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NGDN_BOVIN
ID   NGDN_BOVIN              Reviewed;         315 AA.
AC   Q2KII6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Neuroguidin;
DE   AltName: Full=EIF4E-binding protein;
GN   Name=NGDN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the translational repression of cytoplasmic
CC       polyadenylation element (CPE)-containing mRNAs. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CPEB1 and EIF4E. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC       {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection,
CC       dendrite {ECO:0000250}. Cell projection, filopodium {ECO:0000250}.
CC       Note=Detected in axons, dendrites and filopodia. Colocalized with EIF4E
CC       in neurites. Translocated from nucleolus to nuclear foci in response to
CC       UV damage (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SAS10 family. {ECO:0000305}.
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DR   EMBL; BC112624; AAI12625.1; -; mRNA.
DR   RefSeq; NP_001039924.1; NM_001046459.1.
DR   AlphaFoldDB; Q2KII6; -.
DR   SMR; Q2KII6; -.
DR   STRING; 9913.ENSBTAP00000012628; -.
DR   PaxDb; Q2KII6; -.
DR   PRIDE; Q2KII6; -.
DR   Ensembl; ENSBTAT00000012628; ENSBTAP00000012628; ENSBTAG00000009595.
DR   GeneID; 539602; -.
DR   KEGG; bta:539602; -.
DR   CTD; 25983; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009595; -.
DR   VGNC; VGNC:32059; NGDN.
DR   eggNOG; KOG3117; Eukaryota.
DR   GeneTree; ENSGT00500000044922; -.
DR   HOGENOM; CLU_031901_0_0_1; -.
DR   InParanoid; Q2KII6; -.
DR   OMA; GYGGEEW; -.
DR   OrthoDB; 1511802at2759; -.
DR   TreeFam; TF313713; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000009595; Expressed in oocyte and 104 other tissues.
DR   ExpressionAtlas; Q2KII6; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR007146; Sas10/Utp3/C1D.
DR   PANTHER; PTHR13237; PTHR13237; 1.
DR   Pfam; PF04000; Sas10_Utp3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell projection; Centromere; Chromosome; Coiled coil;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Translation regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT   CHAIN           2..315
FT                   /note="Neuroguidin"
FT                   /id="PRO_0000269246"
FT   REGION          41..174
FT                   /note="Necessary for interaction with EIF4E"
FT                   /evidence="ECO:0000250"
FT   REGION          123..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          5..42
FT                   /evidence="ECO:0000255"
FT   COILED          181..205
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        264..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..315
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
SQ   SEQUENCE   315 AA;  35766 MW;  A81FB585EE7449BA CRC64;
     MAAPEVLESD LPNAVALLKN LQEQVMAVTA QVQTLTKKVQ AKAYPTEKGL SLLEVKDQLL
     LMYLMDLSHL ILDKASGGSL QGHPAVLRLV EIRTVLEKLR PLDQKLKYQI DKLVKTAVTG
     SLSENDPLRF KPHPSNMMSK LSSEDEEEDE AEEGQSGASG KKSGKGTAKK YVPPRLVPVH
     YDETEAEREK KRLERAKRRA LSSSVIRELK EQYSDAPEEI RDARHPHVTR QSQEDQHRIN
     YEESMMVRLS VSKREKGRRK RANVMSSQLH SLTHFSDISA LTGGTPHLDE DQNPTKKRKK
     IPKKGRKKKG FRRRR
 
 
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