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Q9BV57

- MTND_HUMAN

UniProt

Q9BV57 - MTND_HUMAN

Protein

1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase

Gene

ADI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). Also down-regulates cell migration mediated by MMP14. Necessary for hepatitis C virus replication in an otherwise non-permissive cell line.2 PublicationsUniRule annotation

    Catalytic activityi

    1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate.1 PublicationUniRule annotation

    Cofactori

    Binds 1 iron ion per monomer. Can also use other divalent metal cations.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi88 – 881Iron or nickelUniRule annotation
    Metal bindingi90 – 901Iron or nickelUniRule annotation
    Metal bindingi94 – 941Iron or nickelUniRule annotation
    Metal bindingi133 – 1331Iron or nickelUniRule annotation

    GO - Molecular functioni

    1. acireductone dioxygenase [iron(II)-requiring] activity Source: Reactome
    2. iron ion binding Source: UniProtKB-HAMAP
    3. oxidoreductase activity Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB
    3. polyamine metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. sulfur amino acid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_75881. Methionine salvage pathway.
    UniPathwayiUPA00904; UER00878.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenaseUniRule annotation (EC:1.13.11.54UniRule annotation)
    Alternative name(s):
    Acireductone dioxygenase (Fe(2+)-requiring)UniRule annotation
    Short name:
    ARDUniRule annotation
    Short name:
    Fe-ARDUniRule annotation
    Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1UniRule annotation
    Short name:
    MTCBP-1UniRule annotation
    Submergence-induced protein-like factor
    Short name:
    Sip-L
    Gene namesi
    Name:ADI1UniRule annotation
    Synonyms:MTCBP1UniRule annotation
    ORF Names:HMFT1638
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:30576. ADI1.

    Subcellular locationi

    Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Localizes to the plasma membrane when complexed to MMP14.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. Golgi apparatus Source: HPA
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi94 – 941E → A: Loss of aci-reductone dioxygenase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA143485291.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1791791,2-dihydroxy-3-keto-5-methylthiopentene dioxygenasePRO_0000162942Add
    BLAST

    Proteomic databases

    MaxQBiQ9BV57.
    PaxDbiQ9BV57.
    PRIDEiQ9BV57.

    PTM databases

    PhosphoSiteiQ9BV57.

    Expressioni

    Tissue specificityi

    Detected in heart, colon, lung, stomach, brain, spleen, liver, skeletal muscle and kidney.2 Publications

    Gene expression databases

    BgeeiQ9BV57.
    CleanExiHS_ADI1.
    GenevestigatoriQ9BV57.

    Organism-specific databases

    HPAiHPA035403.

    Interactioni

    Subunit structurei

    Monomer By similarity. Interacts with MMP14.1 PublicationUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MMP14P502814EBI-992807,EBI-992788

    Protein-protein interaction databases

    BioGridi120547. 6 interactions.
    IntActiQ9BV57. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BV57.
    SMRiQ9BV57. Positions 1-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acireductone dioxygenase (ARD) family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1791.
    HOVERGENiHBG081992.
    InParanoidiQ9BV57.
    KOiK08967.
    OMAiTTDESNY.
    OrthoDBiEOG73FQP0.
    PhylomeDBiQ9BV57.
    TreeFamiTF300231.

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    HAMAPiMF_03154. Salvage_MtnD_euk.
    InterProiIPR004313. Acireductn_dOase_family.
    IPR027496. MTCBP-1_eukaryotes.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PANTHERiPTHR23418. PTHR23418. 1 hit.
    PfamiPF03079. ARD. 1 hit.
    [Graphical view]
    SUPFAMiSSF51182. SSF51182. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BV57-1) [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

    MVQAWYMDDA PGDPRQPHRP DPGRPVGLEQ LRRLGVLYWK LDADKYENDP    50
    ELEKIRRERN YSWMDIITIC KDKLPNYEEK IKMFYEEHLH LDDEIRYILD 100
    GSGYFDVRDK EDQWIRIFME KGDMVTLPAG IYHRFTVDEK NYTKAMRLFV 150
    GEPVWTAYNR PADHFEARGQ YVKFLAQTA 179
    Length:179
    Mass (Da):21,498
    Last modified:June 1, 2001 - v1
    Checksum:i92E13B9718D44C27
    GO
    Isoform 2 (identifier: Q9BV57-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: MVQAWYMDDAPGDPRQPHRPDPGRPVGLEQLRRLGVLYWK → MSVKSSKLMFLCHGSSRSLHSGSLTSCNTGVCCS

    Note: No experimental confirmation available.

    Show »
    Length:173
    Mass (Da):20,332
    Checksum:i5AE5570210391A36
    GO

    Sequence cautioni

    The sequence AAL25800.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD38646.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAD96187.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31Q → L in BAA91901. (PubMed:14702039)Curated
    Sequence conflicti108 – 1081R → G in BAD96187. 1 PublicationCurated
    Sequence conflicti170 – 1701Q → K in AAP97173. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4040MVQAW…VLYWK → MSVKSSKLMFLCHGSSRSLH SGSLTSCNTGVCCS in isoform 2. 1 PublicationVSP_015822Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB158319 mRNA. Translation: BAD10866.1.
    AF087863 mRNA. Translation: AAP97173.1.
    AB073609 mRNA. Translation: BAD38646.1. Different initiation.
    AK001775 mRNA. Translation: BAA91901.1.
    AK127473 mRNA. Translation: BAC86996.1.
    AK222467 mRNA. Translation: BAD96187.1. Different initiation.
    AC142528 Genomic DNA. Translation: AAX82038.1.
    AC114810 Genomic DNA. Translation: AAY24022.1.
    CH471053 Genomic DNA. Translation: EAX01064.1.
    CH471053 Genomic DNA. Translation: EAX01065.1.
    BC001467 mRNA. Translation: AAH01467.1.
    AF403478 mRNA. Translation: AAL25800.1. Different initiation.
    CCDSiCCDS1653.1. [Q9BV57-1]
    RefSeqiNP_060739.2. NM_018269.3. [Q9BV57-1]
    XP_005264753.1. XM_005264696.1. [Q9BV57-2]
    UniGeneiHs.502773.

    Genome annotation databases

    EnsembliENST00000327435; ENSP00000333666; ENSG00000182551. [Q9BV57-1]
    ENST00000382093; ENSP00000371525; ENSG00000182551. [Q9BV57-2]
    GeneIDi55256.
    KEGGihsa:55256.
    UCSCiuc002qxp.4. human. [Q9BV57-1]

    Polymorphism databases

    DMDMi74733289.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB158319 mRNA. Translation: BAD10866.1 .
    AF087863 mRNA. Translation: AAP97173.1 .
    AB073609 mRNA. Translation: BAD38646.1 . Different initiation.
    AK001775 mRNA. Translation: BAA91901.1 .
    AK127473 mRNA. Translation: BAC86996.1 .
    AK222467 mRNA. Translation: BAD96187.1 . Different initiation.
    AC142528 Genomic DNA. Translation: AAX82038.1 .
    AC114810 Genomic DNA. Translation: AAY24022.1 .
    CH471053 Genomic DNA. Translation: EAX01064.1 .
    CH471053 Genomic DNA. Translation: EAX01065.1 .
    BC001467 mRNA. Translation: AAH01467.1 .
    AF403478 mRNA. Translation: AAL25800.1 . Different initiation.
    CCDSi CCDS1653.1. [Q9BV57-1 ]
    RefSeqi NP_060739.2. NM_018269.3. [Q9BV57-1 ]
    XP_005264753.1. XM_005264696.1. [Q9BV57-2 ]
    UniGenei Hs.502773.

    3D structure databases

    ProteinModelPortali Q9BV57.
    SMRi Q9BV57. Positions 1-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120547. 6 interactions.
    IntActi Q9BV57. 2 interactions.

    PTM databases

    PhosphoSitei Q9BV57.

    Polymorphism databases

    DMDMi 74733289.

    Proteomic databases

    MaxQBi Q9BV57.
    PaxDbi Q9BV57.
    PRIDEi Q9BV57.

    Protocols and materials databases

    DNASUi 55256.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327435 ; ENSP00000333666 ; ENSG00000182551 . [Q9BV57-1 ]
    ENST00000382093 ; ENSP00000371525 ; ENSG00000182551 . [Q9BV57-2 ]
    GeneIDi 55256.
    KEGGi hsa:55256.
    UCSCi uc002qxp.4. human. [Q9BV57-1 ]

    Organism-specific databases

    CTDi 55256.
    GeneCardsi GC02M003501.
    HGNCi HGNC:30576. ADI1.
    HPAi HPA035403.
    MIMi 613400. gene.
    neXtProti NX_Q9BV57.
    PharmGKBi PA143485291.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1791.
    HOVERGENi HBG081992.
    InParanoidi Q9BV57.
    KOi K08967.
    OMAi TTDESNY.
    OrthoDBi EOG73FQP0.
    PhylomeDBi Q9BV57.
    TreeFami TF300231.

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00878 .
    Reactomei REACT_75881. Methionine salvage pathway.

    Miscellaneous databases

    ChiTaRSi ADI1. human.
    GeneWikii ADI1.
    GenomeRNAii 55256.
    NextBioi 59336.
    PROi Q9BV57.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BV57.
    CleanExi HS_ADI1.
    Genevestigatori Q9BV57.

    Family and domain databases

    Gene3Di 2.60.120.10. 1 hit.
    HAMAPi MF_03154. Salvage_MtnD_euk.
    InterProi IPR004313. Acireductn_dOase_family.
    IPR027496. MTCBP-1_eukaryotes.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    PANTHERi PTHR23418. PTHR23418. 1 hit.
    Pfami PF03079. ARD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51182. SSF51182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumors."
      Uekita T., Gotoh I., Kinoshita T., Itoh Y., Sato H., Shiomi T., Okada Y., Seiki M.
      J. Biol. Chem. 279:12734-12743(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MMP14, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Fibroblast.
    2. "Cloning and expression of a new human cDNA homologous to O.sativa submergence induced protein 2 (sip2) mRNA."
      Fan Y.X., Yu L., Ding J.B., Hu P.R., Fu S.N., Zhao S.Y.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
      Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
      Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hepatoblastoma.
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Ovarian carcinoma and Thalamus.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adipose tissue.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Placenta.
    9. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
      Xu G., Shin S.B., Jaffrey S.R.
      Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-30.
      Tissue: Leukemic T-cell.
    10. "Identification of a hepatic factor capable of supporting hepatitis C virus replication in a nonpermissive cell line."
      Yeh C.-T., Lai H.-Y., Chen T.-C., Chu C.-M., Liaw Y.-F.
      J. Virol. 75:11017-11024(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-179, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Liver.
    11. "Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway."
      Hirano W., Gotoh I., Uekita T., Seiki M.
      Genes Cells 10:565-574(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-94.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMTND_HUMAN
    AccessioniPrimary (citable) accession number: Q9BV57
    Secondary accession number(s): D6W4Y3
    , Q53HW3, Q53QD3, Q57YV7, Q68CK2, Q6ZSF7, Q7Z512, Q96P85, Q9NV57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 122 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 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3