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Protein

Nuclease-sensitive element-binding protein 1

Gene

YBX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity
The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei219 – 2202Cleavage; by 20S proteasomal protease

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: ProtInc
  • GTPase binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • single-stranded DNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Mitogen, Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.
SignaLinkiP67809.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:YBX1
Synonyms:NSEP1, YB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8014. YBX1.

Subcellular locationi

  • Cytoplasm
  • Nucleus
  • Cytoplasmic granule 1 Publication
  • 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.

GO - Cellular componenti

  • CRD-mediated mRNA stability complex Source: UniProtKB
  • cytoplasm Source: HPA
  • cytoplasmic stress granule Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • histone pre-mRNA 3'end processing complex Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • nuclear membrane Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: ProtInc
  • ribonucleoprotein complex Source: UniProtKB
  • U12-type spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi102 – 1021S → A: Loss of phosphorylation by PKB/AKT1. Inhibits translocation to the nucleus and tumor cell growth. 1 Publication
Mutagenesisi301 – 3011K → A: Abrogates unconventional secretion. 1 Publication
Mutagenesisi304 – 3041K → A: Abrogates unconventional secretion. 1 Publication

Organism-specific databases

PharmGKBiPA31791.

Polymorphism and mutation databases

BioMutaiYBX1.
DMDMi54040031.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 324323Nuclease-sensitive element-binding protein 1PRO_0000100219Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei102 – 1021Phosphoserine; by PKB/AKT12 Publications
Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei162 – 1621Phosphotyrosine1 Publication
Modified residuei165 – 1651Phosphoserine4 Publications
Modified residuei167 – 1671Phosphoserine4 Publications
Modified residuei174 – 1741Phosphoserine6 Publications
Modified residuei176 – 1761Phosphoserine6 Publications
Modified residuei301 – 3011N6-acetyllysine1 Publication
Modified residuei304 – 3041N6-acetyllysine1 Publication
Modified residuei314 – 3141Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated by RBBP6; leading to a decrease of YBX1 transcactivational ability.1 Publication
In the absence of phosphorylation the protein is retained in the cytoplasm.2 Publications
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).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP67809.
PaxDbiP67809.
PRIDEiP67809.

PTM databases

PhosphoSiteiP67809.

Miscellaneous databases

PMAP-CutDBP67809.

Expressioni

Gene expression databases

BgeeiP67809.
CleanExiHS_YBX1.
ExpressionAtlasiP67809. baseline.
GenevisibleiP67809. HS.

Organism-specific databases

HPAiCAB005875.
HPA040304.
HPA057159.

Interactioni

Subunit structurei

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. Interacts with DERA.By similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C1QBPQ070216EBI-354065,EBI-347528
CTCFQ087052EBI-354065,EBI-932806From a different organism.
DHX9Q0821110EBI-354065,EBI-352022
EP300Q094722EBI-354065,EBI-447295
FBXO33Q7Z6M25EBI-354065,EBI-8555452
HNRNPDQ14103-43EBI-354065,EBI-432545
LSM3P623102EBI-354065,EBI-348239
PITX2Q996973EBI-354065,EBI-1175211

Protein-protein interaction databases

BioGridi110959. 151 interactions.
DIPiDIP-29405N.
IntActiP67809. 301 interactions.
MINTiMINT-5001202.
STRINGi9606.ENSP00000361626.

Structurei

Secondary structure

1
324
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 6712Combined sources
Turni68 – 714Combined sources
Beta strandi72 – 776Combined sources
Turni78 – 814Combined sources
Beta strandi82 – 876Combined sources
Helixi88 – 903Combined sources
Beta strandi108 – 1158Combined sources
Beta strandi117 – 1259Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H95NMR-A52-129[»]
ProteinModelPortaliP67809.
SMRiP67809. Positions 52-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP67809.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 12565CSDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 7157Interaction with ss-DNAAdd
BLAST

Sequence similaritiesi

Contains 1 CSD (cold-shock) domain.Curated

Phylogenomic databases

eggNOGiCOG1278.
GeneTreeiENSGT00390000009256.
HOGENOMiHOG000116439.
HOVERGENiHBG008757.
InParanoidiP67809.
KOiK09276.
OMAiRRYPPYY.
PhylomeDBiP67809.
TreeFamiTF317306.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF00313. CSD. 1 hit.
[Graphical view]
PRINTSiPR00050. COLDSHOCK.
SMARTiSM00357. CSP. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS00352. COLD_SHOCK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P67809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEAETQQP PAAPPAAPAL SAADTKPGTT GSGAGSGGPG GLTSAAPAGG
60 70 80 90 100
DKKVIATKVL GTVKWFNVRN GYGFINRNDT KEDVFVHQTA IKKNNPRKYL
110 120 130 140 150
RSVGDGETVE FDVVEGEKGA EAANVTGPGG VPVQGSKYAA DRNHYRRYPR
160 170 180 190 200
RRGPPRNYQQ NYQNSESGEK NEGSESAPEG QAQQRRPYRR RRFPPYYMRR
210 220 230 240 250
PYGRRPQYSN PPVQGEVMEG ADNQGAGEQG RPVRQNMYRG YRPRFRRGPP
260 270 280 290 300
RQRQPREDGN EEDKENQGDE TQGQQPPQRR YRRNFNYRRR RPENPKPQDG
310 320
KETKAADPPA ENSSAPEAEQ GGAE
Length:324
Mass (Da):35,924
Last modified:January 23, 2007 - v3
Checksum:iDF0114BF974AEDB8
GO

Sequence cautioni

The sequence AAA35750.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAA59949.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAA61308.1 differs from that shown. Reason: Frameshift at position 314. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201A → E in AAA61308 (PubMed:3174636).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS470.1.
PIRiI39382.
S34426.
RefSeqiNP_004550.2. NM_004559.3.
UniGeneiHs.473583.

Genome annotation databases

EnsembliENST00000321358; ENSP00000361626; ENSG00000065978.
GeneIDi4904.
KEGGihsa:4904.
UCSCiuc001chs.3. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS470.1.
PIRiI39382.
S34426.
RefSeqiNP_004550.2. NM_004559.3.
UniGeneiHs.473583.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H95NMR-A52-129[»]
ProteinModelPortaliP67809.
SMRiP67809. Positions 52-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110959. 151 interactions.
DIPiDIP-29405N.
IntActiP67809. 301 interactions.
MINTiMINT-5001202.
STRINGi9606.ENSP00000361626.

PTM databases

PhosphoSiteiP67809.

Polymorphism and mutation databases

BioMutaiYBX1.
DMDMi54040031.

Proteomic databases

MaxQBiP67809.
PaxDbiP67809.
PRIDEiP67809.

Protocols and materials databases

DNASUi4904.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321358; ENSP00000361626; ENSG00000065978.
GeneIDi4904.
KEGGihsa:4904.
UCSCiuc001chs.3. human.

Organism-specific databases

CTDi4904.
GeneCardsiGC01P043148.
H-InvDBHIX0037767.
HIX0172381.
HGNCiHGNC:8014. YBX1.
HPAiCAB005875.
HPA040304.
HPA057159.
MIMi154030. gene.
neXtProtiNX_P67809.
PharmGKBiPA31791.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1278.
GeneTreeiENSGT00390000009256.
HOGENOMiHOG000116439.
HOVERGENiHBG008757.
InParanoidiP67809.
KOiK09276.
OMAiRRYPPYY.
PhylomeDBiP67809.
TreeFamiTF317306.

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.
SignaLinkiP67809.

Miscellaneous databases

ChiTaRSiYBX1. human.
EvolutionaryTraceiP67809.
GeneWikiiY_box_binding_protein_1.
GenomeRNAii4904.
NextBioi18871.
PMAP-CutDBP67809.
PROiP67809.
SOURCEiSearch...

Gene expression databases

BgeeiP67809.
CleanExiHS_YBX1.
ExpressionAtlasiP67809. baseline.
GenevisibleiP67809. HS.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF00313. CSD. 1 hit.
[Graphical view]
PRINTSiPR00050. COLDSHOCK.
SMARTiSM00357. CSP. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS00352. COLD_SHOCK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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. 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. "DERA is the human deoxyribose phosphate aldolase and is involved in stress response."
    Salleron L., Magistrelli G., Mary C., Fischer N., Bairoch A., Lane L.
    Biochim. Biophys. Acta 1843:2913-2925(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DERA, SUBCELLULAR LOCATION.
  34. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-174 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  35. "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.

Entry informationi

Entry nameiYBOX1_HUMAN
AccessioniPrimary (citable) accession number: P67809
Secondary accession number(s): P16990
, P16991, Q14972, Q15325, Q5FVF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.