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Q9H0A0

- NAT10_HUMAN

UniProt

Q9H0A0 - NAT10_HUMAN

Protein

N-acetyltransferase 10

Gene

NAT10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Has protein acetyltransferase activity in vitro. Can acetylate both histones and microtubules. Histone acetylation may regulate transcription and mitotic chromosome de-condensation. Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization. Acetylates alpha-tubulin, which may affect microtubule stability and cell division.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi284 – 2918ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. N-acetyltransferase activity Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetyltransferase 10 (EC:2.3.1.-)
    Gene namesi
    Name:NAT10
    Synonyms:ALP, KIAA1709
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:29830. NAT10.

    Subcellular locationi

    Nucleusnucleolus 3 Publications
    Note: Nucleolar in interphase and redistributes to the perichromosomal layer and to the midbody during telophase.

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA143485555.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10251025N-acetyltransferase 10PRO_0000215883Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei426 – 4261N6-acetyllysine1 Publication
    Modified residuei934 – 9341Phosphoserine1 Publication
    Modified residuei984 – 9841Phosphoserine1 Publication
    Modified residuei987 – 9871Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H0A0.
    PaxDbiQ9H0A0.
    PRIDEiQ9H0A0.

    2D gel databases

    SWISS-2DPAGEQ9H0A0.

    PTM databases

    PhosphoSiteiQ9H0A0.

    Expressioni

    Inductioni

    Transcriptionally activated by genotoxic agents; possible role in DNA damage and induction of cellular resistance to genotoxic agents.1 Publication

    Gene expression databases

    ArrayExpressiQ9H0A0.
    BgeeiQ9H0A0.
    CleanExiHS_NAT10.
    GenevestigatoriQ9H0A0.

    Organism-specific databases

    HPAiCAB035546.

    Interactioni

    Subunit structurei

    Interacts with SUN1 (via N-terminus). Also interacts with TERT.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LYARQ9NX581EBI-876527,EBI-713507

    Protein-protein interaction databases

    BioGridi120521. 24 interactions.
    IntActiQ9H0A0. 18 interactions.
    MINTiMINT-2817086.
    STRINGi9606.ENSP00000257829.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H0A0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini558 – 753196N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni702 – 1025324Required for localization to the nucleolus and midbodyAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi989 – 102537Lys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the UPF0202 family.Curated
    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1444.
    HOGENOMiHOG000210833.
    HOVERGENiHBG052206.
    InParanoidiQ9H0A0.
    KOiK14521.
    OMAiKFLQQMV.
    OrthoDBiEOG7QK0B5.
    PhylomeDBiQ9H0A0.
    TreeFamiTF300601.

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR013562. DUF1726.
    IPR000182. GNAT_dom.
    IPR007807. Helicase_dom.
    IPR027992. tRNA_bind_dom.
    [Graphical view]
    PfamiPF08351. DUF1726. 1 hit.
    PF13718. GNAT_acetyltr_2. 1 hit.
    PF05127. Helicase_RecD. 1 hit.
    PF13725. tRNA_bind_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H0A0-1) [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

    MHRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK     50
    ARPSVLWCYK KELGFSSHRK KRMRQLQKKI KNGTLNIKQD DPFELFIAAT 100
    NIRYCYYNET HKILGNTFGM CVLQDFEALT PNLLARTVET VEGGGLVVIL 150
    LRTMNSLKQL YTVTMDVHSR YRTEAHQDVV GRFNERFILS LASCKKCLVI 200
    DDQLNILPIS SHVATMEALP PQTPDESLGP SDLELRELKE SLQDTQPVGV 250
    LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG 300
    AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIIQSLNPE 350
    FNKAVIRVNV FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS 400
    LLGPYLVFMA STINGYEGTG RSLSLKLIQQ LRQQSAQSQV STTAENKTTT 450
    TARLASARTL YEVSLQESIR YAPGDAVEKW LNDLLCLDCL NITRIVSGCP 500
    LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN SPNDLQMLSD 550
    APAHHLFCLL PPVPPTQNAL PEVLAVIQVC LEGEISRQSI LNSLSRGKKA 600
    SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM 650
    YYEGRFPCLE EKVLETPQEI HTVSSEAVSL LEEVITPRKD LPPLLLKLNE 700
    RPAERLDYLG VSYGLTPRLL KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK 750
    TLTDEDEADQ GGWLAAFWKD FRRRFLALLS YQFSTFSPSL ALNIIQNRNM 800
    GKPAQPALSR EELEALFLPY DLKRLEMYSR NMVDYHLIMD MIPAISRIYF 850
    LNQLGDLALS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR 900
    KVVKLFNEVQ EKAIEEQMVA AKDVVMEPTM KTLSDDLDEA AKEFQEKHKK 950
    EVGKLKSMDL SEYIIRGDDE EWNEVLNKAG PNASIISLKS DKKRKLEAKQ 1000
    EPKQSKKLKN RETKNKKDMK LKRKK 1025
    Length:1,025
    Mass (Da):115,730
    Last modified:November 30, 2010 - v2
    Checksum:i88734933A46EB0EE
    GO
    Isoform 2 (identifier: Q9H0A0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Show »
    Length:953
    Mass (Da):107,297
    Checksum:iFC718FD5410FEAAA
    GO

    Sequence cautioni

    The sequence AAO49126.1 differs from that shown. Reason: Frameshift at position 981.
    The sequence BAB21800.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261F → L in BAA91800. (PubMed:14702039)Curated
    Sequence conflicti162 – 1621T → A in AAO49126. (PubMed:14592445)Curated
    Sequence conflicti315 – 3151S → C in BAB13995. (PubMed:14702039)Curated
    Sequence conflicti405 – 4051Y → C in BAG57396. (PubMed:14702039)Curated
    Sequence conflicti879 – 8791Q → R in BAB13995. (PubMed:14702039)Curated
    Sequence conflicti971 – 9711E → G in BAG57396. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti461 – 4611Y → H.6 Publications
    Corresponds to variant rs2957516 [ dbSNP | Ensembl ].
    VAR_059858
    Natural varianti983 – 9831A → T.
    Corresponds to variant rs36006049 [ dbSNP | Ensembl ].
    VAR_061894

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_054018Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051496 mRNA. Translation: BAB21800.1. Different initiation.
    AL136882 mRNA. Translation: CAB66816.1.
    AK001636 mRNA. Translation: BAA91800.1.
    AK022241 mRNA. Translation: BAB13995.1.
    AK294044 mRNA. Translation: BAG57396.1.
    AC090469 Genomic DNA. No translation available.
    BC035558 mRNA. Translation: AAH35558.1.
    AF489535 mRNA. Translation: AAO49126.1. Frameshift.
    CCDSiCCDS44568.1. [Q9H0A0-2]
    CCDS7889.1. [Q9H0A0-1]
    RefSeqiNP_001137502.1. NM_001144030.1.
    NP_078938.2. NM_024662.2.
    XP_005253056.1. XM_005252999.1. [Q9H0A0-1]
    UniGeneiHs.577281.

    Genome annotation databases

    EnsembliENST00000257829; ENSP00000257829; ENSG00000135372. [Q9H0A0-1]
    ENST00000531159; ENSP00000433011; ENSG00000135372. [Q9H0A0-2]
    GeneIDi55226.
    KEGGihsa:55226.
    UCSCiuc001mvk.3. human. [Q9H0A0-1]

    Polymorphism databases

    DMDMi313104140.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051496 mRNA. Translation: BAB21800.1 . Different initiation.
    AL136882 mRNA. Translation: CAB66816.1 .
    AK001636 mRNA. Translation: BAA91800.1 .
    AK022241 mRNA. Translation: BAB13995.1 .
    AK294044 mRNA. Translation: BAG57396.1 .
    AC090469 Genomic DNA. No translation available.
    BC035558 mRNA. Translation: AAH35558.1 .
    AF489535 mRNA. Translation: AAO49126.1 . Frameshift.
    CCDSi CCDS44568.1. [Q9H0A0-2 ]
    CCDS7889.1. [Q9H0A0-1 ]
    RefSeqi NP_001137502.1. NM_001144030.1.
    NP_078938.2. NM_024662.2.
    XP_005253056.1. XM_005252999.1. [Q9H0A0-1 ]
    UniGenei Hs.577281.

    3D structure databases

    ProteinModelPortali Q9H0A0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120521. 24 interactions.
    IntActi Q9H0A0. 18 interactions.
    MINTi MINT-2817086.
    STRINGi 9606.ENSP00000257829.

    PTM databases

    PhosphoSitei Q9H0A0.

    Polymorphism databases

    DMDMi 313104140.

    2D gel databases

    SWISS-2DPAGE Q9H0A0.

    Proteomic databases

    MaxQBi Q9H0A0.
    PaxDbi Q9H0A0.
    PRIDEi Q9H0A0.

    Protocols and materials databases

    DNASUi 55226.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257829 ; ENSP00000257829 ; ENSG00000135372 . [Q9H0A0-1 ]
    ENST00000531159 ; ENSP00000433011 ; ENSG00000135372 . [Q9H0A0-2 ]
    GeneIDi 55226.
    KEGGi hsa:55226.
    UCSCi uc001mvk.3. human. [Q9H0A0-1 ]

    Organism-specific databases

    CTDi 55226.
    GeneCardsi GC11P034084.
    HGNCi HGNC:29830. NAT10.
    HPAi CAB035546.
    MIMi 609221. gene.
    neXtProti NX_Q9H0A0.
    PharmGKBi PA143485555.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1444.
    HOGENOMi HOG000210833.
    HOVERGENi HBG052206.
    InParanoidi Q9H0A0.
    KOi K14521.
    OMAi KFLQQMV.
    OrthoDBi EOG7QK0B5.
    PhylomeDBi Q9H0A0.
    TreeFami TF300601.

    Miscellaneous databases

    ChiTaRSi NAT10. human.
    GeneWikii NAT10.
    GenomeRNAii 55226.
    NextBioi 35500237.
    PROi Q9H0A0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H0A0.
    Bgeei Q9H0A0.
    CleanExi HS_NAT10.
    Genevestigatori Q9H0A0.

    Family and domain databases

    Gene3Di 3.40.630.30. 2 hits.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR013562. DUF1726.
    IPR000182. GNAT_dom.
    IPR007807. Helicase_dom.
    IPR027992. tRNA_bind_dom.
    [Graphical view ]
    Pfami PF08351. DUF1726. 1 hit.
    PF13718. GNAT_acetyltr_2. 1 hit.
    PF05127. Helicase_RecD. 1 hit.
    PF13725. tRNA_bind_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    PROSITEi PS51186. GNAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-461.
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-461.
      Tissue: Testis.
    3. "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), VARIANT HIS-461.
      Tissue: Cerebellum and Mammary gland.
    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] (ISOFORM 1), VARIANT HIS-461.
      Tissue: Brain.
    6. "Molecular cloning of a novel human gene encoding histone acetyltransferase-like protein involved in transcriptional activation of hTERT."
      Lv J., Liu H., Wang Q., Tang Z., Hou L., Zhang B.
      Biochem. Biophys. Res. Commun. 311:506-513(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-1025, FUNCTION, SUBCELLULAR LOCATION, VARIANT HIS-461.
      Tissue: Cervix carcinoma.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Histone acetyltransferase hALP and nuclear membrane protein hsSUN1 function in de-condensation of mitotic chromosomes."
      Chi Y.-H., Haller K., Peloponese J.-M. Jr., Jeang K.-T.
      J. Biol. Chem. 282:27447-27458(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SUN1.
    9. "Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation."
      Fu D., Collins K.
      Mol. Cell 28:773-785(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TERT.
    10. "DNA damage induces N-acetyltransferase NAT10 gene expression through transcriptional activation."
      Liu H., Ling Y., Gong Y., Sun Y., Hou L., Zhang B.
      Mol. Cell. Biochem. 300:249-258(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY GENOTOXIC AGENTS.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-934; SER-984 AND SER-987, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "NAT10, a nucleolar protein, localizes to the midbody and regulates cytokinesis and acetylation of microtubules."
      Shen Q., Zheng X., McNutt M.A., Guang L., Sun Y., Wang J., Gong Y., Hou L., Zhang B.
      Exp. Cell Res. 315:1653-1667(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "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-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNAT10_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0A0
    Secondary accession number(s): B4DFD5
    , E7ESU4, E9PMN9, Q86WK5, Q9C0F4, Q9HA61, Q9NVF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 127 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. SIMILARITY comments
      Index of protein domains and families
    6. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    External Data

    Dasty 3