Genomics 4:198-205(1989)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; PROTEIN SEQUENCE OF N-TERMINUS; PARTIAL PROTEIN SEQUENCE; VARIANTS HIS-532 AND VAL-671; Structure of the human methylmalonyl-CoA mutase (MUT) locus.
Nham S.U.; Wilkemeyer M.F.; Ledley F.D.;
Genomics 8:710-716(1990)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS HIS-532 AND VAL-671; VARIANT MMAM THR-505; Clustering of mutations in methylmalonyl CoA mutase associated with mut-methylmalonic acidemia.
Crane A.M.; Ledley F.D.;
Am. J. Hum. Genet. 55:42-50(1994)
Cited for: VARIANTS MMAM CYS-626; GLU-630; ASP-648 AND TRP-694; VARIANT HIS-532; Spectrum of mutations in mut methylmalonic acidemia and identification of a common Hispanic mutation and haplotype.
Worgan L.C.; Niles K.; Tirone J.C.; Hofmann A.; Verner A.; Sammak A.; Kucic T.; Lepage P.; Rosenblatt D.S.;
Hum. Mutat. 27:31-43(2006)
Cited for: VARIANTS MMAM LEU-86; GLU-87; HIS-93; ARG-94; VAL-94; ARG-95; ARG-105; CYS-108; GLY-108; HIS-108; SER-145; SER-174; VAL-186; LYS-189; GLU-191; GLU-197; ARG-203; CYS-215; SER-215; HIS-218; TYR-219; GLN-228; ILE-230; ASN-231; ASN-262; TYR-265; SER-281; GLU-291; SER-305; PHE-306; VAL-312; CYS-316; THR-324; LEU-346 DEL; ARG-347; TYR-350; CYS-369; HIS-369; PRO-370; GLU-377; HIS-383; PRO-383; ARG-386; ASN-386; HIS-388; SER-389 DEL; ILE-412 DEL; ARG-426; ASP-427; PRO-518; TYR-560; ARG-566; SER-573; ARG-615; CYS-616; ARG-623; GLU-630; GLY-633; ARG-637; ARG-642; ARG-678; ARG-685; TRP-694; LYS-700; ARG-703 AND VAL-717; VARIANTS VAL-69; THR-499; HIS-532 AND VAL-671; Microarray based mutational analysis of patients with methylmalonic acidemia: identification of 10 no vel mutations.
Duendar H.; Oezguel R.K.; Guezel-Ozantuerk A.; Dursun A.; Sivri S.; Aliefendioglu D.; Coskun T.; Tokatli A.;
Mol. Genet. Metab. 106:419-423(2012)
Cited for: VARIANTS MMAM GLY-137; TYR-219; SER-305; PHE-328; ILE-387; GLU-454; GLU-514; LEU-615; THR-615; VAL-625 AND PHE-674; VARIANTS THR-499; HIS-532 AND VAL-671;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.