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Q9NRK6

- ABCBA_HUMAN

UniProt

Q9NRK6 - ABCBA_HUMAN

Protein

ATP-binding cassette sub-family B member 10, mitochondrial

Gene

ABCB10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    May mediate critical mitochondrial transport functions related to heme biosynthesis.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi527 – 5348ATP

    GO - Molecular functioni

    1. ATPase activity, coupled to transmembrane movement of substances Source: RefGenome
    2. ATP binding Source: UniProtKB-KW
    3. transporter activity Source: UniProtKB

    GO - Biological processi

    1. transmembrane transport Source: RefGenome
    2. transport Source: UniProtKB

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.6.3.43. 2681.
    ReactomeiREACT_111108. Mitochondrial ABC transporters.

    Protein family/group databases

    TCDBi3.A.1.201.17. the atp-binding cassette (abc) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-binding cassette sub-family B member 10, mitochondrial
    Alternative name(s):
    ATP-binding cassette transporter 10
    Short name:
    ABC transporter 10 protein
    Mitochondrial ATP-binding cassette 2
    Short name:
    M-ABC2
    Gene namesi
    Name:ABCB10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:41. ABCB10.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of mitochondrial membrane Source: UniProtKB
    2. mitochondrial inner membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24385.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 105105Mitochondrion1 PublicationAdd
    BLAST
    Chaini106 – 738633ATP-binding cassette sub-family B member 10, mitochondrialPRO_0000000255Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei265 – 2651N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NRK6.
    PaxDbiQ9NRK6.
    PRIDEiQ9NRK6.

    PTM databases

    PhosphoSiteiQ9NRK6.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in bone marrow, expressed at intermediate to high levels in skeletal muscle, small intestine, thyroid, heart, brain, placenta, liver, pancreas, prostate, testis, ovary, leukocyte, stomach, spinal cord, lymph node, trachea and adrenal gland, and low levels are found in lung, kidney, spleen, thymus and colon.

    Gene expression databases

    ArrayExpressiQ9NRK6.
    BgeeiQ9NRK6.
    CleanExiHS_ABCB10.
    GenevestigatoriQ9NRK6.

    Organism-specific databases

    HPAiCAB044063.
    CAB044065.

    Interactioni

    Subunit structurei

    Homodimer or homooligomer.2 Publications

    Protein-protein interaction databases

    BioGridi117020. 9 interactions.
    IntActiQ9NRK6. 1 interaction.
    STRINGi9606.ENSP00000355637.

    Structurei

    Secondary structure

    1
    738
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi154 – 16411
    Helixi165 – 1673
    Helixi168 – 18518
    Helixi188 – 20114
    Helixi208 – 25548
    Helixi260 – 2656
    Helixi268 – 28518
    Helixi288 – 31023
    Helixi312 – 35948
    Helixi361 – 3666
    Helixi370 – 42253
    Helixi428 – 46942
    Turni485 – 4873
    Beta strandi492 – 4998
    Beta strandi502 – 5043
    Beta strandi509 – 5179
    Beta strandi522 – 5265
    Helixi530 – 54011
    Beta strandi547 – 5537
    Helixi558 – 5603
    Helixi563 – 5686
    Beta strandi569 – 5735
    Beta strandi581 – 5833
    Helixi584 – 5896
    Beta strandi592 – 5943
    Turni595 – 5973
    Helixi600 – 60910
    Helixi613 – 6175
    Beta strandi619 – 6213
    Helixi622 – 6243
    Beta strandi628 – 6314
    Helixi636 – 65015
    Beta strandi653 – 6586
    Helixi666 – 68015
    Beta strandi683 – 6886
    Helixi692 – 6976
    Beta strandi698 – 7047
    Beta strandi706 – 7138
    Helixi715 – 7195

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZDQX-ray2.85A152-738[»]
    4AYTX-ray2.85A152-738[»]
    4AYWX-ray3.30A1-738[»]
    4AYXX-ray2.90A152-738[»]
    ProteinModelPortaliQ9NRK6.
    SMRiQ9NRK6. Positions 153-722.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini106 – 17065Mitochondrial intermembraneSequence AnalysisAdd
    BLAST
    Topological domaini192 – 21524Mitochondrial matrixSequence AnalysisAdd
    BLAST
    Topological domaini237 – 31276Mitochondrial intermembraneSequence AnalysisAdd
    BLAST
    Topological domaini334 – 40774Mitochondrial matrixSequence AnalysisAdd
    BLAST
    Topological domaini429 – 4302Mitochondrial intermembraneSequence Analysis
    Topological domaini452 – 738287Mitochondrial matrixSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei171 – 19121HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei216 – 23621HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei313 – 33321HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei408 – 42821HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei431 – 45121HelicalPROSITE-ProRule annotationAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini171 – 457287ABC transmembrane type-1PROSITE-ProRule annotationAdd
    BLAST
    Domaini492 – 731240ABC transporterPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ABC transmembrane type-1 domain.PROSITE-ProRule annotation
    Contains 1 ABC transporter domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1132.
    HOVERGENiHBG008358.
    InParanoidiQ9NRK6.
    KOiK05657.
    OMAiIEVNRYN.
    OrthoDBiEOG7Z3F4H.
    PhylomeDBiQ9NRK6.
    TreeFamiTF105198.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR011527. ABC1_TM_dom.
    IPR003439. ABC_transporter-like.
    IPR017871. ABC_transporter_CS.
    IPR001140. ABC_transptr_TM_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00664. ABC_membrane. 1 hit.
    PF00005. ABC_tran. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF90123. SSF90123. 1 hit.
    PROSITEiPS50929. ABC_TM1F. 1 hit.
    PS00211. ABC_TRANSPORTER_1. 1 hit.
    PS50893. ABC_TRANSPORTER_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9NRK6-1 [UniParc]FASTAAdd to Basket

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    MRGPPAWPLR LLEPPSPAEP GRLLPVACVW AAASRVPGSL SPFTGLRPAR    50
    LWGAGPALLW GVGAARRWRS GCRGGGPGAS RGVLGLARLL GLWARGPGSC 100
    RCGAFAGPGA PRLPRARFPG GPAAAAWAGD EAWRRGPAAP PGDKGRLRPA 150
    AAGLPEARKL LGLAYPERRR LAAAVGFLTM SSVISMSAPF FLGKIIDVIY 200
    TNPTVDYSDN LTRLCLGLSA VFLCGAAANA IRVYLMQTSG QRIVNRLRTS 250
    LFSSILRQEV AFFDKTRTGE LINRLSSDTA LLGRSVTENL SDGLRAGAQA 300
    SVGISMMFFV SPNLATFVLS VVPPVSIIAV IYGRYLRKLT KVTQDSLAQA 350
    TQLAEERIGN VRTVRAFGKE MTEIEKYASK VDHVMQLARK EAFARAGFFG 400
    ATGLSGNLIV LSVLYKGGLL MGSAHMTVGE LSSFLMYAFW VGISIGGLSS 450
    FYSELMKGLG AGGRLWELLE REPKLPFNEG VILNEKSFQG ALEFKNVHFA 500
    YPARPEVPIF QDFSLSIPSG SVTALVGPSG SGKSTVLSLL LRLYDPASGT 550
    ISLDGHDIRQ LNPVWLRSKI GTVSQEPILF SCSIAENIAY GADDPSSVTA 600
    EEIQRVAEVA NAVAFIRNFP QGFNTVVGEK GVLLSGGQKQ RIAIARALLK 650
    NPKILLLDEA TSALDAENEY LVQEALDRLM DGRTVLVIAH RLSTIKNANM 700
    VAVLDQGKIT EYGKHEELLS KPNGIYRKLM NKQSFISA 738
    Length:738
    Mass (Da):79,148
    Last modified:April 3, 2007 - v2
    Checksum:iC68B4FAC0F8B7E43
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti393 – 3931F → V in AAF78198. (PubMed:10922475)Curated
    Sequence conflicti511 – 5111Q → K in AAA84438. (PubMed:7766993)Curated
    Sequence conflicti558 – 5636IRQLNP → NPSAKPS in AAA84438. (PubMed:7766993)Curated
    Sequence conflicti606 – 6116VAEVAN → GLKGQ in BAB20265. 1 PublicationCurated
    Sequence conflicti615 – 6228FIRNFPQG → SPEFPPR in AAA84438. (PubMed:7766993)Curated
    Sequence conflicti691 – 6911R → S in AAA84438. (PubMed:7766993)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501A → S.1 Publication
    Corresponds to variant rs4148756 [ dbSNP | Ensembl ].
    VAR_013702
    Natural varianti242 – 2421R → G.
    Corresponds to variant rs17584642 [ dbSNP | Ensembl ].
    VAR_048133
    Natural varianti471 – 4711R → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035735
    Natural varianti545 – 5451D → N.1 Publication
    Corresponds to variant rs35698797 [ dbSNP | Ensembl ].
    VAR_031435

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF216833 mRNA. Translation: AAF78198.1.
    AB013380 mRNA. Translation: BAB20265.1.
    AL121990 Genomic DNA. Translation: CAI22012.1.
    CH471098 Genomic DNA. Translation: EAW69901.1.
    BC064930 mRNA. Translation: AAH64930.1.
    U18237 mRNA. Translation: AAA84438.1.
    CCDSiCCDS1580.1.
    RefSeqiNP_036221.2. NM_012089.2.
    UniGeneiHs.17614.

    Genome annotation databases

    EnsembliENST00000344517; ENSP00000355637; ENSG00000135776.
    GeneIDi23456.
    KEGGihsa:23456.
    UCSCiuc001htp.4. human.

    Polymorphism databases

    DMDMi143811359.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    ABCMdb

    Database for mutations in ABC proteins

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF216833 mRNA. Translation: AAF78198.1 .
    AB013380 mRNA. Translation: BAB20265.1 .
    AL121990 Genomic DNA. Translation: CAI22012.1 .
    CH471098 Genomic DNA. Translation: EAW69901.1 .
    BC064930 mRNA. Translation: AAH64930.1 .
    U18237 mRNA. Translation: AAA84438.1 .
    CCDSi CCDS1580.1.
    RefSeqi NP_036221.2. NM_012089.2.
    UniGenei Hs.17614.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZDQ X-ray 2.85 A 152-738 [» ]
    4AYT X-ray 2.85 A 152-738 [» ]
    4AYW X-ray 3.30 A 1-738 [» ]
    4AYX X-ray 2.90 A 152-738 [» ]
    ProteinModelPortali Q9NRK6.
    SMRi Q9NRK6. Positions 153-722.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117020. 9 interactions.
    IntActi Q9NRK6. 1 interaction.
    STRINGi 9606.ENSP00000355637.

    Protein family/group databases

    TCDBi 3.A.1.201.17. the atp-binding cassette (abc) superfamily.

    PTM databases

    PhosphoSitei Q9NRK6.

    Polymorphism databases

    DMDMi 143811359.

    Proteomic databases

    MaxQBi Q9NRK6.
    PaxDbi Q9NRK6.
    PRIDEi Q9NRK6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344517 ; ENSP00000355637 ; ENSG00000135776 .
    GeneIDi 23456.
    KEGGi hsa:23456.
    UCSCi uc001htp.4. human.

    Organism-specific databases

    CTDi 23456.
    GeneCardsi GC01M229652.
    H-InvDB HIX0028493.
    HGNCi HGNC:41. ABCB10.
    HPAi CAB044063.
    CAB044065.
    MIMi 605454. gene.
    neXtProti NX_Q9NRK6.
    PharmGKBi PA24385.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1132.
    HOVERGENi HBG008358.
    InParanoidi Q9NRK6.
    KOi K05657.
    OMAi IEVNRYN.
    OrthoDBi EOG7Z3F4H.
    PhylomeDBi Q9NRK6.
    TreeFami TF105198.

    Enzyme and pathway databases

    BRENDAi 3.6.3.43. 2681.
    Reactomei REACT_111108. Mitochondrial ABC transporters.

    Miscellaneous databases

    GenomeRNAii 23456.
    NextBioi 45747.
    PROi Q9NRK6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRK6.
    Bgeei Q9NRK6.
    CleanExi HS_ABCB10.
    Genevestigatori Q9NRK6.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR011527. ABC1_TM_dom.
    IPR003439. ABC_transporter-like.
    IPR017871. ABC_transporter_CS.
    IPR001140. ABC_transptr_TM_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00664. ABC_membrane. 1 hit.
    PF00005. ABC_tran. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF90123. SSF90123. 1 hit.
    PROSITEi PS50929. ABC_TM1F. 1 hit.
    PS00211. ABC_TRANSPORTER_1. 1 hit.
    PS50893. ABC_TRANSPORTER_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "M-ABC2, a new human mitochondrial ATP-binding cassette membrane protein."
      Zhang F., Hogue D.L., Liu L., Fisher C.L., Hui D., Childs S., Ling V.
      FEBS Lett. 478:89-94(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-545.
      Tissue: Lymphoblast.
    2. "Human mono ATP-binding cassette protein."
      Ito K., Suzuki H., Sugiyama Y.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
    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].
      Tissue: Eye.
    6. "Characterization and mapping of three new mammalian ATP-binding transporter genes from an EST database."
      Allikmets R., Gerrard B., Glavac D., Ravnik-Glavac M., Jenkins N.A., Gilbert D.J., Copeland N.G., Modi W., Dean M.
      Mamm. Genome 6:114-117(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 510-738.
    7. "Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me)."
      Graf S.A., Haigh S.E., Corson E.D., Shirihai O.S.
      J. Biol. Chem. 279:42954-42963(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSIT PEPTIDE CLEAVAGE SITE, SUBUNIT.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 152-738 ALONE AND IN COMPLEX WITH ATP ANALOGS, ATP-BINDING REGION, SUBUNIT.
    11. "Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population."
      Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., Higuchi S., Nakamura Y.
      J. Hum. Genet. 47:38-50(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-150.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-471.

    Entry informationi

    Entry nameiABCBA_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRK6
    Secondary accession number(s): Q13040, Q6P1Q8, Q9H3V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 2, 2002
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3