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O95149

- SPN1_HUMAN

UniProt

O95149 - SPN1_HUMAN

Protein

Snurportin-1

Gene

SNUPN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs.1 Publication

    GO - Molecular functioni

    1. protein transporter activity Source: InterPro
    2. RNA cap binding Source: ProtInc

    GO - Biological processi

    1. gene expression Source: Reactome
    2. ncRNA metabolic process Source: Reactome
    3. protein import into nucleus Source: InterPro
    4. RNA metabolic process Source: Reactome
    5. snRNA import into nucleus Source: InterPro
    6. spliceosomal snRNP assembly Source: Reactome

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_11066. snRNP Assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Snurportin-1
    Alternative name(s):
    RNA U transporter 1
    Gene namesi
    Name:SNUPN
    Synonyms:RNUT1, SPN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:14245. SNUPN.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor importin beta. It is re-exported to the cytoplasm by the XPO1-dependent nuclear export receptor pathway.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nuclear pore Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi27 – 271R → A: Abolishes interaction with KPNB1 and m3G-cap U1 snRNP import receptor activity. 1 Publication
    Mutagenesisi107 – 1071W → A: Reduces binding to m3G-cap structure, interaction with XPO1 and snRNP import receptor activity. 2 Publications
    Mutagenesisi203 – 2075FRFYW → A: Reduces binding to m3G-cap structure.
    Mutagenesisi276 – 2761W → A: Reduces binding to m3G-cap structure, interaction with XPO1 and snRNP import receptor activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA34611.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 360360Snurportin-1PRO_0000191071Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei75 – 751Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95149.
    PaxDbiO95149.
    PeptideAtlasiO95149.
    PRIDEiO95149.

    PTM databases

    PhosphoSiteiO95149.

    Expressioni

    Gene expression databases

    ArrayExpressiO95149.
    BgeeiO95149.
    CleanExiHS_SNUPN.
    GenevestigatoriO95149.

    Organism-specific databases

    HPAiCAB005004.

    Interactioni

    Subunit structurei

    Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Component of a nuclear export receptor complex composed of KPNB1, Ran, SNUPN and XPO1. Found in a trimeric export complex with SNUPN, Ran and XPO1. Interacts with DDX20, IPO7, KPNB1, SMN1, SNRPB and XPO1. Interacts directly with XPO1. Its interaction with XPO1 and binding to m3G-cap U snRNPs appears to be mutually exclusive.4 Publications

    Protein-protein interaction databases

    BioGridi115384. 16 interactions.
    DIPiDIP-48513N.
    IntActiO95149. 11 interactions.
    MINTiMINT-1378592.
    STRINGi9606.ENSP00000309831.

    Structurei

    Secondary structure

    360
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 1010
    Beta strandi21 – 233
    Helixi28 – 303
    Helixi42 – 6019
    Turni61 – 633
    Beta strandi97 – 1004
    Beta strandi102 – 1076
    Helixi115 – 1184
    Beta strandi119 – 13517
    Beta strandi138 – 1425
    Beta strandi144 – 1463
    Beta strandi148 – 1525
    Beta strandi155 – 1595
    Beta strandi161 – 1633
    Beta strandi165 – 1673
    Beta strandi170 – 1778
    Helixi178 – 1803
    Beta strandi182 – 19110
    Helixi201 – 21111
    Turni212 – 2143
    Turni216 – 2194
    Beta strandi225 – 2317
    Beta strandi234 – 2363
    Helixi239 – 2468
    Beta strandi254 – 26310
    Beta strandi268 – 27710
    Helixi279 – 2813
    Helixi282 – 2865
    Beta strandi291 – 2933
    Helixi294 – 2963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XK5X-ray2.40A97-300[»]
    2P8QX-ray2.35B25-64[»]
    2Q5DX-ray3.20C/D25-64[»]
    2QNAX-ray2.84B1-66[»]
    3GB8X-ray2.90B1-328[»]
    3GJXX-ray2.50B/E1-360[»]
    3LWWX-ray3.15B/D25-64[»]
    3NBYX-ray3.42B/E15-360[»]
    3NBZX-ray2.80B/E15-360[»]
    3NC0X-ray2.90B/E15-360[»]
    ProteinModelPortaliO95149.
    SMRiO95149. Positions 12-360.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95149.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 7363IBBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 159159Necessary for interaction with XPO1Add
    BLAST
    Regioni1 – 6565Necessary for interaction with KPNB1 and m3G-cap U1 and U5 snRNP import receptor activityAdd
    BLAST
    Regioni208 – 328121Necessary for binding to the m3G-cap structureAdd
    BLAST

    Sequence similaritiesi

    Belongs to the snurportin family.Curated
    Contains 1 IBB domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG317385.
    HOGENOMiHOG000012990.
    HOVERGENiHBG053257.
    InParanoidiO95149.
    KOiK13151.
    OrthoDBiEOG7J70GG.
    PhylomeDBiO95149.
    TreeFamiTF313108.

    Family and domain databases

    InterProiIPR002652. Importin-a_IBB.
    IPR017336. Snurportin-1.
    IPR024721. Snurportin-1_N.
    [Graphical view]
    PfamiPF11538. Snurportin1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037955. Snurportin-1. 1 hit.
    PROSITEiPS51214. IBB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O95149-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL    50
    QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN 100
    QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN 150
    RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ 200
    TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF 250
    PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD 300
    YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS TPKLKGSSHS 350
    PDHPGCLMEN 360
    Length:360
    Mass (Da):41,143
    Last modified:May 1, 1999 - v1
    Checksum:i50B456D1C23B4BA1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039029 mRNA. Translation: AAC70906.1.
    CR456811 mRNA. Translation: CAG33092.1.
    AK289475 mRNA. Translation: BAF82164.1.
    CH471136 Genomic DNA. Translation: EAW99245.1.
    CH471136 Genomic DNA. Translation: EAW99246.1.
    BC004203 mRNA. Translation: AAH04203.1.
    CCDSiCCDS10281.1.
    RefSeqiNP_001036046.1. NM_001042581.1.
    NP_001036053.1. NM_001042588.1.
    NP_005692.1. NM_005701.3.
    UniGeneiHs.21577.

    Genome annotation databases

    EnsembliENST00000308588; ENSP00000309831; ENSG00000169371.
    ENST00000564644; ENSP00000454852; ENSG00000169371.
    ENST00000564675; ENSP00000458053; ENSG00000169371.
    ENST00000567134; ENSP00000456224; ENSG00000169371.
    GeneIDi10073.
    KEGGihsa:10073.
    UCSCiuc002ban.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039029 mRNA. Translation: AAC70906.1 .
    CR456811 mRNA. Translation: CAG33092.1 .
    AK289475 mRNA. Translation: BAF82164.1 .
    CH471136 Genomic DNA. Translation: EAW99245.1 .
    CH471136 Genomic DNA. Translation: EAW99246.1 .
    BC004203 mRNA. Translation: AAH04203.1 .
    CCDSi CCDS10281.1.
    RefSeqi NP_001036046.1. NM_001042581.1.
    NP_001036053.1. NM_001042588.1.
    NP_005692.1. NM_005701.3.
    UniGenei Hs.21577.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XK5 X-ray 2.40 A 97-300 [» ]
    2P8Q X-ray 2.35 B 25-64 [» ]
    2Q5D X-ray 3.20 C/D 25-64 [» ]
    2QNA X-ray 2.84 B 1-66 [» ]
    3GB8 X-ray 2.90 B 1-328 [» ]
    3GJX X-ray 2.50 B/E 1-360 [» ]
    3LWW X-ray 3.15 B/D 25-64 [» ]
    3NBY X-ray 3.42 B/E 15-360 [» ]
    3NBZ X-ray 2.80 B/E 15-360 [» ]
    3NC0 X-ray 2.90 B/E 15-360 [» ]
    ProteinModelPortali O95149.
    SMRi O95149. Positions 12-360.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115384. 16 interactions.
    DIPi DIP-48513N.
    IntActi O95149. 11 interactions.
    MINTi MINT-1378592.
    STRINGi 9606.ENSP00000309831.

    PTM databases

    PhosphoSitei O95149.

    Proteomic databases

    MaxQBi O95149.
    PaxDbi O95149.
    PeptideAtlasi O95149.
    PRIDEi O95149.

    Protocols and materials databases

    DNASUi 10073.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308588 ; ENSP00000309831 ; ENSG00000169371 .
    ENST00000564644 ; ENSP00000454852 ; ENSG00000169371 .
    ENST00000564675 ; ENSP00000458053 ; ENSG00000169371 .
    ENST00000567134 ; ENSP00000456224 ; ENSG00000169371 .
    GeneIDi 10073.
    KEGGi hsa:10073.
    UCSCi uc002ban.3. human.

    Organism-specific databases

    CTDi 10073.
    GeneCardsi GC15M075890.
    HGNCi HGNC:14245. SNUPN.
    HPAi CAB005004.
    MIMi 607902. gene.
    neXtProti NX_O95149.
    PharmGKBi PA34611.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG317385.
    HOGENOMi HOG000012990.
    HOVERGENi HBG053257.
    InParanoidi O95149.
    KOi K13151.
    OrthoDBi EOG7J70GG.
    PhylomeDBi O95149.
    TreeFami TF313108.

    Enzyme and pathway databases

    Reactomei REACT_11066. snRNP Assembly.

    Miscellaneous databases

    EvolutionaryTracei O95149.
    GeneWikii SNUPN.
    GenomeRNAii 10073.
    NextBioi 38077.
    PROi O95149.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95149.
    Bgeei O95149.
    CleanExi HS_SNUPN.
    Genevestigatori O95149.

    Family and domain databases

    InterProi IPR002652. Importin-a_IBB.
    IPR017336. Snurportin-1.
    IPR024721. Snurportin-1_N.
    [Graphical view ]
    Pfami PF11538. Snurportin1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037955. Snurportin-1. 1 hit.
    PROSITEi PS51214. IBB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure."
      Huber J., Cronshagen U., Kadokura M., Marshallsay C., Wada T., Sekine M., Luehrmann R.
      EMBO J. 17:4114-4126(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-52; 54-69; 128-144; 211-221 AND 323-327, FUNCTION IN U SNRNP NUCLEAR IMPORT, INTERACTION WITH KPNB1, RNA-BINDING.
      Tissue: Brain.
    2. "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].
    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].
      Tissue: Cerebellum.
    4. 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].
      Tissue: Uterus.
    6. Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, INTERACTION WITH IPO7; KPNB1 AND XPO1, IDENTIFICATION IN A TRIMERIC EXPORT COMPLEX WITH XPO1 AND RAN, SUBCELLULAR LOCATION.
    7. "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta."
      Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.
      Hum. Mol. Genet. 11:1785-1795(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN IMPORT SNRNP COMPLEX, INTERACTION WITH DDX20; SMN1 AND SNRPB, SUBCELLULAR LOCATION.
    8. Cited for: MUTAGENESIS OF ARG-27; TRP-107; 203-PHE--TRP-207 AND TRP-276, RNA-BINDING.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structural basis for m3G-cap-mediated nuclear import of spliceosomal UsnRNPs by snurportin1."
      Strasser A., Dickmanns A., Luehrmann R., Ficner R.
      EMBO J. 24:2235-2243(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 97-300 IN COMPLEX WITH M3G-CAP, MUTAGENESIS OF TRP-107 AND TRP-276.

    Entry informationi

    Entry nameiSPN1_HUMAN
    AccessioniPrimary (citable) accession number: O95149
    Secondary accession number(s): A6NE34, A8K0B0, D3DW76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 118 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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