UT14A_MOUSE
ID UT14A_MOUSE Reviewed; 767 AA.
AC Q640M1; A2AFX7; Q6A094; Q6EJB4; Q6P6L1; Q9CZK8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=U3 small nucleolar RNA-associated protein 14 homolog A;
DE AltName: Full=Juvenile spermatogonial depletion-like X-linked protein;
DE Short=Jsd-like X-linked protein;
GN Name=Utp14a; Synonyms=JsdX, Kiaa0266;
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 [MRNA] (ISOFORM 1).
RX PubMed=15258580; DOI=10.1038/ng1390;
RA Bradley J., Baltus A., Skaletsky H., Royce-Tolland M., Dewar K., Page D.C.;
RT "An X-to-autosome retrogene is required for spermatogenesis in mice.";
RL Nat. Genet. 36:872-876(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Jaw;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=15289605; DOI=10.1073/pnas.0401130101;
RA Rohozinski J., Bishop C.E.;
RT "The mouse juvenile spermatogonial depletion (jsd) phenotype is due to a
RT mutation in the X-derived retrogene, mUtp14b.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11695-11700(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31 AND SER-37, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [8]
RP CITRULLINATION AT ARG-431 AND ARG-586.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
CC -!- FUNCTION: May be required for ribosome biogenesis. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DHX37. {ECO:0000250|UniProtKB:Q9BVJ6}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q640M1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q640M1-2; Sequence=VSP_014477, VSP_014478;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15289605}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- MISCELLANEOUS: The mouse genome also contains the Utp14b gene, an
CC autosomal retrotransposed copy of this X-linked gene. Evolution of
CC autosomal retrogenes from X-linked progenitors compensates for X-
CC chromosome silencing during male meiosis.
CC -!- SIMILARITY: Belongs to the UTP14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH62165.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAQ87011.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD32202.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY316163; AAQ87011.1; ALT_FRAME; mRNA.
DR EMBL; AK172924; BAD32202.1; ALT_INIT; mRNA.
DR EMBL; AK012492; BAB28277.1; -; mRNA.
DR EMBL; AL672246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062165; AAH62165.1; ALT_SEQ; mRNA.
DR EMBL; BC082590; AAH82590.1; -; mRNA.
DR CCDS; CCDS30107.1; -. [Q640M1-1]
DR RefSeq; NP_082552.1; NM_028276.1. [Q640M1-1]
DR AlphaFoldDB; Q640M1; -.
DR SMR; Q640M1; -.
DR BioGRID; 215433; 3.
DR STRING; 10090.ENSMUSP00000079538; -.
DR iPTMnet; Q640M1; -.
DR PhosphoSitePlus; Q640M1; -.
DR EPD; Q640M1; -.
DR jPOST; Q640M1; -.
DR MaxQB; Q640M1; -.
DR PaxDb; Q640M1; -.
DR PeptideAtlas; Q640M1; -.
DR PRIDE; Q640M1; -.
DR ProteomicsDB; 298256; -. [Q640M1-1]
DR ProteomicsDB; 298257; -. [Q640M1-2]
DR DNASU; 72554; -.
DR Ensembl; ENSMUST00000080713; ENSMUSP00000079538; ENSMUSG00000063785. [Q640M1-1]
DR GeneID; 72554; -.
DR KEGG; mmu:72554; -.
DR UCSC; uc009tca.1; mouse. [Q640M1-2]
DR UCSC; uc009tcb.1; mouse. [Q640M1-1]
DR CTD; 10813; -.
DR MGI; MGI:1919804; Utp14a.
DR VEuPathDB; HostDB:ENSMUSG00000063785; -.
DR eggNOG; KOG2172; Eukaryota.
DR GeneTree; ENSGT00390000008142; -.
DR HOGENOM; CLU_012635_1_0_1; -.
DR InParanoid; Q640M1; -.
DR OMA; RESKWAK; -.
DR OrthoDB; 370022at2759; -.
DR PhylomeDB; Q640M1; -.
DR TreeFam; TF314531; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 72554; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Utp14a; mouse.
DR PRO; PR:Q640M1; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q640M1; protein.
DR Bgee; ENSMUSG00000063785; Expressed in undifferentiated genital tubercle and 229 other tissues.
DR Genevisible; Q640M1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR InterPro; IPR006709; SSU_processome_Utp14.
DR PANTHER; PTHR14150; PTHR14150; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Citrullination; Coiled coil; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW Ubl conjugation.
FT CHAIN 1..767
FT /note="U3 small nucleolar RNA-associated protein 14 homolog
FT A"
FT /id="PRO_0000065734"
FT REGION 23..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 317..346
FT /evidence="ECO:0000255"
FT COMPBIAS 397..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 431
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 586
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT CROSSLNK 447
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT CROSSLNK 518
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT VAR_SEQ 180..194
FT /note="ARTPLEQEVFNLLHK -> GILQLRDCQNLRRDF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014477"
FT VAR_SEQ 195..767
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014478"
SQ SEQUENCE 767 AA; 87265 MW; CCF90AEA9CFB2593 CRC64;
MNSIKATKGL LALSQQDDLM DLTSNYPLSA SEDEGDSDGE RKHQKLLEAI GSLSGKNRWK
LPERSEAGLK VSEFNVSSEG SGEKLALSDL LGPLKPSSSL AAVKKQLSRV KSKKTLELPL
HKREVEQIHR EVAFSKTSQT LSKWDSVVQK NREAEQLVFP LEKEPSSFAP MEHVFREWKA
RTPLEQEVFN LLHKNKQPVT DPLLTPVEKA SLKAMSLEEA KIRRAELQRA RALQSYYEAR
ARRMKKIKSK KYHKIVKKGK AKKALKDFEQ LRKVDPDAAL EELEKMEKAR MMERMSLKHQ
NSGKWAKSKA IMAKYDLEAR QAMQEQLAKN KELTQKLQVV SESEEEGGAD EEEALVPDIV
NEVQKTADGP NPWMLRSCSR DAKENEIQAD SEQLPESAAH EFPENEENDK PVAEEDELLK
ELEKRRSLRK RSELNQAAEP LGNQETKDST SQEVLSELRA LSKKLSKENH LSKKQKKSPA
KAVDLVWEEE PAPEEDEPLL LQRPERMRTL EELEELGKED SLPNKERPRP SVEGEQVRRN
PQNHSKGKNK KEQMISLQNL LTTRTPSVTS LALPTTVEEL EDEGARDQKQ MIKEAFAGDD
VIKEFLKEKR EAIQANKPKA VDLTLPGWGE WGGMNLKPSA RKRRRFLIKA PEGPPRKDKN
LPNVIISEKR NIHAAAHQVR VLPYPFTHHQ QFERTIQNPI GSTWNTQRAF QKLTAPKVVT
KPGHIIKPIT AEDVDCRSSP RSDVPVMQSN PKQHSKHQKQ RKKSSIG
