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Nuclease-sensitive element-binding protein 1 (CCAAT-binding transcription factor I subunit A) (CBF-A) (Enhancer factor I subunit A) (EFI-A) (Y-box transcription factor) (Y-box-binding protein 1) (YB-1) (p50)

 YBOX1_RABIT             Reviewed;         324 AA.
Q28618;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 117.
RecName: Full=Nuclease-sensitive element-binding protein 1;
AltName: Full=CCAAT-binding transcription factor I subunit A;
Short=CBF-A;
AltName: Full=Enhancer factor I subunit A;
Short=EFI-A;
AltName: Full=Y-box transcription factor;
AltName: Full=Y-box-binding protein 1;
Short=YB-1;
AltName: Full=p50;
Name=YBX1; Synonyms=NSEP1, YB1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Bone marrow;
PubMed=7852402; DOI=10.1074/jbc.270.7.3186;
Evdokimova V.M., Wei C.L., Sitikov A.S., Simonenko P.N., Lazarev O.A.,
Vasilenko K.S., Ustinov V.A., Hershey J.W., Ovchinnikov L.P.;
"The major protein of messenger ribonucleoprotein particles in somatic
cells is a member of the Y-box binding transcription factor family.";
J. Biol. Chem. 270:3186-3192(1995).
[2]
PARTIAL PROTEIN SEQUENCE, PROTEOLYTIC CLEAVAGE BY 20S PROTEASOMAL
PROTEASE, AND SUBCELLULAR LOCATION.
PubMed=16193061; DOI=10.1038/sj.emboj.7600830;
Sorokin A.V., Selyutina A.A., Skabkin M.A., Guryanov S.G.,
Nazimov I.V., Richard C., Th'ng J., Yau J., Sorensen P.H.B.,
Ovchinnikov L.P., Evdokimova V.;
"Proteasome-mediated cleavage of the Y-box-binding protein 1 is linked
to DNA-damage stress response.";
EMBO J. 24:3602-3612(2005).
[3]
FUNCTION.
PubMed=11574481; DOI=10.1093/emboj/20.19.5491;
Evdokimova V., Ruzanov P., Imataka H., Raught B., Svitkin Y.,
Ovchinnikov L.P., Sonenberg N.;
"The major mRNA-associated protein YB-1 is a potent 5' cap-dependent
mRNA stabilizer.";
EMBO J. 20:5491-5502(2001).
[4]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=12582179; DOI=10.1074/jbc.M209145200;
Nekrasov M.P., Ivshina M.P., Chernov K.G., Kovrigina E.A.,
Evdokimova V.M., Thomas A.A.M., Hershey J.W.B., Ovchinnikov L.P.;
"The mRNA-binding protein YB-1 (p50) prevents association of the
eukaryotic initiation factor eIF4G with mRNA and inhibits protein
synthesis at the initiation stage.";
J. Biol. Chem. 278:13936-13943(2003).
[5]
MUTAGENESIS OF SER-102, PHOSPHORYLATION AT SER-102, SUBCELLULAR
LOCATION, INTERACTION WITH AKT1, AND FUNCTION.
PubMed=16354698; DOI=10.1128/MCB.26.1.277-292.2006;
Evdokimova V., Ruzanov P., Anglesio M.S., Sorokin A.V.,
Ovchinnikov L.P., Buckley J., Triche T.J., Sonenberg N.,
Sorensen P.H.B.;
"Akt-mediated YB-1 phosphorylation activates translation of silent
mRNA species.";
Mol. Cell. Biol. 26:277-292(2006).
-!- FUNCTION: Mediates pre-mRNA alternative splicing regulation. Binds
to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'). Regulates
the transcription of numerous genes. Promotes separation of DNA
strands that contain mismatches or are modified by cisplatin. Has
endonucleolytic activity and can introduce nicks or breaks into
double-stranded DNA (in vitro). May play a role in DNA repair.
Component of the CRD-mediated complex that promotes MYC mRNA
stability. Binds to splice sites in pre-mRNA and regulates splice
site selection. Its transcriptional activity on the multidrug
resistance gene MDR1 is enhanced in presence of the APEX1
acetylated form at 'Lys-6' and 'Lys-7'. Binds preferentially to
the 5'-[CU]CUGCG-3' motif in vitro (By similarity). Binds and
stabilizes cytoplasmic mRNA. Contributes to the regulation of
translation by modulating the interaction between the mRNA and
eukaryotic initiation factors. {ECO:0000250|UniProtKB:P67809,
ECO:0000269|PubMed:11574481, ECO:0000269|PubMed:12582179,
ECO:0000269|PubMed:16354698, ECO:0000269|PubMed:7852402}.
-!- FUNCTION: The secreted form acts as an extracellular mitogen and
stimulates cell migration and proliferation.
{ECO:0000250|UniProtKB:P67809, ECO:0000269|PubMed:11574481,
ECO:0000269|PubMed:12582179, ECO:0000269|PubMed:16354698,
ECO:0000269|PubMed:7852402}.
-!- SUBUNIT: Identified in a histone pre-mRNA complex, at least
composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Component
of the coding region determinant (CRD)-mediated complex, composed
of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identification in a
mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU,
IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
YBX1. Identified in a IGF2BP1-dependent mRNP granule complex
containing untranslated mRNAs. Interacts with AKT1, MBNL1,
IGF2BP1, SFRS9, ALYREF/THOC4, MSH2, XRCC5, RBBP6, WRN and NCL.
Component of the U11/U12 snRNPs that are part of the U12-type
spliceosome. Can bind to DNA as a homomeric form, (EFI-A)n or as a
heteromeric form in association with EFI-B. Homodimer in the
presence of ATP. Can form heterotrimer with PURA and PURB.
Interacts (via C-terminus) with APEX1 (via N-terminus); the
interaction is increased with APEX1 acetylated at 'Lys-6' and
'Lys-7'. Interacts with AGO1 and AGO2. Interacts with ANKRD2.
Interacts with DERA (By similarity). Component of cytoplasmic
messenger ribonucleoprotein particles (mRNPs). Interacts with
FMR1; this interaction occurs in association with polyribosome (By
similarity). Interacts with ZBTB7B (By similarity).
{ECO:0000250|UniProtKB:P62960, ECO:0000250|UniProtKB:P67809,
ECO:0000269|PubMed:12582179, ECO:0000269|PubMed:16354698}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasmic granule.
Secreted {ECO:0000250|UniProtKB:P67809}. Note=Localized with DDX1,
MBNL1 and TIAL1 in stress granules upon stress. Secreted by
mesangial and monocytic cells after inflammatory challenges (By
similarity). Shuttles between nucleus and cytoplasm. Predominantly
cytoplasmic in proliferating cells. Cytotoxic stress and DNA
damage enhance translocation to the nucleus. Localized in
cytoplasmic mRNP granules containing untranslated mRNAs.
{ECO:0000250|UniProtKB:P62960}.
-!- PTM: Ubiquitinated by RBBP6; leading to a decrease of YBX1
transcactivational ability. {ECO:0000250|UniProtKB:P62960}.
-!- PTM: In the absence of phosphorylation the protein is retained in
the cytoplasm (By similarity). Phosphorylation by PKB/AKT1 reduces
interaction with cytoplasmic mRNA. {ECO:0000250|UniProtKB:P62960,
ECO:0000269|PubMed:16354698}.
-!- PTM: Cleaved by a 20S proteasomal protease in response to agents
that damage DNA. Cleavage takes place in the absence of
ubiquitination and ATP. The resulting N-terminal fragment
accumulates in the nucleus. {ECO:0000269|PubMed:16193061}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U16821; AAA66069.1; -; mRNA.
PIR; A55971; A55971.
RefSeq; NP_001076254.1; NM_001082785.1.
UniGene; Ocu.6201; -.
ProteinModelPortal; Q28618; -.
SMR; Q28618; -.
BioGrid; 1172602; 2.
STRING; 9986.ENSOCUP00000019994; -.
iPTMnet; Q28618; -.
PRIDE; Q28618; -.
GeneID; 100009583; -.
KEGG; ocu:100009583; -.
CTD; 4904; -.
eggNOG; KOG3070; Eukaryota.
eggNOG; COG1278; LUCA.
HOGENOM; HOG000116439; -.
HOVERGEN; HBG008757; -.
InParanoid; Q28618; -.
KO; K09276; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd04458; CSP_CDS; 1.
InterPro; IPR019844; Cold-shock_CS.
InterPro; IPR011129; CSD.
InterPro; IPR002059; CSP_DNA-bd.
InterPro; IPR012340; NA-bd_OB-fold.
Pfam; PF00313; CSD; 1.
PRINTS; PR00050; COLDSHOCK.
SMART; SM00357; CSP; 1.
SUPFAM; SSF50249; SSF50249; 1.
PROSITE; PS00352; CSD_1; 1.
PROSITE; PS51857; CSD_2; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Isopeptide bond; Mitogen;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Repressor; RNA-binding; Secreted; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P67809}.
CHAIN 2 324 Nuclease-sensitive element-binding
protein 1.
/FTId=PRO_0000227814.
DOMAIN 58 128 CSD.
REGION 15 71 Interaction with ss-DNA. {ECO:0000250}.
COMPBIAS 185 291 Arg-rich.
SITE 219 220 Cleavage; by 20S proteasomal protease.
{ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P67809}.
MOD_RES 102 102 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:16354698}.
MOD_RES 162 162 Phosphotyrosine.
{ECO:0000250|UniProtKB:P67809}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000250|UniProtKB:P67809}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000250|UniProtKB:P67809}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000250|UniProtKB:P67809}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000250|UniProtKB:P67809}.
MOD_RES 301 301 N6-acetyllysine.
{ECO:0000250|UniProtKB:P67809}.
MOD_RES 304 304 N6-acetyllysine.
{ECO:0000250|UniProtKB:P67809}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000250|UniProtKB:P67809}.
CROSSLNK 26 26 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P67809}.
CROSSLNK 137 137 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P67809}.
MUTAGEN 102 102 S->A: Abolishes phosphorylation by
PKB/AKT1. {ECO:0000269|PubMed:16354698}.
SEQUENCE 324 AA; 35824 MW; B2700FD2E61BF8B9 CRC64;
MSSEAETQQP PAAPPAAPAL SAAETKPGTT GSGAGSGGPG GLTSAAPAGG DKKVIATKVL
GTVKWFNVRN GYGFINRNDT KEDVFVHQTA IKKNNPRKYL RSVGDGETVE FDVVEGEKGA
EAANVTGPGG VPVQGSKYAA DRNHYRRYPR RRGPPRNYQQ NYQNSESGEK NEGSESAPEG
QAQQRRPYRR RRFPPYYMRR PYGRRPQYSN PPVQGEVMEG ADNQGAGEQG RPVRQNMYRG
YRPRFRRGPP RQRQPREDGN EEDKENQGDE TQGQQPPPSR YRRNFNYRRR RPDNPKPQDG
KETKAADPPA ENSSAPEAEQ GGAE


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