RRP15_HUMAN
ID RRP15_HUMAN Reviewed; 282 AA.
AC Q9Y3B9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=RRP15-like protein;
DE AltName: Full=Ribosomal RNA-processing protein 15;
GN Name=RRP15; Synonyms=KIAA0507; ORFNames=CGI-115;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-282.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-266; SER-276 AND
RP SER-280, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11 AND THR-104, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11; SER-58; SER-67 AND SER-266, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-19; THR-104 AND
RP SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-179; LYS-208 AND
RP LYS-239, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRP15 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34110.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH20641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC020641; AAH20641.1; ALT_INIT; mRNA.
DR EMBL; AF151873; AAD34110.1; ALT_INIT; mRNA.
DR CCDS; CCDS1520.2; -.
DR RefSeq; NP_057136.2; NM_016052.3.
DR AlphaFoldDB; Q9Y3B9; -.
DR SMR; Q9Y3B9; -.
DR BioGRID; 119224; 115.
DR IntAct; Q9Y3B9; 33.
DR MINT; Q9Y3B9; -.
DR STRING; 9606.ENSP00000355899; -.
DR GlyGen; Q9Y3B9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3B9; -.
DR PhosphoSitePlus; Q9Y3B9; -.
DR BioMuta; RRP15; -.
DR DMDM; 124053370; -.
DR EPD; Q9Y3B9; -.
DR jPOST; Q9Y3B9; -.
DR MassIVE; Q9Y3B9; -.
DR MaxQB; Q9Y3B9; -.
DR PaxDb; Q9Y3B9; -.
DR PeptideAtlas; Q9Y3B9; -.
DR PRIDE; Q9Y3B9; -.
DR ProteomicsDB; 86008; -.
DR Antibodypedia; 20731; 79 antibodies from 15 providers.
DR DNASU; 51018; -.
DR Ensembl; ENST00000366932.4; ENSP00000355899.3; ENSG00000067533.6.
DR GeneID; 51018; -.
DR KEGG; hsa:51018; -.
DR MANE-Select; ENST00000366932.4; ENSP00000355899.3; NM_016052.4; NP_057136.2.
DR UCSC; uc001hlj.3; human.
DR CTD; 51018; -.
DR DisGeNET; 51018; -.
DR GeneCards; RRP15; -.
DR HGNC; HGNC:24255; RRP15.
DR HPA; ENSG00000067533; Low tissue specificity.
DR MIM; 611193; gene.
DR neXtProt; NX_Q9Y3B9; -.
DR OpenTargets; ENSG00000067533; -.
DR PharmGKB; PA162402123; -.
DR VEuPathDB; HostDB:ENSG00000067533; -.
DR eggNOG; KOG2974; Eukaryota.
DR GeneTree; ENSGT00390000001960; -.
DR HOGENOM; CLU_079732_0_0_1; -.
DR InParanoid; Q9Y3B9; -.
DR OMA; EDEPAWA; -.
DR OrthoDB; 1522334at2759; -.
DR PhylomeDB; Q9Y3B9; -.
DR TreeFam; TF106119; -.
DR PathwayCommons; Q9Y3B9; -.
DR SignaLink; Q9Y3B9; -.
DR BioGRID-ORCS; 51018; 673 hits in 1087 CRISPR screens.
DR ChiTaRS; RRP15; human.
DR GeneWiki; RRP15; -.
DR GenomeRNAi; 51018; -.
DR Pharos; Q9Y3B9; Tdark.
DR PRO; PR:Q9Y3B9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y3B9; protein.
DR Bgee; ENSG00000067533; Expressed in secondary oocyte and 194 other tissues.
DR Genevisible; Q9Y3B9; HS.
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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CHAIN 2..282
FT /note="RRP15-like protein"
FT /id="PRO_0000273213"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..144
FT /evidence="ECO:0000255"
FT COMPBIAS 47..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 9
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT VARIANT 32
FT /note="A -> V (in dbSNP:rs34358288)"
FT /id="VAR_053813"
FT VARIANT 149
FT /note="K -> N (in dbSNP:rs11118075)"
FT /id="VAR_030112"
FT VARIANT 230
FT /note="K -> R (in dbSNP:rs3737978)"
FT /id="VAR_030113"
FT CONFLICT 23
FT /note="K -> N (in Ref. 2; AAD34110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 31484 MW; 3FB1E3D861FB938F CRC64;
MAAAAPDSRV SEEENLKKTP KKKMKMVTGA VASVLEDEAT DTSDSEGSCG SEKDHFYSDD
DAIEADSEGD AEPCDKENEN DGESSVGTNM GWADAMAKVL NKKTPESKPT ILVKNKKLEK
EKEKLKQERL EKIKQRDKRL EWEMMCRVKP DVVQDKETER NLQRIATRGV VQLFNAVQKH
QKNVDEKVKE AGSSMRKRAK LISTVSKKDF ISVLRGMDGS TNETASSRKK PKAKQTEVKS
EEGPGWTILR DDFMMGASMK DWDKESDGPD DSRPESASDS DT
