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Q9Y4U1

- MMAC_HUMAN

UniProt

Q9Y4U1 - MMAC_HUMAN

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Protein

Methylmalonic aciduria and homocystinuria type C protein

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

Functioni

May be involved in the binding and intracellular trafficking of cobalamin (vitamin B12).

Pathwayi

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW

GO - Biological processi

  1. cobalamin biosynthetic process Source: UniProtKB-UniPathway
  2. cobalamin metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
  4. vitamin metabolic process Source: Reactome
  5. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Cobalamin, Cobalt

Enzyme and pathway databases

ReactomeiREACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169169. Defective MMACHC causes methylmalonic aciduria and homocystinuria type cblC.
REACT_169256. Defective MMADHC causes methylmalonic aciduria and homocystinuria type cblD.
UniPathwayiUPA00148.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonic aciduria and homocystinuria type C protein
Gene namesi
Name:MMACHC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:24525. MMACHC.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Methylmalonic aciduria and homocystinuria type cblC (MMAHCC) [MIM:277400]: A disorder of cobalamin metabolism characterized by decreased levels of the coenzymes adenosylcobalamin (AdoCbl) and methylcobalamin (MeCbl). Affected individuals may have developmental, hematologic, neurologic, metabolic, ophthalmologic, and dermatologic clinical findings. Although considered a disease of infancy or childhood, some individuals develop symptoms in adulthood.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271Q → R in MMAHCC. 1 Publication
VAR_024770
Natural varianti116 – 1161L → P in MMAHCC. 1 Publication
VAR_024771
Natural varianti122 – 1221H → R in MMAHCC. 1 Publication
VAR_024772
Natural varianti130 – 1301Y → H in MMAHCC. 1 Publication
VAR_024773
Natural varianti147 – 1471G → A in MMAHCC. 1 Publication
Corresponds to variant rs140522266 [ dbSNP | Ensembl ].
VAR_024774
Natural varianti147 – 1471G → D in MMAHCC. 1 Publication
VAR_024775
Natural varianti156 – 1561G → D in MMAHCC. 1 Publication
VAR_024776
Natural varianti157 – 1571W → C in MMAHCC. 1 Publication
VAR_024777
Natural varianti161 – 1611R → G in MMAHCC. 1 Publication
VAR_024778
Natural varianti161 – 1611R → Q in MMAHCC. 1 Publication
VAR_024779
Natural varianti189 – 1891R → S in MMAHCC. 1 Publication
VAR_024780
Natural varianti193 – 1931L → P in MMAHCC. 1 Publication
VAR_024781
Natural varianti206 – 2061R → P in MMAHCC. 1 Publication
VAR_024782
Natural varianti206 – 2061R → W in MMAHCC. 1 Publication
VAR_024783

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi277400. phenotype.
603174. phenotype.
Orphaneti79282. Methylmalonic acidemia with homocystinuria, type cblC.
PharmGKBiPA142671348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Methylmalonic aciduria and homocystinuria type C proteinPRO_0000076258Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei245 – 2451Phosphoserine1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication
Modified residuei275 – 2751Phosphoserine2 Publications
Modified residuei279 – 2791Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y4U1.
PaxDbiQ9Y4U1.
PRIDEiQ9Y4U1.

PTM databases

PhosphoSiteiQ9Y4U1.

Expressioni

Tissue specificityi

Widely expressed. Expressed at higher level in fetal liver. Also expressed in spleen, lymph node, thymus and bone marrow. Weakly or not expressed in peripheral blood leukocytes.1 Publication

Gene expression databases

BgeeiQ9Y4U1.
CleanExiHS_MMACHC.
GenevestigatoriQ9Y4U1.

Organism-specific databases

HPAiHPA027394.
HPA027399.
HPA027402.

Interactioni

Protein-protein interaction databases

BioGridi117458. 2 interactions.
STRINGi9606.ENSP00000361154.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614
Helixi17 – 193
Beta strandi21 – 277
Helixi28 – 325
Helixi37 – 393
Beta strandi47 – 548
Helixi58 – 614
Helixi63 – 664
Beta strandi74 – 763
Helixi78 – 9316
Beta strandi100 – 1034
Helixi104 – 1063
Beta strandi113 – 1153
Helixi117 – 1237
Beta strandi126 – 1305
Helixi132 – 1343
Beta strandi135 – 1373
Beta strandi148 – 1514
Turni152 – 1543
Beta strandi159 – 17012
Helixi186 – 19813
Helixi200 – 2023
Helixi204 – 2074
Helixi217 – 2226
Helixi226 – 2294
Turni235 – 2373

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SBYX-ray2.71A/B1-244[»]
3SBZX-ray2.00A1-244[»]
3SC0X-ray1.95A1-238[»]
3SOMX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-282[»]
ProteinModelPortaliQ9Y4U1.
SMRiQ9Y4U1. Positions 2-238.

Miscellaneous databases

EvolutionaryTraceiQ9Y4U1.

Family & Domainsi

Sequence similaritiesi

Belongs to the MMACHC family.

Phylogenomic databases

eggNOGiNOG80998.
HOGENOMiHOG000231413.
HOVERGENiHBG080267.
InParanoidiQ9Y4U1.
KOiK14618.
OMAiWYNELLP.
PhylomeDBiQ9Y4U1.
TreeFamiTF332476.

Sequencei

Sequence statusi: Complete.

Q9Y4U1-1 [UniParc]FASTAAdd to Basket

« Hide

MEPKVAELKQ KIEDTLCPFG FEVYPFQVAW YNELLPPAFH LPLPGPTLAF    50
LVLSTPAMFD RALKPFLQSC HLRMLTDPVD QCVAYHLGRV RESLPELQIE 100
IIADYEVHPN RRPKILAQTA AHVAGAAYYY QRQDVEADPW GNQRISGVCI 150
HPRFGGWFAI RGVVLLPGIE VPDLPPRKPH DCVPTRADRI ALLEGFNFHW 200
RDWTYRDAVT PQERYSEEQK AYFSTPPAQR LALLGLAQPS EKPSSPSPDL 250
PFTTPAPKKP GNPSRARSWL SPRVSPPASP GP 282
Length:282
Mass (Da):31,728
Last modified:January 10, 2006 - v3
Checksum:i3A7E6BC774CB5D17
GO

Sequence cautioni

The sequence AAH06122.3 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271Q → R in MMAHCC. 1 Publication
VAR_024770
Natural varianti116 – 1161L → P in MMAHCC. 1 Publication
VAR_024771
Natural varianti122 – 1221H → R in MMAHCC. 1 Publication
VAR_024772
Natural varianti130 – 1301Y → H in MMAHCC. 1 Publication
VAR_024773
Natural varianti147 – 1471G → A in MMAHCC. 1 Publication
Corresponds to variant rs140522266 [ dbSNP | Ensembl ].
VAR_024774
Natural varianti147 – 1471G → D in MMAHCC. 1 Publication
VAR_024775
Natural varianti156 – 1561G → D in MMAHCC. 1 Publication
VAR_024776
Natural varianti157 – 1571W → C in MMAHCC. 1 Publication
VAR_024777
Natural varianti161 – 1611R → G in MMAHCC. 1 Publication
VAR_024778
Natural varianti161 – 1611R → Q in MMAHCC. 1 Publication
VAR_024779
Natural varianti189 – 1891R → S in MMAHCC. 1 Publication
VAR_024780
Natural varianti193 – 1931L → P in MMAHCC. 1 Publication
VAR_024781
Natural varianti206 – 2061R → P in MMAHCC. 1 Publication
VAR_024782
Natural varianti206 – 2061R → W in MMAHCC. 1 Publication
VAR_024783
Natural varianti271 – 2711S → G.
Corresponds to variant rs35219601 [ dbSNP | Ensembl ].
VAR_038805

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001E → G in CAB45693. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL080062 mRNA. Translation: CAB45693.2.
AL451136 Genomic DNA. Translation: CAI13094.1.
BC006122 mRNA. Translation: AAH06122.3. Different initiation.
CCDSiCCDS41324.1.
PIRiT12462.
RefSeqiNP_056321.2. NM_015506.2.
UniGeneiHs.13024.

Genome annotation databases

EnsembliENST00000401061; ENSP00000383840; ENSG00000132763.
GeneIDi25974.
KEGGihsa:25974.
UCSCiuc009vxv.3. human.

Polymorphism databases

DMDMi85681045.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL080062 mRNA. Translation: CAB45693.2 .
AL451136 Genomic DNA. Translation: CAI13094.1 .
BC006122 mRNA. Translation: AAH06122.3 . Different initiation.
CCDSi CCDS41324.1.
PIRi T12462.
RefSeqi NP_056321.2. NM_015506.2.
UniGenei Hs.13024.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3SBY X-ray 2.71 A/B 1-244 [» ]
3SBZ X-ray 2.00 A 1-244 [» ]
3SC0 X-ray 1.95 A 1-238 [» ]
3SOM X-ray 2.40 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-282 [» ]
ProteinModelPortali Q9Y4U1.
SMRi Q9Y4U1. Positions 2-238.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117458. 2 interactions.
STRINGi 9606.ENSP00000361154.

Chemistry

DrugBanki DB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

PTM databases

PhosphoSitei Q9Y4U1.

Polymorphism databases

DMDMi 85681045.

Proteomic databases

MaxQBi Q9Y4U1.
PaxDbi Q9Y4U1.
PRIDEi Q9Y4U1.

Protocols and materials databases

DNASUi 25974.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000401061 ; ENSP00000383840 ; ENSG00000132763 .
GeneIDi 25974.
KEGGi hsa:25974.
UCSCi uc009vxv.3. human.

Organism-specific databases

CTDi 25974.
GeneCardsi GC01P045965.
GeneReviewsi MMACHC.
H-InvDB HIX0000532.
HGNCi HGNC:24525. MMACHC.
HPAi HPA027394.
HPA027399.
HPA027402.
MIMi 277400. phenotype.
603174. phenotype.
609831. gene.
neXtProti NX_Q9Y4U1.
Orphaneti 79282. Methylmalonic acidemia with homocystinuria, type cblC.
PharmGKBi PA142671348.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG80998.
HOGENOMi HOG000231413.
HOVERGENi HBG080267.
InParanoidi Q9Y4U1.
KOi K14618.
OMAi WYNELLP.
PhylomeDBi Q9Y4U1.
TreeFami TF332476.

Enzyme and pathway databases

UniPathwayi UPA00148 .
Reactomei REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169169. Defective MMACHC causes methylmalonic aciduria and homocystinuria type cblC.
REACT_169256. Defective MMADHC causes methylmalonic aciduria and homocystinuria type cblD.

Miscellaneous databases

ChiTaRSi MMACHC. human.
EvolutionaryTracei Q9Y4U1.
GeneWikii MMACHC.
GenomeRNAii 25974.
NextBioi 47614.
PROi Q9Y4U1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y4U1.
CleanExi HS_MMACHC.
Genevestigatori Q9Y4U1.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] OF 4-282.
    Tissue: Lung.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-275 AND SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Subcellular location of MMACHC and MMADHC, two human proteins central to intracellular vitamin B(12) metabolism."
    Mah W., Deme J.C., Watkins D., Fung S., Janer A., Shoubridge E.A., Rosenblatt D.S., Coulton J.W.
    Mol. Genet. Metab. 108:112-118(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. Cited for: VARIANTS MMAHCC ARG-27; PRO-116; ARG-122; HIS-130; ASP-147; ALA-147; ASP-156; CYS-157; GLY-161; GLN-161; SER-189; PRO-193; TRP-206 AND PRO-206, TISSUE SPECIFICITY.

Entry informationi

Entry nameiMMAC_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4U1
Secondary accession number(s): Q5T157, Q9BRQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: September 3, 2014
This is version 101 of the entry and version 3 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 1
    Human chromosome 1: 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

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