CI114_MOUSE
ID CI114_MOUSE Reviewed; 385 AA.
AC Q3UHX9; Q8BQY9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative methyltransferase C9orf114 homolog {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
DE AltName: Full=Centromere protein 32 {ECO:0000250|UniProtKB:Q5T280};
DE Short=CENP-32 {ECO:0000250|UniProtKB:Q5T280};
DE AltName: Full=Kinetochore-associated protein {ECO:0000250|UniProtKB:Q5T280};
DE AltName: Full=SPOUT domain-containing methyltransferase 1 {ECO:0000312|MGI:MGI:106544};
GN Name=Spout1 {ECO:0000312|MGI:MGI:106544}; Synonyms=D2Wsu81e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for association of the centrosomes with the poles of
CC the bipolar mitotic spindle during metaphase. Also involved in
CC chromosome alignment. May promote centrosome maturation probably by
CC recruiting A-kinase anchor protein AKAP9 to centrosomes in early
CC mitosis. Binds specifically to miRNA MIR145 hairpin, regulates MIR145
CC expression at a postranscriptional level (By similarity).
CC {ECO:0000250|UniProtKB:Q5T280}.
CC -!- SUBUNIT: Interacts with INCA1. {ECO:0000250|UniProtKB:Q5T280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q5T280}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q5T280}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q5T280}.
CC Note=Associated with the outer kinetochore.
CC {ECO:0000250|UniProtKB:Q5T280}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UHX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UHX9-2; Sequence=VSP_018611;
CC -!- MISCELLANEOUS: [Isoform 1]: May be due to intron retention.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; AK046148; BAC32613.1; -; mRNA.
DR EMBL; AK147162; BAE27727.1; -; mRNA.
DR CCDS; CCDS15873.2; -. [Q3UHX9-1]
DR RefSeq; NP_766248.3; NM_172660.4. [Q3UHX9-1]
DR AlphaFoldDB; Q3UHX9; -.
DR SMR; Q3UHX9; -.
DR BioGRID; 230664; 32.
DR STRING; 10090.ENSMUSP00000097793; -.
DR iPTMnet; Q3UHX9; -.
DR PhosphoSitePlus; Q3UHX9; -.
DR EPD; Q3UHX9; -.
DR jPOST; Q3UHX9; -.
DR MaxQB; Q3UHX9; -.
DR PaxDb; Q3UHX9; -.
DR PeptideAtlas; Q3UHX9; -.
DR PRIDE; Q3UHX9; -.
DR ProteomicsDB; 285445; -. [Q3UHX9-1]
DR ProteomicsDB; 285446; -. [Q3UHX9-2]
DR Antibodypedia; 17713; 49 antibodies from 11 providers.
DR DNASU; 227695; -.
DR Ensembl; ENSMUST00000100220; ENSMUSP00000097793; ENSMUSG00000039660. [Q3UHX9-1]
DR GeneID; 227695; -.
DR KEGG; mmu:227695; -.
DR UCSC; uc008jbl.2; mouse. [Q3UHX9-1]
DR CTD; 51490; -.
DR MGI; MGI:106544; Spout1.
DR VEuPathDB; HostDB:ENSMUSG00000039660; -.
DR eggNOG; KOG3925; Eukaryota.
DR GeneTree; ENSGT00390000016537; -.
DR HOGENOM; CLU_017233_4_0_1; -.
DR InParanoid; Q3UHX9; -.
DR OMA; FPIHKDL; -.
DR OrthoDB; 867236at2759; -.
DR PhylomeDB; Q3UHX9; -.
DR TreeFam; TF105821; -.
DR BioGRID-ORCS; 227695; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Spout1; mouse.
DR PRO; PR:Q3UHX9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UHX9; protein.
DR Bgee; ENSMUSG00000039660; Expressed in spermatid and 187 other tissues.
DR Genevisible; Q3UHX9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0031616; C:spindle pole centrosome; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035196; P:miRNA processing; ISS:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISS: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 Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Kinetochore; Methyltransferase; Mitosis;
KW Reference proteome; Transferase.
FT CHAIN 1..385
FT /note="Putative methyltransferase C9orf114 homolog"
FT /id="PRO_0000238469"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018611"
FT CONFLICT 258
FT /note="G -> C (in Ref. 1; BAC32613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42958 MW; 729C59EC15F8B93F CRC64;
MAERPRKRPC GPGEHGQRVE WRKWKQQKKE EKKKWKDLKI MKKLERQRAQ EEEAKRQEEE
EEAAAQRSNQ GRPYTLSVAL PGSILDNAQS PELRTYLAGQ IARACTIFCV DEIVVFDEEG
QDTKSVEGEF RGVGKKGQAC VQLARILQYL ECPQYLRKAF FPKHQDLQFA GILNPLDSPH
HMRQDEESEF REGVVVDRPT KAGHGSLVNC GMKKEVKIDK KLDPGLRVTV RLNQQQLPEC
KTYKGTVVSS QDPRTKAGLY WGYTVRLASC LSAVFAEAPF QDGYDLTIGT SERGSDVASA
QLPSFRHALV VFGGLQGLEA AVDADPNLEV ADPSVLFDFY VNTCLSQGSR TIRTEEAILI
SLAALQPGLT QVGSRPASPL SGPRM
