RRP7A_HUMAN
ID RRP7A_HUMAN Reviewed; 280 AA.
AC Q9Y3A4; A4FTX2; B2RBG4; Q0VAD0; Q5JZ94; Q6P4B5; Q8IVR9; Q8IVY0; Q8N5Q3;
AC Q8NEY6; Q9Y3H5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ribosomal RNA-processing protein 7 homolog A;
DE AltName: Full=Gastric cancer antigen Zg14;
GN Name=RRP7A; ORFNames=CGI-96;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-85.
RC TISSUE=Brain, Duodenum, Liver, Lymph, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-280.
RC TISSUE=Gastric adenocarcinoma;
RX PubMed=12087473; DOI=10.1038/sj.bjc.6600321;
RA Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.;
RT "Serological identification and expression analysis of gastric cancer-
RT associated genes.";
RL Br. J. Cancer 86:1824-1830(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, 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 INVOLVEMENT IN MCPH28, VARIANT MCPH28 CYS-155, CHARACTERIZATION OF VARIANT
RP MCPH28 CYS-155, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH NOL6.
RX PubMed=33199730; DOI=10.1038/s41467-020-19658-0;
RA Farooq M., Lindbaek L., Krogh N., Doganli C., Keller C., Moennich M.,
RA Goncalves A.B., Sakthivel S., Mang Y., Fatima A., Andersen V.S.,
RA Hussain M.S., Eiberg H., Hansen L., Kjaer K.W., Gopalakrishnan J.,
RA Pedersen L.B., Moellgaard K., Nielsen H., Baig S.M., Tommerup N.,
RA Christensen S.T., Larsen L.A.;
RT "RRP7A links primary microcephaly to dysfunction of ribosome biogenesis,
RT resorption of primary cilia, and neurogenesis.";
RL Nat. Commun. 11:5816-5816(2020).
CC -!- FUNCTION: Nucleolar protein that is involved in ribosomal RNA (rRNA)
CC processing (PubMed:33199730). Also plays a role in primary cilia
CC resorption, and cell cycle progression in neurogenesis and neocortex
CC development (PubMed:33199730). {ECO:0000269|PubMed:33199730}.
CC -!- SUBUNIT: Interacts with NOL6; required for NOL6 localization to
CC nucleolus. {ECO:0000269|PubMed:33199730}.
CC -!- INTERACTION:
CC Q9Y3A4; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-7223720, EBI-742909;
CC Q9Y3A4; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-7223720, EBI-5278764;
CC Q9Y3A4; O95257: GADD45G; NbExp=3; IntAct=EBI-7223720, EBI-448202;
CC Q9Y3A4; Q9UBB9: TFIP11; NbExp=5; IntAct=EBI-7223720, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:33199730}.
CC Cell projection, cilium {ECO:0000269|PubMed:33199730}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:33199730}.
CC -!- TISSUE SPECIFICITY: Expressed in the apical radial glial cells in the
CC developing brain. {ECO:0000269|PubMed:33199730}.
CC -!- DISEASE: Microcephaly 28, primary, autosomal recessive (MCPH28)
CC [MIM:619453]: A form of microcephaly, a disease defined as a head
CC circumference more than 3 standard deviations below the age, sex and
CC ethnically matched mean. Brain weight is markedly reduced and the
CC cerebral cortex is disproportionately small. MCPH28 is an autosomal
CC recessive form characterized by reduced head size (down to -8 SD) and
CC variably impaired intellectual development apparent from early
CC childhood. {ECO:0000269|PubMed:33199730}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the RRP7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31838.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL022316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK314650; BAG37211.1; -; mRNA.
DR EMBL; BC031838; AAH31838.1; ALT_INIT; mRNA.
DR EMBL; BC041639; AAH41639.1; -; mRNA.
DR EMBL; BC042335; AAH42335.1; -; mRNA.
DR EMBL; BC063537; AAH63537.1; -; mRNA.
DR EMBL; BC073834; AAH73834.1; -; mRNA.
DR EMBL; BC121118; AAI21119.1; -; mRNA.
DR EMBL; BC121119; AAI21120.1; -; mRNA.
DR EMBL; AY039240; AAK68659.1; -; mRNA.
DR CCDS; CCDS14036.1; -.
DR RefSeq; NP_056518.2; NM_015703.4.
DR PDB; 7MQ8; EM; 3.60 A; NI=1-280.
DR PDB; 7MQ9; EM; 3.87 A; NI=1-280.
DR PDB; 7MQA; EM; 2.70 A; NI=1-280.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q9Y3A4; -.
DR SMR; Q9Y3A4; -.
DR BioGRID; 118153; 99.
DR IntAct; Q9Y3A4; 31.
DR MINT; Q9Y3A4; -.
DR STRING; 9606.ENSP00000321449; -.
DR iPTMnet; Q9Y3A4; -.
DR PhosphoSitePlus; Q9Y3A4; -.
DR BioMuta; RRP7A; -.
DR DMDM; 66774227; -.
DR EPD; Q9Y3A4; -.
DR jPOST; Q9Y3A4; -.
DR MassIVE; Q9Y3A4; -.
DR MaxQB; Q9Y3A4; -.
DR PaxDb; Q9Y3A4; -.
DR PeptideAtlas; Q9Y3A4; -.
DR PRIDE; Q9Y3A4; -.
DR ProteomicsDB; 85996; -.
DR Antibodypedia; 277; 131 antibodies from 26 providers.
DR DNASU; 27341; -.
DR Ensembl; ENST00000323013.7; ENSP00000321449.6; ENSG00000189306.11.
DR GeneID; 27341; -.
DR KEGG; hsa:27341; -.
DR MANE-Select; ENST00000323013.7; ENSP00000321449.6; NM_015703.5; NP_056518.2.
DR UCSC; uc003bcq.4; human.
DR CTD; 27341; -.
DR GeneCards; RRP7A; -.
DR HGNC; HGNC:24286; RRP7A.
DR HPA; ENSG00000189306; Low tissue specificity.
DR MIM; 619449; gene.
DR MIM; 619453; phenotype.
DR neXtProt; NX_Q9Y3A4; -.
DR OpenTargets; ENSG00000189306; -.
DR PharmGKB; PA162402175; -.
DR VEuPathDB; HostDB:ENSG00000189306; -.
DR eggNOG; KOG4008; Eukaryota.
DR GeneTree; ENSGT00390000018482; -.
DR HOGENOM; CLU_036234_2_1_1; -.
DR InParanoid; Q9Y3A4; -.
DR OMA; FIRLMDP; -.
DR OrthoDB; 1607176at2759; -.
DR PhylomeDB; Q9Y3A4; -.
DR TreeFam; TF313949; -.
DR PathwayCommons; Q9Y3A4; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9Y3A4; -.
DR BioGRID-ORCS; 27341; 652 hits in 1045 CRISPR screens.
DR ChiTaRS; RRP7A; human.
DR GeneWiki; CTA-126B4.3; -.
DR GenomeRNAi; 27341; -.
DR Pharos; Q9Y3A4; Tbio.
DR PRO; PR:Q9Y3A4; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9Y3A4; protein.
DR Bgee; ENSG00000189306; Expressed in mucosa of transverse colon and 112 other tissues.
DR ExpressionAtlas; Q9Y3A4; baseline and differential.
DR Genevisible; Q9Y3A4; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0032545; C:CURI complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0034456; C:UTP-C complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR GO; GO:0061523; P:cilium disassembly; IMP:UniProtKB.
DR GO; GO:1902570; P:protein localization to nucleolus; IMP:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR CDD; cd12294; RRM_Rrp7A; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR040447; RRM_Rrp7.
DR InterPro; IPR040446; RRP7.
DR InterPro; IPR024326; RRP7_C.
DR InterPro; IPR034890; Rrp7A_RRM.
DR PANTHER; PTHR13191; PTHR13191; 1.
DR Pfam; PF17799; RRM_Rrp7; 1.
DR Pfam; PF12923; RRP7; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cytoplasm; Cytoskeleton; Disease variant;
KW Intellectual disability; Nucleus; Phosphoprotein; Primary microcephaly;
KW Reference proteome; RNA-binding.
FT CHAIN 1..280
FT /note="Ribosomal RNA-processing protein 7 homolog A"
FT /id="PRO_0000082008"
FT DOMAIN 61..90
FT /note="RRM"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VARIANT 75
FT /note="L -> M (in dbSNP:rs8139383)"
FT /id="VAR_052227"
FT VARIANT 85
FT /note="V -> I (in dbSNP:rs1812240)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052228"
FT VARIANT 88
FT /note="V -> I (in dbSNP:rs11553441)"
FT /id="VAR_052229"
FT VARIANT 155
FT /note="W -> C (in MCPH28; increased proteolytic
FT degradation; decreased recruitment to the nucleolus;
FT decreased interaction with NOL6; decreased function in
FT localization of NOL6 to the nucleolus; loss of function in
FT rRNA processing; changed function in cilia resorption)"
FT /evidence="ECO:0000269|PubMed:33199730"
FT /id="VAR_086134"
FT CONFLICT 16..17
FT /note="RI -> SA (in Ref. 4; AAH31838)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="E -> K (in Ref. 2; BAG37211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 32334 MW; 3625D609B0FF2F76 CRC64;
MVARRRKCAA RDPEDRIPSP LGYAAIPIKF SEKQQASHYL YVRAHGVRQG TKSTWPQKRT
LFVLNVPPYC TEESLSRLLS TCGLVQSVEL QEKPDLAESP KESRSKFFHP KPVPGFQVAY
VVFQKPSGVS AALALKGPLL VSTESHPVKS GIHKWISDYA DSVPDPEALR VEVDTFMEAY
DQKIAEEEAK AKEEEGVPDE EGWVKVTRRG RRPVLPRTEA ASLRVLERER RKRSRKELLN
FYAWQHRESK MEHLAQLRKK FEEDKQRIEL LRAQRKFRPY
