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HEK2_KLULA
ID   HEK2_KLULA              Reviewed;         383 AA.
AC   Q6CNI6;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Heterogeneous nuclear rnp K-like protein 2;
DE   AltName: Full=KH domain-containing protein 1;
GN   Name=HEK2; Synonyms=KHD1; OrderedLocusNames=KLLA0E12321g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: RNA-binding protein involved in the correct localization of
CC       transcripts in the cell. RNA localization is a widespread mechanism for
CC       achieving localized protein synthesis. Involved in structural and
CC       functional organization of telomeric chromatin and regulates silencing
CC       at the HMR locus (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds RNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, P-body
CC       {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, telomere
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HEK2 family. {ECO:0000305}.
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DR   EMBL; CR382125; CAG99590.1; -; Genomic_DNA.
DR   RefSeq; XP_454503.1; XM_454503.1.
DR   AlphaFoldDB; Q6CNI6; -.
DR   SMR; Q6CNI6; -.
DR   STRING; 28985.XP_454503.1; -.
DR   PRIDE; Q6CNI6; -.
DR   EnsemblFungi; CAG99590; CAG99590; KLLA0_E12321g.
DR   GeneID; 2894562; -.
DR   KEGG; kla:KLLA0_E12321g; -.
DR   eggNOG; KOG2190; Eukaryota.
DR   HOGENOM; CLU_022670_2_0_1; -.
DR   InParanoid; Q6CNI6; -.
DR   OMA; SIAKEPH; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0008298; P:intracellular mRNA localization; IEA:EnsemblFungi.
DR   GO; GO:0048255; P:mRNA stabilization; IEA:EnsemblFungi.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IEA:EnsemblFungi.
DR   Gene3D; 3.30.1370.10; -; 3.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   SUPFAM; SSF54791; SSF54791; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   3: Inferred from homology;
KW   Chromatin regulator; Chromosome; Cytoplasm; mRNA transport; Nucleus;
KW   Reference proteome; Repeat; RNA-binding; Telomere; Translation regulation;
KW   Transport.
FT   CHAIN           1..383
FT                   /note="Heterogeneous nuclear rnp K-like protein 2"
FT                   /id="PRO_0000408189"
FT   DOMAIN          58..122
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          161..226
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          256..321
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REGION          332..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   383 AA;  42140 MW;  66A03B0144077091 CRC64;
     MSSSADNSNN SSSRFPAAVD SINNNSNSIN DASQFHNSYN EVNEINNDTN SQVNNGNNIT
     FHVLVSLKEA AKIIGPQGNT IETIRRENDI KIGISPREKS CSDRLLNVSG PPRQVANSLG
     QVLRVLTTDY EPEEHVFKHL RFMLPPASKE EIEDPEKWKQ IGNLRLICTN PQISSVIGQQ
     GAKIKKLIET HTVKLVASKH FLPDSKDRVL EIQGFPTSVA NCINEIAELF IQDDVHVPPR
     TLPRYYPHSK HTKEIQVSQT LAIPKEFVGA LLGVGGNRIA NLRKFTKTKI VIGQDPTENG
     DRIFTVWGND QKSVKLAQTM LLKNLEVEKK RREEHEASLK DGSSVPAAAA ASAATSISAS
     GANQNDSIHT PVSDNESPVV FTE
 
 
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