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   25-JAN-2012, entry version 86.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT VAL-9.
RX   MEDLINE=99198583; 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
CC   -!- FUNCTION: Major constituent of messenger ribonucleoprotein
CC       particles (mRNPs). Involved in the regulation of the stability
CC       and/or translation of germ cell mRNAs. Binds to Y-box consensus
CC       promoter element. Binds to full length mRNA with high affinity in
CC       a sequence-independent manner. Binds to short RNA sequences
CC       containing the consensus site 5'-UCCAUCA-3' with low affinity and
CC       limited sequence specificity. Its binding with maternal mRNAs is
CC       necessary for its cytoplasmic retention. May mark specific mRNAs
CC       (those transcribed from Y-box promoters) in the nucleus for
CC       cytoplasmic storage, thereby linking transcription and mRNA
CC       storage/translational delay (By similarity).
CC   -!- SUBUNIT: Found in a mRNP complex with PABPC1 and CSDA (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in oocytes and testicular germ cells
CC       in the stage of spermatogonia to spermatocyte. Also observed
CC       placental trophoblasts, as well as in vascular smooth muscle cells
CC       in the pulmonary artery, myocardium, and skeletal muscle.
CC       Undetectable in epithelial cells in respiratory, gastrointestinal,
CC       and urogenital tracts. Up-regulated in various carcinomas and germ
CC       cell tumors (at protein level).
CC   -!- PTM: Phosphorylated during oocyte maturation and dephosphorylated
CC       following egg activation. Phosphorylated in vitro by a kinase
CC       activity associated with testicular mRNPs. Dephosphorylation leads
CC       to a decrease in its affinity to bind RNA in vitro (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 CSD (cold-shock) domain.
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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   IPI; IPI00250153; -.
DR   RefSeq; NP_057066.2; NM_015982.3.
DR   UniGene; Hs.567494; -.
DR   ProteinModelPortal; Q9Y2T7; -.
DR   SMR; Q9Y2T7; 87-164.
DR   STRING; Q9Y2T7; -.
DR   PhosphoSite; Q9Y2T7; -.
DR   DMDM; 116242847; -.
DR   PRIDE; Q9Y2T7; -.
DR   Ensembl; ENST00000007699; ENSP00000007699; ENSG00000006047.
DR   GeneID; 51087; -.
DR   KEGG; hsa:51087; -.
DR   UCSC; uc002gfq.2; human.
DR   CTD; 51087; -.
DR   GeneCards; GC17M007191; -.
DR   H-InvDB; HIX0013491; -.
DR   HGNC; HGNC:17948; YBX2.
DR   HPA; CAB012332; -.
DR   MIM; 611447; gene.
DR   neXtProt; NX_Q9Y2T7; -.
DR   PharmGKB; PA142670560; -.
DR   GeneTree; ENSGT00390000009256; -.
DR   HOGENOM; HBG125145; -.
DR   HOVERGEN; HBG079361; -.
DR   InParanoid; Q9Y2T7; -.
DR   OMA; GDPTTTI; -.
DR   OrthoDB; EOG46DM3W; -.
DR   PhylomeDB; Q9Y2T7; -.
DR   NextBio; 53755; -.
DR   ArrayExpress; Q9Y2T7; -.
DR   Bgee; Q9Y2T7; -.
DR   CleanEx; HS_YBX2; -.
DR   Genevestigator; Q9Y2T7; -.
DR   GermOnline; ENSG00000006047; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0009386; P:translational attenuation; TAS:ProtInc.
DR   InterPro; IPR019844; Cold-shock_CS.
DR   InterPro; IPR011129; Cold_shock_prot.
DR   InterPro; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   KO; K09277; -.
DR   Pfam; PF00313; CSD; 1.
DR   PRINTS; PR00050; COLDSHOCK.
DR   SMART; SM00357; CSP; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   PROSITE; PS00352; COLD_SHOCK; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; DNA-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; RNA-binding.
FT   CHAIN         1    364       Y-box-binding protein 2.
FT                                /FTId=PRO_0000100225.
FT   DOMAIN       93    163       CSD.
FT   REGION       87    169       Required for cytoplasmic retention (By
FT                                similarity).
FT   REGION      217    364       Required for mRNA-binding.
FT   COMPBIAS     35     67       Gly-rich.
FT   COMPBIAS    185    352       Pro-rich.
FT   MOD_RES     116    116       N6-acetyllysine.
FT   VARIANT       9      9       G -> V (in dbSNP:rs222859).
FT                                /FTId=VAR_027916.
FT   VARIANT      63     63       S -> P (in dbSNP:rs8069533).
FT                                /FTId=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
//