UT14A_BOVIN
ID UT14A_BOVIN Reviewed; 770 AA.
AC Q3T0Q8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=U3 small nucleolar RNA-associated protein 14 homolog A;
GN Name=UTP14A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UTP14 family. {ECO:0000305}.
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DR EMBL; BT030541; ABQ12981.1; -; mRNA.
DR EMBL; BC102296; AAI02297.1; -; mRNA.
DR RefSeq; NP_001029413.1; NM_001034241.2.
DR AlphaFoldDB; Q3T0Q8; -.
DR SMR; Q3T0Q8; -.
DR STRING; 9913.ENSBTAP00000017524; -.
DR PaxDb; Q3T0Q8; -.
DR PRIDE; Q3T0Q8; -.
DR Ensembl; ENSBTAT00000017524; ENSBTAP00000017524; ENSBTAG00000013671.
DR GeneID; 505324; -.
DR KEGG; bta:505324; -.
DR CTD; 10813; -.
DR VEuPathDB; HostDB:ENSBTAG00000013671; -.
DR eggNOG; KOG2172; Eukaryota.
DR GeneTree; ENSGT00390000008142; -.
DR HOGENOM; CLU_012635_1_0_1; -.
DR InParanoid; Q3T0Q8; -.
DR OMA; RESKWAK; -.
DR OrthoDB; 370022at2759; -.
DR TreeFam; TF314531; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000013671; Expressed in uterine horn and 106 other tissues.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Citrullination; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..770
FT /note="U3 small nucleolar RNA-associated protein 14 homolog
FT A"
FT /id="PRO_0000290354"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..68
FT /evidence="ECO:0000255"
FT COILED 217..291
FT /evidence="ECO:0000255"
FT COILED 318..348
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVJ6"
FT MOD_RES 588
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT CROSSLNK 449
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"
SQ SEQUENCE 770 AA; 88087 MW; 4DD335742F898BC1 CRC64;
MNANQAAESN LLASNQQKEL EDLPKDYPLS TSEDEGDKDE ERKHQKLLES ISSLNGKDRQ
KLADRSEASL KVSEFSVSSE GSGEKLVLSD LLEPVKTSSS LAAVKKQLNR VKSKKTVELP
LHREEIERIH REVAFNKSSQ ILSKWDPVVL KNRQAEQLVF PLSKPQSAFA PIEHVVNGWK
AGTPLEQEIF NLLHKNKQPV TDPLLTPVEK ASLKAMSLEE VKMRRAELQR ARALQSYYEA
RARREKRIKS KKYHRILKKG KAKQALKDFE KLQKVNPAAA LEELEKLDKA RMMERMSLKH
QNSGKWAKSK AIMAKYDLEA RQAMQEQLAR NKELTQKVRA ASESEEEGEG QEEEEEPLVP
DLVNEVQIKA NGLNPWMFRN HFIDAKEAEV QKDLEDPAEP EAQETSESEE EKAVVEEETL
LKEFEERRSL RQKSELNHMA EPVHRRVTKD PSSQEVLSDL RALCQKLRTE NHQSGKQELS
SARTAQREEP AREEEEPMLL QRPERARTLD ELEELGREGC VENEELPRTA VEGLQLEKNL
SNHIGAPKEK KRKEQMIDLQ NLLTTKSPSV KSLAVPTTVQ ELEDEEERDQ RQIIKEAFAG
DDVIRDFLKE KREAVEASKP KDLDLTLPGW GEWGGIGLKP SAKKRRRFLI KAPEGPPRKD
KNLPNVIINE KRNTHAAAHQ VQVLPHPFTH HQQFERTIQT PVGSTWNTQR AFQKLTMPKV
VTKPGHIIKP IKAEDVGYRS SSRSDLSVVQ RNPKRLSIRH KKHLENNCVD
