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Q13438

- OS9_HUMAN

UniProt

Q13438 - OS9_HUMAN

Protein

Protein OS-9

Gene

OS9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei130 – 1301Carbohydrate
    Binding sitei182 – 1821Carbohydrate
    Binding sitei188 – 1881Carbohydrate
    Binding sitei212 – 2121Carbohydrate
    Binding sitei218 – 2181Carbohydrate

    GO - Molecular functioni

    1. glycoprotein binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    2. protein retention in ER lumen Source: UniProtKB
    3. protein targeting Source: Ensembl
    4. protein ubiquitination Source: UniProtKB
    5. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    6. response to endoplasmic reticulum stress Source: UniProtKB

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein OS-9
    Alternative name(s):
    Amplified in osteosarcoma 9
    Gene namesi
    Name:OS9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:16994. OS9.

    Subcellular locationi

    Endoplasmic reticulum lumen 3 Publications

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB
    2. Hrd1p ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi188 – 1881R → A: Loss of glycan-binding activity and partial inhibition of ERAD of the misfolded glycoprotein NHK (PubMed:19346256). Reduced interaction with SEL1L (PubMed:18264092) not confirmed in (PubMed:19346256). 3 Publications

    Organism-specific databases

    PharmGKBiPA164724245.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 667642Protein OS-9PRO_0000021951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi110 ↔ 123
    Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi181 ↔ 216
    Disulfide bondi196 ↔ 228

    Post-translational modificationi

    Intramolecular disulfide bonds.
    Isoform 1 and isoform 2 are N-glycosylated.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ13438.
    PaxDbiQ13438.
    PRIDEiQ13438.

    PTM databases

    PhosphoSiteiQ13438.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Found as well in all tumor cell lines analyzed, amplified in sarcomas. Highly expressed in osteosarcoma SJSA-1 and rhabdomyosarcoma Rh30 cell lines. Isoform 2 is the major isoform detected in all cell types examined.

    Inductioni

    Up-regulated in response to endoplasmic reticulum stress (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ13438.
    BgeeiQ13438.
    GenevestigatoriQ13438.

    Organism-specific databases

    HPAiCAB011518.
    HPA013694.

    Interactioni

    Subunit structurei

    Probably part of the HRD1 ubiquitin ligase complex composed at least of SYVN1/HRD1 and SEL1L with which it interacts directly. Through this complex it may interact with ERLEC1 and HSPA5. Interacts with DERL2. Interacts with HSP90B1 and CREB3.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EGLN1Q9GZT94EBI-725454,EBI-1174818
    HIF1AQ166659EBI-725454,EBI-447269

    Protein-protein interaction databases

    BioGridi116156. 46 interactions.
    DIPiDIP-37493N.
    IntActiQ13438. 24 interactions.
    MINTiMINT-1187753.
    STRINGi9606.ENSP00000318165.

    Structurei

    Secondary structure

    1
    667
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi111 – 1155
    Beta strandi118 – 1236
    Turni124 – 1263
    Beta strandi127 – 1315
    Beta strandi143 – 15513
    Beta strandi169 – 1768
    Turni182 – 1843
    Beta strandi189 – 1968
    Beta strandi206 – 2149
    Beta strandi217 – 2248
    Helixi225 – 2273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3AIHX-ray2.10A/B108-229[»]
    ProteinModelPortaliQ13438.
    SMRiQ13438. Positions 109-228.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13438.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini108 – 17871PRKCSHAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi414 – 42916Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the OS-9 family.Curated
    Contains 1 PRKCSH domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG309879.
    HOGENOMiHOG000293348.
    HOVERGENiHBG000974.
    InParanoidiQ13438.
    KOiK10088.
    OMAiRYHSQTY.
    OrthoDBiEOG7R8315.
    PhylomeDBiQ13438.
    TreeFamiTF314309.

    Family and domain databases

    Gene3Di2.70.130.10. 1 hit.
    InterProiIPR009011. Man6P_isomerase_rcpt-bd_dom.
    IPR012913. PRKCSH.
    [Graphical view]
    PfamiPF07915. PRKCSH. 1 hit.
    [Graphical view]
    SUPFAMiSSF50911. SSF50911. 1 hit.

    Sequences (8)i

    Sequence statusi: Complete.

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

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13438-1) [UniParc]FASTAAdd to Basket

    Also known as: OS-9-1

    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

    MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV    50
    MGGQSQSSDV VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE 100
    LLSPMRDAPC LLKTKDWWTY EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS 150
    AFDWDDETAK ASKQHRLKRY HSQTYGNGSK CDLNGRPREA EVRFLCDEGA 200
    GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA PQAILCHPSL 250
    QPEEYMAYVQ RQADSKQYGD KIIEELQDLG PQVWSETKSG VAPQKMAGAS 300
    PTKDDSKDSD FWKMLNEPED QAPGGEEVPA EEQDPSPEAA DSASGAPNDF 350
    QNNVQVKVIR SPADLIRFIE ELKGGTKKGK PNIGQEQPVD DAAEVPQREP 400
    EKERGDPERQ REMEEEEDED EDEDEDEDER QLLGEFEKEL EGILLPSDRD 450
    RLRSEVKAGM ERELENIIQE TEKELDPDGL KKESERDRAM LALTSTLNKL 500
    IKRLEEKQSP ELVKKHKKKR VVPKKPPPSP QPTEEDPEHR VRVRVTKLRL 550
    GGPNQDLTVL EMKRENPQLK QIEGLVKELL EREGLTAAGK IEIKIVRPWA 600
    EGTEEGARWL TDEDTRNLKE IFFNILVPGA EEAQKERQRQ KELESNYRRV 650
    WGSPGGEGTG DLDEFDF 667

    Note: Major isoform.

    Length:667
    Mass (Da):75,562
    Last modified:November 1, 1996 - v1
    Checksum:i65BA3F66CEC58756
    GO
    Isoform 2 (identifier: Q13438-2) [UniParc]FASTAAdd to Basket

    Also known as: OS-9-2

    The sequence of this isoform differs from the canonical sequence as follows:
         534-588: Missing.

    Note: Major isoform.

    Show »
    Length:612
    Mass (Da):69,246
    Checksum:i1FD06F7B23101015
    GO
    Isoform 3 (identifier: Q13438-3) [UniParc]FASTAAdd to Basket

    Also known as: OS-9-3

    The sequence of this isoform differs from the canonical sequence as follows:
         456-470: Missing.
         534-588: Missing.

    Show »
    Length:597
    Mass (Da):67,505
    Checksum:i7D00C1EA449B3DA1
    GO
    Isoform 4 (identifier: Q13438-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         456-470: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:652
    Mass (Da):73,821
    Checksum:i7D44F2347B609055
    GO
    Isoform 5 (identifier: Q13438-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         161-193: Missing.
         263-263: A → AV
         534-588: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:580
    Mass (Da):65,520
    Checksum:iBE4EEA80CF8EA076
    GO
    Isoform 6 (identifier: Q13438-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         142-193: Missing.
         534-588: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:560
    Mass (Da):63,155
    Checksum:iEBF3F8A812BDAF60
    GO
    Isoform 7 (identifier: Q13438-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         263-263: A → AV
         534-588: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:613
    Mass (Da):69,346
    Checksum:i353DE17278AB9546
    GO
    Isoform 8 (identifier: Q13438-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         55-113: Missing.
         456-470: Missing.
         534-588: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:538
    Mass (Da):60,847
    Checksum:i30188F4A2A67AD8E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71L → V in CAG33072. 1 PublicationCurated
    Sequence conflicti194 – 1941F → V in BAG64798. (PubMed:14702039)Curated
    Sequence conflicti371 – 3711E → G in BAG56939. (PubMed:14702039)Curated
    Sequence conflicti497 – 4971L → F in BAG64798. (PubMed:14702039)Curated
    Sequence conflicti522 – 5221V → I in BAG60733. (PubMed:14702039)Curated
    Sequence conflicti653 – 6531S → P in BAG56939. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti305 – 3051D → N.1 Publication
    Corresponds to variant rs141986192 [ dbSNP | Ensembl ].
    VAR_069062
    Natural varianti398 – 3981R → W.
    Corresponds to variant rs1804598 [ dbSNP | Ensembl ].
    VAR_011897
    Natural varianti454 – 4541S → L.
    Corresponds to variant rs34764811 [ dbSNP | Ensembl ].
    VAR_034364

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei55 – 11359Missing in isoform 8. 1 PublicationVSP_046770Add
    BLAST
    Alternative sequencei142 – 19352Missing in isoform 6. 1 PublicationVSP_046001Add
    BLAST
    Alternative sequencei161 – 19333Missing in isoform 5. 1 PublicationVSP_044701Add
    BLAST
    Alternative sequencei263 – 2631A → AV in isoform 5 and isoform 7. 1 PublicationVSP_044702
    Alternative sequencei456 – 47015Missing in isoform 3, isoform 4 and isoform 8. 1 PublicationVSP_004352Add
    BLAST
    Alternative sequencei534 – 58855Missing in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8. 3 PublicationsVSP_004353Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41635 mRNA. Translation: AAB06495.1.
    AB002805 Genomic DNA. Translation: BAA24362.1.
    AB002806 mRNA. Translation: BAA24363.1.
    AK291374 mRNA. Translation: BAF84063.1.
    AK293435 mRNA. Translation: BAG56939.1.
    AK296770 mRNA. Translation: BAG59349.1.
    AK298532 mRNA. Translation: BAG60733.1.
    AK303858 mRNA. Translation: BAG64798.1.
    CR456791 mRNA. Translation: CAG33072.1.
    AC025165 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97045.1.
    CH471054 Genomic DNA. Translation: EAW97046.1.
    CH471054 Genomic DNA. Translation: EAW97047.1.
    BC000532 mRNA. Translation: AAH00532.1.
    BC007254 mRNA. Translation: AAH07254.1.
    BC023513 mRNA. Translation: AAH23513.2.
    U81031 Genomic DNA. Translation: AAC39523.2.
    CCDSiCCDS31843.1. [Q13438-1]
    CCDS31844.1. [Q13438-2]
    CCDS31845.1. [Q13438-4]
    CCDS31846.1. [Q13438-3]
    CCDS58246.1. [Q13438-6]
    CCDS58247.1. [Q13438-7]
    CCDS58248.1. [Q13438-5]
    CCDS58249.1. [Q13438-8]
    PIRiJC5889.
    RefSeqiNP_001017956.1. NM_001017956.2. [Q13438-2]
    NP_001017957.1. NM_001017957.2. [Q13438-3]
    NP_001017958.1. NM_001017958.2. [Q13438-4]
    NP_001248349.1. NM_001261420.1. [Q13438-7]
    NP_001248350.1. NM_001261421.1. [Q13438-5]
    NP_001248351.1. NM_001261422.1. [Q13438-6]
    NP_001248352.1. NM_001261423.1. [Q13438-8]
    NP_006803.1. NM_006812.3. [Q13438-1]
    UniGeneiHs.527861.

    Genome annotation databases

    GeneIDi10956.
    KEGGihsa:10956.
    UCSCiuc001spj.3. human. [Q13438-1]
    uc001spk.3. human. [Q13438-4]
    uc001spn.3. human.

    Polymorphism databases

    DMDMi3024310.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41635 mRNA. Translation: AAB06495.1 .
    AB002805 Genomic DNA. Translation: BAA24362.1 .
    AB002806 mRNA. Translation: BAA24363.1 .
    AK291374 mRNA. Translation: BAF84063.1 .
    AK293435 mRNA. Translation: BAG56939.1 .
    AK296770 mRNA. Translation: BAG59349.1 .
    AK298532 mRNA. Translation: BAG60733.1 .
    AK303858 mRNA. Translation: BAG64798.1 .
    CR456791 mRNA. Translation: CAG33072.1 .
    AC025165 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97045.1 .
    CH471054 Genomic DNA. Translation: EAW97046.1 .
    CH471054 Genomic DNA. Translation: EAW97047.1 .
    BC000532 mRNA. Translation: AAH00532.1 .
    BC007254 mRNA. Translation: AAH07254.1 .
    BC023513 mRNA. Translation: AAH23513.2 .
    U81031 Genomic DNA. Translation: AAC39523.2 .
    CCDSi CCDS31843.1. [Q13438-1 ]
    CCDS31844.1. [Q13438-2 ]
    CCDS31845.1. [Q13438-4 ]
    CCDS31846.1. [Q13438-3 ]
    CCDS58246.1. [Q13438-6 ]
    CCDS58247.1. [Q13438-7 ]
    CCDS58248.1. [Q13438-5 ]
    CCDS58249.1. [Q13438-8 ]
    PIRi JC5889.
    RefSeqi NP_001017956.1. NM_001017956.2. [Q13438-2 ]
    NP_001017957.1. NM_001017957.2. [Q13438-3 ]
    NP_001017958.1. NM_001017958.2. [Q13438-4 ]
    NP_001248349.1. NM_001261420.1. [Q13438-7 ]
    NP_001248350.1. NM_001261421.1. [Q13438-5 ]
    NP_001248351.1. NM_001261422.1. [Q13438-6 ]
    NP_001248352.1. NM_001261423.1. [Q13438-8 ]
    NP_006803.1. NM_006812.3. [Q13438-1 ]
    UniGenei Hs.527861.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AIH X-ray 2.10 A/B 108-229 [» ]
    ProteinModelPortali Q13438.
    SMRi Q13438. Positions 109-228.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116156. 46 interactions.
    DIPi DIP-37493N.
    IntActi Q13438. 24 interactions.
    MINTi MINT-1187753.
    STRINGi 9606.ENSP00000318165.

    PTM databases

    PhosphoSitei Q13438.

    Polymorphism databases

    DMDMi 3024310.

    Proteomic databases

    MaxQBi Q13438.
    PaxDbi Q13438.
    PRIDEi Q13438.

    Protocols and materials databases

    DNASUi 10956.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 10956.
    KEGGi hsa:10956.
    UCSCi uc001spj.3. human. [Q13438-1 ]
    uc001spk.3. human. [Q13438-4 ]
    uc001spn.3. human.

    Organism-specific databases

    CTDi 10956.
    GeneCardsi GC12P058088.
    HGNCi HGNC:16994. OS9.
    HPAi CAB011518.
    HPA013694.
    MIMi 609677. gene.
    neXtProti NX_Q13438.
    PharmGKBi PA164724245.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309879.
    HOGENOMi HOG000293348.
    HOVERGENi HBG000974.
    InParanoidi Q13438.
    KOi K10088.
    OMAi RYHSQTY.
    OrthoDBi EOG7R8315.
    PhylomeDBi Q13438.
    TreeFami TF314309.

    Miscellaneous databases

    ChiTaRSi OS9. human.
    EvolutionaryTracei Q13438.
    GeneWikii OS9_(gene).
    GenomeRNAii 10956.
    NextBioi 35464261.
    PROi Q13438.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13438.
    Bgeei Q13438.
    Genevestigatori Q13438.

    Family and domain databases

    Gene3Di 2.70.130.10. 1 hit.
    InterProi IPR009011. Man6P_isomerase_rcpt-bd_dom.
    IPR012913. PRKCSH.
    [Graphical view ]
    Pfami PF07915. PRKCSH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50911. SSF50911. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence analysis of a gene (OS-9) ubiquitously expressed in human tissues and amplified in sarcomas."
      Su Y.A., Hutter C.M., Trent J.M., Meltzer P.S.
      Mol. Carcinog. 15:270-275(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Genomic organization of the OS-9 gene amplified in human sarcomas."
      Kimura Y., Nakazawa M., Tsuchiya N., Asakawa S., Shimizu N., Yamada M.
      J. Biochem. 122:1190-1195(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    3. "Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines."
      Kimura Y., Nakazawa M., Yamada M.
      J. Biochem. 123:876-882(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), CHARACTERIZATION, ALTERNATIVE SPLICING (ISOFORMS 2 AND 3).
      Tissue: Promyelocytic leukemia.
    4. "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 2; 4; 5; 6 AND 8), VARIANT ASN-305.
      Tissue: Brain, Tongue and Trachea.
    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] (ISOFORM 2).
    6. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Muscle.
    9. "Transcript mapping in a 46-kb sequenced region at the core of 12q13.3 amplification in human cancers."
      Elkahloun A.G., Krizman D.B., Wang Z., Hofmann T.A., Roe B.A., Meltzer P.S.
      Genomics 42:295-301(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-667.
    10. "OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum."
      Wang Y., Fu X., Gaiser S., Koettgen M., Kramer-Zucker A., Walz G., Wegierski T.
      J. Biol. Chem. 282:36561-36570(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRPV4 MATURATION.
    11. "A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal."
      Bernasconi R., Pertel T., Luban J., Molinari M.
      J. Biol. Chem. 283:16446-16454(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, DISULFIDE BONDS, GLYCOSYLATION, INDUCTION, MUTAGENESIS OF ARG-188.
    12. "Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP."
      Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.
      J. Biol. Chem. 283:20914-20924(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERLEC1; HSPA5; SEL1L AND SYVN1.
    13. "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD."
      Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.
      Nat. Cell Biol. 10:272-282(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSP90B1; SEL1L AND SYVN1, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ARG-188.
    14. "Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans."
      Hosokawa N., Kamiya Y., Kamiya D., Kato K., Nagata K.
      J. Biol. Chem. 284:17061-17068(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A LECTIN, MUTAGENESIS OF ARG-188.
    15. "Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins."
      Alcock F., Swanton E.
      J. Mol. Biol. 385:1032-1042(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MISFOLDED GLYCOPROTEIN UBIQUITINATION, SUBCELLULAR LOCATION, GLYCOSYLATION, INTERACTION WITH DERL2; HRD1 AND SEL1L, INDUCTION BY ER STRESS.
    16. "DC-STAMP interacts with ER-resident transcription factor LUMAN which becomes activated during DC maturation."
      Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.A., Looman M.W., Hendriks I.A., Jansen B.J., Adema G.J.
      Mol. Immunol. 47:1963-1973(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CREB3.
    17. "Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation."
      Satoh T., Chen Y., Hu D., Hanashima S., Yamamoto K., Yamaguchi Y.
      Mol. Cell 40:905-916(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 108-229 IN COMPLEX WITH MANNOPENTAOSE, FUNCTION, DISULFIDE BONDS.

    Entry informationi

    Entry nameiOS9_HUMAN
    AccessioniPrimary (citable) accession number: Q13438
    Secondary accession number(s): A6NDD1
    , A6NFR7, A6NLB2, A8K5Q9, B4DE28, B4DPX1, B4E1I6, E7ENT8, E7EW91, F8VUH2, G3XA88, O00579, Q6IBL2, Q8IZ58, Q9BW99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 124 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 12
      Human chromosome 12: 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