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Protein

Nicotinamide riboside kinase 1

Gene

NMRK1

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

Functioni

Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). The enzyme also phosphorylates the antitumor drugs tiazofurin and 3-deazaguanosine.1 Publication

Catalytic activityi

ATP + 1-(beta-D-ribofuranosyl)-nicotinamide = ADP + beta-nicotinamide D-ribonucleotide.2 Publications
ATP + beta-D-ribosylnicotinate = ADP + nicotinate beta-D-ribonucleotide.2 Publications

Kineticsi

  1. KM=0.088 mM for nicotinamide riboside (with ATP as cosubstrate)2 Publications
  2. KM=0.068 mM for nicotinamide riboside (with GTP as cosubstrate)2 Publications
  3. KM=0.27 mM for tiazofurin (with ATP as cosubstrate)2 Publications
  4. KM=0.051 mM for nicotinic acid riboside (with ATP as cosubstrate)2 Publications
  5. KM=17 mM for uridine (with ATP as cosubstrate)2 Publications

    pH dependencei

    Optimum pH is 6.5-9.2 Publications

    Pathwayi: NAD(+) biosynthesis

    This protein is involved in the pathway NAD(+) biosynthesis, which is part of Cofactor biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi17 – 171MagnesiumCombined sources1 Publication
    Active sitei36 – 361Proton acceptorCombined sources1 Publication
    Metal bindingi36 – 361MagnesiumCombined sources1 Publication
    Binding sitei128 – 1281ATPCombined sources1 Publication
    Binding sitei129 – 1291SubstrateCombined sources1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 189ATPCombined sources2 Publications
    Nucleotide bindingi132 – 1343ATPCombined sources2 Publications
    Nucleotide bindingi172 – 1743ATPCombined sources1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.173. 2681.
    UniPathwayiUPA00253.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nicotinamide riboside kinase 1 (EC:2.7.1.222 Publications)
    Short name:
    NRK 1
    Short name:
    NmR-K 1
    Alternative name(s):
    Nicotinic acid riboside kinase 1 (EC:2.7.1.1732 Publications)
    Ribosylnicotinamide kinase 1
    Short name:
    RNK 1
    Ribosylnicotinic acid kinase 1
    Gene namesi
    Name:NMRK1
    Synonyms:C9orf95, NRK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:26057. NMRK1.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161K → A: Loss of activity. 1 Publication
    Mutagenesisi36 – 361D → A: Loss of activity. 2 Publications
    Mutagenesisi56 – 561D → A: Loss of activity. 1 Publication
    Mutagenesisi98 – 981E → A: Loss of activity. 1 Publication
    Mutagenesisi138 – 1381D → A: Almost no effect. 1 Publication

    Organism-specific databases

    PharmGKBiPA134946592.

    Polymorphism and mutation databases

    BioMutaiNMRK1.
    DMDMi50401180.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 199199Nicotinamide riboside kinase 1PRO_0000215891Add
    BLAST

    Proteomic databases

    EPDiQ9NWW6.
    MaxQBiQ9NWW6.
    PaxDbiQ9NWW6.
    PRIDEiQ9NWW6.

    PTM databases

    iPTMnetiQ9NWW6.
    PhosphoSiteiQ9NWW6.

    Expressioni

    Gene expression databases

    BgeeiQ9NWW6.
    CleanExiHS_C9orf95.
    ExpressionAtlasiQ9NWW6. baseline and differential.
    GenevisibleiQ9NWW6. HS.

    Organism-specific databases

    HPAiHPA049795.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TAX1BP1Q86VP13EBI-10315485,EBI-529518

    Protein-protein interaction databases

    BioGridi120317. 2 interactions.
    IntActiQ9NWW6. 1 interaction.
    STRINGi9606.ENSP00000354387.

    Structurei

    Secondary structure

    1
    199
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 118Combined sources
    Helixi16 – 249Combined sources
    Beta strandi30 – 345Combined sources
    Helixi35 – 384Combined sources
    Helixi42 – 443Combined sources
    Helixi58 – 603Combined sources
    Helixi63 – 7715Combined sources
    Beta strandi94 – 985Combined sources
    Helixi106 – 1083Combined sources
    Turni109 – 1113Combined sources
    Beta strandi113 – 1197Combined sources
    Helixi122 – 13110Combined sources
    Helixi142 – 1454Combined sources
    Helixi147 – 15711Combined sources
    Helixi158 – 1603Combined sources
    Beta strandi166 – 1694Combined sources
    Helixi174 – 18512Combined sources
    Turni186 – 1883Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P0EX-ray1.80A2-189[»]
    2QG6X-ray1.50A1-199[»]
    2QL6X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-199[»]
    2QSYX-ray1.95A2-189[»]
    2QSZX-ray1.90A2-189[»]
    2QT0X-ray1.92A2-189[»]
    2QT1X-ray1.32A2-189[»]
    ProteinModelPortaliQ9NWW6.
    SMRiQ9NWW6. Positions 2-189.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NWW6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni36 – 394Substrate bindingCombined sources2 Publications
    Regioni55 – 562Substrate bindingCombined sources2 Publications
    Regioni134 – 1352Substrate bindingCombined sources2 Publications

    Sequence similaritiesi

    Belongs to the uridine kinase family. NRK subfamily.Curated

    Phylogenomic databases

    eggNOGiKOG3308. Eukaryota.
    COG0572. LUCA.
    GeneTreeiENSGT00510000046782.
    HOGENOMiHOG000043899.
    HOVERGENiHBG052669.
    InParanoidiQ9NWW6.
    KOiK10524.
    PhylomeDBiQ9NWW6.
    TreeFamiTF105395.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR000764. Uridine_kinase-like.
    [Graphical view]
    PRINTSiPR00988. URIDINKINASE.
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9NWW6-1) [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

            10         20         30         40         50
    MKTFIIGISG VTNSGKTTLA KNLQKHLPNC SVISQDDFFK PESEIETDKN
    60 70 80 90 100
    GFLQYDVLEA LNMEKMMSAI SCWMESARHS VVSTDQESAE EIPILIIEGF
    110 120 130 140 150
    LLFNYKPLDT IWNRSYFLTI PYEECKRRRS TRVYQPPDSP GYFDGHVWPM
    160 170 180 190
    YLKYRQEMQD ITWEVVYLDG TKSEEDLFLQ VYEDLIQELA KQKCLQVTA
    Length:199
    Mass (Da):23,193
    Last modified:October 1, 2000 - v1
    Checksum:i0A0803461F40EA32
    GO
    Isoform 2 (identifier: Q9NWW6-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         106-130: KPLDTIWNRSYFLTIPYEECKRRRS → N

    Note: No experimental confirmation available.
    Show »
    Length:175
    Mass (Da):20,153
    Checksum:iD197E46A962E45A7
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei106 – 13025KPLDT…KRRRS → N in isoform 2. 1 PublicationVSP_012676Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY611480 mRNA. Translation: AAT11928.1.
    AK000566 mRNA. Translation: BAA91259.1.
    AL133548 Genomic DNA. Translation: CAH71570.1.
    AL133548 Genomic DNA. Translation: CAH71571.1.
    CH471089 Genomic DNA. Translation: EAW62568.1.
    BC001366 mRNA. Translation: AAH01366.1.
    BC036804 mRNA. Translation: AAH36804.1.
    CCDSiCCDS47981.1. [Q9NWW6-2]
    CCDS6650.1. [Q9NWW6-1]
    RefSeqiNP_001121075.1. NM_001127603.1. [Q9NWW6-2]
    NP_060351.1. NM_017881.2. [Q9NWW6-1]
    XP_006717226.1. XM_006717163.2. [Q9NWW6-1]
    UniGeneiHs.494186.

    Genome annotation databases

    EnsembliENST00000361092; ENSP00000354387; ENSG00000106733. [Q9NWW6-1]
    ENST00000376808; ENSP00000366004; ENSG00000106733. [Q9NWW6-2]
    GeneIDi54981.
    KEGGihsa:54981.
    UCSCiuc004ajr.5. human. [Q9NWW6-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY611480 mRNA. Translation: AAT11928.1.
    AK000566 mRNA. Translation: BAA91259.1.
    AL133548 Genomic DNA. Translation: CAH71570.1.
    AL133548 Genomic DNA. Translation: CAH71571.1.
    CH471089 Genomic DNA. Translation: EAW62568.1.
    BC001366 mRNA. Translation: AAH01366.1.
    BC036804 mRNA. Translation: AAH36804.1.
    CCDSiCCDS47981.1. [Q9NWW6-2]
    CCDS6650.1. [Q9NWW6-1]
    RefSeqiNP_001121075.1. NM_001127603.1. [Q9NWW6-2]
    NP_060351.1. NM_017881.2. [Q9NWW6-1]
    XP_006717226.1. XM_006717163.2. [Q9NWW6-1]
    UniGeneiHs.494186.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P0EX-ray1.80A2-189[»]
    2QG6X-ray1.50A1-199[»]
    2QL6X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-199[»]
    2QSYX-ray1.95A2-189[»]
    2QSZX-ray1.90A2-189[»]
    2QT0X-ray1.92A2-189[»]
    2QT1X-ray1.32A2-189[»]
    ProteinModelPortaliQ9NWW6.
    SMRiQ9NWW6. Positions 2-189.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi120317. 2 interactions.
    IntActiQ9NWW6. 1 interaction.
    STRINGi9606.ENSP00000354387.

    PTM databases

    iPTMnetiQ9NWW6.
    PhosphoSiteiQ9NWW6.

    Polymorphism and mutation databases

    BioMutaiNMRK1.
    DMDMi50401180.

    Proteomic databases

    EPDiQ9NWW6.
    MaxQBiQ9NWW6.
    PaxDbiQ9NWW6.
    PRIDEiQ9NWW6.

    Protocols and materials databases

    DNASUi54981.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000361092; ENSP00000354387; ENSG00000106733. [Q9NWW6-1]
    ENST00000376808; ENSP00000366004; ENSG00000106733. [Q9NWW6-2]
    GeneIDi54981.
    KEGGihsa:54981.
    UCSCiuc004ajr.5. human. [Q9NWW6-1]

    Organism-specific databases

    CTDi54981.
    GeneCardsiNMRK1.
    HGNCiHGNC:26057. NMRK1.
    HPAiHPA049795.
    MIMi608704. gene.
    neXtProtiNX_Q9NWW6.
    PharmGKBiPA134946592.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3308. Eukaryota.
    COG0572. LUCA.
    GeneTreeiENSGT00510000046782.
    HOGENOMiHOG000043899.
    HOVERGENiHBG052669.
    InParanoidiQ9NWW6.
    KOiK10524.
    PhylomeDBiQ9NWW6.
    TreeFamiTF105395.

    Enzyme and pathway databases

    UniPathwayiUPA00253.
    BRENDAi2.7.1.173. 2681.

    Miscellaneous databases

    ChiTaRSiNMRK1. human.
    EvolutionaryTraceiQ9NWW6.
    GenomeRNAii54981.
    PROiQ9NWW6.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NWW6.
    CleanExiHS_C9orf95.
    ExpressionAtlasiQ9NWW6. baseline and differential.
    GenevisibleiQ9NWW6. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR000764. Uridine_kinase-like.
    [Graphical view]
    PRINTSiPR00988. URIDINKINASE.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes establish a Preiss-Handler independent route to NAD+ in fungi and humans."
      Bieganowski P., Brenner C.
      Cell 117:495-502(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY.
    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] (ISOFORM 1).
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Colon and Hippocampus.
    6. "Purification and properties of a human nicotinamide ribonucleoside kinase."
      Sasiak K., Saunders P.P.
      Arch. Biochem. Biophys. 333:414-418(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Tissue: Placenta.
    7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 2-189 IN COMPLEXES WITH ATP AND SUBSTRATES, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-36 AND GLU-98.
    9. "Crystal structure of human nicotinamide riboside kinase."
      Khan J.A., Xiang S., Tong L.
      Structure 15:1005-1013(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH NUCLEOSIDE MONOPHOSPHATE; ADP AND TIAZOFURIN, MUTAGENESIS OF LYS-16; ASP-36; ASP-56 AND ASP-138.

    Entry informationi

    Entry nameiNRK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NWW6
    Secondary accession number(s): Q5W124, Q8N430
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 1, 2000
    Last modified: June 8, 2016
    This is version 117 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 9
      Human chromosome 9: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.