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Q9BXB4

- OSB11_HUMAN

UniProt

Q9BXB4 - OSB11_HUMAN

Protein

Oxysterol-binding protein-related protein 11

Gene

OSBPL11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (11 Feb 2002)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. fat cell differentiation Source: BHF-UCL
    2. lipid transport Source: UniProtKB-KW
    3. positive regulation of sequestering of triglyceride Source: BHF-UCL

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oxysterol-binding protein-related protein 11
    Short name:
    ORP-11
    Short name:
    OSBP-related protein 11
    Gene namesi
    Name:OSBPL11
    Synonyms:ORP11, OSBP12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:16397. OSBPL11.

    Subcellular locationi

    Late endosome membrane 1 Publication. Golgi apparatustrans-Golgi network membrane 1 Publication
    Note: Localizes at the Golgi-late endosome interface.

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB-SubCell
    2. late endosome membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32825.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 747747Oxysterol-binding protein-related protein 11PRO_0000100381Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei15 – 151PhosphoserineBy similarity
    Modified residuei27 – 271Phosphothreonine4 Publications
    Modified residuei62 – 621Phosphotyrosine1 Publication
    Modified residuei172 – 1721Phosphoserine1 Publication
    Modified residuei174 – 1741Phosphoserine1 Publication
    Modified residuei177 – 1771PhosphoserineBy similarity
    Modified residuei181 – 1811Phosphoserine4 Publications
    Modified residuei189 – 1891Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BXB4.
    PaxDbiQ9BXB4.
    PRIDEiQ9BXB4.

    PTM databases

    PhosphoSiteiQ9BXB4.

    Expressioni

    Tissue specificityi

    Present at highest levels in ovary, testis, kidney, liver, stomach, brain, and adipose tissue. Strong expression (at protein level) in epithelial cells of kidney tubules, testicular tubules, caecum, and skin.1 Publication

    Gene expression databases

    ArrayExpressiQ9BXB4.
    BgeeiQ9BXB4.
    CleanExiHS_OSBPL11.
    GenevestigatoriQ9BXB4.

    Organism-specific databases

    HPAiHPA039144.

    Interactioni

    Subunit structurei

    Heterodimer with OSBPL9.1 Publication

    Protein-protein interaction databases

    BioGridi125386. 11 interactions.
    IntActiQ9BXB4. 1 interaction.
    STRINGi9606.ENSP00000296220.

    Structurei

    Secondary structure

    1
    747
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi62 – 709
    Turni71 – 733
    Beta strandi74 – 829
    Turni84 – 863
    Beta strandi88 – 947
    Helixi95 – 973
    Beta strandi98 – 1003
    Beta strandi103 – 1075
    Beta strandi117 – 1215
    Beta strandi123 – 1253
    Beta strandi128 – 1303
    Beta strandi133 – 1353
    Helixi140 – 16021

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D9XNMR-A59-165[»]
    ProteinModelPortaliQ9BXB4.
    SMRiQ9BXB4. Positions 59-165, 368-747.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BXB4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 15598PHPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PH domain binds phosphoinositides.1 Publication

    Sequence similaritiesi

    Belongs to the OSBP family.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG262374.
    HOGENOMiHOG000233871.
    HOVERGENiHBG053376.
    InParanoidiQ9BXB4.
    OMAiVTNHAPL.
    OrthoDBiEOG7PK8ZG.
    PhylomeDBiQ9BXB4.
    TreeFamiTF312807.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR000648. Oxysterol-bd.
    IPR018494. Oxysterol-bd_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PANTHERiPTHR10972. PTHR10972. 1 hit.
    PfamiPF01237. Oxysterol_BP. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    [Graphical view]
    PROSITEiPS01013. OSBP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BXB4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQGGEPVSTM KVSESEGKLE GQATAVTPNK NSSCGGGISS SSSSRGGSAK    50
    GWQYSDHMEN VYGYLMKYTN LVTGWQYRFF VLNNEAGLLE YFVNEQSRNQ 100
    KPRGTLQLAG AVISPSDEDS HTFTVNAASG EQYKLRATDA KERQHWVSRL 150
    QICTQHHTEA IGKNNPPLKS RSFSLASSSN SPISQRRPSQ NAISFFNVGH 200
    SKLQSLSKRT NLPPDHLVEV REMMSHAEGQ QRDLIRRIEC LPTSGHLSSL 250
    DQDLLMLKAT SMATMNCLND CFHILQLQHA SHQKGSLPSG TTIEWLEPKI 300
    SLSNHYKNGA DQPFATDQSK PVAVPEEQPV AESGLLAREP EEINADDEIE 350
    DTCDHKEDDL GAVEEQRSVI LHLLSQLKLG MDLTRVVLPT FILEKRSLLE 400
    MYADFMSHPD LFIAITNGAT AEDRMIRFVE YYLTSFHEGR KGAIAKKPYN 450
    PIIGETFHCS WKMPKSEVAS SVFSSSSTQG VTNHAPLSGE SLTQVGSDCY 500
    TVRFVAEQVS HHPPVSGFYA ECTERKMCVN AHVWTKSKFL GMSIGVTMVG 550
    EGILSLLEHG EEYTFSLPCA YARSILTVPW VELGGKVSVN CAKTGYSASI 600
    TFHTKPFYGG KLHRVTAEVK HNITNTVVCR VQGEWNSVLE FTYSNGETKY 650
    VDLTKLAVTK KRVRPLEKQD PFESRRLWKN VTDSLRESEI DKATEHKHTL 700
    EERQRTEERH RTETGTPWKT KYFIKEGDGW VYHKPLWKII PTTQPAE 747
    Length:747
    Mass (Da):83,643
    Last modified:February 11, 2002 - v2
    Checksum:iB443D3BDE8AE5FB6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti184 – 1841S → L in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036100

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF392454 mRNA. Translation: AAL40667.1.
    AK292702 mRNA. Translation: BAF85391.1.
    CH471052 Genomic DNA. Translation: EAW79389.1.
    BC065213 mRNA. Translation: AAH65213.1.
    AF346292 mRNA. Translation: AAK31141.1.
    CCDSiCCDS3033.1.
    RefSeqiNP_073613.2. NM_022776.4.
    UniGeneiHs.477440.

    Genome annotation databases

    EnsembliENST00000296220; ENSP00000296220; ENSG00000144909.
    GeneIDi114885.
    KEGGihsa:114885.
    UCSCiuc003eic.3. human.

    Polymorphism databases

    DMDMi20139127.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF392454 mRNA. Translation: AAL40667.1 .
    AK292702 mRNA. Translation: BAF85391.1 .
    CH471052 Genomic DNA. Translation: EAW79389.1 .
    BC065213 mRNA. Translation: AAH65213.1 .
    AF346292 mRNA. Translation: AAK31141.1 .
    CCDSi CCDS3033.1.
    RefSeqi NP_073613.2. NM_022776.4.
    UniGenei Hs.477440.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D9X NMR - A 59-165 [» ]
    ProteinModelPortali Q9BXB4.
    SMRi Q9BXB4. Positions 59-165, 368-747.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125386. 11 interactions.
    IntActi Q9BXB4. 1 interaction.
    STRINGi 9606.ENSP00000296220.

    PTM databases

    PhosphoSitei Q9BXB4.

    Polymorphism databases

    DMDMi 20139127.

    Proteomic databases

    MaxQBi Q9BXB4.
    PaxDbi Q9BXB4.
    PRIDEi Q9BXB4.

    Protocols and materials databases

    DNASUi 114885.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296220 ; ENSP00000296220 ; ENSG00000144909 .
    GeneIDi 114885.
    KEGGi hsa:114885.
    UCSCi uc003eic.3. human.

    Organism-specific databases

    CTDi 114885.
    GeneCardsi GC03M125278.
    HGNCi HGNC:16397. OSBPL11.
    HPAi HPA039144.
    MIMi 606739. gene.
    neXtProti NX_Q9BXB4.
    PharmGKBi PA32825.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262374.
    HOGENOMi HOG000233871.
    HOVERGENi HBG053376.
    InParanoidi Q9BXB4.
    OMAi VTNHAPL.
    OrthoDBi EOG7PK8ZG.
    PhylomeDBi Q9BXB4.
    TreeFami TF312807.

    Miscellaneous databases

    ChiTaRSi OSBPL11. human.
    EvolutionaryTracei Q9BXB4.
    GeneWikii OSBPL11.
    GenomeRNAii 114885.
    NextBioi 79389.
    PROi Q9BXB4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BXB4.
    Bgeei Q9BXB4.
    CleanExi HS_OSBPL11.
    Genevestigatori Q9BXB4.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR000648. Oxysterol-bd.
    IPR018494. Oxysterol-bd_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    PANTHERi PTHR10972. PTHR10972. 1 hit.
    Pfami PF01237. Oxysterol_BP. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    [Graphical view ]
    PROSITEi PS01013. OSBP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A family of 12 human genes containing oxysterol-binding domains."
      Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.
      Genomics 78:185-196(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Thymus.
    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].
      Tissue: Skin.
    5. "The OSBP-related protein family in humans."
      Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C., Staels B., Ikonen E., Olkkonen V.M.
      J. Lipid Res. 42:1203-1213(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-315.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; SER-181 AND SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; TYR-62; SER-172; SER-174 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at the Golgi-late endosome interface."
      Zhou Y., Li S., Mayranpaa M.I., Zhong W., Back N., Yan D., Olkkonen V.M.
      Exp. Cell Res. 316:3304-3316(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; SER-181 AND SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Solution structure of the PH domain of oxysterol binding protein-related protein 11 from human."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 59-165.
    18. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-184.

    Entry informationi

    Entry nameiOSB11_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXB4
    Secondary accession number(s): A8K9I7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 11, 2002
    Last sequence update: February 11, 2002
    Last modified: October 1, 2014
    This is version 114 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 3
      Human chromosome 3: 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