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PRUN2_RAT
ID   PRUN2_RAT               Reviewed;         322 AA.
AC   Q5BJR4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protein prune homolog 2;
DE   AltName: Full=BNIP2 motif-containing molecule at the C-terminal region 1;
GN   Name=Prune2; Synonyms=Bmcc1;
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: May play an important role in regulating differentiation,
CC       survival and aggressiveness of the tumor cells. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; BC091368; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; Q5BJR4; -.
DR   STRING; 10116.ENSRNOP00000051678; -.
DR   jPOST; Q5BJR4; -.
DR   PaxDb; Q5BJR4; -.
DR   PRIDE; Q5BJR4; -.
DR   Ensembl; ENSRNOT00000054794; ENSRNOP00000051678; ENSRNOG00000015088.
DR   UCSC; RGD:1311350; rat.
DR   RGD; 1311350; Prune2.
DR   eggNOG; KOG4129; Eukaryota.
DR   GeneTree; ENSGT00940000154422; -.
DR   HOGENOM; CLU_039135_3_0_1; -.
DR   InParanoid; Q5BJR4; -.
DR   OMA; NREDYHE; -.
DR   PRO; PR:Q5BJR4; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015088; Expressed in cerebellum and 19 other tissues.
DR   Genevisible; Q5BJR4; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; -; 1.
DR   InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   Pfam; PF12496; BNIP2; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; SSF52087; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Cytoplasm; Reference proteome.
FT   CHAIN           1..322
FT                   /note="Protein prune homolog 2"
FT                   /id="PRO_0000274883"
FT   DOMAIN          130..291
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..78
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   322 AA;  36980 MW;  65428A8110300C30 CRC64;
     MDIHFEEGVL SPSATDMRPE PPNSLDLNGS HPRRIKLTAP NINLSLDQSE GSILSDDNLD
     SPDEIDINVD ELDTPDEADS FEYPGHEDPM ANRSSGQESE SIPEYTAEEE REDNRLWRTV
     VIGEQEQRID MKVIEPYRRV ISHGGYYGDG LNAIIVFAAC FLPDSSRADY HYVMENLFLY
     VISTLELMVA EDYMIVYLNG ATPRRKMPGL GWMKKCYQMI DRRLRKNLKS FIIVHPSWFI
     RTILAVTRPF ISSKFSSKIK YVSSLSELSG LIPMDCIHIP ESIIKYDEEK SFKRSVRTSC
     LYNDPEMTSM EKDIDMKLKE KP
 
 
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