YBOX2_HUMAN
ID YBOX2_HUMAN Reviewed; 364 AA.
AC Q9Y2T7; D3DTP1; Q8N4P0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Y-box-binding protein 2;
DE AltName: Full=Contrin;
DE AltName: Full=DNA-binding protein C;
DE Short=Dbpc;
DE AltName: Full=Germ cell-specific Y-box-binding protein;
DE AltName: Full=MSY2 homolog;
GN Name=YBX2; Synonyms=CSDA3, MSY2;
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], TISSUE SPECIFICITY, AND VARIANT VAL-9.
RX PubMed=10100484;
RA Tekur S., Pawlak A., Guellaen G., Hecht N.B.;
RT "Contrin, the human homologue of a germ-cell Y-box-binding protein:
RT cloning, expression, and chromosomal localization.";
RL J. Androl. 20:135-144(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-9.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-9.
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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16479255; DOI=10.1038/sj.bjc.6602987;
RA Kohno Y., Matsuki Y., Tanimoto A., Izumi H., Uchiumi T., Kohno K.,
RA Shimajiri S., Sasaguri Y.;
RT "Expression of Y-box-binding protein dbpC/contrin, a potentially new
RT cancer/testis antigen.";
RL Br. J. Cancer 94:710-716(2006).
CC -!- FUNCTION: Major constituent of messenger ribonucleoprotein particles
CC (mRNPs). Involved in the regulation of the stability and/or translation
CC of germ cell mRNAs. Binds to Y-box consensus promoter element. Binds to
CC full-length mRNA with high affinity in a sequence-independent manner.
CC Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-
CC 3' with low affinity and limited sequence specificity. Its binding with
CC maternal mRNAs is necessary for its cytoplasmic retention. May mark
CC specific mRNAs (those transcribed from Y-box promoters) in the nucleus
CC for cytoplasmic storage, thereby linking transcription and mRNA
CC storage/translational delay (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a mRNP complex with PABPC1 and YBX3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16479255}. Nucleus
CC {ECO:0000269|PubMed:16479255}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes and testicular germ cells in
CC the stage of spermatogonia to spermatocyte. Also observed placental
CC trophoblasts, as well as in vascular smooth muscle cells in the
CC pulmonary artery, myocardium, and skeletal muscle. Undetectable in
CC epithelial cells in respiratory, gastrointestinal, and urogenital
CC tracts. Up-regulated in various carcinomas and germ cell tumors (at
CC protein level). {ECO:0000269|PubMed:10100484,
CC ECO:0000269|PubMed:16479255}.
CC -!- PTM: Phosphorylated during oocyte maturation and dephosphorylated
CC following egg activation. Phosphorylated in vitro by a kinase activity
CC associated with testicular mRNPs. Dephosphorylation leads to a decrease
CC in its affinity to bind RNA in vitro (By similarity). {ECO:0000250}.
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DR EMBL; AF096834; AAD30662.1; -; mRNA.
DR EMBL; CH471108; EAW90223.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90224.1; -; Genomic_DNA.
DR EMBL; BC033800; AAH33800.1; -; mRNA.
DR EMBL; BC047760; AAH47760.1; -; mRNA.
DR CCDS; CCDS11098.1; -.
DR RefSeq; NP_057066.2; NM_015982.3.
DR AlphaFoldDB; Q9Y2T7; -.
DR SMR; Q9Y2T7; -.
DR BioGRID; 119277; 416.
DR IntAct; Q9Y2T7; 17.
DR MINT; Q9Y2T7; -.
DR STRING; 9606.ENSP00000007699; -.
DR GlyGen; Q9Y2T7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2T7; -.
DR PhosphoSitePlus; Q9Y2T7; -.
DR BioMuta; YBX2; -.
DR DMDM; 116242847; -.
DR EPD; Q9Y2T7; -.
DR jPOST; Q9Y2T7; -.
DR MassIVE; Q9Y2T7; -.
DR MaxQB; Q9Y2T7; -.
DR PaxDb; Q9Y2T7; -.
DR PeptideAtlas; Q9Y2T7; -.
DR PRIDE; Q9Y2T7; -.
DR ProteomicsDB; 85899; -.
DR Antibodypedia; 3229; 330 antibodies from 36 providers.
DR DNASU; 51087; -.
DR Ensembl; ENST00000007699.10; ENSP00000007699.5; ENSG00000006047.13.
DR Ensembl; ENST00000672150.1; ENSP00000499890.1; ENSG00000288504.1.
DR GeneID; 51087; -.
DR KEGG; hsa:51087; -.
DR MANE-Select; ENST00000007699.10; ENSP00000007699.5; NM_015982.4; NP_057066.2.
DR UCSC; uc002gfq.3; human.
DR CTD; 51087; -.
DR DisGeNET; 51087; -.
DR GeneCards; YBX2; -.
DR HGNC; HGNC:17948; YBX2.
DR HPA; ENSG00000006047; Tissue enriched (testis).
DR MIM; 611447; gene.
DR neXtProt; NX_Q9Y2T7; -.
DR OpenTargets; ENSG00000006047; -.
DR PharmGKB; PA142670560; -.
DR VEuPathDB; HostDB:ENSG00000006047; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000159816; -.
DR HOGENOM; CLU_063071_0_1_1; -.
DR InParanoid; Q9Y2T7; -.
DR OMA; GQTQSDQ; -.
DR OrthoDB; 1431946at2759; -.
DR PhylomeDB; Q9Y2T7; -.
DR TreeFam; TF317306; -.
DR PathwayCommons; Q9Y2T7; -.
DR SignaLink; Q9Y2T7; -.
DR BioGRID-ORCS; 51087; 15 hits in 1092 CRISPR screens.
DR ChiTaRS; YBX2; human.
DR GeneWiki; YBX2; -.
DR GenomeRNAi; 51087; -.
DR Pharos; Q9Y2T7; Tbio.
DR PRO; PR:Q9Y2T7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y2T7; protein.
DR Bgee; ENSG00000006047; Expressed in right testis and 93 other tissues.
DR ExpressionAtlas; Q9Y2T7; baseline and differential.
DR Genevisible; Q9Y2T7; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0048599; P:oocyte development; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0009386; P:translational attenuation; TAS:ProtInc.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00313; CSD; 1.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..364
FT /note="Y-box-binding protein 2"
FT /id="PRO_0000100225"
FT DOMAIN 93..163
FT /note="CSD"
FT REGION 33..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..169
FT /note="Required for cytoplasmic retention"
FT /evidence="ECO:0000250"
FT REGION 155..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..364
FT /note="Required for mRNA-binding"
FT COMPBIAS 348..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2C8"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2C8"
FT VARIANT 9
FT /note="G -> V (in dbSNP:rs222859)"
FT /evidence="ECO:0000269|PubMed:10100484,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_027916"
FT VARIANT 63
FT /note="S -> P (in dbSNP:rs8069533)"
FT /id="VAR_027917"
SQ SEQUENCE 364 AA; 38518 MW; 0B16DEF46F4634FA CRC64;
MSEVEAAAGA TAVPAATVPA TAAGVVAVVV PVPAGEPQKG GGAGGGGGAA SGPAAGTPSA
PGSRTPGNPA TAVSGTPAPP ARSQADKPVL AIQVLGTVKW FNVRNGYGFI NRNDTKEDVF
VHQTAIKRNN PRKFLRSVGD GETVEFDVVE GEKGAEATNV TGPGGVPVKG SRYAPNRRKS
RRFIPRPPSV APPPMVAEIP SAGTGPGSKG ERAEDSGQRP RRWCPPPFFY RRRFVRGPRP
PNQQQPIEGT DRVEPKETAP LEGHQQQGDE RVPPPRFRPR YRRPFRPRPR QQPTTEGGDG
ETKPSQGPAD GSRPEPQRPR NRPYFQRRRQ QAPGPQQAPG PRQPAAPETS APVNSGDPTT
TILE
