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Protein

Snurportin-1

Gene

SNUPN

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

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. snRNA import into nucleus Source: InterPro
  5. spliceosomal snRNP assembly Source: Reactome
Complete GO annotation...

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 Componenti: 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: UniProtKB
  3. nuclear pore Source: ProtInc
Complete GO annotation...

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. 1 Publication
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

BgeeiO95149.
CleanExiHS_SNUPN.
ExpressionAtlasiO95149. baseline and differential.
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. 22 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 – 1010Combined sources
Beta strandi21 – 233Combined sources
Helixi28 – 303Combined sources
Helixi42 – 6019Combined sources
Turni61 – 633Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi102 – 1076Combined sources
Helixi115 – 1184Combined sources
Beta strandi119 – 13517Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi170 – 1778Combined sources
Helixi178 – 1803Combined sources
Beta strandi182 – 19110Combined sources
Helixi201 – 21111Combined sources
Turni212 – 2143Combined sources
Turni216 – 2194Combined sources
Beta strandi225 – 2317Combined sources
Beta strandi234 – 2363Combined sources
Helixi239 – 2468Combined sources
Beta strandi254 – 26310Combined sources
Beta strandi268 – 27710Combined sources
Helixi279 – 2813Combined sources
Helixi282 – 2865Combined sources
Beta strandi291 – 2933Combined sources
Helixi294 – 2963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00510000047494.
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

        10         20         30         40         50
MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL
60 70 80 90 100
QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN
110 120 130 140 150
QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN
160 170 180 190 200
RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ
210 220 230 240 250
TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF
260 270 280 290 300
PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD
310 320 330 340 350
YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS TPKLKGSSHS
360
PDHPGCLMEN
Length:360
Mass (Da):41,143
Last modified:May 1, 1999 - v1
Checksum:i50B456D1C23B4BA1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi115384. 22 interactions.
DIPiDIP-48513N.
IntActiO95149. 11 interactions.
MINTiMINT-1378592.
STRINGi9606.ENSP00000309831.

PTM databases

PhosphoSiteiO95149.

Proteomic databases

MaxQBiO95149.
PaxDbiO95149.
PeptideAtlasiO95149.
PRIDEiO95149.

Protocols and materials databases

DNASUi10073.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10073.
GeneCardsiGC15M075890.
HGNCiHGNC:14245. SNUPN.
HPAiCAB005004.
MIMi607902. gene.
neXtProtiNX_O95149.
PharmGKBiPA34611.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG317385.
GeneTreeiENSGT00510000047494.
HOGENOMiHOG000012990.
HOVERGENiHBG053257.
InParanoidiO95149.
KOiK13151.
OrthoDBiEOG7J70GG.
PhylomeDBiO95149.
TreeFamiTF313108.

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.

Miscellaneous databases

ChiTaRSiSNUPN. human.
EvolutionaryTraceiO95149.
GeneWikiiSNUPN.
GenomeRNAii10073.
NextBioi38077.
PROiO95149.
SOURCEiSearch...

Gene expression databases

BgeeiO95149.
CleanExiHS_SNUPN.
ExpressionAtlasiO95149. baseline and differential.
GenevestigatoriO95149.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1997) [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 (MAY-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(2003) [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(2003) [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(2001) [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(2009) [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(2010) [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(2004) [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: March 4, 2015
This is version 122 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.