P67809 (YBOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	YBX1
Synonyms:	NSEP1, YB1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.11 Ref.21 Ref.23 Ref.26 Ref.29 The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation. Ref.7 Ref.8 Ref.9 Ref.11 Ref.21 Ref.23 Ref.26 Ref.29
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 mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and 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, 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 EIF2C1 and EIF2C2. Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.17 Ref.18 Ref.20 Ref.21 Ref.23 Ref.32
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.11 Ref.13 Ref.18 Ref.21 Ref.26 Ref.29
Post-translational modification	Ubiquitinated by RBBP6; leading to a decrease of YBX1 transcactivational ability. Ref.20 Ref.22 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 process	Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Secreted
Ligand	DNA-binding RNA-binding
Molecular function	Activator Mitogen Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	CRD-mediated mRNA stabilization Inferred from mutant phenotype Ref.29. Source: UniProtKB nuclear mRNA splicing, via spliceosome Traceable author statement. Source: Reactome positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	CRD-mediated mRNA stability complex Inferred from direct assay Ref.29. Source: UniProtKB U12-type spliceosomal complex Inferred from direct assay Ref.12. Source: UniProtKB cytoplasmic stress granule Inferred from direct assay Ref.21. Source: UniProtKB extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell histone pre-mRNA 3'end processing complex Inferred from sequence or structural similarity. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular function	RNA binding Inferred from direct assay Ref.28. Source: UniProtKB double-stranded DNA binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.18Ref.17Ref.21Ref.23Ref.20. Source: UniProtKB sequence-specific DNA binding transcription factor activity Traceable author statement. Source: ProtInc single-stranded DNA binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTCF	Q08705	2	EBI-354065,EBI-932806	From a different organism.
EP300	Q09472	2	EBI-354065,EBI-447295
HNRNPD	Q14103-4	3	EBI-354065,EBI-432545

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 324

323

Nuclease-sensitive element-binding protein 1

PRO_0000100219

Regions

Domain

61 – 125

65

CSD

Region

15 – 71

57

Interaction with ss-DNA

Sites

Site

219 – 220

2

Cleavage; by 20S proteasomal protease

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.6

Modified residue

102

1

Phosphoserine; by PKB/AKT1 Ref.13

Modified residue

162

1

Phosphotyrosine Ref.14 Ref.25

Modified residue

165

1

Phosphoserine Ref.6 Ref.16 Ref.24 Ref.25 Ref.30

Modified residue

167

1

Phosphoserine Ref.16 Ref.25 Ref.30

Modified residue

174

1

Phosphoserine Ref.15 Ref.16 Ref.24 Ref.25 Ref.30

Modified residue

176

1

Phosphoserine Ref.15 Ref.24 Ref.25 Ref.30

Modified residue

301

1

N6-acetyllysine Ref.26

Modified residue

304

1

N6-acetyllysine Ref.26

Modified residue

313

1

Phosphoserine Ref.25 Ref.27

Modified residue

314

1

Phosphoserine Ref.15 Ref.19 Ref.25

Cross-link

137

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.22

Experimental info

Mutagenesis

102

1

S → A: Loss of phosphorylation by PKB/AKT1. Inhibits translocation to the nucleus and tumor cell growth. Ref.13

Mutagenesis

301

1

K → A: Abrogates unconventional secretion. Ref.26

Mutagenesis

304

1

K → A: Abrogates unconventional secretion. Ref.26

Sequence conflict

120

1

A → E in AAA61308. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

324

Helix Strand Turn

Details...

Beta strand

56 – 67

12

Turn

68 – 71

4

Beta strand

72 – 77

6

Turn

78 – 81

4

Beta strand

82 – 87

6

Helix

88 – 90

3

Beta strand

108 – 115

8

Beta strand

117 – 125

9

Sequences

	Sequence		Length	Mass (Da)
	P67809 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DF0114BF974AEDB8	FASTA	324	35,924
	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

References

	« Hide 'large scale' referencesShow '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: 2977358] [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: 3174636] [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: 1891370] [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: 8188694] [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: 15489334] [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, 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: 10817758] [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: 11698476] [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: 12604611] [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: 14559993] [Abstract] Cited for: INTERACTION WITH SFRS12.
[11]	"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: 14718551] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH THOC4; NCL; XRCC5; WRN AND MSH2.
[12]	"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: 15146077] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, MASS SPECTROMETRY.
[13]	"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: 15806160] [Abstract] Cited for: PHOSPHORYLATION AT SER-102, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-102.
[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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, MASS SPECTROMETRY.
[15]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-176 AND SER-314, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167 AND SER-174, MASS SPECTROMETRY. Tissue: Prostate cancer.
[17]	"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: 17932509] [Abstract] Cited for: INTERACTION WITH EIF2C1 AND EIF2C2.
[18]	"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: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[19]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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: 18851979] [Abstract] Cited for: INTERACTION WITH RBBP6, UBIQUITINATION.
[21]	"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: 18335541] [Abstract] Cited for: FUNCTION, INTERACTION WITH MBNL1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[22]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-137, 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: 18809583] [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-174 AND SER-176, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162; SER-165; SER-167; SER-174; SER-176; SER-313 AND SER-314, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19483673] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-301 AND LYS-304, ACETYLATION AT LYS-301 AND LYS-304.
[27]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, MASS SPECTROMETRY.
[28]	"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: 19561594] [Abstract] Cited for: RNA-BINDING.
[29]	"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: 19029303] [Abstract] Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[30]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167; SER-174 AND SER-176, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]	"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: 11851341] [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.

IPI

IPI00031812.

PIR

I39382.
S34426.

RefSeq

NP_004550.2. NM_004559.3.

UniGene

Hs.473583.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H95	NMR	-	A	52-129	[»]

ProteinModelPortal

P67809.

SMR

P67809. Positions 52-129.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29405N.

IntAct

P67809. 37 interactions.

MINT

MINT-5001202.

STRING

P67809.

PTM databases

PhosphoSite

P67809.

Polymorphism databases

DMDM

54040031.

Proteomic databases

PRIDE

P67809.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000321358; ENSP00000361626; ENSG00000065978.

GeneID

4904.

KEGG

hsa:4904.

UCSC

uc001chs.1. human.

Organism-specific databases

CTD

4904.

GeneCards

GC01P043148.

H-InvDB

HIX0000491.

HGNC

HGNC:8014. YBX1.

HPA

CAB005875.
HPA040304.

MIM

154030. gene.

neXtProt

NX_P67809.

PharmGKB

PA31791.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG008757.

InParanoid

P67809.

OMA

NEGAENI.

OrthoDB

EOG46DM3W.

PhylomeDB

P67809.

Enzyme and pathway databases

Pathway_Interaction_DB

ptp1bpathway. Signaling events mediated by PTP1B.

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P67809.

CleanEx

HS_YBX1.

Genevestigator

P67809.

GermOnline

ENSG00000065978. Homo sapiens.

Family and domain databases

InterPro

IPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
[Graphical view]

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.

KO

K09276.

Pfam

PF00313. CSD. 1 hit.
[Graphical view]

PRINTS

PR00050. COLDSHOCK.

SMART

SM00357. CSP. 1 hit.
[Graphical view]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

PROSITE

PS00352. COLD_SHOCK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

18871.

PMAP-CutDB

P67809.

SOURCE

Search...

Entry information

Entry name

YBOX1_HUMAN

Accession

Primary (citable) accession number: P67809
Secondary accession number(s): P16990 , P16991, Q14972, Q15325, Q5FVF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.