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RL14_PIG
ID   RL14_PIG                Reviewed;         213 AA.
AC   A1XQU3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=60S ribosomal protein L14;
GN   Name=RPL14;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Longissimus dorsi muscle;
RA   Cai G., Chen Y., Wang C., Li J., Peng G., Zhang H.;
RT   "Generation and analysis of cDNA sequences derived from a porcine skeletal
RT   muscle library.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC       large ribonucleoprotein complex responsible for the synthesis of
CC       proteins in the cell. {ECO:0000250|UniProtKB:P50914}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000250|UniProtKB:P50914}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50914}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL14 family.
CC       {ECO:0000305}.
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DR   EMBL; DQ629165; ABK55649.1; -; mRNA.
DR   RefSeq; NP_001090947.1; NM_001097478.1.
DR   PDB; 3J7O; EM; 3.50 A; M=1-213.
DR   PDB; 3J7P; EM; 3.50 A; M=1-213.
DR   PDB; 3J7Q; EM; 3.50 A; M=1-213.
DR   PDB; 3J7R; EM; 3.90 A; M=1-213.
DR   PDBsum; 3J7O; -.
DR   PDBsum; 3J7P; -.
DR   PDBsum; 3J7Q; -.
DR   PDBsum; 3J7R; -.
DR   AlphaFoldDB; A1XQU3; -.
DR   SMR; A1XQU3; -.
DR   STRING; 9823.ENSSSCP00000012018; -.
DR   PaxDb; A1XQU3; -.
DR   PeptideAtlas; A1XQU3; -.
DR   PRIDE; A1XQU3; -.
DR   GeneID; 100037994; -.
DR   KEGG; ssc:100037994; -.
DR   CTD; 9045; -.
DR   eggNOG; KOG3421; Eukaryota.
DR   InParanoid; A1XQU3; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0015934; C:large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd06088; KOW_RPL14; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR002784; Ribosomal_L14e_dom.
DR   InterPro; IPR039660; Ribosomal_protein_L14.
DR   InterPro; IPR041985; RPL14_KOW.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11127; PTHR11127; 1.
DR   Pfam; PF01929; Ribosomal_L14e; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
FT   CHAIN           1..213
FT                   /note="60S ribosomal protein L14"
FT                   /id="PRO_0000289658"
FT   REPEAT          169..173
FT                   /note="1-1; approximate"
FT   REPEAT          174..178
FT                   /note="1-2"
FT   REPEAT          179..183
FT                   /note="1-3"
FT   REPEAT          184..188
FT                   /note="1-4"
FT   REPEAT          191..193
FT                   /note="2-1"
FT   REPEAT          194..196
FT                   /note="2-2"
FT   REGION          166..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..188
FT                   /note="4 X 5 AA tandem repeats of Q-K-A-[APS]-X"
FT   REGION          191..196
FT                   /note="2 X 3 AA tandem repeats of K-G-Q"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50914"
FT   MOD_RES         85
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50914"
FT   MOD_RES         85
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CR57"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50914"
FT   MOD_RES         202
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CR57"
FT   CROSSLNK        124
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P50914"
SQ   SEQUENCE   213 AA;  23330 MW;  33E71C1581616B65 CRC64;
     MVFRRFVEVG RVAYVSFGPH AGKLVAIVDV IDQNRALVDG PCTQVRRQAM PFKCMQLTDF
     ILKFPHSARQ KYVRKAWEKA DINAKWAATR WAKKIEAREK KAKMTDFDRY KVMKARKMRN
     RLIKLEVKKL QKAALLKASP KKALAKGAAA AAAAAAAKVP VKKITTAGKK APAQKAPAQK
     AAGQKAAPPP KAQKVQKPPA QKAPAPKASG EKA
 
 
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