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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.4 Publications

GO - Molecular functioni

  • protein transporter activity Source: InterPro
  • RNA cap binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169371-MONOMER.
ReactomeiR-HSA-191859. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:14245. SNUPN.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nuclear pore Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27R → A: Abolishes interaction with KPNB1 and m3G-cap U1 snRNP import receptor activity. 1 Publication1
Mutagenesisi107W → A: Reduces binding to m3G-cap structure, interaction with XPO1 and snRNP import receptor activity. 2 Publications1
Mutagenesisi203 – 207FRFYW → A: Reduces binding to m3G-cap structure. 1 Publication5
Mutagenesisi276W → A: Reduces binding to m3G-cap structure, interaction with XPO1 and snRNP import receptor activity. 2 Publications1

Organism-specific databases

DisGeNETi10073.
OpenTargetsiENSG00000169371.
PharmGKBiPA34611.

Polymorphism and mutation databases

BioMutaiSNUPN.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001910711 – 360Snurportin-1Add BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei75PhosphoserineCombined sources1
Modified residuei350PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO95149.
MaxQBiO95149.
PaxDbiO95149.
PeptideAtlasiO95149.
PRIDEiO95149.

PTM databases

iPTMnetiO95149.
PhosphoSitePlusiO95149.

Expressioni

Gene expression databases

BgeeiENSG00000169371.
CleanExiHS_SNUPN.
ExpressionAtlasiO95149. baseline and differential.
GenevisibleiO95149. HS.

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 (via IBB domain) with KPNB1; the interaction is direct. Interacts with DDX20, IPO7, SMN1, SNRPB and XPO1. Interacts directly with XPO1. Its interaction with XPO1 and binding to m3G-cap U snRNPs appears to be mutually exclusive.7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei105Interaction with m3G-cap structureCombined sources1 Publication1
Sitei144Interaction with m3G-cap structureCombined sources1 Publication1
Sitei276Interaction with m3G-cap structureCombined sources1 Publication1

Protein-protein interaction databases

BioGridi115384. 30 interactors.
DIPiDIP-48513N.
IntActiO95149. 17 interactors.
MINTiMINT-1378592.
STRINGi9606.ENSP00000309831.

Structurei

Secondary structure

1360
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 10Combined sources10
Beta strandi21 – 23Combined sources3
Helixi28 – 30Combined sources3
Helixi42 – 60Combined sources19
Turni61 – 63Combined sources3
Beta strandi97 – 100Combined sources4
Beta strandi102 – 107Combined sources6
Helixi115 – 118Combined sources4
Beta strandi119 – 135Combined sources17
Beta strandi138 – 142Combined sources5
Beta strandi144 – 146Combined sources3
Beta strandi148 – 152Combined sources5
Beta strandi155 – 159Combined sources5
Beta strandi161 – 163Combined sources3
Beta strandi165 – 167Combined sources3
Beta strandi170 – 177Combined sources8
Helixi178 – 180Combined sources3
Beta strandi182 – 191Combined sources10
Beta strandi197 – 199Combined sources3
Helixi201 – 211Combined sources11
Turni212 – 214Combined sources3
Turni216 – 219Combined sources4
Beta strandi225 – 231Combined sources7
Beta strandi234 – 236Combined sources3
Helixi239 – 246Combined sources8
Beta strandi254 – 263Combined sources10
Beta strandi268 – 277Combined sources10
Helixi279 – 281Combined sources3
Helixi282 – 286Combined sources5
Beta strandi291 – 293Combined sources3
Helixi294 – 296Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5DISX-ray2.85C1-287[»]
ProteinModelPortaliO95149.
SMRiO95149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95149.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 73IBBPROSITE-ProRule annotationAdd BLAST63

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 159Necessary for interaction with XPO11 PublicationAdd BLAST159
Regioni1 – 65Necessary for interaction with KPNB1 and m3G-cap U1 and U5 snRNP import receptor activity2 PublicationsAdd BLAST65
Regioni127 – 129Interaction with m3G-cap structureCombined sources1 Publication3
Regioni208 – 328Necessary for binding to the m3G-cap structure1 PublicationAdd BLAST121

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3132. Eukaryota.
ENOG410XQNJ. LUCA.
GeneTreeiENSGT00510000047494.
HOGENOMiHOG000012990.
HOVERGENiHBG053257.
InParanoidiO95149.
KOiK13151.
OMAiYHRQTHY.
OrthoDBiEOG091G0PL0.
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.4. 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
PDB 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[»]
5DISX-ray2.85C1-287[»]
ProteinModelPortaliO95149.
SMRiO95149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115384. 30 interactors.
DIPiDIP-48513N.
IntActiO95149. 17 interactors.
MINTiMINT-1378592.
STRINGi9606.ENSP00000309831.

PTM databases

iPTMnetiO95149.
PhosphoSitePlusiO95149.

Polymorphism and mutation databases

BioMutaiSNUPN.

Proteomic databases

EPDiO95149.
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.4. human.

Organism-specific databases

CTDi10073.
DisGeNETi10073.
GeneCardsiSNUPN.
HGNCiHGNC:14245. SNUPN.
HPAiCAB005004.
MIMi607902. gene.
neXtProtiNX_O95149.
OpenTargetsiENSG00000169371.
PharmGKBiPA34611.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3132. Eukaryota.
ENOG410XQNJ. LUCA.
GeneTreeiENSGT00510000047494.
HOGENOMiHOG000012990.
HOVERGENiHBG053257.
InParanoidiO95149.
KOiK13151.
OMAiYHRQTHY.
OrthoDBiEOG091G0PL0.
PhylomeDBiO95149.
TreeFamiTF313108.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169371-MONOMER.
ReactomeiR-HSA-191859. snRNP Assembly.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000169371.
CleanExiHS_SNUPN.
ExpressionAtlasiO95149. baseline and differential.
GenevisibleiO95149. HS.

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...

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: November 2, 2016
This is version 140 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

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 one 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.