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Q9CZD0 (MMAC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylmalonic aciduria and homocystinuria type C protein homolog
Gene names
Name:Mmachc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis.

Sequence similarities

Belongs to the MMACHC family.

Sequence caution

The sequence AAH54756.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB25214.1 differs from that shown. Reason: Frameshift at position 13.

The sequence BAC39135.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   LigandCobalamin
Cobalt
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcobalamin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_functioncobalamin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 279279Methylmalonic aciduria and homocystinuria type C protein homolog
PRO_0000076259

Amino acid modifications

Modified residue2471Phosphoserine By similarity
Modified residue2721Phosphoserine By similarity
Modified residue2761Phosphoserine By similarity

Experimental info

Sequence conflict141D → G in BAB28451. Ref.1
Sequence conflict2391P → H in BAB28451. Ref.1
Sequence conflict2561K → T in BAB28451. Ref.1
Sequence conflict2601S → Y in BAB28451. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CZD0 [UniParc].

Last modified January 10, 2006. Version 2.
Checksum: 178FAEB388691B09

FASTA27931,648
        10         20         30         40         50         60 
MEPRVAELKQ KIEDTLCPFG FEVYPFQVAW YNELLPPAFH LPFPGPTLAF LVLSTPAMFD 

        70         80         90        100        110        120 
RALKPFLKSC HFQTLRDPVD QCVSYHLRSV TEKFPEVHME VIADYEVHPN RRPKILAQTA 

       130        140        150        160        170        180 
AHVAGAAYYY QRQDVDADPW GTQHIAGVCI HPRFGGWFAI RGVMLLPGIE VPNLPPRKPP 

       190        200        210        220        230        240 
DCVPTRAGRI TLLEGFNFHW RDWTYRDAVT PEERYSEEQK IYFSTPPAQR LALLGLAQPS 

       250        260        270 
EHPSTTSELP LSLLTKPQNS RRARSWLSPS VSPPVSPGP 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain and Pancreas.
[2]"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].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK007725 mRNA. Translation: BAB25214.1. Frameshift.
AK012761 mRNA. Translation: BAB28451.1.
AK084194 mRNA. Translation: BAC39135.1. Different initiation.
BC054756 mRNA. Translation: AAH54756.1. Different initiation.
RefSeqNP_080238.2. NM_025962.3.
UniGeneMm.252785.

3D structure databases

ProteinModelPortalQ9CZD0.
SMRQ9CZD0. Positions 2-238.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9CZD0.

Proteomic databases

PRIDEQ9CZD0.

Protocols and materials databases

DNASU67096.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030453; ENSMUSP00000030453; ENSMUSG00000028690.
GeneID67096.
KEGGmmu:67096.
UCSCuc008uhe.1. mouse.

Organism-specific databases

CTD25974.
MGIMGI:1914346. Mmachc.

Phylogenomic databases

eggNOGNOG80998.
GeneTreeENSGT00390000003464.
HOGENOMHOG000231413.
HOVERGENHBG080267.
InParanoidQ9CZD0.
KOK14618.
OMAWYNELLP.
OrthoDBEOG786H43.
PhylomeDBQ9CZD0.
TreeFamTF332476.

Enzyme and pathway databases

UniPathwayUPA00148.

Gene expression databases

BgeeQ9CZD0.
GenevestigatorQ9CZD0.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSMMACHC. mouse.
NextBio323562.
PROQ9CZD0.
SOURCESearch...

Entry information

Entry nameMMAC_MOUSE
AccessionPrimary (citable) accession number: Q9CZD0
Secondary accession number(s): Q9D8S7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: April 16, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot