Reviewed, UniProtKB/Swiss-Prot Q9NZI8 (IF2B1_HUMAN)

Names and origin

Protein names

Recommended name:
    Insulin-like growth factor 2 mRNA-binding protein 1
      Short name=IGF2 mRNA-binding protein 1
      Short name=IMP-1
Alternative name(s):
    IGF-II mRNA-binding protein 1
    Coding region determinant-binding protein
      Short name=CRD-BP
    VICKZ family member 1
    Zip code-binding protein 1
      Short name=Zipcode-binding protein 1
      Short name=ZBP-1

Gene names

Name:	IGF2BP1
Synonyms:	CRDBP, VICKZ1, ZBP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	RNA-binding factor that affects mRNA nuclear export, localization, stability and translation. Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Regulates mRNA stability during the integrated cellular stress response (ISR) in stress granules (SGs). Stabilizes the BTRC/FBW1A mRNA from degradation by disrupting miRNA-dependent interaction with AGO2. Identified in a HCV IRES-mediated translation complex, that enhances translation at the Hepatitis C virus (HCV) RNA-replicon via the internal ribosome entry site (IRES), but does not affect 5'cap-dependent translation. Acts as a HIV-1 retrovirus restriction factor that reduces HIV-1 assembly by inhibiting viral RNA packaging, assembly and processing of HIV-1 GAG protein on cellular membranes. Binds to mRNAs in stress granules (SGs). Binds to the stem-loop IV of the 5'UTR and to the variable region and the poly(U-C) motif of the 3'UTR of the HCV RNA-replicon. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulates its subcellular localization and translation. Binds both to the coding region mRNA stability determinant (CRD) and to AU-rich sequences in the 3'-UTR of the MYC and CD44 mRNAs and stabilizes these mRNAs. Binds to the fourth and fifth exons of the oncofetal H19 and neuron-specific TAU mRNAs and regulates their localizations. Binds to the adenine-rich autoregulatory sequence (ARS) 5'-UTR of the PABPC1 mRNA and is involved in its translational repression. The RNA-binding activity to ARS is stimulated by PABPC1. Binds to the coding sequence region of BTRC/FBW1A mRNA and mediates stabilization of BTRC/FBW1A and MYC mRNAs in response to beta-catenin signaling. Binding to RNA employs a cooperative, sequential mechanism of homo- or heterodimerisation. Also involved in growth or survival of lung-cancer cells. Protects the MYC and MDR-1 mRNAs from cleavage by a endoribonuclease, thus prolonging their stabilities By similarity. Binds to the 3'-UTR axonal localization signal (ALS) of TAU mRNA By similarity. Binds to a conserved 54-nucleotide element in the 3'-UTR of the beta actin mRNA known as the 'zipcode' By similarity. Promotes translocation of the beta-actin mRNA to dendrites By similarity. May act as a regulator of mRNA transport to activated synapses in response to synaptic activity By similarity. Ref.2 Ref.3 Ref.5 Ref.6 Ref.7 Ref.14 Ref.16 Ref.17 Ref.19 Ref.21 Ref.25 Ref.30 Ref.31 Ref.32
Subunit structure	Can form homo- and heterodimers with IGF2BP1 or IGF2BP3. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Interacts (via the KH domains) with HIV-1 GAG (via the second zinc finger motif of NC). Associates (via the RRM domains and KH domains) with HIV-1 particles. 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. Interacts with DHX9, ELAVL2, HNRNPA2B1, HNRNPC, HNRNPH1, HNRNPU, IGF2BP2, IGF2BP3, ILF2, PABPC1 and YBX1. Found in a RNP granule complex with FMR1. Interacts with FMR1. Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Interacts through the third and fourth KH domains with PABPC1 in a RNA-independent manner. Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP By similarity. Interacts with ELAVL4 in a RNA-dependent manner By similarity. Associates with microtubules and polysomes By similarity. Ref.25 Ref.9 Ref.10 Ref.15 Ref.22
Subcellular location	Nucleus. Cytoplasm. Cell projection › lamellipodium. Cell projection › dendrite By similarity. Cell projection › dendritic spine By similarity. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Targeted to stress granules (SGs), but not processing bodies (PBs), during cellular stress. Colocalizes with G3BP1 and TIAL1 in SGs. Colocalizes with HIV-1 GAG at the cell edges. Found in lamellipodia of the leading edge, in the perinuclear region, and beneath the plasma membrane. The subcytoplasmic localization is cell specific and regulated by cell contact and growth. Colocalized with H19 RNA at lamellipodia. Colocalized with CD44 mRNA in RNP granules. Nuclear export is mediated by XPO1/CRM1. In motile cells, is transported towards the leading edge into the cortical region of the lamellipodia where it is connected to microfilaments By similarity. Present in the form of granules and into F-actin-rich protrusion of dendrites, spines and subsynaptic sites By similarity. Colocalizes with beta-actin mRNA in dendrites and spines By similarity. Exhibited rapid, bidirectional movements in dendrites and spines By similarity. Neuronal depolarization by KCl induces its rapid efflux from the cell body into dendrites By similarity. Ref.2 Ref.6 Ref.14 Ref.16 Ref.25 Ref.31 Ref.9 Ref.22 Ref.4 Ref.8
Tissue specificity	Expressed in fetal liver, fetal lung, fetal kidney, fetal thymus, fetal placenta, fetal follicles of ovary, gonocytes of testis, oocytes, spermatogonia and semen (at protein level). Expressed in testicular and lung cancer (at protein level). Expressed in kidney, prostate, trachea, testis and lung cancer. Ref.2 Ref.19 Ref.12
Induction	Up-regulated in response to beta-catenin activation. Ref.17
Domain	The third and fourth KH domains encompasse the protein dimerization motif and are necessary and sufficient for RNA binding. The four KH domains are important for granule formation and SGs targeting. Contains two nuclear export signals, situated within the second and fourth KH domains. The four KH domains are important to suppress HIV-1 infectivity.
Post-translational modification	Phosphorylated. Phosphorylation may influence mRNA translation By similarity. Ref.13 Ref.18 Ref.20 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29 Ref.33
Sequence similarities	Belongs to the RRM IMP/VICKZ family. Contains 4 KH domains. Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	Translation regulation
Cellular component	Cell projection Cytoplasm Nucleus
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	CRD-mediated mRNA stabilization Ref.31 Inferred from direct assay. Source: UniProtKB negative regulation of translation Ref.2 Inferred from direct assay. Source: UniProtKB regulation of cytokine biosynthetic process Ref.2 Inferred by curator. Source: UniProtKB regulation of mRNA stability involved in response to stress Ref.16 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	CRD-mediated mRNA stability complex Ref.31 Inferred from direct assay. Source: UniProtKB dendritic spine Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA stress granule Ref.16 Inferred from direct assay. Source: UniProtKB
Molecular function	mRNA 5'-UTR binding Ref.2 Inferred from direct assay. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Ref.22 Inferred from physical interaction. Source: UniProtKB translation regulator activity Ref.2 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARHGDIA	P52565	1	EBI-1053892,EBI-712693
CNBP	P62633	1	EBI-1053892,EBI-1047529
GSK3B	P49841	1	EBI-1053892,EBI-373586
ILK	Q13418	1	EBI-1053892,EBI-747644
PRKRA	O75569	1	EBI-1053892,EBI-713955
PUF60	Q9UHX1	1	EBI-1053892,EBI-1053259
SMYD2	Q9NRG4	1	EBI-1053892,EBI-1055671

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 577	577	Insulin-like growth factor 2 mRNA-binding protein 1		PRO_0000282533
Regions
	Domain	2 – 75	74	RRM 1
	Domain	81 – 156	76	RRM 2
	Domain	195 – 260	66	KH 1
	Domain	276 – 343	68	KH 2
	Domain	405 – 470	66	KH 3
	Domain	487 – 553	67	KH 4
	Region	187 – 570	384	Necessary for interaction with ELAVL4 and binding to TAU mRNA By similarity
	Region	312 – 323	12	Sufficient for nuclear export
	Region	485 – 495	11	Sufficient for nuclear export
Amino acid modifications
	Modified residue	181	1	Phosphoserine Ref.13 Ref.18 Ref.20 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29 Ref.33
	Modified residue	446	1	Phosphothreonine Ref.29
Experimental info
	Mutagenesis	213	1	K → E: Decreases RNA-binding affinity, decreases cytoplasmic granular formation and increases nuclear localization; when associated with E-294 and E-423.
	Mutagenesis	294	1	K → E: Decreases RNA-binding affinity, decreases cytoplasmic granular formation and increases nuclear localization; when associated with E-213 and E-423.
	Mutagenesis	318	1	L → A: Diminishes export activity.
	Mutagenesis	320	1	L → A: Diminishes export activity.
	Mutagenesis	423	1	K → E: Decreases RNA-binding affinity, decreases cytoplasmic granular formation and increases nuclear localization; when associated with E-294 and E-213.
	Mutagenesis	485	1	E → A: Loss of export activity.
	Mutagenesis	486	1	V → A: Loss of export activity.
	Mutagenesis	488	1	L → A: Loss of export activity.
	Mutagenesis	492	1	I → A: Loss of export activity.
	Mutagenesis	505	1	K → E: Decreases RNA-binding affinity, loss of cytoplasmic granular formation, increases nuclear localization.
	Sequence conflict	10	1	Missing AA sequence Ref.2
	Sequence conflict	320	1	Missing AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NZI8-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 0749A060F252D81D	FASTA	577	63,456
	10 20 30 40 50 60 MNKLYIGNLN ESVTPADLEK VFAEHKISYS GQFLVKSGYA FVDCPDEHWA MKAIETFSGK 70 80 90 100 110 120 VELQGKRLEI EHSVPKKQRS RKIQIRNIPP QLRWEVLDSL LAQYGTVENC EQVNTESETA 130 140 150 160 170 180 VVNVTYSNRE QTRQAIMKLN GHQLENHALK VSYIPDEQIA QGPENGRRGG FGSRGQPRQG 190 200 210 220 230 240 SPVAAGAPAK QQQVDIPLRL LVPTQYVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA 250 260 270 280 290 300 EKAISVHSTP EGCSSACKMI LEIMHKEAKD TKTADEVPLK TLAHNNFVGR LIGKEGRNLK 310 320 330 340 350 360 KVEQDTETKI TISSLQDLTL YNPERTITVK GAIENCCRAE QEIMKKVREA YENDVAAMSL 370 380 390 400 410 420 QSHLTPGLNL AAVGLFPASS SAVPPPPSSV TGAAPYSSFM QAPEQEMVQV FIPAQAVGAI 430 440 450 460 470 480 IGKKGQHIKQ LSRFASASIK IAPPETPDSK VRMVIITGPP EAQFKAQGRI YGKLKEENFF 490 500 510 520 530 540 GPKEEVKLET HIRVPASAAG RVIGKGGKTV NELQNLTAAE VVVPRDQTPD ENDQVIVKII 550 560 570 GHFYASQMAQ RKIRDILAQV KQQHQKGQSN QAQARRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ectopic expression of a KH-domain containing protein, highly homologous to both human IMP-1 and mouse CRD-BP, in benign and malignant mesenchymal tumors." Ioannidis P., Trangas T., Dimitriadis E., Samiotaki M., Panoutsakopoulos G., Kyriazoglou I., Voutzoulias S., Tsiapalis C.M., Kittas C., Agnantis N., Pandis N. Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development." Nielsen J., Christiansen J., Lykke-Andersen J., Johnsen A.H., Wewer U.M., Nielsen F.C. Mol. Cell. Biol. 19:1262-1270(1999) [PubMed: 9891060] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-19; 26-35; 309-324 AND 508-525, FUNCTION, RNA-BINDING, ASSOCIATION WITH A MRNP COMPLEX, TISSUE SPECIFICITY, GENE NOMENCLATURE, SUBCELLULAR LOCATION.
[3]	"The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex." Patel G.P., Ma S., Bag J. Nucleic Acids Res. 33:7074-7089(2005) [PubMed: 16356927] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-35; 66-75 AND 510-524, FUNCTION, IDENTIFICATION IN A MRNP COMPLEX WITH PABPC1 AND CSDE1, IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING.
[4]	"The c-myc coding region determinant-binding protein: a member of a family of KH domain RNA-binding proteins." Doyle G.A., Betz N.A., Leeds P.F., Fleisig A.J., Prokipcak R.D., Ross J. Nucleic Acids Res. 26:5036-5044(1998) [PubMed: 9801297] [Abstract] Cited for: PROTEIN SEQUENCE OF 413-429 AND 510-524, SUBCELLULAR LOCATION, RNA-BINDING.
[5]	"Purification and properties of a protein that binds to the C-terminal coding region of human c-myc mRNA." Prokipcak R.D., Herrick D.J., Ross J. J. Biol. Chem. 269:9261-9269(1994) [PubMed: 8132663] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[6]	"H19 RNA binds four molecules of insulin-like growth factor II mRNA-binding protein." Runge S., Nielsen F.C., Nielsen J., Lykke-Andersen J., Wewer U.M., Christiansen J. J. Biol. Chem. 275:29562-29569(2000) [PubMed: 10875929] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING.
[7]	"Regulation of c-myc mRNA decay by translational pausing in a coding region instability determinant." Lemm I., Ross J. Mol. Cell. Biol. 22:3959-3969(2002) [PubMed: 12024010] [Abstract] Cited for: FUNCTION.
[8]	"Nuclear transit of human zipcode-binding protein IMP1." Nielsen J., Adolph S.K., Rajpert-De Meyts E., Lykke-Andersen J., Koch G., Christiansen J., Nielsen F.C. Biochem. J. 376:383-391(2003) [PubMed: 12921532] [Abstract] Cited for: MUTAGENESIS, SUBCELLULAR LOCATION.
[9]	"Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs." Rackham O., Brown C.M. EMBO J. 23:3346-3355(2004) [PubMed: 15282548] [Abstract] Cited for: IDENTIFICATION IN A RNP GRANULE COMPLEX WITH FMR1, INTERACTION WITH FMR1, RNA-BINDING, SUBCELLULAR LOCATION.
[10]	"Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability." Nielsen J., Kristensen M.A., Willemoes M., Nielsen F.C., Christiansen J. Nucleic Acids Res. 32:4368-4376(2004) [PubMed: 15314207] [Abstract] Cited for: SUBUNIT, RNA-BINDING.
[11]	"VICKZ proteins: a multi-talented family of regulatory RNA-binding proteins." Yisraeli J.K. Biol. Cell 97:87-96(2005) [PubMed: 15601260] [Abstract] Cited for: REVIEW.
[12]	"Expression of IGF-II mRNA-binding proteins (IMPs) in gonads and testicular cancer." Hammer N.A., Hansen T.O., Byskov A.G., Rajpert-De Meyts E., Groendahl M.L., Bredkjaer H.E., Wewer U.M., Christiansen J., Nielsen F.C. Reproduction 130:203-212(2005) [PubMed: 16049158] [Abstract] Cited for: TISSUE SPECIFICITY.
[13]	"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-181, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"RNA-binding IMPs promote cell adhesion and invadopodia formation." Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M., Christiansen J., Nielsen F.C. EMBO J. 25:1456-1468(2006) [PubMed: 16541107] [Abstract] Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
[15]	"IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory translational control element of PABP-mRNA through the KH III-IV domain." Patel G.P., Bag J. FEBS J. 273:5678-5690(2006) [PubMed: 17212783] [Abstract] Cited for: INTERACTION WITH PABPC1, RNA-BINDING.
[16]	"ZBP1 regulates mRNA stability during cellular stress." Stoehr N., Lederer M., Reinke C., Meyer S., Hatzfeld M., Singer R.H., Huettelmaier S. J. Cell Biol. 175:527-534(2006) [PubMed: 17101699] [Abstract] Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
[17]	"CRD-BP mediates stabilization of betaTrCP1 and c-myc mRNA in response to beta-catenin signaling." Noubissi F.K., Elcheva I., Bhatia N., Shakoori A., Ougolkov A., Liu J., Minamoto T., Ross J., Fuchs S.Y., Spiegelman V.S. Nature 441:898-901(2006) [PubMed: 16778892] [Abstract] Cited for: FUNCTION, RNA-BINDING, INDUCTION.
[18]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"Increased expression of insulin-like growth factor-II messenger RNA-binding protein 1 is associated with tumor progression in patients with lung cancer." Kato T., Hayama S., Yamabuki T., Ishikawa N., Miyamoto M., Ito T., Tsuchiya E., Kondo S., Nakamura Y., Daigo Y. Clin. Cancer Res. 13:434-442(2007) [PubMed: 17255263] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[20]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Epithelium.
[21]	"ZBP2 facilitates binding of ZBP1 to beta-actin mRNA during transcription." Pan F., Huettelmaier S., Singer R.H., Gu W. Mol. Cell. Biol. 27:8340-8351(2007) [PubMed: 17893325] [Abstract] Cited for: FUNCTION.
[22]	"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 DHX9; ELAVL2; HNRNPA2B1; HNRNPC; HNRNPH1; HNRNPU; IGF2BP2; IGF2BP3; ILF2; PABPC1 AND YBX1, RNA-BINDING, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[23]	"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-181, MASS SPECTROMETRY.
[24]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY.
[25]	"Insulin-like growth factor II mRNA binding protein 1 associates with Gag protein of human immunodeficiency virus type 1, and its overexpression affects virus assembly." Zhou Y., Rong L., Lu J., Pan Q., Liang C. J. Virol. 82:5683-5692(2008) [PubMed: 18385235] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIV-1 GAG, SUBCELLULAR LOCATION.
[26]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY.
[27]	"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-181, MASS SPECTROMETRY.
[28]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[29]	"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 SER-181 AND THR-446, MASS SPECTROMETRY.
[30]	"CRD-BP protects the coding region of betaTrCP1 mRNA from miR-183-mediated degradation." Elcheva I., Goswami S., Noubissi F.K., Spiegelman V.S. Mol. Cell 35:240-246(2009) [PubMed: 19647520] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[31]	"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.
[32]	"IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR." Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., Ostareck-Lederer A., Ostareck D.H. RNA 15:1528-1542(2009) [PubMed: 19541769] [Abstract] Cited for: FUNCTION, RNA-BINDING, IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
[33]	"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-181, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF198254 mRNA. Translation: AAF37203.1.
IPI	IPI00008557.
RefSeq	NP_006537.3.
UniGene	Hs.144936
3D structure databases
HSSP	HSSP built from PDB template 2CQH based on UniProtKB Q9Y6M1.
SMR	Q9NZI8. Positions 1-154, 74-161, 197-347, 406-557.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NZI8. 16 interactions.
STRING	Q9NZI8.
PTM databases
PhosphoSite	Q9NZI8.
Proteomic databases
PeptideAtlas	Q9NZI8.
PRIDE	Q9NZI8.
Genome annotation databases
Ensembl	ENST00000290341; ENSP00000290341; ENSG00000159217; Homo sapiens. [Genome view]
GeneID	10642.
UCSC	uc002iom.1. human.
Organism-specific databases
CTD	10642.
GeneCards	GC17P044430.
HGNC	HGNC:28866. IGF2BP1.
HPA	HPA021367.
MIM	608288. gene.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18446.
HOGENOM	HBG403151.
HOVERGEN	Q9NZI8.
InParanoid	Q9NZI8.
Gene expression databases
ArrayExpress	Q9NZI8.
Bgee	Q9NZI8.
CleanEx	HS_IGF2BP1. HS_ZBP1.
Genevestigator	Q9NZI8.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR004087. KH. IPR004088. KH_type_1. IPR018111. KH_type_1_subgr. IPR000504. RRM_RNP1. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
Pfam	PF00013. KH_1. 4 hits. PF00076. RRM_1. 2 hits. [Graphical view]
SMART	SM00322. KH. 4 hits. SM00360. RRM. 2 hits. [Graphical view]
PROSITE	PS50084. KH_TYPE_1. 4 hits. PS50102. RRM. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	40447.
SOURCE	Search...

Entry information

Entry name

IF2B1_HUMAN

Accession

Primary (citable) accession number: Q9NZI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.