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Protein

Importin subunit beta-5

Gene

KAP114

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of TATA-binding protein (TBP) and of histones H2A and H2B.2 Publications

GO - Molecular functioni

  • protein transporter activity Source: SGD

GO - Biological processi

  • mRNA transport Source: UniProtKB-KW
  • protein import into nucleus Source: SGD
  • transcription factor import into nucleus Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30713-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit beta-5
Alternative name(s):
114 kDa karyopherin
Karyopherin subunit beta-5
Karyopherin-114
Gene namesi
Name:KAP114
Ordered Locus Names:YGL241W
ORF Names:HRC1004
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL241W.
SGDiS000003210. KAP114.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: GO_Central
  • nuclear envelope Source: GO_Central
  • nuclear pore Source: UniProtKB-SubCell
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10041004Importin subunit beta-5PRO_0000120778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP53067.

Interactioni

Subunit structurei

Interacts with NAP1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GSP1P328353EBI-9174,EBI-7926
MMS21P386322EBI-9174,EBI-11017
SPT15P133933EBI-9174,EBI-19129

Protein-protein interaction databases

BioGridi32999. 40 interactions.
DIPiDIP-5881N.
IntActiP53067. 23 interactions.
MINTiMINT-630657.

Structurei

3D structure databases

ProteinModelPortaliP53067.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 10080Importin N-terminalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the importin beta family.Curated
Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000008224.
HOGENOMiHOG000113058.
InParanoidiP53067.
OMAiCEKSLPF.
OrthoDBiEOG71K6BB.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53067-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDINELIIGA QSADKHTREV AETQLLQWCD SDASQVFKAL ANVALQHEAS
60 70 80 90 100
LESRQFALLS LRKLITMYWS PGFESYRSTS NVEIDVKDFI REVLLKLCLN
110 120 130 140 150
DNENTKIKNG ASYCIVQISA VDFPDQWPQL LTVIYDAISH QHSLNAMSLL
160 170 180 190 200
NEIYDDVVSE EMFFEGGIGL ATMEIVFKVL NTETSTLIAK IAALKLLKAC
210 220 230 240 250
LLQMSSHNEY DEASRKSFVS QCLATSLQIL GQLLTLNFGN VDVISQLKFK
260 270 280 290 300
SIIYENLVFI KNDFSRKHFS SELQKQFKIM AIQDLENVTH INANVETTES
310 320 330 340 350
EPLLETVHDC SIYIVEFLTS VCTLQFSVEE MNKIITSLTI LCQLSSETRE
360 370 380 390 400
IWTSDFNTFV SKETGLAASY NVRDQANEFF TSLPNPQLSL IFKVVSNDIE
410 420 430 440 450
HSTCNYSTLE SLLYLLQCIL LNDDEITGEN IDQSLQILIK TLENILVSQE
460 470 480 490 500
IPELILARAI LTIPRVLDKF IDALPDIKPL TSAFLAKSLN LALKSDKELI
510 520 530 540 550
KSATLIAFTY YCYFAELDSV LGPEVCSETQ EKVIRIINQV SSDAEEDTNG
560 570 580 590 600
ALMEVLSQVI SYNPKEPHSR KEILQAEFHL VFTISSEDPA NVQVVVQSQE
610 620 630 640 650
CLEKLLDNIN MDNYKNYIEL CLPSFINVLD SNNANNYRYS PLLSLVLEFI
660 670 680 690 700
TVFLKKKPND GFLPDEINQY LFEPLAKVLA FSTEDETLQL ATEAFSYLIF
710 720 730 740 750
NTDTRAMEPR LMDIMKVLER LLSLEVSDSA AMNVGPLVVA IFTRFSKEIQ
760 770 780 790 800
PLIGRILEAV VVRLIKTQNI STEQNLLSVL CFLTCNDPKQ TVDFLSSFQI
810 820 830 840 850
DNTDALTLVM RKWIEAFEVI RGEKRIKENI VALSNLFFLN DKRLQKVVVN
860 870 880 890 900
GNLIPYEGDL IITRSMAKKM PDRYVQVPLY TKIIKLFVSE LSFQSKQPNP
910 920 930 940 950
EQLITSDIKQ EVVNANKDDD NDDWEDVDDV LDYDKLKEYI DDDVDEEADD
960 970 980 990 1000
DSDDITGLMD VKESVVQLLV RFFKEVASKD VSGFHCIYET LSDSERKVLS

EALL
Length:1,004
Mass (Da):113,921
Last modified:October 1, 1996 - v1
Checksum:i1F4C02AA6AB2FF39
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49149 Genomic DNA. Translation: CAA89014.1.
Z72763 Genomic DNA. Translation: CAA96960.1.
BK006941 Genomic DNA. Translation: DAA07878.1.
PIRiS53939.
RefSeqiNP_011273.1. NM_001181107.1.

Genome annotation databases

EnsemblFungiiYGL241W; YGL241W; YGL241W.
GeneIDi852610.
KEGGisce:YGL241W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49149 Genomic DNA. Translation: CAA89014.1.
Z72763 Genomic DNA. Translation: CAA96960.1.
BK006941 Genomic DNA. Translation: DAA07878.1.
PIRiS53939.
RefSeqiNP_011273.1. NM_001181107.1.

3D structure databases

ProteinModelPortaliP53067.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32999. 40 interactions.
DIPiDIP-5881N.
IntActiP53067. 23 interactions.
MINTiMINT-630657.

Proteomic databases

MaxQBiP53067.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL241W; YGL241W; YGL241W.
GeneIDi852610.
KEGGisce:YGL241W.

Organism-specific databases

EuPathDBiFungiDB:YGL241W.
SGDiS000003210. KAP114.

Phylogenomic databases

GeneTreeiENSGT00390000008224.
HOGENOMiHOG000113058.
InParanoidiP53067.
OMAiCEKSLPF.
OrthoDBiEOG71K6BB.

Enzyme and pathway databases

BioCyciYEAST:G3O-30713-MONOMER.

Miscellaneous databases

PROiP53067.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left arm of chromosome VII, reveals the presence of eight open reading frames."
    Vandenbol M., Durand P., Portetelle D., Hilger F.
    Yeast 11:1519-1523(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The importin/karyopherin Kap114 mediates the nuclear import of TATA-binding protein."
    Morehouse H., Buratowski R.M., Silver P.A., Buratowski S.
    Proc. Natl. Acad. Sci. U.S.A. 96:12542-12547(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TBP IMPORT.
  5. "Nuclear import of histone H2A and H2B is mediated by a network of karyopherins."
    Mosammaparast N., Jackson K.R., Guo Y., Brame C.J., Shabanowitz J., Hunt D.F., Pemberton L.F.
    J. Cell Biol. 153:251-262(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE H2A/H2B IMPORT.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
    Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
    Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIMB5_YEAST
AccessioniPrimary (citable) accession number: P53067
Secondary accession number(s): D6VV94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2940 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.