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Q9HCC0

- MCCB_HUMAN

UniProt

Q9HCC0 - MCCB_HUMAN

Protein

Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

Gene

MCCC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism.1 Publication

    Catalytic activityi

    ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA.1 Publication

    Kineticsi

    kcat is 4.0 sec(-1).

    1. KM=45 µM for ATP1 Publication
    2. KM=74 µM for 3-methylcrotonyl-CoA1 Publication

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. methylcrotonoyl-CoA carboxylase activity Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. biotin metabolic process Source: Reactome
    2. branched-chain amino acid catabolic process Source: Reactome
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. coenzyme A metabolic process Source: Ensembl
    5. leucine catabolic process Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. vitamin metabolic process Source: Reactome
    8. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000131844-MONOMER.
    ReactomeiREACT_11153. Biotin transport and metabolism.
    REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
    REACT_197. Branched-chain amino acid catabolism.
    UniPathwayiUPA00363; UER00861.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (EC:6.4.1.4)
    Short name:
    MCCase subunit beta
    Alternative name(s):
    3-methylcrotonyl-CoA carboxylase 2
    3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit
    3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
    Gene namesi
    Name:MCCC2
    Synonyms:MCCB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6937. MCCC2.

    Subcellular locationi

    Mitochondrion matrix 2 Publications

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Methylcrotonoyl-CoA carboxylase 2 deficiency (MCC2D) [MIM:210210]: An autosomal recessive disorder of leucine catabolism. The phenotype is variable, ranging from neonatal onset with severe neurological involvement to asymptomatic adults. There is a characteristic organic aciduria with massive excretion of 3-hydroxyisovaleric acid and 3-methylcrotonylglycine, usually in combination with a severe secondary carnitine deficiency.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991E → Q in MCC2D; severe and mild form. 1 Publication
    Corresponds to variant rs28934883 [ dbSNP | Ensembl ].
    VAR_012792
    Natural varianti155 – 1551R → Q in MCC2D; mild form. 1 Publication
    VAR_012793
    Natural varianti167 – 1671C → R in MCC2D. 1 Publication
    Corresponds to variant rs28934884 [ dbSNP | Ensembl ].
    VAR_012794
    Natural varianti173 – 1731S → L in MCC2D; severe form. 1 Publication
    VAR_012795
    Natural varianti193 – 1931R → C in MCC2D; mild form. 1 Publication
    VAR_012796
    Natural varianti218 – 2181A → T in MCC2D. 1 Publication
    VAR_012797
    Natural varianti268 – 2681R → T in MCC2D; asymptomatic form. 1 Publication
    VAR_012798
    Natural varianti280 – 2801D → Y in MCC2D. 1 Publication
    Corresponds to variant rs119103226 [ dbSNP | Ensembl ].
    VAR_067199
    Natural varianti310 – 3101P → R in MCC2D; mild form. 1 Publication
    VAR_012799
    Natural varianti339 – 3391V → M in MCC2D; severe form. 1 Publication
    VAR_012800
    Natural varianti437 – 4371I → V in MCC2D; mild form.
    VAR_012801
    Natural varianti459 – 4591P → S in MCC2D. 1 Publication
    VAR_067200

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi210210. phenotype.
    Orphaneti6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
    PharmGKBiPA30681.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2222Mitochondrion1 PublicationAdd
    BLAST
    Chaini23 – 563541Methylcrotonoyl-CoA carboxylase beta chain, mitochondrialPRO_0000000291Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701N6-acetyllysine; alternateBy similarity
    Modified residuei70 – 701N6-succinyllysine; alternateBy similarity
    Modified residuei141 – 1411N6-succinyllysineBy similarity
    Modified residuei495 – 4951N6-acetyllysine; alternateBy similarity
    Modified residuei495 – 4951N6-succinyllysine; alternateBy similarity
    Modified residuei511 – 5111N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9HCC0.
    PaxDbiQ9HCC0.
    PRIDEiQ9HCC0.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00784044.

    PTM databases

    PhosphoSiteiQ9HCC0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HCC0.
    BgeeiQ9HCC0.
    CleanExiHS_MCCC2.
    GenevestigatoriQ9HCC0.

    Organism-specific databases

    HPAiHPA038300.
    HPA038301.

    Interactioni

    Subunit structurei

    Probably a dodecamer composed of six biotin-containing alpha subunits (MCCC1) and six beta (MCCC2) subunits.

    Protein-protein interaction databases

    BioGridi122050. 18 interactions.
    IntActiQ9HCC0. 12 interactions.
    MINTiMINT-8051924.
    STRINGi9606.ENSP00000343657.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HCC0.
    SMRiQ9HCC0. Positions 28-563.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 557503CarboxyltransferaseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni343 – 37230Acyl-CoA bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AccD/PCCB family.Curated
    Contains 1 carboxyltransferase domain.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG4799.
    HOGENOMiHOG000218692.
    HOVERGENiHBG052424.
    InParanoidiQ9HCC0.
    KOiK01969.
    OMAiYSSARCW.
    PhylomeDBiQ9HCC0.
    TreeFamiTF300446.

    Family and domain databases

    Gene3Di3.90.226.10. 2 hits.
    InterProiIPR000022. Carboxyl_trans.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    [Graphical view]
    PfamiPF01039. Carboxyl_trans. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 2 hits.
    PROSITEiPS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HCC0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MWAVLRLALR PCARASPAGP RAYHGDSVAS LGTQPDLGSA LYQENYKQMK    50
    ALVNQLHERV EHIKLGGGEK ARALHISRGK LLPRERIDNL IDPGSPFLEL 100
    SQFAGYQLYD NEEVPGGGII TGIGRVSGVE CMIIANDATV KGGAYYPVTV 150
    KKQLRAQEIA MQNRLPCIYL VDSGGAYLPR QADVFPDRDH FGRTFYNQAI 200
    MSSKNIAQIA VVMGSCTAGG AYVPAMADEN IIVRKQGTIF LAGPPLVKAA 250
    TGEEVSAEDL GGADLHCRKS GVSDHWALDD HHALHLTRKV VRNLNYQKKL 300
    DVTIEPSEEP LFPADELYGI VGANLKRSFD VREVIARIVD GSRFTEFKAF 350
    YGDTLVTGFA RIFGYPVGIV GNNGVLFSES AKKGTHFVQL CCQRNIPLLF 400
    LQNITGFMVG REYEAEGIAK DGAKMVAAVA CAQVPKITLI IGGSYGAGNY 450
    GMCGRAYSPR FLYIWPNARI SVMGGEQAAN VLATITKDQR AREGKQFSSA 500
    DEAALKEPII KKFEEEGNPY YSSARVWDDG IIDPADTRLV LGLSFSAALN 550
    APIEKTDFGI FRM 563
    Length:563
    Mass (Da):61,333
    Last modified:March 1, 2001 - v1
    Checksum:i8E3D401AF52DC7D2
    GO
    Isoform 2 (identifier: Q9HCC0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         209-246: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:525
    Mass (Da):57,519
    Checksum:i344050ABB7A9DE8A
    GO

    Sequence cautioni

    The sequence AAH14897.1 differs from that shown. Reason: Frameshift at position 359.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991E → Q in MCC2D; severe and mild form. 1 Publication
    Corresponds to variant rs28934883 [ dbSNP | Ensembl ].
    VAR_012792
    Natural varianti155 – 1551R → Q in MCC2D; mild form. 1 Publication
    VAR_012793
    Natural varianti167 – 1671C → R in MCC2D. 1 Publication
    Corresponds to variant rs28934884 [ dbSNP | Ensembl ].
    VAR_012794
    Natural varianti173 – 1731S → L in MCC2D; severe form. 1 Publication
    VAR_012795
    Natural varianti193 – 1931R → C in MCC2D; mild form. 1 Publication
    VAR_012796
    Natural varianti218 – 2181A → T in MCC2D. 1 Publication
    VAR_012797
    Natural varianti268 – 2681R → T in MCC2D; asymptomatic form. 1 Publication
    VAR_012798
    Natural varianti280 – 2801D → Y in MCC2D. 1 Publication
    Corresponds to variant rs119103226 [ dbSNP | Ensembl ].
    VAR_067199
    Natural varianti310 – 3101P → R in MCC2D; mild form. 1 Publication
    VAR_012799
    Natural varianti339 – 3391V → M in MCC2D; severe form. 1 Publication
    VAR_012800
    Natural varianti437 – 4371I → V in MCC2D; mild form.
    VAR_012801
    Natural varianti459 – 4591P → S in MCC2D. 1 Publication
    VAR_067200
    Natural varianti478 – 4781A → G.
    Corresponds to variant rs35068278 [ dbSNP | Ensembl ].
    VAR_038630

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei209 – 24638Missing in isoform 2. 1 PublicationVSP_000069Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050049 mRNA. Translation: BAB16880.1.
    AB050050 Genomic DNA. Translation: BAB41121.1.
    AF310971 mRNA. Translation: AAG53094.1.
    AF301000 mRNA. Translation: AAK16404.1.
    AF261884 mRNA. Translation: AAK49409.1.
    AC138832 Genomic DNA. No translation available.
    CH471084 Genomic DNA. Translation: EAW95693.1.
    BC014897 mRNA. Translation: AAH14897.1. Frameshift.
    BC065027 mRNA. Translation: AAH65027.1.
    AL079298 mRNA. Translation: CAB45194.1.
    CCDSiCCDS34184.1. [Q9HCC0-1]
    RefSeqiNP_071415.1. NM_022132.4. [Q9HCC0-1]
    XP_005248624.1. XM_005248567.1. [Q9HCC0-2]
    UniGeneiHs.604789.

    Genome annotation databases

    EnsembliENST00000340941; ENSP00000343657; ENSG00000131844. [Q9HCC0-1]
    GeneIDi64087.
    KEGGihsa:64087.
    UCSCiuc003kbs.4. human. [Q9HCC0-1]

    Polymorphism databases

    DMDMi20138731.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050049 mRNA. Translation: BAB16880.1 .
    AB050050 Genomic DNA. Translation: BAB41121.1 .
    AF310971 mRNA. Translation: AAG53094.1 .
    AF301000 mRNA. Translation: AAK16404.1 .
    AF261884 mRNA. Translation: AAK49409.1 .
    AC138832 Genomic DNA. No translation available.
    CH471084 Genomic DNA. Translation: EAW95693.1 .
    BC014897 mRNA. Translation: AAH14897.1 . Frameshift.
    BC065027 mRNA. Translation: AAH65027.1 .
    AL079298 mRNA. Translation: CAB45194.1 .
    CCDSi CCDS34184.1. [Q9HCC0-1 ]
    RefSeqi NP_071415.1. NM_022132.4. [Q9HCC0-1 ]
    XP_005248624.1. XM_005248567.1. [Q9HCC0-2 ]
    UniGenei Hs.604789.

    3D structure databases

    ProteinModelPortali Q9HCC0.
    SMRi Q9HCC0. Positions 28-563.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122050. 18 interactions.
    IntActi Q9HCC0. 12 interactions.
    MINTi MINT-8051924.
    STRINGi 9606.ENSP00000343657.

    Chemistry

    DrugBanki DB00121. Biotin.

    PTM databases

    PhosphoSitei Q9HCC0.

    Polymorphism databases

    DMDMi 20138731.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00784044.

    Proteomic databases

    MaxQBi Q9HCC0.
    PaxDbi Q9HCC0.
    PRIDEi Q9HCC0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340941 ; ENSP00000343657 ; ENSG00000131844 . [Q9HCC0-1 ]
    GeneIDi 64087.
    KEGGi hsa:64087.
    UCSCi uc003kbs.4. human. [Q9HCC0-1 ]

    Organism-specific databases

    CTDi 64087.
    GeneCardsi GC05P070918.
    HGNCi HGNC:6937. MCCC2.
    HPAi HPA038300.
    HPA038301.
    MIMi 210210. phenotype.
    609014. gene.
    neXtProti NX_Q9HCC0.
    Orphaneti 6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
    PharmGKBi PA30681.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4799.
    HOGENOMi HOG000218692.
    HOVERGENi HBG052424.
    InParanoidi Q9HCC0.
    KOi K01969.
    OMAi YSSARCW.
    PhylomeDBi Q9HCC0.
    TreeFami TF300446.

    Enzyme and pathway databases

    UniPathwayi UPA00363 ; UER00861 .
    BioCyci MetaCyc:ENSG00000131844-MONOMER.
    Reactomei REACT_11153. Biotin transport and metabolism.
    REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
    REACT_197. Branched-chain amino acid catabolism.

    Miscellaneous databases

    GenomeRNAii 64087.
    NextBioi 65884.
    PROi Q9HCC0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HCC0.
    Bgeei Q9HCC0.
    CleanExi HS_MCCC2.
    Genevestigatori Q9HCC0.

    Family and domain databases

    Gene3Di 3.90.226.10. 2 hits.
    InterProi IPR000022. Carboxyl_trans.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    [Graphical view ]
    Pfami PF01039. Carboxyl_trans. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52096. SSF52096. 2 hits.
    PROSITEi PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human non-biotin containing subunit gene of 3-methylcrotonyl-CoA carboxylase (MCCB)."
      Fukuda T., Otsuka H., Morishita R., Takemoto Y., Sone M., Nakao M., Abe S., Kondo I.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANTS MCC2D ARG-167 AND THR-218.
    3. "The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency."
      Baumgartner M.R., Almashanu S., Suormala T., Obie C., Cole R.N., Packman S., Baumgartner E.R., Valle D.
      J. Clin. Invest. 107:495-504(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MCC2D GLN-99; GLN-155; LEU-173; CYS-193; ARG-310 AND MET-339.
    4. "Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency."
      Holzinger A., Roeschinger W., Lagler F., Mayerhofer P.U., Lichtner P., Kattenfeld T., Thuy L.P., Nyhan W.L., Koch H.G., Muntau A.C., Roscher A.A.
      Hum. Mol. Genet. 10:1299-1306(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MCC2D THR-268.
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 2).
      Tissue: Testis and Uterus.
    8. Cited for: PROTEIN SEQUENCE OF 23-28, SUBCELLULAR LOCATION.
      Tissue: Kidney.
    9. "Expression, purification, characterization of human 3-methylcrotonyl-CoA carboxylase (MCCC)."
      Chu C.H., Cheng D.
      Protein Expr. Purif. 53:421-427(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    10. The European IMAGE consortium
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 469-563.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Mutational spectrum in eight Korean patients with 3-methylcrotonyl-CoA carboxylase deficiency."
      Cho S.Y., Park H.D., Lee Y.W., Ki C.S., Lee S.Y., Sohn Y.B., Park S.W., Kim S.H., Ji S., Kim S.J., Choi E.W., Kim C.H., Ko A.R., Paik K.H., Lee D.H., Jin D.K.
      Clin. Genet. 81:96-98(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MCC2D TYR-280 AND SER-459.

    Entry informationi

    Entry nameiMCCB_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCC0
    Secondary accession number(s): A6NIY9, Q96C27, Q9Y4L7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 136 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3