ZCRB1_HUMAN
ID ZCRB1_HUMAN Reviewed; 217 AA.
AC Q8TBF4; Q6PJX0; Q96TA6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Zinc finger CCHC-type and RNA-binding motif-containing protein 1;
DE AltName: Full=U11/U12 small nuclear ribonucleoprotein 31 kDa protein;
DE Short=U11/U12 snRNP 31 kDa protein;
DE Short=U11/U12-31K;
GN Name=ZCRB1;
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 [MRNA], SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16959469; DOI=10.1016/j.ygeno.2006.07.009;
RA Wang H., Gao M.X., Li L., Wang B., Hori N., Sato K.;
RT "Isolation, expression, and characterization of the human ZCRB1 gene mapped
RT to 12q12.";
RL Genomics 89:59-69(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-131.
RC TISSUE=Brain, and Lung;
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 IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S.,
RA Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in
RT the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-210 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP STRUCTURE BY NMR OF 1-87.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in zinc finger CCHC-type and RNA
RT binding motif 1.";
RL Submitted (JUN-2007) to the PDB data bank.
CC -!- SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type
CC spliceosome. {ECO:0000269|PubMed:15146077}.
CC -!- INTERACTION:
CC Q8TBF4; P04792: HSPB1; NbExp=3; IntAct=EBI-11124401, EBI-352682;
CC Q8TBF4; O43933: PEX1; NbExp=3; IntAct=EBI-11124401, EBI-988601;
CC Q8TBF4; O76024: WFS1; NbExp=3; IntAct=EBI-11124401, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:16959469}.
CC -!- INDUCTION: Up-regulated by morphine. Down-regulated at 30-36 degrees
CC Celsius while it is up-regulated at 39 degrees Celsius.
CC {ECO:0000269|PubMed:16959469}.
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DR EMBL; AB062361; BAB56132.1; -; mRNA.
DR EMBL; CH471111; EAW57842.1; -; Genomic_DNA.
DR EMBL; BC010177; AAH10177.1; -; mRNA.
DR EMBL; BC022543; AAH22543.1; -; mRNA.
DR EMBL; BK005200; DAA05498.1; -; mRNA.
DR CCDS; CCDS8740.1; -.
DR RefSeq; NP_149105.3; NM_033114.3.
DR PDB; 2E5H; NMR; -; A=1-87.
DR PDBsum; 2E5H; -.
DR AlphaFoldDB; Q8TBF4; -.
DR SMR; Q8TBF4; -.
DR BioGRID; 124524; 133.
DR CORUM; Q8TBF4; -.
DR IntAct; Q8TBF4; 62.
DR STRING; 9606.ENSP00000266529; -.
DR iPTMnet; Q8TBF4; -.
DR PhosphoSitePlus; Q8TBF4; -.
DR BioMuta; ZCRB1; -.
DR DMDM; 158931154; -.
DR EPD; Q8TBF4; -.
DR jPOST; Q8TBF4; -.
DR MassIVE; Q8TBF4; -.
DR MaxQB; Q8TBF4; -.
DR PaxDb; Q8TBF4; -.
DR PeptideAtlas; Q8TBF4; -.
DR PRIDE; Q8TBF4; -.
DR ProteomicsDB; 74010; -.
DR Antibodypedia; 25048; 127 antibodies from 25 providers.
DR DNASU; 85437; -.
DR Ensembl; ENST00000266529.8; ENSP00000266529.3; ENSG00000139168.9.
DR Ensembl; ENST00000677694.1; ENSP00000503171.1; ENSG00000139168.9.
DR Ensembl; ENST00000679269.1; ENSP00000503413.1; ENSG00000139168.9.
DR GeneID; 85437; -.
DR KEGG; hsa:85437; -.
DR MANE-Select; ENST00000266529.8; ENSP00000266529.3; NM_033114.4; NP_149105.3.
DR UCSC; uc001rmz.4; human.
DR CTD; 85437; -.
DR DisGeNET; 85437; -.
DR GeneCards; ZCRB1; -.
DR HGNC; HGNC:29620; ZCRB1.
DR HPA; ENSG00000139168; Tissue enhanced (brain).
DR MIM; 610750; gene.
DR neXtProt; NX_Q8TBF4; -.
DR OpenTargets; ENSG00000139168; -.
DR PharmGKB; PA143485674; -.
DR VEuPathDB; HostDB:ENSG00000139168; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00730000111061; -.
DR HOGENOM; CLU_059455_1_0_1; -.
DR InParanoid; Q8TBF4; -.
DR OMA; RXVTIMK; -.
DR OrthoDB; 1422822at2759; -.
DR PhylomeDB; Q8TBF4; -.
DR TreeFam; TF106263; -.
DR PathwayCommons; Q8TBF4; -.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-9682706; Replication of the SARS-CoV-1 genome.
DR Reactome; R-HSA-9694686; Replication of the SARS-CoV-2 genome.
DR SignaLink; Q8TBF4; -.
DR BioGRID-ORCS; 85437; 444 hits in 1049 CRISPR screens.
DR ChiTaRS; ZCRB1; human.
DR EvolutionaryTrace; Q8TBF4; -.
DR GenomeRNAi; 85437; -.
DR Pharos; Q8TBF4; Tdark.
DR PRO; PR:Q8TBF4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TBF4; protein.
DR Bgee; ENSG00000139168; Expressed in medial globus pallidus and 194 other tissues.
DR ExpressionAtlas; Q8TBF4; baseline and differential.
DR Genevisible; Q8TBF4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:HGNC-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IC:HGNC-UCL.
DR CDD; cd12393; RRM_ZCRB1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR044598; ZCRB1.
DR InterPro; IPR034219; ZCRB1_RRM.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR46259; PTHR46259; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..217
FT /note="Zinc finger CCHC-type and RNA-binding motif-
FT containing protein 1"
FT /id="PRO_0000252373"
FT DOMAIN 10..88
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 105..122
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 120..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 131
FT /note="P -> Q (in dbSNP:rs17852093)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027845"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2E5H"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:2E5H"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:2E5H"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2E5H"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2E5H"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2E5H"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:2E5H"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2E5H"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2E5H"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2E5H"
SQ SEQUENCE 217 AA; 24592 MW; CC0C2BB6D2E42444 CRC64;
MSGGLAPSKS TVYVSNLPFS LTNNDLYRIF SKYGKVVKVT IMKDKDTRKS KGVAFILFLD
KDSAQNCTRA INNKQLFGRV IKASIAIDNG RAAEFIRRRN YFDKSKCYEC GESGHLSYAC
PKNMLGEREP PKKKEKKKKK KAPEPEEEIE EVEESEDEGE DPALDSLSQA IAFQQAKIEE
EQKKWKPSSG VPSTSDDSRR PRIKKSTYFS DEEELSD
