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Q8IVH4

- MMAA_HUMAN

UniProt

Q8IVH4 - MMAA_HUMAN

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Protein

Methylmalonic aciduria type A protein, mitochondrial

Gene

MMAA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei292 – 2921GTP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi150 – 1589GTP
Nucleotide bindingi328 – 3303GTP

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. cobalamin biosynthetic process Source: UniProtKB-UniPathway
  3. cobalamin metabolic process Source: Reactome
  4. fatty acid beta-oxidation Source: Reactome
  5. short-chain fatty acid catabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
  7. vitamin metabolic process Source: Reactome
  8. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169313. Defective MUT causes methylmalonic aciduria mut type.
REACT_169316. Defective MMAA causes methylmalonic aciduria type cblA.
REACT_993. Propionyl-CoA catabolism.
UniPathwayiUPA00148.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonic aciduria type A protein, mitochondrial (EC:3.6.-.-)
Gene namesi
Name:MMAA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:18871. MMAA.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Methylmalonic aciduria type cblA (MMAA) [MIM:251100]: A disorder of methylmalonate and cobalamin metabolism due to defective synthesis of adenosylcobalamin.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891L → P in MMAA. 1 Publication
VAR_020835
Natural varianti145 – 1451R → Q in MMAA. 1 Publication
Corresponds to variant rs200577967 [ dbSNP | Ensembl ].
VAR_020836
Natural varianti207 – 2071Y → C in MMAA. 2 Publications
VAR_017202
Natural varianti218 – 2181G → E in MMAA. 1 Publication
VAR_020837
Natural varianti359 – 3591R → G in MMAA. 1 Publication
VAR_038804
Natural varianti359 – 3591R → Q in MMAA. 1 Publication
VAR_020838

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi251100. phenotype.
Orphaneti79310. Vitamin B12-responsive methylmalonic acidemia type cblA.
PharmGKBiPA134912808.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6565MitochondrionSequence AnalysisAdd
BLAST
Chaini66 – 418353Methylmalonic aciduria type A protein, mitochondrialPRO_0000002285Add
BLAST

Proteomic databases

MaxQBiQ8IVH4.
PaxDbiQ8IVH4.
PRIDEiQ8IVH4.

PTM databases

PhosphoSiteiQ8IVH4.

Expressioni

Tissue specificityi

Widely expressed. Highest expression is observed in liver and skeletal muscle.

Gene expression databases

BgeeiQ8IVH4.
CleanExiHS_MMAA.
ExpressionAtlasiQ8IVH4. baseline and differential.
GenevestigatoriQ8IVH4.

Organism-specific databases

HPAiHPA037361.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi127933. 3 interactions.
STRINGi9606.ENSP00000281317.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi80 – 9415
Helixi98 – 10912
Helixi113 – 13523
Turni136 – 1394
Beta strandi144 – 1496
Helixi156 – 16914
Beta strandi174 – 1785
Beta strandi206 – 2094
Helixi224 – 23310
Beta strandi237 – 2426
Helixi250 – 2545
Beta strandi258 – 2647
Beta strandi284 – 2885
Helixi293 – 2953
Helixi296 – 31015
Beta strandi323 – 3264
Turni329 – 3313
Helixi335 – 35218
Helixi354 – 38128
Helixi383 – 39715
Helixi403 – 41513

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WWWX-ray2.64A/B/C/D72-418[»]
ProteinModelPortaliQ8IVH4.
SMRiQ8IVH4. Positions 73-416.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IVH4.

Family & Domainsi

Sequence similaritiesi

Belongs to the ArgK family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1703.
GeneTreeiENSGT00390000009908.
HOVERGENiHBG045588.
InParanoidiQ8IVH4.
KOiK07588.
OMAiWMLLSNG.
OrthoDBiEOG7BCNBZ.
PhylomeDBiQ8IVH4.
TreeFamiTF313243.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR005129. ArgK.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF03308. ArgK. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00750. lao. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8IVH4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPMLLPHPHQ HFLKGLLRAP FRCYHFIFHS STHLGSGIPC AQPFNSLGLH
60 70 80 90 100
CTKWMLLSDG LKRKLCVQTT LKDHTEGLSD KEQRFVDKLY TGLIQGQRAC
110 120 130 140 150
LAEAITLVES THSRKKELAQ VLLQKVLLYH REQEQSNKGK PLAFRVGLSG
160 170 180 190 200
PPGAGKSTFI EYFGKMLTER GHKLSVLAVD PSSCTSGGSL LGDKTRMTEL
210 220 230 240 250
SRDMNAYIRP SPTRGTLGGV TRTTNEAILL CEGAGYDIIL IETVGVGQSE
260 270 280 290 300
FAVADMVDMF VLLLPPAGGD ELQGIKRGII EMADLVAVTK SDGDLIVPAR
310 320 330 340 350
RIQAEYVSAL KLLRKRSQVW KPKVIRISAR SGEGISEMWD KMKDFQDLML
360 370 380 390 400
ASGELTAKRR KQQKVWMWNL IQESVLEHFR THPTVREQIP LLEQKVLIGA
410
LSPGLAADFL LKAFKSRD
Length:418
Mass (Da):46,538
Last modified:March 1, 2003 - v1
Checksum:iAD9EA19DDB8DEEF8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891L → P in MMAA. 1 Publication
VAR_020835
Natural varianti145 – 1451R → Q in MMAA. 1 Publication
Corresponds to variant rs200577967 [ dbSNP | Ensembl ].
VAR_020836
Natural varianti207 – 2071Y → C in MMAA. 2 Publications
VAR_017202
Natural varianti218 – 2181G → E in MMAA. 1 Publication
VAR_020837
Natural varianti359 – 3591R → G in MMAA. 1 Publication
VAR_038804
Natural varianti359 – 3591R → Q in MMAA. 1 Publication
VAR_020838
Natural varianti363 – 3631Q → H.1 Publication
Corresponds to variant rs2270655 [ dbSNP | Ensembl ].
VAR_020423

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF524846
, AF524841, AF524842, AF524843, AF524844, AF524845 Genomic DNA. Translation: AAN77287.1.
AK126662 mRNA. Translation: BAG54352.1.
CH471056 Genomic DNA. Translation: EAX05036.1.
BC101178 mRNA. Translation: AAI01179.1.
BC101179 mRNA. Translation: AAI01180.1.
CCDSiCCDS3766.1.
RefSeqiNP_758454.1. NM_172250.2.
XP_006714181.1. XM_006714118.1.
UniGeneiHs.452864.

Genome annotation databases

EnsembliENST00000281317; ENSP00000281317; ENSG00000151611.
GeneIDi166785.
KEGGihsa:166785.
UCSCiuc003ikh.4. human.

Polymorphism databases

DMDMi38258173.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF524846
, AF524841 , AF524842 , AF524843 , AF524844 , AF524845 Genomic DNA. Translation: AAN77287.1 .
AK126662 mRNA. Translation: BAG54352.1 .
CH471056 Genomic DNA. Translation: EAX05036.1 .
BC101178 mRNA. Translation: AAI01179.1 .
BC101179 mRNA. Translation: AAI01180.1 .
CCDSi CCDS3766.1.
RefSeqi NP_758454.1. NM_172250.2.
XP_006714181.1. XM_006714118.1.
UniGenei Hs.452864.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WWW X-ray 2.64 A/B/C/D 72-418 [» ]
ProteinModelPortali Q8IVH4.
SMRi Q8IVH4. Positions 73-416.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127933. 3 interactions.
STRINGi 9606.ENSP00000281317.

Chemistry

DrugBanki DB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

PTM databases

PhosphoSitei Q8IVH4.

Polymorphism databases

DMDMi 38258173.

Proteomic databases

MaxQBi Q8IVH4.
PaxDbi Q8IVH4.
PRIDEi Q8IVH4.

Protocols and materials databases

DNASUi 166785.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000281317 ; ENSP00000281317 ; ENSG00000151611 .
GeneIDi 166785.
KEGGi hsa:166785.
UCSCi uc003ikh.4. human.

Organism-specific databases

CTDi 166785.
GeneCardsi GC04P146540.
GeneReviewsi MMAA.
HGNCi HGNC:18871. MMAA.
HPAi HPA037361.
MIMi 251100. phenotype.
607481. gene.
neXtProti NX_Q8IVH4.
Orphaneti 79310. Vitamin B12-responsive methylmalonic acidemia type cblA.
PharmGKBi PA134912808.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1703.
GeneTreei ENSGT00390000009908.
HOVERGENi HBG045588.
InParanoidi Q8IVH4.
KOi K07588.
OMAi WMLLSNG.
OrthoDBi EOG7BCNBZ.
PhylomeDBi Q8IVH4.
TreeFami TF313243.

Enzyme and pathway databases

UniPathwayi UPA00148 .
Reactomei REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169313. Defective MUT causes methylmalonic aciduria mut type.
REACT_169316. Defective MMAA causes methylmalonic aciduria type cblA.
REACT_993. Propionyl-CoA catabolism.

Miscellaneous databases

EvolutionaryTracei Q8IVH4.
GeneWikii MMAA.
GenomeRNAii 166785.
NextBioi 88619.
PROi Q8IVH4.
SOURCEi Search...

Gene expression databases

Bgeei Q8IVH4.
CleanExi HS_MMAA.
ExpressionAtlasi Q8IVH4. baseline and differential.
Genevestigatori Q8IVH4.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR005129. ArgK.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF03308. ArgK. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00750. lao. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements."
    Dobson C.M., Wai T., Leclerc D., Wilson A., Wu X., Dore C., Hudson T., Rosenblatt D.S., Gravel R.A.
    Proc. Natl. Acad. Sci. U.S.A. 99:15554-15559(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MMAA CYS-207.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation."
    Froese D.S., Kochan G., Muniz J.R., Wu X., Gileadi C., Ugochukwu E., Krysztofinska E., Gravel R.A., Oppermann U., Yue W.W.
    J. Biol. Chem. 285:38204-38213(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 72-418 IN COMPLEX WITH GDP, SUBUNIT.
  6. "Mutations in the MMAA gene in patients with the cblA disorder of vitamin B(12) metabolism."
    Lerner-Ellis J.P., Dobson C.M., Wai T., Watkins D., Tirone J.C., Leclerc D., Dore C., Lepage P., Gravel R.A., Rosenblatt D.S.
    Hum. Mutat. 24:509-516(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MMAA PRO-89; GLN-145; CYS-207; GLU-218 AND GLN-359, VARIANT HIS-363.
  7. "Mutation analysis of the MMAA and MMAB genes in Japanese patients with vitamin B(12)-responsive methylmalonic acidemia: identification of a prevalent MMAA mutation."
    Yang X., Sakamoto O., Matsubara Y., Kure S., Suzuki Y., Aoki Y., Suzuki Y., Sakura N., Takayanagi M., Iinuma K., Ohura T.
    Mol. Genet. Metab. 82:329-333(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MMAA GLY-359.

Entry informationi

Entry nameiMMAA_HUMAN
AccessioniPrimary (citable) accession number: Q8IVH4
Secondary accession number(s): B3KX40, Q495G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3