RRP15_RAT
ID RRP15_RAT Reviewed; 280 AA.
AC Q5M947;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=RRP15-like protein;
DE AltName: Full=Ribosomal RNA-processing protein 15;
GN Name=Rrp15;
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=Ovary;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION BY
RP 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 -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRP15 family. {ECO:0000305}.
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DR EMBL; BC087649; AAH87649.1; -; mRNA.
DR RefSeq; NP_001009702.1; NM_001009702.1.
DR AlphaFoldDB; Q5M947; -.
DR SMR; Q5M947; -.
DR STRING; 10116.ENSRNOP00000003359; -.
DR iPTMnet; Q5M947; -.
DR PhosphoSitePlus; Q5M947; -.
DR PaxDb; Q5M947; -.
DR PRIDE; Q5M947; -.
DR Ensembl; ENSRNOT00000003359; ENSRNOP00000003359; ENSRNOG00000002450.
DR GeneID; 360895; -.
DR KEGG; rno:360895; -.
DR UCSC; RGD:1306106; rat.
DR CTD; 51018; -.
DR RGD; 1306106; Rrp15.
DR eggNOG; KOG2974; Eukaryota.
DR GeneTree; ENSGT00390000001960; -.
DR HOGENOM; CLU_079732_0_0_1; -.
DR InParanoid; Q5M947; -.
DR OMA; EDEPAWA; -.
DR OrthoDB; 1522334at2759; -.
DR PhylomeDB; Q5M947; -.
DR TreeFam; TF106119; -.
DR PRO; PR:Q5M947; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002450; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q5M947; RN.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR InterPro; IPR012459; Rrp15.
DR PANTHER; PTHR13245; PTHR13245; 1.
DR Pfam; PF07890; Rrp15p; 1.
PE 1: Evidence at protein level;
KW Acetylation; Citrullination; Coiled coil; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CHAIN 2..280
FT /note="RRP15-like protein"
FT /id="PRO_0000273215"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..45
FT /evidence="ECO:0000255"
FT COILED 107..143
FT /evidence="ECO:0000255"
FT COMPBIAS 15..30
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 9
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
SQ SEQUENCE 280 AA; 30926 MW; BB79E8042006459A CRC64;
MAAAVQDSRV NPGGKLKRSP KKKKKMKKVA KAAVSKLEDE LKDSSGGEGS CESEMDDSDD
GAAEADSEDN VESCEEENEV AAESSAGTNS GWADAMAKIL NKKTPKSKPT ILTKNKELEK
EKEKLKQERL EKRKQIDKKR EWEMLCRVKP DVIKDKEAER NLQRIATRGV VQLFNAVQKH
QRNVDEKVKE VGGSIRKRAK LMSTVSKKDF ISVLRGMDGA SENSSAGKSP KARQTEVKSE
EGPGWKILRD DFMMGASMKD WDKESEGEEP ADGQAGSASH
