UT14C_HUMAN
ID UT14C_HUMAN Reviewed; 766 AA.
AC Q5TAP6; Q5FWG3; Q92555;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=U3 small nucleolar RNA-associated protein 14 homolog C;
GN Name=UTP14C; Synonyms=KIAA0266;
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 MRNA].
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-85.
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 [4]
RP TISSUE SPECIFICITY, AND FUNCTION.
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 [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).
CC -!- FUNCTION: Essential for spermatogenesis. May be required specifically
CC for ribosome biogenesis and hence protein synthesis during male meiosis
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:15289605}.
CC -!- INTERACTION:
CC Q5TAP6; P13196: ALAS1; NbExp=3; IntAct=EBI-11737646, EBI-3905054;
CC Q5TAP6; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-11737646, EBI-11975051;
CC Q5TAP6; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-11737646, EBI-3866279;
CC Q5TAP6; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-11737646, EBI-739624;
CC Q5TAP6; Q96CN9: GCC1; NbExp=3; IntAct=EBI-11737646, EBI-746252;
CC Q5TAP6; Q08379: GOLGA2; NbExp=5; IntAct=EBI-11737646, EBI-618309;
CC Q5TAP6; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-11737646, EBI-11163335;
CC Q5TAP6; Q9UJC3: HOOK1; NbExp=3; IntAct=EBI-11737646, EBI-746704;
CC Q5TAP6; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-11737646, EBI-10961706;
CC Q5TAP6; O75564-2: JRK; NbExp=3; IntAct=EBI-11737646, EBI-17181882;
CC Q5TAP6; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-11737646, EBI-2556193;
CC Q5TAP6; O76011: KRT34; NbExp=3; IntAct=EBI-11737646, EBI-1047093;
CC Q5TAP6; P23508: MCC; NbExp=3; IntAct=EBI-11737646, EBI-307531;
CC Q5TAP6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11737646, EBI-16439278;
CC Q5TAP6; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11737646, EBI-11522433;
CC Q5TAP6; Q15742: NAB2; NbExp=3; IntAct=EBI-11737646, EBI-8641936;
CC Q5TAP6; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-11737646, EBI-14066006;
CC Q5TAP6; Q15276: RABEP1; NbExp=3; IntAct=EBI-11737646, EBI-447043;
CC Q5TAP6; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-11737646, EBI-726876;
CC Q5TAP6; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-11737646, EBI-11523345;
CC Q5TAP6; Q13077: TRAF1; NbExp=3; IntAct=EBI-11737646, EBI-359224;
CC Q5TAP6; Q12933: TRAF2; NbExp=3; IntAct=EBI-11737646, EBI-355744;
CC Q5TAP6; P14373: TRIM27; NbExp=3; IntAct=EBI-11737646, EBI-719493;
CC Q5TAP6; P40222: TXLNA; NbExp=3; IntAct=EBI-11737646, EBI-359793;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:15289605}.
CC -!- MISCELLANEOUS: Encoded by an autosomal retrotransposed copy of the X-
CC linked gene UTP14A. Evolution of autosomal retrogenes from X-linked
CC progenitors compensates for X-chromosome silencing during male meiosis.
CC -!- SIMILARITY: Belongs to the UTP14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13396.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D87455; BAA13396.2; ALT_INIT; mRNA.
DR EMBL; AL139082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089407; AAH89407.1; -; mRNA.
DR CCDS; CCDS31978.1; -.
DR RefSeq; NP_067677.4; NM_021645.5.
DR AlphaFoldDB; Q5TAP6; -.
DR SMR; Q5TAP6; -.
DR BioGRID; 115073; 46.
DR IntAct; Q5TAP6; 31.
DR MINT; Q5TAP6; -.
DR STRING; 9606.ENSP00000428619; -.
DR iPTMnet; Q5TAP6; -.
DR PhosphoSitePlus; Q5TAP6; -.
DR BioMuta; UTP14C; -.
DR DMDM; 68566167; -.
DR EPD; Q5TAP6; -.
DR jPOST; Q5TAP6; -.
DR MassIVE; Q5TAP6; -.
DR MaxQB; Q5TAP6; -.
DR PaxDb; Q5TAP6; -.
DR PeptideAtlas; Q5TAP6; -.
DR PRIDE; Q5TAP6; -.
DR ProteomicsDB; 64855; -.
DR Antibodypedia; 49851; 19 antibodies from 11 providers.
DR DNASU; 9724; -.
DR Ensembl; ENST00000521776.2; ENSP00000428619.1; ENSG00000253797.2.
DR GeneID; 9724; -.
DR KEGG; hsa:9724; -.
DR MANE-Select; ENST00000521776.2; ENSP00000428619.1; NM_021645.6; NP_067677.4.
DR UCSC; uc058xgb.1; human.
DR CTD; 9724; -.
DR DisGeNET; 9724; -.
DR GeneCards; UTP14C; -.
DR HGNC; HGNC:20321; UTP14C.
DR HPA; ENSG00000253797; Low tissue specificity.
DR MalaCards; UTP14C; -.
DR MIM; 608969; gene.
DR neXtProt; NX_Q5TAP6; -.
DR OpenTargets; ENSG00000253797; -.
DR PharmGKB; PA134944828; -.
DR VEuPathDB; HostDB:ENSG00000253797; -.
DR eggNOG; KOG2172; Eukaryota.
DR GeneTree; ENSGT00390000008142; -.
DR HOGENOM; CLU_012635_1_0_1; -.
DR InParanoid; Q5TAP6; -.
DR OMA; EHALSGW; -.
DR OrthoDB; 370022at2759; -.
DR PhylomeDB; Q5TAP6; -.
DR TreeFam; TF314531; -.
DR PathwayCommons; Q5TAP6; -.
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; Q5TAP6; -.
DR BioGRID-ORCS; 9724; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; UTP14C; human.
DR GenomeRNAi; 9724; -.
DR Pharos; Q5TAP6; Tdark.
DR PRO; PR:Q5TAP6; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5TAP6; protein.
DR Bgee; ENSG00000253797; Expressed in ventricular zone and 89 other tissues.
DR ExpressionAtlas; Q5TAP6; baseline and differential.
DR Genevisible; Q5TAP6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR006709; SSU_processome_Utp14.
DR PANTHER; PTHR14150; PTHR14150; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Differentiation; Isopeptide bond;
KW Meiosis; Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW Spermatogenesis; Ubl conjugation.
FT CHAIN 1..766
FT /note="U3 small nucleolar RNA-associated protein 14 homolog
FT C"
FT /id="PRO_0000065736"
FT REGION 14..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..245
FT /evidence="ECO:0000255"
FT COILED 316..346
FT /evidence="ECO:0000255"
FT COILED 452..470
FT /evidence="ECO:0000255"
FT COMPBIAS 26..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT CROSSLNK 121
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 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT CROSSLNK 732
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT VARIANT 85
FT /note="G -> V (in dbSNP:rs3742289)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_022812"
FT VARIANT 101
FT /note="T -> A (in dbSNP:rs3742290)"
FT /id="VAR_022813"
FT VARIANT 319
FT /note="R -> H (in dbSNP:rs17402034)"
FT /id="VAR_051482"
SQ SEQUENCE 766 AA; 87188 MW; 4C90F0754A042986 CRC64;
MNVNQVAENL ALSHQEELVD LPKNYPLSEN EDEGDSDGER KHQKLLEAII SLDGKNRRKL
AERSEASLKV SEFSVSSEGS GEKLGLADLL EPVKTSSSLA TVKKQLNRVK SKKVVELPLN
KEKIEQIHRE VAFSKTSQVL SKWDPIILKN QQAEQLVFPL GKEQPAIAPI EHALSGWKAR
TPLEQEIFNL LHKNKQPVTD PLLTPMEKAS LQAMSLEEAK MHRAELQRAR ALQSYYEAKA
RKEKKIKSKK YHKVVKKGKA KKALKEFEQL QKVNPTVALE EMEKIENARM MERMSLKHQN
SGKWAKSKAI MAKYDLEARQ AMQEQLAKNK ELTQKLQVAS ESEEEEGGTE VEELLVPHVA
NEVQMNVDGP NPWMFRSCTS DTKEAATQED PEQVPELAAH EVSASEAEER PVAEEEILLR
EFEERQSLRK RSELNQDAEP ASSQETKDSS SQEVLSELRA LSQKLKEKHQ SRKQKASSEG
TVPQVQREEP APEEAEPLLL QRSERVQTLE ELEELGKEDC FQNKELPRPV LEGQQSERTP
NNRPDAPKEK KEKEQLINLQ NFLTTQSPSV RSLAVPTIIE ELEDEEERDQ RQMIKEAFAG
DDVIRDFLKE KREAVEASKP KDVDLTLPGW GEWGGVGLKP SAKKRRQFLI KAPEGPPRKD
KNLPNVIISE KRNIHAAAHQ VQVLPYPFTH HRQFERTIQT PIGSTWNTQR AFQKLTTPKV
VTKPGHIIKP IKAEDVGYQS SSRSDLPVIQ RNPKRITTRH NKEEKL
