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GTPB4_RAT
ID   GTPB4_RAT               Reviewed;         637 AA.
AC   Q99P77;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=GTP-binding protein 4;
DE   AltName: Full=Chronic renal failure gene protein;
DE   AltName: Full=Nucleolar GTP-binding protein 1;
GN   Name=Gtpbp4; Synonyms=Crfg, Nog1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=11316846; DOI=10.1681/asn.v125883;
RA   Laping N.J., Olson B.A., Zhu Y.;
RT   "Identification of a novel nuclear guanosine triphosphate-binding protein
RT   differentially expressed in renal disease.";
RL   J. Am. Soc. Nephrol. 12:883-890(2001).
CC   -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit.
CC       {ECO:0000250|UniProtKB:Q9BZE4}.
CC   -!- SUBUNIT: Associates with pre-60S ribosomal particles. Interacts with
CC       MINAS-60 (product of an alternative open reading frame of RBM10).
CC       {ECO:0000250|UniProtKB:Q9BZE4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9BZE4}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. NOG subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU01047}.
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DR   EMBL; AF325355; AAK13446.1; -; mRNA.
DR   AlphaFoldDB; Q99P77; -.
DR   SMR; Q99P77; -.
DR   IntAct; Q99P77; 1.
DR   STRING; 10116.ENSRNOP00000064860; -.
DR   jPOST; Q99P77; -.
DR   PRIDE; Q99P77; -.
DR   UCSC; RGD:620783; rat.
DR   RGD; 620783; Gtpbp4.
DR   eggNOG; KOG1490; Eukaryota.
DR   InParanoid; Q99P77; -.
DR   PhylomeDB; Q99P77; -.
DR   PRO; PR:Q99P77; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR   GO; GO:0005525; F:GTP binding; ISS:HGNC-UCL.
DR   GO; GO:0003924; F:GTPase activity; ISS:HGNC-UCL.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:RGD.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISS:HGNC-UCL.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:HGNC-UCL.
DR   GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:HGNC-UCL.
DR   GO; GO:0033342; P:negative regulation of collagen binding; ISS:HGNC-UCL.
DR   GO; GO:0008156; P:negative regulation of DNA replication; ISS:HGNC-UCL.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:HGNC-UCL.
DR   GO; GO:0050821; P:protein stabilization; ISS:HGNC-UCL.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:HGNC-UCL.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR024926; NOG1.
DR   InterPro; IPR041623; NOG1_N.
DR   InterPro; IPR010674; NOG1_Rossman_fold_dom.
DR   InterPro; IPR012973; NOG_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF06858; NOG1; 1.
DR   Pfam; PF17835; NOG1_N; 1.
DR   Pfam; PF08155; NOGCT; 1.
DR   PIRSF; PIRSF038919; NOG1; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51710; G_OBG; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; GTP-binding; Isopeptide bond; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribosome biogenesis; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT   CHAIN           2..637
FT                   /note="GTP-binding protein 4"
FT                   /id="PRO_0000195025"
FT   DOMAIN          169..340
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   REGION          499..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..625
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175..182
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         221..225
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         289..292
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT   MOD_RES         103
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT   MOD_RES         559
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT   CROSSLNK        103
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT   CROSSLNK        332
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE4"
FT   CROSSLNK        535
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE4"
SQ   SEQUENCE   637 AA;  74288 MW;  5CBF5FA48140F702 CRC64;
     MAHYNFKKIT VVPSAKDFID LTLSKTQRKT PTVIHKHYQI HRIRHFYMRK VKFTQQNYHD
     RLSQILSDFP KLDDIHPFYA DLMNILYDKD HYKLALGQIN IAKNLVDNVA KDYVRLMKYG
     DSLYRCKQLK RAALGRMCTI IKRQRQSLEY LEQVRQHLSR LPTIDPNTRT LLLCGYPNVG
     KSSFINKVTR ADVDVQPYAF TTKSLFVGHV DYKYLRWQVV DTPGILDHPL EDRNTIEMQA
     ITALAHLRAA VLYVMDLSEQ CGHGLKEQLG LFQNIRPLFI NKPLIVVASK CEVKRIAELS
     EEDQKIFLDL QAEGFPVIET STLTEEGVIQ VKTEACDRLL AHRVETKMKG NKVNEVLNRL
     HLAVPNKRDD KERPPFIPEG VVARRKRMEI AEPKKKRERD LELEMGDDYI LDLQKYWDLM
     NSSEKYDKIP EIWEGHNAAD YIDPAIMKKL EELEKGKKSS EQLLGSMPVS LRVKTRKWWK
     IRQLAKQIRE KKKLKILQSK EKNTQGPRMP RTAKKVQRAD LENEMRSLGV DMDDKDNAHY
     AVRARRSRSV TRKRKREESV PPSSIARSRS RSCSKTPRDV SGLRDVKMVK KAKTMMKKAQ
     KKMNRLGKKG EADRHVFDMK PKHLLSGKRK AGKKERR
 
 
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