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O75449

- KTNA1_HUMAN

UniProt

O75449 - KTNA1_HUMAN

Protein

Katanin p60 ATPase-containing subunit A1

Gene

KATNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.UniRule annotation

    Catalytic activityi

    ATP + H2O = ADP + phosphate.UniRule annotation

    Enzyme regulationi

    ATPase activity is stimulated by microtubules, which promote homooligomerization. ATP-dependent microtubule severing is stimulated by interaction with KATNB1.UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi249 – 2568ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. microtubule binding Source: UniProtKB
    3. microtubule-severing ATPase activity Source: UniProtKB-EC
    4. protein binding Source: UniProtKB
    5. protein heterodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cytoplasmic microtubule organization Source: Ensembl
    2. microtubule bundle formation Source: Ensembl
    3. microtubule severing Source: UniProtKB-HAMAP
    4. mitotic interphase Source: UniProtKB
    5. mitotic nuclear division Source: UniProtKB-KW
    6. negative regulation of neuron projection development Source: Ensembl
    7. neuron migration Source: Ensembl
    8. protein localization Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Katanin p60 ATPase-containing subunit A1UniRule annotation (EC:3.6.4.3UniRule annotation)
    Short name:
    Katanin p60 subunit A1UniRule annotation
    Alternative name(s):
    p60 kataninUniRule annotation
    Gene namesi
    Name:KATNA1UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6216. KATNA1.

    Subcellular locationi

    Cytoplasm. Midbody. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome UniRule annotation. Cytoplasmcytoskeletonspindle pole
    Note: Predominantly cytoplasmic. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1.

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. centrosome Source: UniProtKB-HAMAP
    3. cytoplasm Source: UniProtKB
    4. growth cone Source: Ensembl
    5. lipid particle Source: Ensembl
    6. microtubule Source: UniProtKB-KW
    7. midbody Source: UniProtKB
    8. neuronal cell body Source: Ensembl
    9. nucleus Source: Ensembl
    10. plasma membrane Source: Ensembl
    11. spindle Source: UniProtKB
    12. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi255 – 2551K → A: Abolishes ATP dependent microtubule severing activity and localization to spindle poles. 2 Publications
    Mutagenesisi308 – 3081D → N: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-309. 1 Publication
    Mutagenesisi309 – 3091E → N: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-308. 1 Publication

    Organism-specific databases

    PharmGKBiPA30017.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 491491Katanin p60 ATPase-containing subunit A1PRO_0000084594Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421Phosphoserine; by DYRK21 PublicationUniRule annotation
    Modified residuei109 – 1091Phosphoserine; by DYRK21 PublicationUniRule annotation
    Modified residuei133 – 1331Phosphothreonine; by DYRK21 PublicationUniRule annotation
    Modified residuei170 – 1701Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation.4 PublicationsUniRule annotation
    Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex, leading to its proteasomal degradation. Ubiquitinated by the EDVP E3 ligase complex and subsequently targeted for proteasomal degradation.1 PublicationUniRule annotation

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO75449.
    PaxDbiO75449.
    PRIDEiO75449.

    PTM databases

    PhosphoSiteiO75449.

    Expressioni

    Gene expression databases

    ArrayExpressiO75449.
    BgeeiO75449.
    CleanExiHS_KATNA1.
    GenevestigatoriO75449.

    Organism-specific databases

    HPAiHPA036207.

    Interactioni

    Subunit structurei

    Can homooligomerize into hexameric rings, which may be promoted by interaction with microtubules By similarity. Interacts with KATNB1, which may serve as a targeting subunit. Interacts with dynein and NDEL1 By similarity. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP complex). Interacts with KLHL42 (via the kelch domains). Interacts with CUL3; the interaction is enhanced by KLHL42.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi116285. 21 interactions.
    STRINGi9606.ENSP00000335106.

    Structurei

    3D structure databases

    ProteinModelPortaliO75449.
    SMRiO75449. Positions 1-72, 166-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 185185Interaction with microtubulesAdd
    BLAST
    Regioni1 – 7575Interaction with dynein and NDEL1By similarityAdd
    BLAST
    Regioni1 – 2929Interaction with KATNB1Add
    BLAST

    Domaini

    The N-terminus is sufficient for interaction with microtubules, although high affinity binding to microtubules also requires an intact C-terminal domain and ATP, which promotes oligomerization.UniRule annotation

    Sequence similaritiesi

    Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0464.
    HOGENOMiHOG000225142.
    HOVERGENiHBG057074.
    InParanoidiO75449.
    KOiK07767.
    OMAiSQYSDPK.
    OrthoDBiEOG7SFHWZ.
    PhylomeDBiO75449.
    TreeFamiTF323170.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_03023. Katanin_p60_A1.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR028596. KATNA1.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00674. AAA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75449-1) [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

    MSLLMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTYLQQ    50
    KWQQVWQEIN VEAKHVKDIM KTLESFKLDS TPLKAAQHDL PASEGEVWSM 100
    PVPVERRPSP GPRKRQSSQY SDPKSHGNRP STTVRVHRSS AQNVHNDRGK 150
    AVRCREKKEQ NKGREEKNKS PAAVTEPETN KFDSTGYDKD LVEALERDII 200
    SQNPNVRWDD IADLVEAKKL LKEAVVLPMW MPEFFKGIRR PWKGVLMVGP 250
    PGTGKTLLAK AVATECKTTF FNVSSSTLTS KYRGESEKLV RLLFEMARFY 300
    SPATIFIDEI DSICSRRGTS EEHEASRRVK AELLVQMDGV GGTSENDDPS 350
    KMVMVLAATN FPWDIDEALR RRLEKRIYIP LPSAKGREEL LRISLRELEL 400
    ADDVDLASIA ENMEGYSGAD ITNVCRDASL MAMRRRIEGL TPEEIRNLSK 450
    EEMHMPTTME DFEMALKKVS KSVSAADIER YEKWIFEFGS C 491
    Length:491
    Mass (Da):55,965
    Last modified:November 1, 1998 - v1
    Checksum:iF431594F478491DD
    GO
    Isoform 2 (identifier: O75449-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         168-243: Missing.
         384-387: AKGR → GMRP
         388-491: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:311
    Mass (Da):35,319
    Checksum:i9DF635C4E51147C7
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei168 – 24376Missing in isoform 2. 1 PublicationVSP_012948Add
    BLAST
    Alternative sequencei384 – 3874AKGR → GMRP in isoform 2. 1 PublicationVSP_012949
    Alternative sequencei388 – 491104Missing in isoform 2. 1 PublicationVSP_012950Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF056022 mRNA. Translation: AAC25114.1.
    AL078581, BX276089 Genomic DNA. Translation: CAI19504.1.
    AL078581, BX276089 Genomic DNA. Translation: CAI19505.1.
    BX276089, AL078581 Genomic DNA. Translation: CAI16431.1.
    BX276089, AL078581 Genomic DNA. Translation: CAI16432.1.
    CH471051 Genomic DNA. Translation: EAW47793.1.
    CH471051 Genomic DNA. Translation: EAW47795.1.
    BC050428 mRNA. Translation: AAH50428.1.
    CCDSiCCDS5217.1. [O75449-1]
    CCDS56456.1. [O75449-2]
    RefSeqiNP_001191005.1. NM_001204076.1. [O75449-2]
    NP_008975.1. NM_007044.3. [O75449-1]
    XP_005266861.1. XM_005266804.1. [O75449-1]
    UniGeneiHs.450175.

    Genome annotation databases

    EnsembliENST00000335643; ENSP00000335180; ENSG00000186625. [O75449-2]
    ENST00000335647; ENSP00000335106; ENSG00000186625. [O75449-1]
    ENST00000367411; ENSP00000356381; ENSG00000186625. [O75449-1]
    GeneIDi11104.
    KEGGihsa:11104.
    UCSCiuc003qmr.2. human. [O75449-1]
    uc003qmt.3. human. [O75449-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF056022 mRNA. Translation: AAC25114.1 .
    AL078581 , BX276089 Genomic DNA. Translation: CAI19504.1 .
    AL078581 , BX276089 Genomic DNA. Translation: CAI19505.1 .
    BX276089 , AL078581 Genomic DNA. Translation: CAI16431.1 .
    BX276089 , AL078581 Genomic DNA. Translation: CAI16432.1 .
    CH471051 Genomic DNA. Translation: EAW47793.1 .
    CH471051 Genomic DNA. Translation: EAW47795.1 .
    BC050428 mRNA. Translation: AAH50428.1 .
    CCDSi CCDS5217.1. [O75449-1 ]
    CCDS56456.1. [O75449-2 ]
    RefSeqi NP_001191005.1. NM_001204076.1. [O75449-2 ]
    NP_008975.1. NM_007044.3. [O75449-1 ]
    XP_005266861.1. XM_005266804.1. [O75449-1 ]
    UniGenei Hs.450175.

    3D structure databases

    ProteinModelPortali O75449.
    SMRi O75449. Positions 1-72, 166-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116285. 21 interactions.
    STRINGi 9606.ENSP00000335106.

    PTM databases

    PhosphoSitei O75449.

    Proteomic databases

    MaxQBi O75449.
    PaxDbi O75449.
    PRIDEi O75449.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335643 ; ENSP00000335180 ; ENSG00000186625 . [O75449-2 ]
    ENST00000335647 ; ENSP00000335106 ; ENSG00000186625 . [O75449-1 ]
    ENST00000367411 ; ENSP00000356381 ; ENSG00000186625 . [O75449-1 ]
    GeneIDi 11104.
    KEGGi hsa:11104.
    UCSCi uc003qmr.2. human. [O75449-1 ]
    uc003qmt.3. human. [O75449-2 ]

    Organism-specific databases

    CTDi 11104.
    GeneCardsi GC06M149957.
    HGNCi HGNC:6216. KATNA1.
    HPAi HPA036207.
    MIMi 606696. gene.
    neXtProti NX_O75449.
    PharmGKBi PA30017.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0464.
    HOGENOMi HOG000225142.
    HOVERGENi HBG057074.
    InParanoidi O75449.
    KOi K07767.
    OMAi SQYSDPK.
    OrthoDBi EOG7SFHWZ.
    PhylomeDBi O75449.
    TreeFami TF323170.

    Miscellaneous databases

    ChiTaRSi KATNA1. human.
    GeneWikii KATNA1.
    GenomeRNAii 11104.
    NextBioi 42220.
    PROi O75449.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75449.
    Bgeei O75449.
    CleanExi HS_KATNA1.
    Genevestigatori O75449.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_03023. Katanin_p60_A1.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR028596. KATNA1.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00674. AAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Katanin is responsible for the M-phase microtubule-severing activity in Xenopus eggs."
      McNally F.J., Thomas S.
      Mol. Biol. Cell 9:1847-1861(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 2).
      Tissue: Brain.
    5. "Two domains of p80 katanin regulate microtubule severing and spindle pole targeting by p60 katanin."
      McNally K.P., Bazirgan O.A., McNally F.J.
      J. Cell Sci. 113:1623-1633(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KATNB1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-255; ASP-308 AND GLU-309.
    6. "Katanin inhibition prevents the redistribution of gamma-tubulin at mitosis."
      Buster D., McNally K., McNally F.J.
      J. Cell Sci. 115:1083-1092(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-255.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "The Cul3/Klhdc5 E3 ligase regulates p60/katanin and is required for normal mitosis in mammalian cells."
      Cummings C.M., Bentley C.A., Perdue S.A., Baas P.W., Singer J.D.
      J. Biol. Chem. 284:11663-11675(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY THE BCR(KLHL42) COMPLEX, SUBCELLULAR LOCATION.
    9. "Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase."
      Maddika S., Chen J.
      Nat. Cell Biol. 11:409-419(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-42; SER-109 AND THR-133 BY DYRK2, FUNCTION AS KATNA1 KINASE, INTERACTION WITH EDVP COMPLEX.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKTNA1_HUMAN
    AccessioniPrimary (citable) accession number: O75449
    Secondary accession number(s): E1P5A3
    , Q5TFA8, Q5TFA9, Q86VN2, Q9NU52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 115 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, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3