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O00422

- SAP18_HUMAN

UniProt

O00422 - SAP18_HUMAN

Protein

Histone deacetylase complex subunit SAP18

Gene

SAP18

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

    Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function.4 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    3. positive regulation of apoptotic process Source: UniProtKB
    4. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
    5. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    6. RNA splicing Source: UniProtKB-KW
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_200856. NoRC negatively regulates rRNA expression.
    SignaLinkiO00422.

    Protein family/group databases

    TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase complex subunit SAP18
    Alternative name(s):
    18 kDa Sin3-associated polypeptide
    2HOR0202
    Cell growth-inhibiting gene 38 protein
    Sin3-associated polypeptide p18
    Gene namesi
    Name:SAP18
    ORF Names:GIG38
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:10530. SAP18.

    Subcellular locationi

    Nucleus. Cytoplasm. Nucleus speckle
    Note: Shuttles between the nucleus and the cytoplasm. Colocalizes with ACIN1 and SRSF2 in nuclear speckles.

    GO - Cellular componenti

    1. ASAP complex Source: UniProtKB
    2. cytoplasm Source: HPA
    3. histone deacetylase complex Source: ProtInc
    4. nuclear speck Source: UniProtKB
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi118 – 1181D → A: Abolishes splicing regulation activity and interaction with RNPS1 and ACIN1; when associated with A-121. 1 Publication
    Mutagenesisi121 – 1211T → A: Abolishes splicing regulation activity and interaction with RNPS1 and ACIN1; when associated with A-118. 1 Publication
    Mutagenesisi126 – 1261K → A: No effect on splicing regulation activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34940.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 153152Histone deacetylase complex subunit SAP18PRO_0000220975Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO00422.
    PaxDbiO00422.
    PeptideAtlasiO00422.
    PRIDEiO00422.

    PTM databases

    PhosphoSiteiO00422.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    BgeeiO00422.
    CleanExiHS_SAP18.
    GenevestigatoriO00422.

    Organism-specific databases

    HPAiCAB012273.
    HPA011352.

    Interactioni

    Subunit structurei

    Found in a mRNA splicing-dependent exon junction complex (EJC). Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) and PSAP complexes consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably are formed mutually exclusive. For the ASAP complex, the association of SAP18 seems to require a preformed RNPS1:ACIN1 complex. Forms a complex with SIN3A and HDAC1. Interacts with SUFU.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HDAC1Q135472EBI-1044156,EBI-301834

    Protein-protein interaction databases

    BioGridi115573. 95 interactions.
    DIPiDIP-33590N.
    IntActiO00422. 12 interactions.
    MINTiMINT-5002140.
    STRINGi9606.ENSP00000371973.

    Structurei

    Secondary structure

    1
    153
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni22 – 243
    Beta strandi28 – 3710
    Helixi43 – 453
    Turni52 – 543
    Beta strandi55 – 606
    Helixi66 – 7611
    Helixi78 – 814
    Beta strandi86 – 916
    Beta strandi95 – 984
    Beta strandi104 – 1129
    Helixi122 – 1254
    Beta strandi132 – 1387
    Beta strandi144 – 1474

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HDENMR-A6-149[»]
    ProteinModelPortaliO00422.
    SMRiO00422. Positions 6-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00422.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni93 – 15361Involved in splicing regulation activityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SAP18 family.Curated

    Phylogenomic databases

    eggNOGiNOG249491.
    HOGENOMiHOG000238745.
    HOVERGENiHBG003465.
    InParanoidiO00422.
    KOiK14324.
    OrthoDBiEOG79SDZS.
    PhylomeDBiO00422.
    TreeFamiTF313032.

    Family and domain databases

    InterProiIPR017250. Hist_deAcase_cplx_SAP18.
    IPR010516. SAP18.
    [Graphical view]
    PANTHERiPTHR13082. PTHR13082. 1 hit.
    PfamiPF06487. SAP18. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037637. HDAC_SAP18. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    O00422-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN    50
    VPSSELQIYT WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFTDVKRPG 100
    YRVKEIGSTM SGRKGTDDSM TLQSQKFQIG DYLDIAITPP NRAPPPSGRM 150
    RPY 153
    Length:153
    Mass (Da):17,561
    Last modified:July 1, 1997 - v1
    Checksum:iC7E479FFE9CA5774
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141K → E in AAF21220. 1 PublicationCurated
    Sequence conflicti146 – 1461P → T in AAH30836. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96915 mRNA. Translation: AAC51322.1.
    U78303 mRNA. Translation: AAF21220.1.
    AF153608 mRNA. Translation: AAD41090.1.
    AY550970 mRNA. Translation: AAT52216.1.
    CR457035 mRNA. Translation: CAG33316.1.
    AK311748 mRNA. Translation: BAG34691.1.
    AL158032 Genomic DNA. Translation: CAH69949.1.
    CH471075 Genomic DNA. Translation: EAX08291.1.
    BC030836 mRNA. Translation: AAH30836.1.
    RefSeqiNP_005861.2. NM_005870.4.
    UniGeneiHs.524899.

    Genome annotation databases

    EnsembliENST00000607003; ENSP00000475925; ENSG00000150459.
    GeneIDi10284.
    KEGGihsa:10284.
    UCSCiuc001uns.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96915 mRNA. Translation: AAC51322.1 .
    U78303 mRNA. Translation: AAF21220.1 .
    AF153608 mRNA. Translation: AAD41090.1 .
    AY550970 mRNA. Translation: AAT52216.1 .
    CR457035 mRNA. Translation: CAG33316.1 .
    AK311748 mRNA. Translation: BAG34691.1 .
    AL158032 Genomic DNA. Translation: CAH69949.1 .
    CH471075 Genomic DNA. Translation: EAX08291.1 .
    BC030836 mRNA. Translation: AAH30836.1 .
    RefSeqi NP_005861.2. NM_005870.4.
    UniGenei Hs.524899.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HDE NMR - A 6-149 [» ]
    ProteinModelPortali O00422.
    SMRi O00422. Positions 6-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115573. 95 interactions.
    DIPi DIP-33590N.
    IntActi O00422. 12 interactions.
    MINTi MINT-5002140.
    STRINGi 9606.ENSP00000371973.

    Protein family/group databases

    TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    PTM databases

    PhosphoSitei O00422.

    Proteomic databases

    MaxQBi O00422.
    PaxDbi O00422.
    PeptideAtlasi O00422.
    PRIDEi O00422.

    Protocols and materials databases

    DNASUi 10284.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000607003 ; ENSP00000475925 ; ENSG00000150459 .
    GeneIDi 10284.
    KEGGi hsa:10284.
    UCSCi uc001uns.3. human.

    Organism-specific databases

    CTDi 10284.
    GeneCardsi GC13P021714.
    H-InvDB HIX0011163.
    HGNCi HGNC:10530. SAP18.
    HPAi CAB012273.
    HPA011352.
    MIMi 602949. gene.
    neXtProti NX_O00422.
    PharmGKBi PA34940.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249491.
    HOGENOMi HOG000238745.
    HOVERGENi HBG003465.
    InParanoidi O00422.
    KOi K14324.
    OrthoDBi EOG79SDZS.
    PhylomeDBi O00422.
    TreeFami TF313032.

    Enzyme and pathway databases

    Reactomei REACT_200856. NoRC negatively regulates rRNA expression.
    SignaLinki O00422.

    Miscellaneous databases

    ChiTaRSi SAP18. human.
    EvolutionaryTracei O00422.
    GeneWikii SAP18.
    GenomeRNAii 10284.
    NextBioi 38964.
    PROi O00422.
    SOURCEi Search...

    Gene expression databases

    Bgeei O00422.
    CleanExi HS_SAP18.
    Genevestigatori O00422.

    Family and domain databases

    InterProi IPR017250. Hist_deAcase_cplx_SAP18.
    IPR010516. SAP18.
    [Graphical view ]
    PANTHERi PTHR13082. PTHR13082. 1 hit.
    Pfami PF06487. SAP18. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037637. HDAC_SAP18. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex."
      Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.
      Cell 89:357-364(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SIN3A AND HDAC1.
    2. "Characterization of proteins interacting with CAMPGEF."
      Kawasaki H., Housman D.E., Graybiel A.M.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "A catalogue of genes in the human dermal papilla cells as identified by expressed sequence tags."
      Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Lee H.D., Kim J.C.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Hair follicle dermal papilla.
    4. "Identification of a human cell growth inhibiting gene."
      Kim J.W.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "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].
      Tissue: Brain cortex.
    7. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Hypothalamus.
    10. Cited for: IDENTIFICATION IN THE ASAP COMPLEX, FUNCTION OF THE ASAP COMPLEX.
    11. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
      Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
      RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION IN THE ASAP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. "Human SAP18 mediates assembly of a splicing regulatory multiprotein complex via its ubiquitin-like fold."
      Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A., Schulze-Osthoff K., Schaal H., Schwerk C.
      RNA 16:2442-2454(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNPS1 AND ACIN1, MUTAGENESIS OF ASP-118; THR-121 AND LYS-126.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
      Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
      Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Structure of SAP18: a ubiquitin fold in histone deacetylase complex assembly."
      McCallum S.A., Bazan J.F., Merchant M., Yin J., Pan B., de Sauvage F.J., Fairbrother W.J.
      Biochemistry 45:11974-11982(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 6-149, INTERACTION WITH SUFU.

    Entry informationi

    Entry nameiSAP18_HUMAN
    AccessioniPrimary (citable) accession number: O00422
    Secondary accession number(s): B2R494
    , Q2TTR4, Q6IAW9, Q8N606, Q9UF14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 132 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 13
      Human chromosome 13: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3