CI114_HUMAN
ID CI114_HUMAN Reviewed; 376 AA.
AC Q5T280; Q0D2P6; Q6P469; Q6PGP9; Q6PIJ1; Q6PJV9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Putative methyltransferase C9orf114 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
DE AltName: Full=Centromere protein 32 {ECO:0000303|PubMed:25657325};
DE Short=CENP-32 {ECO:0000303|PubMed:25657325};
DE AltName: Full=Kinetochore-associated protein {ECO:0000303|PubMed:20813266};
DE AltName: Full=SPOUT domain-containing methyltransferase 1 {ECO:0000312|HGNC:HGNC:26933};
GN Name=SPOUT1 {ECO:0000312|HGNC:HGNC:26933}; Synonyms=C9orf114;
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=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-130 AND THR-369.
RC TISSUE=Brain, Eye, Leukocyte, Ovary, and 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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
RN [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25657325; DOI=10.1091/mbc.e14-09-1366;
RA Ohta S., Wood L., Toramoto I., Yagyu K., Fukagawa T., Earnshaw W.C.;
RT "CENP-32 is required to maintain centrosomal dominance in bipolar spindle
RT assembly.";
RL Mol. Biol. Cell 26:1225-1237(2015).
RN [6]
RP FUNCTION, AND MIRNA-BINDING.
RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA Lehmann G., Schall K., Urlaub H., Meister G.;
RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL Mol. Cell 66:270-284(2017).
RN [7]
RP INTERACTION WITH INCA1.
RX PubMed=21750715; DOI=10.1371/journal.pone.0021505;
RA Zhang F., Baeumer N., Rode M., Ji P., Zhang T., Berdel W.E.,
RA Mueller-Tidow C.;
RT "The inhibitor of growth protein 5 (ING5) depends on INCA1 as a co-factor
RT for its antiproliferative effects.";
RL PLoS ONE 6:E21505-E21505(2011).
CC -!- FUNCTION: Required for association of the centrosomes with the poles of
CC the bipolar mitotic spindle during metaphase (PubMed:20813266,
CC PubMed:25657325). Also involved in chromosome alignment
CC (PubMed:20813266). May promote centrosome maturation probably by
CC recruiting A-kinase anchor protein AKAP9 to centrosomes in early
CC mitosis (PubMed:25657325). Binds specifically to miRNA MIR145 hairpin,
CC regulates MIR145 expression at a postranscriptional level
CC (PubMed:28431233). {ECO:0000269|PubMed:20813266,
CC ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:28431233}.
CC -!- SUBUNIT: Interacts with INCA1. {ECO:0000269|PubMed:21750715}.
CC -!- INTERACTION:
CC Q5T280; Q0VD86: INCA1; NbExp=2; IntAct=EBI-2880213, EBI-6509505;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:25657325}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:20813266, ECO:0000269|PubMed:25657325}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:25657325}. Note=Associated with the outer
CC kinetochore. {ECO:0000269|PubMed:20813266}.
CC -!- MISCELLANEOUS: Depletion with RNAi causes a significant accumulation of
CC cells in later prometaphase with misaligned chromosomes.
CC {ECO:0000269|PubMed:20813266}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; AL441992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010579; AAH10579.1; -; mRNA.
DR EMBL; BC033677; AAH33677.1; -; mRNA.
DR EMBL; BC039590; AAH39590.1; -; mRNA.
DR EMBL; BC046133; AAH46133.1; -; mRNA.
DR EMBL; BC063644; AAH63644.1; -; mRNA.
DR EMBL; BC021273; AAH21273.1; -; mRNA.
DR CCDS; CCDS6913.1; -.
DR RefSeq; NP_057474.2; NM_016390.3.
DR PDB; 4RG1; X-ray; 1.86 A; A/B=64-376.
DR PDBsum; 4RG1; -.
DR AlphaFoldDB; Q5T280; -.
DR SMR; Q5T280; -.
DR BioGRID; 119567; 125.
DR IntAct; Q5T280; 29.
DR MINT; Q5T280; -.
DR STRING; 9606.ENSP00000354812; -.
DR iPTMnet; Q5T280; -.
DR PhosphoSitePlus; Q5T280; -.
DR BioMuta; SPOUT1; -.
DR DMDM; 126302532; -.
DR EPD; Q5T280; -.
DR jPOST; Q5T280; -.
DR MassIVE; Q5T280; -.
DR MaxQB; Q5T280; -.
DR PaxDb; Q5T280; -.
DR PeptideAtlas; Q5T280; -.
DR PRIDE; Q5T280; -.
DR ProteomicsDB; 64319; -.
DR Antibodypedia; 17713; 49 antibodies from 11 providers.
DR DNASU; 51490; -.
DR Ensembl; ENST00000361256.10; ENSP00000354812.5; ENSG00000198917.13.
DR GeneID; 51490; -.
DR KEGG; hsa:51490; -.
DR MANE-Select; ENST00000361256.10; ENSP00000354812.5; NM_016390.4; NP_057474.2.
DR UCSC; uc004bwd.3; human.
DR CTD; 51490; -.
DR DisGeNET; 51490; -.
DR GeneCards; SPOUT1; -.
DR HGNC; HGNC:26933; SPOUT1.
DR HPA; ENSG00000198917; Low tissue specificity.
DR MIM; 617614; gene.
DR neXtProt; NX_Q5T280; -.
DR OpenTargets; ENSG00000198917; -.
DR PharmGKB; PA134958095; -.
DR VEuPathDB; HostDB:ENSG00000198917; -.
DR eggNOG; KOG3925; Eukaryota.
DR GeneTree; ENSGT00390000016537; -.
DR HOGENOM; CLU_017233_4_0_1; -.
DR InParanoid; Q5T280; -.
DR OMA; FPIHKDL; -.
DR OrthoDB; 867236at2759; -.
DR PhylomeDB; Q5T280; -.
DR TreeFam; TF105821; -.
DR PathwayCommons; Q5T280; -.
DR SignaLink; Q5T280; -.
DR BioGRID-ORCS; 51490; 781 hits in 1042 CRISPR screens.
DR ChiTaRS; SPOUT1; human.
DR GenomeRNAi; 51490; -.
DR Pharos; Q5T280; Tbio.
DR PRO; PR:Q5T280; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5T280; protein.
DR Bgee; ENSG00000198917; Expressed in granulocyte and 94 other tissues.
DR ExpressionAtlas; Q5T280; baseline and differential.
DR Genevisible; Q5T280; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051661; P:maintenance of centrosome location; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035196; P:miRNA processing; IMP:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:UniProtKB.
DR CDD; cd18086; HsC9orf114-like; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003750; Put_MeTrfase.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR12150; PTHR12150; 1.
DR Pfam; PF02598; Methyltrn_RNA_3; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Kinetochore; Methyltransferase; Mitosis; Reference proteome;
KW RNA-binding; Transferase.
FT CHAIN 1..376
FT /note="Putative methyltransferase C9orf114"
FT /id="PRO_0000238468"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 63
FT /note="A -> V (in dbSNP:rs34500948)"
FT /id="VAR_050844"
FT VARIANT 130
FT /note="T -> R (in dbSNP:rs6478854)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026552"
FT VARIANT 369
FT /note="I -> T (in dbSNP:rs2280843)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026553"
FT CONFLICT 343
FT /note="C -> Y (in Ref. 2; AAH33677)"
FT /evidence="ECO:0000305"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 90..106
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:4RG1"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:4RG1"
FT HELIX 353..372
FT /evidence="ECO:0007829|PDB:4RG1"
SQ SEQUENCE 376 AA; 42009 MW; 30A5AA406834DC27 CRC64;
MAERGRKRPC GPGEHGQRIE WRKWKQQKKE EKKKWKDLKL MKKLERQRAQ EEQAKRLEEE
EAAAEKEDRG RPYTLSVALP GSILDNAQSP ELRTYLAGQI ARACAIFCVD EIVVFDEEGQ
DAKTVEGEFT GVGKKGQACV QLARILQYLE CPQYLRKAFF PKHQDLQFAG LLNPLDSPHH
MRQDEESEFR EGIVVDRPTR PGHGSFVNCG MKKEVKIDKN LEPGLRVTVR LNQQQHPDCK
TYHGKVVSSQ DPRTKAGLYW GYTVRLASCL SAVFAEAPFQ DGYDLTIGTS ERGSDVASAQ
LPNFRHALVV FGGLQGLEAG ADADPNLEVA EPSVLFDLYV NTCPGQGSRT IRTEEAILIS
LAALQPGLIQ AGARHT
