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Q8IVI9

- NOSTN_HUMAN

UniProt

Q8IVI9 - NOSTN_HUMAN

Protein

Nostrin

Gene

NOSTRIN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Multivalent adapter protein which may decrease NOS3 activity by inducing its translocation away from the plasma membrane.3 Publications

    GO - Molecular functioni

    1. DNA binding Source: Ensembl
    2. protein binding Source: IntAct

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. negative regulation of transcription, DNA-templated Source: Ensembl
    3. nitric oxide metabolic process Source: Reactome
    4. regulation of nitric-oxide synthase activity Source: Reactome
    5. signal transduction Source: InterPro
    6. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Endocytosis

    Enzyme and pathway databases

    ReactomeiREACT_12541. NOSTRIN mediated eNOS trafficking.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nostrin
    Alternative name(s):
    BM247 homolog
    Nitric oxide synthase traffic inducer
    Nitric oxide synthase trafficker
    eNOS-trafficking inducer
    Gene namesi
    Name:NOSTRIN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:20203. NOSTRIN.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. endocytic vesicle membrane Source: Reactome
    3. nucleus Source: Ensembl
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134992787.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 506506NostrinPRO_0000289089Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei479 – 4791PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IVI9.
    PaxDbiQ8IVI9.
    PRIDEiQ8IVI9.

    PTM databases

    PhosphoSiteiQ8IVI9.

    Expressioni

    Tissue specificityi

    Expressed at highest levels in heart, kidney, placenta and lung, and at lowest levels in brain, thymus and spleen. Present in vascular endothelial cells and placenta. Over-expressed in placenta from women with pre-eclampsia (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ8IVI9.
    BgeeiQ8IVI9.
    CleanExiHS_NOSTRIN.
    GenevestigatoriQ8IVI9.

    Organism-specific databases

    HPAiHPA044384.

    Interactioni

    Subunit structurei

    Homotrimer. Interacts with DAB2 By similarity. Interacts with NOS3, DNM2, WASL and CAV1.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DNM1Q051933EBI-1391643,EBI-713135
    FGFR1P113625EBI-1391643,EBI-1028277
    NOS3P294749EBI-1391643,EBI-1391623
    WaslO088163EBI-1391643,EBI-6142604From a different organism.

    Protein-protein interaction databases

    BioGridi125446. 4 interactions.
    IntActiQ8IVI9. 14 interactions.
    STRINGi9606.ENSP00000318921.

    Structurei

    Secondary structure

    1
    506
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi441 – 4477
    Beta strandi464 – 4696
    Beta strandi472 – 4743
    Beta strandi476 – 4827
    Beta strandi484 – 4874
    Beta strandi492 – 4976

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YUNNMR-A441-506[»]
    ProteinModelPortaliQ8IVI9.
    SMRiQ8IVI9. Positions 434-506.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IVI9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6666FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini438 – 49760SH3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili160 – 22263Sequence AnalysisAdd
    BLAST

    Domaini

    The SH3 domain mediates interaction with NOS3, DNM2 and WASL.
    The FCH domain is necessary for membrane targeting.

    Sequence similaritiesi

    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG266189.
    HOGENOMiHOG000113830.
    HOVERGENiHBG101730.
    InParanoidiQ8IVI9.
    OMAiHIREMLL.
    PhylomeDBiQ8IVI9.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR011072. HR1_rho-bd.
    IPR028535. Nostrin.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR14167:SF22. PTHR14167:SF22. 1 hit.
    PfamiPF00611. FCH. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF46585. SSF46585. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IVI9-1) [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

    MRDPLTDCPY NKVYKNLKEF SQNGENFCKQ VTSVLQQRAN LEISYAKGLQ    50
    KLASKLSKAL QNTRKSCVSS AWAWASEGMK STADLHQKLG KAIELEAIKP 100
    TYQVLNVQEK KRKSLDNEVE KTANLVISNW NQQIKAKKKL MVSTKKHEAL 150
    FQLVESSKQS MTEKEKRKLL NKLTKSTEKL EKEDENYYQK NMAGYSTRLK 200
    WENTLENCYQ SILELEKERI QLLCNNLNQY SQHISLFGQT LTTCHTQIHC 250
    AISKIDIEKD IQAVMEETAI LSTENKSEFL LTDYFEEDPN SAMDKERRKS 300
    LLKPKLLRLQ RDIEKASKDK EGLERMLKTY SSTSSFSDAK SQKDTAALMD 350
    ENNLKLDLLE ANSYKLSSML AELEQRPQPS HPCSNSIFRW REKEHTHSYV 400
    KISRPFLMKR LENIVSKASS GGQSNPGSST PAPGAAQLSS RLCKALYSFQ 450
    ARQDDELNLE KGDIVIIHEK KEGGWWFGSL NGKKGHFPAA YVEELPSNAG 500
    NTATKA 506
    Length:506
    Mass (Da):57,660
    Last modified:January 11, 2011 - v2
    Checksum:iDC9A6DF5B9C2AED0
    GO
    Isoform 2 (identifier: Q8IVI9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         38-65: Missing.

    Show »
    Length:478
    Mass (Da):54,547
    Checksum:iE8E6E3B37569F432
    GO
    Isoform 3 (identifier: Q8IVI9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-78: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:428
    Mass (Da):48,876
    Checksum:i8819706D71DAC60C
    GO
    Isoform 4 (identifier: Q8IVI9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         209-209: Y → YQVTHSICLYAFWVKRAWGKCVSDLRYQDTFLPGNLPPLWFGYDIVKRLIMRLCSVCL

    Note: No experimental confirmation available.Curated

    Show »
    Length:563
    Mass (Da):64,364
    Checksum:i6FE667B285DD4D54
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti225 – 2251N → D in BAG52717. (PubMed:14702039)Curated
    Isoform 4 (identifier: Q8IVI9-4)
    Sequence conflicti238 – 2381T → I in BAG52717. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti473 – 4731G → E.4 Publications
    Corresponds to variant rs479661 [ dbSNP | Ensembl ].
    VAR_032569

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7878Missing in isoform 3. 1 PublicationVSP_025884Add
    BLAST
    Alternative sequencei38 – 6528Missing in isoform 2. 1 PublicationVSP_025885Add
    BLAST
    Alternative sequencei209 – 2091Y → YQVTHSICLYAFWVKRAWGK CVSDLRYQDTFLPGNLPPLW FGYDIVKRLIMRLCSVCL in isoform 4. 1 PublicationVSP_044995

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ532842 mRNA. Translation: CAD58724.1.
    DQ402497 mRNA. Translation: ABD62889.1.
    AK002203 mRNA. Translation: BAE46614.1.
    AK093444 mRNA. Translation: BAG52717.1.
    AK290254 mRNA. Translation: BAF82943.1.
    AC069137 Genomic DNA. Translation: AAY24097.1.
    AC009475 Genomic DNA. No translation available.
    BC014189 mRNA. Translation: AAH14189.1.
    BC093072 mRNA. Translation: AAH93072.1.
    AL550371 mRNA. No translation available.
    CCDSiCCDS42771.1. [Q8IVI9-1]
    CCDS42772.1. [Q8IVI9-3]
    CCDS54415.1. [Q8IVI9-4]
    CCDS54416.1. [Q8IVI9-2]
    RefSeqiNP_001034813.2. NM_001039724.3. [Q8IVI9-1]
    NP_001165102.1. NM_001171631.1. [Q8IVI9-4]
    NP_001165103.1. NM_001171632.1. [Q8IVI9-2]
    NP_443178.2. NM_052946.3. [Q8IVI9-3]
    UniGeneiHs.189780.

    Genome annotation databases

    EnsembliENST00000317647; ENSP00000318921; ENSG00000163072. [Q8IVI9-1]
    ENST00000397206; ENSP00000380390; ENSG00000163072. [Q8IVI9-3]
    ENST00000397209; ENSP00000380392; ENSG00000163072. [Q8IVI9-2]
    ENST00000421711; ENSP00000401316; ENSG00000163072. [Q8IVI9-2]
    ENST00000444448; ENSP00000394051; ENSG00000163072. [Q8IVI9-4]
    ENST00000445023; ENSP00000404413; ENSG00000163072. [Q8IVI9-3]
    ENST00000458381; ENSP00000402140; ENSG00000163072. [Q8IVI9-4]
    GeneIDi115677.
    KEGGihsa:115677.
    UCSCiuc002uef.3. human.
    uc002ueg.3. human. [Q8IVI9-1]
    uc010fpu.3. human. [Q8IVI9-2]

    Polymorphism databases

    DMDMi317373401.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ532842 mRNA. Translation: CAD58724.1 .
    DQ402497 mRNA. Translation: ABD62889.1 .
    AK002203 mRNA. Translation: BAE46614.1 .
    AK093444 mRNA. Translation: BAG52717.1 .
    AK290254 mRNA. Translation: BAF82943.1 .
    AC069137 Genomic DNA. Translation: AAY24097.1 .
    AC009475 Genomic DNA. No translation available.
    BC014189 mRNA. Translation: AAH14189.1 .
    BC093072 mRNA. Translation: AAH93072.1 .
    AL550371 mRNA. No translation available.
    CCDSi CCDS42771.1. [Q8IVI9-1 ]
    CCDS42772.1. [Q8IVI9-3 ]
    CCDS54415.1. [Q8IVI9-4 ]
    CCDS54416.1. [Q8IVI9-2 ]
    RefSeqi NP_001034813.2. NM_001039724.3. [Q8IVI9-1 ]
    NP_001165102.1. NM_001171631.1. [Q8IVI9-4 ]
    NP_001165103.1. NM_001171632.1. [Q8IVI9-2 ]
    NP_443178.2. NM_052946.3. [Q8IVI9-3 ]
    UniGenei Hs.189780.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YUN NMR - A 441-506 [» ]
    ProteinModelPortali Q8IVI9.
    SMRi Q8IVI9. Positions 434-506.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125446. 4 interactions.
    IntActi Q8IVI9. 14 interactions.
    STRINGi 9606.ENSP00000318921.

    PTM databases

    PhosphoSitei Q8IVI9.

    Polymorphism databases

    DMDMi 317373401.

    Proteomic databases

    MaxQBi Q8IVI9.
    PaxDbi Q8IVI9.
    PRIDEi Q8IVI9.

    Protocols and materials databases

    DNASUi 115677.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317647 ; ENSP00000318921 ; ENSG00000163072 . [Q8IVI9-1 ]
    ENST00000397206 ; ENSP00000380390 ; ENSG00000163072 . [Q8IVI9-3 ]
    ENST00000397209 ; ENSP00000380392 ; ENSG00000163072 . [Q8IVI9-2 ]
    ENST00000421711 ; ENSP00000401316 ; ENSG00000163072 . [Q8IVI9-2 ]
    ENST00000444448 ; ENSP00000394051 ; ENSG00000163072 . [Q8IVI9-4 ]
    ENST00000445023 ; ENSP00000404413 ; ENSG00000163072 . [Q8IVI9-3 ]
    ENST00000458381 ; ENSP00000402140 ; ENSG00000163072 . [Q8IVI9-4 ]
    GeneIDi 115677.
    KEGGi hsa:115677.
    UCSCi uc002uef.3. human.
    uc002ueg.3. human. [Q8IVI9-1 ]
    uc010fpu.3. human. [Q8IVI9-2 ]

    Organism-specific databases

    CTDi 115677.
    GeneCardsi GC02P169643.
    HGNCi HGNC:20203. NOSTRIN.
    HPAi HPA044384.
    MIMi 607496. gene.
    neXtProti NX_Q8IVI9.
    PharmGKBi PA134992787.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266189.
    HOGENOMi HOG000113830.
    HOVERGENi HBG101730.
    InParanoidi Q8IVI9.
    OMAi HIREMLL.
    PhylomeDBi Q8IVI9.

    Enzyme and pathway databases

    Reactomei REACT_12541. NOSTRIN mediated eNOS trafficking.

    Miscellaneous databases

    EvolutionaryTracei Q8IVI9.
    GenomeRNAii 115677.
    NextBioi 79640.
    PROi Q8IVI9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IVI9.
    Bgeei Q8IVI9.
    CleanExi HS_NOSTRIN.
    Genevestigatori Q8IVI9.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR011072. HR1_rho-bd.
    IPR028535. Nostrin.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR14167:SF22. PTHR14167:SF22. 1 hit.
    Pfami PF00611. FCH. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46585. SSF46585. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NOSTRIN: a protein modulating nitric oxide release and subcellular distribution of endothelial nitric oxide synthase."
      Zimmermann K., Opitz N., Dedio J., Renne C., Mueller-Esterl W., Oess S.
      Proc. Natl. Acad. Sci. U.S.A. 99:17167-17172(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH NOS3, SUBCELLULAR LOCATION, FUNCTION, VARIANT GLU-473.
      Tissue: Placenta.
    2. "Molecular characterization of an alternatively spliced variant of human NOSTRIN."
      Beese M., Kirsch T.
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLU-473.
    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 4), VARIANT GLU-473.
      Tissue: Colon, Placenta and Testis.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORMS 1 AND 3), VARIANT GLU-473.
      Tissue: Placenta and Thyroid.
    6. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-304.
      Tissue: Placenta.
    7. "Altered gene expression in cerebral capillaries of stroke-prone spontaneously hypertensive rats."
      Kirsch T., Wellner M., Luft F.C., Haller H., Lippoldt A.
      Brain Res. 910:106-115(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    8. "Expression of endothelial nitric oxide synthase traffic inducer in the placentas of women with pre-eclampsia."
      Xiang W., Chen H., Xu X., Zhang M., Jiang R.
      Int. J. Gynecol. Obstet. 89:103-107(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS."
      Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W., Schilling K.
      J. Cell Sci. 118:5059-5069(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH DNM2 AND WASL, SUBCELLULAR LOCATION, FUNCTION.
    10. "FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN."
      Icking A., Schilling K., Wiesenthal A., Opitz N., Mueller-Esterl W.
      FEBS Lett. 580:223-228(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN."
      Schilling K., Opitz N., Wiesenthal A., Oess S., Tikkanen R., Mueller-Esterl W., Icking A.
      Mol. Biol. Cell 17:3870-3880(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAV1, FUNCTION.
    12. "Solution structure of the SH3 domain of human nostrin."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 439-506.

    Entry informationi

    Entry nameiNOSTN_HUMAN
    AccessioniPrimary (citable) accession number: Q8IVI9
    Secondary accession number(s): A8K2I9
    , B3KSF5, E7EPT9, Q27HG3, Q53S62, Q96CJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 116 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 2
      Human chromosome 2: 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