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P67809 (YBOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclease-sensitive element-binding protein 1
Alternative name(s):
CCAAT-binding transcription factor I subunit A
Short name=CBF-A
DNA-binding protein B
Short name=DBPB
Enhancer factor I subunit A
Short name=EFI-A
Y-box transcription factor
Y-box-binding protein 1
Short name=YB-1
Gene names
Name:YBX1
Synonyms:NSEP1, YB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates pre-mRNA alternative splicing regulation. Binds to splice sites in pre-mRNA and regulates splice site selection. Binds and stabilizes cytoplasmic mRNA. Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors By similarity. Regulates the transcription of numerous genes. 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 to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II 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 preferentially to the 5'-[CU]CUGCG-3' motif in vitro. Ref.7 Ref.8 Ref.9 Ref.12 Ref.22 Ref.23 Ref.26 Ref.28

The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation. Ref.7 Ref.8 Ref.9 Ref.12 Ref.22 Ref.23 Ref.26 Ref.28

Subunit structure

Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 By similarity. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Interacts with IGF2BP1 and RBBP6. Component of cytoplasmic messenger ribonucleoprotein particles (mRNPs). Interacts with AKT1, MBNL1, SFRS9, ALYREF/THOC4, MSH2, XRCC5, WRN and NCL. 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. 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. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.28 Ref.33

Subcellular location

Cytoplasm. Nucleus. Cytoplasmic granule. Secreted. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between nucleus and cytoplasm. Predominantly cytoplasmic in proliferating cells. Cytotoxic stress and DNA damage enhance translocation to the nucleus. Localized with DDX1, MBNL1 and TIAL1 in stress granules upon stress. Secreted by mesangial and monocytic cells after inflammatory challenges. Translocates from the cytoplasm to the nucleus after and colocalizes with APEX1 in nuclear speckles after genotoxic stress. Ref.9 Ref.12 Ref.15 Ref.20 Ref.22 Ref.26 Ref.28

Post-translational modification

Ubiquitinated by RBBP6; leading to a decrease of YBX1 transcactivational ability. Ref.21

In the absence of phosphorylation the protein is retained in the cytoplasm.

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 By similarity.

Sequence similarities

Contains 1 CSD (cold-shock) domain.

Sequence caution

The sequence AAA35750.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAA59949.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAA61308.1 differs from that shown. Reason: Frameshift at position 314.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
Secreted
   LigandDNA-binding
RNA-binding
   Molecular functionActivator
Mitogen
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCRD-mediated mRNA stabilization

Inferred from mutant phenotype Ref.28. Source: UniProtKB

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

negative regulation of striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from direct assay Ref.23. Source: UniProtKB

transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentCRD-mediated mRNA stability complex

Inferred from direct assay Ref.28. Source: UniProtKB

U12-type spliceosomal complex

Inferred from direct assay Ref.13. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic stress granule

Inferred from direct assay Ref.22. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProtKB

histone pre-mRNA 3'end processing complex

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear membrane

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.2. Source: ProtInc

ribonucleoprotein complex

Inferred from direct assay Ref.20. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay Ref.23. Source: UniProtKB

RNA binding

Inferred from direct assay Ref.27. Source: UniProtKB

double-stranded DNA binding

Traceable author statement PubMed 1738588. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.2. Source: ProtInc

single-stranded DNA binding

Traceable author statement PubMed 1738588. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 324323Nuclease-sensitive element-binding protein 1
PRO_0000100219

Regions

Domain61 – 12565CSD
Region15 – 7157Interaction with ss-DNA

Sites

Site219 – 2202Cleavage; by 20S proteasomal protease

Amino acid modifications

Modified residue21N-acetylserine Ref.6
Modified residue1021Phosphoserine; by PKB/AKT1 Ref.15 Ref.29
Modified residue1621Phosphotyrosine Ref.14
Modified residue1651Phosphoserine Ref.6 Ref.29 Ref.30 Ref.32
Modified residue1671Phosphoserine Ref.29 Ref.30 Ref.32
Modified residue1741Phosphoserine Ref.16 Ref.24 Ref.29 Ref.30 Ref.32
Modified residue1761Phosphoserine Ref.16 Ref.24 Ref.29 Ref.30 Ref.32
Modified residue3011N6-acetyllysine Ref.26
Modified residue3041N6-acetyllysine Ref.26
Modified residue3141Phosphoserine Ref.32
Cross-link137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Experimental info

Mutagenesis1021S → A: Loss of phosphorylation by PKB/AKT1. Inhibits translocation to the nucleus and tumor cell growth. Ref.15
Mutagenesis3011K → A: Abrogates unconventional secretion. Ref.26
Mutagenesis3041K → A: Abrogates unconventional secretion. Ref.26
Sequence conflict1201A → E in AAA61308. Ref.2

Secondary structure

............ 324
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P67809 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DF0114BF974AEDB8

FASTA32435,924
        10         20         30         40         50         60 
MSSEAETQQP PAAPPAAPAL SAADTKPGTT GSGAGSGGPG GLTSAAPAGG DKKVIATKVL 

        70         80         90        100        110        120 
GTVKWFNVRN GYGFINRNDT KEDVFVHQTA IKKNNPRKYL RSVGDGETVE FDVVEGEKGA 

       130        140        150        160        170        180 
EAANVTGPGG VPVQGSKYAA DRNHYRRYPR RRGPPRNYQQ NYQNSESGEK NEGSESAPEG 

       190        200        210        220        230        240 
QAQQRRPYRR RRFPPYYMRR PYGRRPQYSN PPVQGEVMEG ADNQGAGEQG RPVRQNMYRG 

       250        260        270        280        290        300 
YRPRFRRGPP RQRQPREDGN EEDKENQGDE TQGQQPPQRR YRRNFNYRRR RPENPKPQDG 

       310        320 
KETKAADPPA ENSSAPEAEQ GGAE 

« Hide

References

« Hide 'large scale' references
[1]"Two human genes isolated by a novel method encode DNA-binding proteins containing a common region of homology."
Sakura H., Maekawa T., Imamoto F., Yasuda K., Ishii S.
Gene 73:499-507(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of the cDNA encoding a protein binding to the major histocompatibility complex class II Y box."
Didier D.K., Schiffenbauer J., Woulfe S.L., Zacheis M., Schwartz B.D.
Proc. Natl. Acad. Sci. U.S.A. 85:7322-7326(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Full length cDNA sequence encoding a nuclease-sensitive element DNA binding protein."
Kolluri R., Kinniburgh A.J.
Nucleic Acids Res. 19:4771-4771(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"A human protein containing a 'cold shock' domain binds specifically to H-DNA upstream from the human gamma-globin genes."
Horwitz E.M., Maloney K.A., Ley T.J.
J. Biol. Chem. 269:14130-14139(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone marrow.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal cortex, Eye, Kidney, Muscle, Placenta, Skin, Testis and Uterus.
[6]Bienvenut W.V.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-53; 70-93; 102-137; 157-185; 205-231; 257-279 AND 305-324, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[7]"Nucleolin and YB-1 are required for JNK-mediated interleukin-2 mRNA stabilization during T-cell activation."
Chen C.-Y., Gherzi R., Andersen J.S., Gaietta G., Juerchott K., Royer H.-D., Mann M., Karin M.
Genes Dev. 14:1236-1248(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
[8]"Y box-binding factor promotes eosinophil survival by stabilizing granulocyte-macrophage colony-stimulating factor mRNA."
Capowski E.E., Esnault S., Bhattacharya S., Malter J.S.
J. Immunol. 167:5970-5976(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection."
Raffetseder U., Frye B., Rauen T., Juerchott K., Royer H.-D., Jansen P.L., Mertens P.R.
J. Biol. Chem. 278:18241-18248(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SFRS9, SUBCELLULAR LOCATION.
[10]"Regulation of alternative splicing by SRrp86 and its interacting proteins."
Li J., Hawkins I.C., Harvey C.D., Jennings J.L., Link A.J., Patton J.G.
Mol. Cell. Biol. 23:7437-7447(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SFRS12.
[11]"The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle."
Kojic S., Medeot E., Guccione E., Krmac H., Zara I., Martinelli V., Valle G., Faulkner G.
J. Mol. Biol. 339:313-325(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKRD2.
[12]"YB-1 promotes strand separation in vitro of duplex DNA containing either mispaired bases or cisplatin modifications, exhibits endonucleolytic activities and binds several DNA repair proteins."
Gaudreault I., Guay D., Lebel M.
Nucleic Acids Res. 32:316-327(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH ALYREF/THOC4; NCL; XRCC5; WRN AND MSH2.
[13]"The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
[14]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the cold shock domain and affects the anchorage-independent growth of breast cancer cells."
Sutherland B.W., Kucab J., Wu J., Lee C., Cheang M.C.U., Yorida E., Turbin D., Dedhar S., Nelson C., Pollak M., Leighton Grimes H., Miller K., Badve S., Huntsman D., Blake-Gilks C., Chen M., Pallen C.J., Dunn S.E.
Oncogene 24:4281-4292(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-102, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-102.
[16]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGO1 AND AGO2.
[19]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[20]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[21]"RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1."
Chibi M., Meyer M., Skepu A., Rees D.J.G., Moolman-Smook J.C., Pugh D.J.
J. Mol. Biol. 384:908-916(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBBP6, UBIQUITINATION.
[22]"MBNL1 associates with YB-1 in cytoplasmic stress granules."
Onishi H., Kino Y., Morita T., Futai E., Sasagawa N., Ishiura S.
J. Neurosci. Res. 86:1994-2002(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MBNL1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[23]"Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated activation of the multidrug resistance gene MDR1."
Chattopadhyay R., Das S., Maiti A.K., Boldogh I., Xie J., Hazra T.K., Kohno K., Mitra S., Bhakat K.K.
Mol. Cell. Biol. 28:7066-7080(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH APEX1.
[24]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Y-box protein-1 is actively secreted through a non-classical pathway and acts as an extracellular mitogen."
Frye B.C., Halfter S., Djudjaj S., Muehlenberg P., Weber S., Raffetseder U., En-Nia A., Knott H., Baron J.M., Dooley S., Bernhagen J., Mertens P.R.
EMBO Rep. 10:783-789(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-301 AND LYS-304, ACETYLATION AT LYS-301 AND LYS-304.
[27]"Rapid and systematic analysis of the RNA recognition specificities of RNA-binding proteins."
Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S., Blencowe B.J., Morris Q., Hughes T.R.
Nat. Biotechnol. 27:667-670(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
[28]"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[29]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-165; SER-167; SER-174 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[30]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167; SER-174 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167; SER-174; SER-176 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1."
Kloks C.P.A.M., Spronk C.A.E.M., Lasonder E., Hoffmann A., Vuister G.W., Grzesiek S., Hilbers C.W.
J. Mol. Biol. 316:317-326(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 52-129, INTERACTION WITH SS-DNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24070 mRNA. Translation: AAA35750.1. Different initiation.
J03827 mRNA. Translation: AAA61308.1. Frameshift.
M83234 mRNA. Translation: AAA59949.1. Frameshift.
L28809 mRNA. Translation: AAA20871.1.
BC002411 mRNA. Translation: AAH02411.1.
BC010430 mRNA. Translation: AAH10430.1.
BC015208 mRNA. Translation: AAH15208.1.
BC038384 mRNA. Translation: AAH38384.1.
BC065571 mRNA. Translation: AAH65571.1.
BC070084 mRNA. Translation: AAH70084.1.
BC071708 mRNA. Translation: AAH71708.1.
BC090038 mRNA. Translation: AAH90038.1.
BC098435 mRNA. Translation: AAH98435.1.
BC106045 mRNA. Translation: AAI06046.1.
PIRI39382.
S34426.
RefSeqNP_004550.2. NM_004559.3.
UniGeneHs.473583.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H95NMR-A52-129[»]
ProteinModelPortalP67809.
SMRP67809. Positions 52-129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110959. 144 interactions.
DIPDIP-29405N.
IntActP67809. 194 interactions.
MINTMINT-5001202.
STRING9606.ENSP00000361626.

PTM databases

PhosphoSiteP67809.

Polymorphism databases

DMDM54040031.

Proteomic databases

PaxDbP67809.
PRIDEP67809.

Protocols and materials databases

DNASU4904.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321358; ENSP00000361626; ENSG00000065978.
GeneID4904.
KEGGhsa:4904.
UCSCuc001chs.3. human.

Organism-specific databases

CTD4904.
GeneCardsGC01P043148.
H-InvDBHIX0037767.
HIX0172381.
HGNCHGNC:8014. YBX1.
HPACAB005875.
HPA040304.
HPA057159.
MIM154030. gene.
neXtProtNX_P67809.
PharmGKBPA31791.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1278.
HOGENOMHOG000116439.
HOVERGENHBG008757.
InParanoidP67809.
KOK09276.
OMAADRNRYR.
PhylomeDBP67809.
TreeFamTF317306.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP67809.

Gene expression databases

BgeeP67809.
CleanExHS_YBX1.
GenevestigatorP67809.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF00313. CSD. 1 hit.
[Graphical view]
PRINTSPR00050. COLDSHOCK.
SMARTSM00357. CSP. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
PROSITEPS00352. COLD_SHOCK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP67809.
GeneWikiY_box_binding_protein_1.
GenomeRNAi4904.
NextBio18871.
PMAP-CutDBP67809.
PROP67809.
SOURCESearch...

Entry information

Entry nameYBOX1_HUMAN
AccessionPrimary (citable) accession number: P67809
Secondary accession number(s): P16990 expand/collapse secondary AC list , P16991, Q14972, Q15325, Q5FVF0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM