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P61972 (NTF2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear transport factor 2

Short name=NTF-2
Gene names
Name:Nutf2
Synonyms:Ntf2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Facilitates protein transport into the nucleus. Interacts with the nucleoporin p62 and with Ran. Acts at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Contains 1 NTF2 domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 127127Nuclear transport factor 2
PRO_0000194777

Regions

Domain10 – 121112NTF2

Amino acid modifications

Modified residue41N6-acetyllysine By similarity

Secondary structure

................. 127
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61972 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 817752F20E262FD3

FASTA12714,478
        10         20         30         40         50         60 
MGDKPIWEQI GSSFIQHYYQ LFDNDRTQLG AIYIDASCLT WEGQQFQGKA AIVEKLSSLP 

        70         80         90        100        110        120 
FQKIQHSITA QDHQPTPDSC IISMVVGQLK ADEDPIMGFH QMFLLKNIND AWVCTNDMFR 


LALHNFG 

« Hide

References

« Hide 'large scale' references
[1]"Crystallization and preliminary X-ray diffraction analysis of nuclear transport factor 2."
Kent H.M., Clarkson W.D., Bullock T.L., Stewart M.
J. Struct. Biol. 116:326-329(1996) [PubMed: 8812990] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CRYSTALLIZATION.
Tissue: Kidney.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[3]"The 1.6-A resolution crystal structure of nuclear transport factor 2 (NTF2)."
Bullock T.L., Clarkson W.D., Kent H.M., Stewart M.
J. Mol. Biol. 260:422-431(1996) [PubMed: 8757804] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[4]"Nuclear protein import is decreased by engineered mutants of nuclear transport factor 2 (NTF2) that do not bind GDP-Ran."
Clarkson W.D., Corbett A.H., Paschal B.M., Kent H.M., McCoy A.J., Gerace L., Silver P.A., Stewart M.
J. Mol. Biol. 272:716-730(1997) [PubMed: 9368653] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[5]"Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran."
Stewart M., Kent H.M., McCoy A.J.
J. Mol. Biol. 277:635-646(1998) [PubMed: 9533885] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH RAN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91651 Genomic DNA. Translation: CAA62839.1.
BC061569 mRNA. Translation: AAH61569.1.
IPIIPI00203502.
RefSeqNP_001007630.1. NM_001007629.1.
UniGeneRn.107980.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2KX-ray2.50A/B1-127[»]
1AR0X-ray2.30A/B1-127[»]
1ASKX-ray2.30A/B1-127[»]
1GY6X-ray1.60A/B1-127[»]
1JB2X-ray2.00A/B1-127[»]
1JB4X-ray2.23A/B1-127[»]
1JB5X-ray2.30A/B1-127[»]
1OUNX-ray2.30A/B1-127[»]
1QMAX-ray2.50A/B/C/D2-127[»]
1U5OX-ray2.50A/B1-127[»]
ProteinModelPortalP61972.
SMRP61972. Positions 3-127.
ModBaseSearch...

Protein-protein interaction databases

IntActP61972. 1 interaction.
STRINGP61972.

PTM databases

PhosphoSiteP61972.

Proteomic databases

PRIDEP61972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025608; ENSRNOP00000025608; ENSRNOG00000018945.
GeneID291981.
KEGGrno:291981.
UCSCNM_001007629. rat.

Organism-specific databases

CTD10204.
RGD1359213. Nutf2.

Phylogenomic databases

eggNOGroNOG14743.
GeneTreeENSGT00510000047030.
HOVERGENHBG025070.
InParanoidP61972.
OMAMLTFETS.
OrthoDBEOG473PSP.
PhylomeDBP61972.

Gene expression databases

ArrayExpressP61972.
GenevestigatorP61972.
GermOnlineENSRNOG00000018945. Rattus norvegicus.

Family and domain databases

InterProIPR002075. NTF2.
IPR018222. Nuclear_transport_factor_2_euk.
[Graphical view]
PfamPF02136. NTF2. 1 hit.
[Graphical view]
PROSITEPS50177. NTF2_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio633551.

Entry information

Entry nameNTF2_RAT
AccessionPrimary (citable) accession number: P61972
Secondary accession number(s): P13662
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: September 21, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families