BCD1_MOUSE
ID BCD1_MOUSE Reviewed; 460 AA.
AC Q3UFB2; B2RW16; Q3TG81;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Box C/D snoRNA protein 1;
DE AltName: Full=Zinc finger HIT domain-containing protein 6;
GN Name=Znhit6; Synonyms=Bcd1;
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=Liver, and Sympathetic ganglion;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
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 box C/D snoRNAs accumulation involved in snoRNA
CC processing, snoRNA transport to the nucleolus and ribosome biogenesis.
CC {ECO:0000250|UniProtKB:Q9NWK9}.
CC -!- SUBUNIT: Interacts with FBL, SNU13, NOP58, NUFIP1, RUVBL1, RUVBL2 and
CC TAF9 (By similarity). Interacts (via HIT-type zinc finger) with the
CC RUVBL1/RUVBL2 complex in the presence of ADP (By similarity).
CC {ECO:0000250|UniProtKB:Q9NWK9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UFB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UFB2-2; Sequence=VSP_023573;
CC -!- SIMILARITY: Belongs to the BCD1 family. {ECO:0000305}.
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DR EMBL; AK148729; BAE28649.1; -; mRNA.
DR EMBL; AK168844; BAE40667.1; -; mRNA.
DR EMBL; CH466532; EDL12001.1; -; Genomic_DNA.
DR EMBL; BC147498; AAI47499.1; -; mRNA.
DR EMBL; BC150966; AAI50967.1; -; mRNA.
DR EMBL; BC150967; AAI50968.1; -; mRNA.
DR EMBL; BC151198; AAI51199.1; -; mRNA.
DR CCDS; CCDS38662.1; -. [Q3UFB2-1]
DR CCDS; CCDS84683.1; -. [Q3UFB2-2]
DR RefSeq; NP_001074563.1; NM_001081094.1. [Q3UFB2-1]
DR RefSeq; NP_001333450.1; NM_001346521.1. [Q3UFB2-2]
DR RefSeq; XP_006501502.1; XM_006501439.2. [Q3UFB2-2]
DR AlphaFoldDB; Q3UFB2; -.
DR SMR; Q3UFB2; -.
DR IntAct; Q3UFB2; 1.
DR MINT; Q3UFB2; -.
DR STRING; 10090.ENSMUSP00000096136; -.
DR iPTMnet; Q3UFB2; -.
DR PhosphoSitePlus; Q3UFB2; -.
DR EPD; Q3UFB2; -.
DR MaxQB; Q3UFB2; -.
DR PaxDb; Q3UFB2; -.
DR PeptideAtlas; Q3UFB2; -.
DR PRIDE; Q3UFB2; -.
DR ProteomicsDB; 273653; -. [Q3UFB2-1]
DR ProteomicsDB; 273654; -. [Q3UFB2-2]
DR Antibodypedia; 19797; 117 antibodies from 22 providers.
DR Ensembl; ENSMUST00000098534; ENSMUSP00000096136; ENSMUSG00000074182. [Q3UFB2-1]
DR Ensembl; ENSMUST00000199033; ENSMUSP00000143306; ENSMUSG00000074182. [Q3UFB2-2]
DR GeneID; 229937; -.
DR KEGG; mmu:229937; -.
DR UCSC; uc008rqo.1; mouse. [Q3UFB2-1]
DR CTD; 54680; -.
DR MGI; MGI:1916996; Znhit6.
DR VEuPathDB; HostDB:ENSMUSG00000074182; -.
DR eggNOG; KOG2858; Eukaryota.
DR GeneTree; ENSGT00390000017201; -.
DR HOGENOM; CLU_583884_0_0_1; -.
DR InParanoid; Q3UFB2; -.
DR OMA; CWHVKLL; -.
DR OrthoDB; 678600at2759; -.
DR PhylomeDB; Q3UFB2; -.
DR TreeFam; TF323923; -.
DR BioGRID-ORCS; 229937; 24 hits in 76 CRISPR screens.
DR ChiTaRS; Znhit6; mouse.
DR PRO; PR:Q3UFB2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3UFB2; protein.
DR Bgee; ENSMUSG00000074182; Expressed in cleaving embryo and 227 other tissues.
DR ExpressionAtlas; Q3UFB2; baseline and differential.
DR Genevisible; Q3UFB2; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070761; C:pre-snoRNP complex; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; ISO:MGI.
DR GO; GO:0000492; P:box C/D snoRNP assembly; ISO:MGI.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR GO; GO:0048254; P:snoRNA localization; ISO:MGI.
DR InterPro; IPR007529; Znf_HIT.
DR Pfam; PF04438; zf-HIT; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..460
FT /note="Box C/D snoRNA protein 1"
FT /id="PRO_0000280240"
FT ZN_FING 211..245
FT /note="HIT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 71
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWK9"
FT VAR_SEQ 1..168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023573"
FT CONFLICT 366
FT /note="K -> E (in Ref. 1; BAE28649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 52213 MW; 9771F853FB9FFD43 CRC64;
MESAAEKEGT PGGGSQRVAE GARPRPAAGG EGARDLDGSP EAGDGEERNG LAGTKTTEDA
EEIKMDLAVV KQEVVDWSDL DSGVADSQWV KQEVEGGPEV KDEKGVLEVK QEADSSLVVK
EEEVDEPEVK EEKVKVKEEV TDWEEVKEED LTIKQELFVG QNVKEEQVMD AAPIKEEGSL
KSEAMEDAKV KEEPQMNPRV GSKRKLALSR CETCGTEEAK YRCPRCMRFS CSLPCVKKHK
ADLTCSGVRD KTAYVSLQQF TEMNLLSDYR FLEDVARTAD KVSRDTFLKR PKRKKYLFFM
KNRARKQGIY LRLLPNGFSK RKENSTVFDH RKQQFCWHVK LQFPQSQAEY IEKRVPDDKT
INEILKPYID PEESDPVIRQ RLKAYAQSQT GVQILMRVEN MQQNMIRYHE LDPYKSLSDN
LKDKVIIEYP TLHVVLRGSS NDKQLLQVKS ESAQKLGNGN
