SLX9_HUMAN
ID SLX9_HUMAN Reviewed; 230 AA.
AC Q9NSI2;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ribosome biogenesis protein SLX9 homolog {ECO:0000305};
GN Name=SLX9 {ECO:0000312|HGNC:HGNC:15811}; Synonyms=C21orf70, FAM207A;
GN ORFNames=PRED56;
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 [MRNA] (ISOFORMS A AND B).
RX PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S.,
RA Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.;
RT "From PREDs and open reading frames to cDNA isolation: revisiting the human
RT chromosome 21 transcription map.";
RL Genomics 78:46-54(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34 AND SER-203, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34 AND SER-203, AND
RP 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).
CC -!- FUNCTION: May be involved in ribosome biogenesis.
CC {ECO:0000250|UniProtKB:P53251}.
CC -!- INTERACTION:
CC Q9NSI2; Q08379: GOLGA2; NbExp=4; IntAct=EBI-5457304, EBI-618309;
CC Q9NSI2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-5457304, EBI-5916454;
CC Q9NSI2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5457304, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P53251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9NSI2-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9NSI2-2; Sequence=VSP_003831;
CC -!- TISSUE SPECIFICITY: Not detected in any tested tissue.
CC -!- SIMILARITY: Belongs to the SLX9 family. {ECO:0000305}.
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DR EMBL; AF391113; AAL34504.1; -; mRNA.
DR EMBL; AF391114; AAL34505.1; -; mRNA.
DR EMBL; AL163301; CAB90492.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC009341; AAH09341.1; -; mRNA.
DR CCDS; CCDS13718.1; -. [Q9NSI2-1]
DR CCDS; CCDS82682.1; -. [Q9NSI2-2]
DR RefSeq; NP_001303912.1; NM_001316983.1.
DR RefSeq; NP_001303913.1; NM_001316984.1. [Q9NSI2-2]
DR RefSeq; NP_001303914.1; NM_001316985.1.
DR RefSeq; NP_001303915.1; NM_001316986.1.
DR RefSeq; NP_001303917.1; NM_001316988.1.
DR RefSeq; NP_478070.1; NM_058190.3. [Q9NSI2-1]
DR AlphaFoldDB; Q9NSI2; -.
DR BioGRID; 124511; 112.
DR IntAct; Q9NSI2; 21.
DR MINT; Q9NSI2; -.
DR STRING; 9606.ENSP00000291634; -.
DR iPTMnet; Q9NSI2; -.
DR PhosphoSitePlus; Q9NSI2; -.
DR BioMuta; FAM207A; -.
DR DMDM; 17865450; -.
DR EPD; Q9NSI2; -.
DR jPOST; Q9NSI2; -.
DR MassIVE; Q9NSI2; -.
DR MaxQB; Q9NSI2; -.
DR PaxDb; Q9NSI2; -.
DR PeptideAtlas; Q9NSI2; -.
DR PRIDE; Q9NSI2; -.
DR ProteomicsDB; 82552; -. [Q9NSI2-1]
DR ProteomicsDB; 82553; -. [Q9NSI2-2]
DR Antibodypedia; 49420; 101 antibodies from 15 providers.
DR DNASU; 85395; -.
DR Ensembl; ENST00000291634.11; ENSP00000291634.6; ENSG00000160256.13. [Q9NSI2-1]
DR Ensembl; ENST00000397826.7; ENSP00000380926.3; ENSG00000160256.13. [Q9NSI2-2]
DR GeneID; 85395; -.
DR KEGG; hsa:85395; -.
DR MANE-Select; ENST00000291634.11; ENSP00000291634.6; NM_058190.4; NP_478070.1.
DR UCSC; uc002zgl.4; human. [Q9NSI2-1]
DR CTD; 85395; -.
DR GeneCards; FAM207A; -.
DR HGNC; HGNC:15811; SLX9.
DR HPA; ENSG00000160256; Low tissue specificity.
DR neXtProt; NX_Q9NSI2; -.
DR OpenTargets; ENSG00000160256; -.
DR VEuPathDB; HostDB:ENSG00000160256; -.
DR eggNOG; ENOG502S25R; Eukaryota.
DR GeneTree; ENSGT00390000015709; -.
DR HOGENOM; CLU_099072_0_0_1; -.
DR InParanoid; Q9NSI2; -.
DR OMA; KIKHVRQ; -.
DR OrthoDB; 1611351at2759; -.
DR PhylomeDB; Q9NSI2; -.
DR TreeFam; TF336348; -.
DR PathwayCommons; Q9NSI2; -.
DR SignaLink; Q9NSI2; -.
DR BioGRID-ORCS; 85395; 84 hits in 1079 CRISPR screens.
DR GenomeRNAi; 85395; -.
DR Pharos; Q9NSI2; Tdark.
DR PRO; PR:Q9NSI2; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9NSI2; protein.
DR Bgee; ENSG00000160256; Expressed in popliteal artery and 149 other tissues.
DR ExpressionAtlas; Q9NSI2; baseline and differential.
DR Genevisible; Q9NSI2; HS.
DR GO; GO:0030686; C:90S preribosome; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:InterPro.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:InterPro.
DR InterPro; IPR028160; Slx9-like.
DR Pfam; PF15341; SLX9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..230
FT /note="Ribosome biogenesis protein SLX9 homolog"
FT /id="PRO_0000079528"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 81..95
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11707072"
FT /id="VSP_003831"
FT VARIANT 212
FT /note="V -> L (in dbSNP:rs3737075)"
FT /id="VAR_021949"
SQ SEQUENCE 230 AA; 25456 MW; BC7D211C02EA0C89 CRC64;
MGKVRGLRAR VHQAAVRPKG EAAPGPAPPA PEATPPPASA AGKDWAFINT NIFARTKIDP
SALVQKLELD VRSVTSVRRG EAGSSARSVP SIRRGAEAKT VLPKKEKMKL RREQWLQKIE
AIKLAEQKHR EERRRRATVV VGDLHPLRDA LPELLGLEAG SRRQARSRES NKPRPSELSR
MSAAQRQQLL EEERTRFQEL LASPAYRASP LVAIGQTLAR QMQLEDGGQL
