NOPC1_HUMAN
ID NOPC1_HUMAN Reviewed; 185 AA.
AC Q8N5I9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=NOP protein chaperone 1 {ECO:0000305};
GN Name=NOPCHAP1 {ECO:0000312|HGNC:HGNC:28628}; Synonyms=C12orf45;
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 GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-66 AND SER-178, AND
RP 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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP 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 [11]
RP FUNCTION, INTERACTION WITH RUVBL1; RUVBL2 AND NOP58, AND SUBCELLULAR
RP LOCATION.
RX PubMed=33367824; DOI=10.1093/nar/gkaa1226;
RA Abel Y., Paiva A.C.F., Bizarro J., Chagot M.E., Santo P.E., Robert M.C.,
RA Quinternet M., Vandermoere F., Sousa P.M.F., Fort P., Charpentier B.,
RA Manival X., Bandeiras T.M., Bertrand E., Verheggen C.;
RT "NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2
RT during box C/D snoRNP biogenesis.";
RL Nucleic Acids Res. 49:1094-1113(2021).
CC -!- FUNCTION: Client-loading PAQosome/R2TP complex cofactor that selects
CC NOP58 to promote box C/D small nucleolar ribonucleoprotein (snoRNP)
CC assembly. Acts as a bridge between NOP58 and the R2TP complex via
CC RUVBL1:RUVBL2. {ECO:0000269|PubMed:33367824}.
CC -!- SUBUNIT: Interacts with NOP58, RUVBL1 and RUVBL2; the interactions are
CC direct and NOPCHAP1 bridges the association of NOP58 with RUVBL1:RUVBL2
CC even in absence of snoRNAs. The interactions with RUVBL1 and RUVBL2 are
CC disrupted upon ATP binding. {ECO:0000269|PubMed:33367824}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:33367824}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32326.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC090051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032326; AAH32326.1; ALT_FRAME; mRNA.
DR CCDS; CCDS41825.1; -.
DR RefSeq; NP_689531.2; NM_152318.2.
DR AlphaFoldDB; Q8N5I9; -.
DR SMR; Q8N5I9; -.
DR BioGRID; 125706; 20.
DR IntAct; Q8N5I9; 12.
DR STRING; 9606.ENSP00000447057; -.
DR iPTMnet; Q8N5I9; -.
DR MetOSite; Q8N5I9; -.
DR PhosphoSitePlus; Q8N5I9; -.
DR BioMuta; C12orf45; -.
DR DMDM; 313104091; -.
DR EPD; Q8N5I9; -.
DR jPOST; Q8N5I9; -.
DR MassIVE; Q8N5I9; -.
DR MaxQB; Q8N5I9; -.
DR PaxDb; Q8N5I9; -.
DR PeptideAtlas; Q8N5I9; -.
DR PRIDE; Q8N5I9; -.
DR ProteomicsDB; 72064; -.
DR Antibodypedia; 48157; 18 antibodies from 9 providers.
DR DNASU; 121053; -.
DR Ensembl; ENST00000552951.7; ENSP00000447057.1; ENSG00000151131.11.
DR GeneID; 121053; -.
DR KEGG; hsa:121053; -.
DR MANE-Select; ENST00000552951.7; ENSP00000447057.1; NM_152318.3; NP_689531.2.
DR UCSC; uc001tlb.4; human.
DR CTD; 121053; -.
DR DisGeNET; 121053; -.
DR GeneCards; NOPCHAP1; -.
DR HGNC; HGNC:28628; NOPCHAP1.
DR HPA; ENSG00000151131; Low tissue specificity.
DR neXtProt; NX_Q8N5I9; -.
DR OpenTargets; ENSG00000151131; -.
DR VEuPathDB; HostDB:ENSG00000151131; -.
DR eggNOG; ENOG502S6C1; Eukaryota.
DR GeneTree; ENSGT00390000000376; -.
DR HOGENOM; CLU_105671_0_0_1; -.
DR InParanoid; Q8N5I9; -.
DR OMA; IIQMDVA; -.
DR OrthoDB; 1478046at2759; -.
DR PhylomeDB; Q8N5I9; -.
DR TreeFam; TF333191; -.
DR PathwayCommons; Q8N5I9; -.
DR SignaLink; Q8N5I9; -.
DR BioGRID-ORCS; 121053; 558 hits in 1054 CRISPR screens.
DR ChiTaRS; C12orf45; human.
DR GenomeRNAi; 121053; -.
DR Pharos; Q8N5I9; Tdark.
DR PRO; PR:Q8N5I9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8N5I9; protein.
DR Bgee; ENSG00000151131; Expressed in body of pancreas and 177 other tissues.
DR ExpressionAtlas; Q8N5I9; baseline and differential.
DR Genevisible; Q8N5I9; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0062064; F:box C/D snoRNP complex binding; IDA:UniProtKB.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:UniProtKB.
DR InterPro; IPR027921; NOPCHAP1.
DR PANTHER; PTHR28674; PTHR28674; 1.
DR Pfam; PF15370; DUF4598; 1.
PE 1: Evidence at protein level;
KW Chaperone; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..185
FT /note="NOP protein chaperone 1"
FT /id="PRO_0000263623"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VARIANT 5
FT /note="G -> S (in dbSNP:rs12580271)"
FT /id="VAR_056833"
FT VARIANT 8
FT /note="K -> Q (in dbSNP:rs1129593)"
FT /id="VAR_060438"
SQ SEQUENCE 185 AA; 20123 MW; 608CDD290D18B257 CRC64;
MEVHGKPKAS PSCSSPTRDS SGVPVSKELL TAGSDGRGGI WDRLLINSQP KSRKTSTLQT
VRIERSPLLD QVQTFLPQMA RANEKLRKEM AAAPPGRFNI ENIDGPHSKV IQMDVALFEM
NQSDSKEVDS SEESSQDSSE NSSESEDEDD SIPSEVTIDN IKLPNSEGGK GKIEVLDSPA
SKKKK
