Q9NZI8 (IF2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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):
Coding region determinant-binding protein
Short name=CRD-BP
IGF-II mRNA-binding protein 1
VICKZ family member 1
Zip code-binding protein 1
Short name=ZBP-1
Short name=Zipcode-binding protein 1

Gene names

Name:	IGF2BP1
Synonyms:	CRDBP, VICKZ1, ZBP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.16 Ref.18 Ref.20 Ref.21 Ref.23 Ref.25 Ref.27 Ref.28 Ref.29 Ref.33
Subunit structure	Can form homodimers 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. Interacts with EIF2C1 and EIF2C2. Ref.5 Ref.11 Ref.12 Ref.17 Ref.22 Ref.24 Ref.25 Ref.28 Ref.29
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.4 Ref.6 Ref.8 Ref.10 Ref.11 Ref.16 Ref.18 Ref.24 Ref.25 Ref.28
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.4 Ref.14 Ref.21
Induction	Up-regulated in response to beta-catenin activation. Ref.20
Domain	The third and fourth KH domains encompass 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. Ref.33
Post-translational modification	Phosphorylated. Phosphorylation may influence mRNA translation By similarity.
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
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CRD-mediated mRNA stabilization Inferred from direct assay Ref.28. Source: UniProtKB RNA localization Inferred from electronic annotation. Source: Compara negative regulation of translation Inferred from direct assay Ref.4. Source: BHF-UCL regulation of cytokine biosynthetic process Inferred by curator Ref.4. Source: BHF-UCL regulation of mRNA stability involved in response to stress Inferred from mutant phenotype Ref.18. Source: UniProtKB
Cellular_component	CRD-mediated mRNA stability complex Inferred from direct assay Ref.28. Source: UniProtKB cytoplasmic stress granule Inferred from direct assay Ref.18. Source: UniProtKB cytosol Traceable author statement. Source: Reactome dendritic spine Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	mRNA 3'-UTR binding Inferred from direct assay Ref.33. Source: UniProtKB mRNA 5'-UTR binding Inferred from direct assay Ref.4. Source: BHF-UCL nucleotide binding Inferred from electronic annotation. Source: InterPro translation regulator activity Inferred from direct assay Ref.4. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NZI8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NZI8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     135-273: Missing.

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.15 Ref.19 Ref.30 Ref.32

Natural variations

Alternative sequence

135 – 273

139

Missing in isoform 2.

VSP_045366

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.4

Sequence conflict

281

1

I → T in AAF37203. Ref.1

Sequence conflict

320

1

Missing AA sequence Ref.4

Sequence conflict

365

1

I → T in AAF37203. Ref.1

Secondary structure

1

.

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577

Helix Strand Turn

Details...

Beta strand

406 – 413

8

Helix

414 – 416

3

Helix

417 – 421

5

Helix

423 – 425

3

Helix

426 – 435

10

Beta strand

438 – 441

4

Beta strand

450 – 458

9

Helix

460 – 476

17

Beta strand

488 – 495

8

Turn

496 – 498

3

Helix

499 – 503

5

Helix

505 – 507

3

Helix

508 – 517

10

Beta strand

520 – 522

3

Beta strand

533 – 541

9

Helix

543 – 560

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 1D036AE5388D05FA	FASTA	577	63,481
	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 ILAHNNFVGR LIGKEGRNLK 310 320 330 340 350 360 KVEQDTETKI TISSLQDLTL YNPERTITVK GAIENCCRAE QEIMKKVREA YENDVAAMSL 370 380 390 400 410 420 QSHLIPGLNL 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
	Isoform 2 [UniParc]. Checksum: 2F615D03F5C00C1E	FASTA	438	48,598
	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 QTRQADEVPL KILAHNNFVG RLIGKEGRNL KKVEQDTETK ITISSLQDLT 190 200 210 220 230 240 LYNPERTITV KGAIENCCRA EQEIMKKVRE AYENDVAAMS LQSHLIPGLN LAAVGLFPAS 250 260 270 280 290 300 SSAVPPPPSS VTGAAPYSSF MQAPEQEMVQ VFIPAQAVGA IIGKKGQHIK QLSRFASASI 310 320 330 340 350 360 KIAPPETPDS KVRMVIITGP PEAQFKAQGR IYGKLKEENF FGPKEEVKLE THIRVPASAA 370 380 390 400 410 420 GRVIGKGGKT VNELQNLTAA EVVVPRDQTP DENDQVIVKI IGHFYASQMA QRKIRDILAQ 430 VKQQHQKGQS NQAQARRK

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] (ISOFORM 1).
[2]	"A novel splice variant of the human IGF2 mRNA-binding protein 1 (IMP1/CRD-BP) isolated from human Hep3B hepatoma cells." Gong H.Y., Hu M.C., Wu J.L. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] [Europe PMC] [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.
[5]	"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] [Europe PMC] [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.
[6]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 413-429 AND 510-524, SUBCELLULAR LOCATION, RNA-BINDING.
[7]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[8]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING.
[9]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS, SUBCELLULAR LOCATION.
[11]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A RNP GRANULE COMPLEX WITH FMR1, INTERACTION WITH FMR1, RNA-BINDING, SUBCELLULAR LOCATION.
[12]	"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] [Europe PMC] [Abstract] Cited for: SUBUNIT, RNA-BINDING.
[13]	"VICKZ proteins: a multi-talented family of regulatory RNA-binding proteins." Yisraeli J.K. Biol. Cell 97:87-96(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[14]	"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] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
[17]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PABPC1, RNA-BINDING.
[18]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
[19]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, RNA-BINDING, INDUCTION.
[21]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[22]	"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 EIF2C1 AND EIF2C2.
[23]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[24]	"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 DHX9; ELAVL2; HNRNPA2B1; HNRNPC; HNRNPH1; HNRNPU; IGF2BP2; IGF2BP3; ILF2; PABPC1 AND YBX1, RNA-BINDING, SUBCELLULAR LOCATION, IDENTIFICATION BY 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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIV-1 GAG, SUBCELLULAR LOCATION.
[26]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[27]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, 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]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, RNA-BINDING, IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
[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-181, MASS SPECTROMETRY. 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-181, MASS SPECTROMETRY.
[33]	"ZBP1 recognition of beta-actin zipcode induces RNA looping." Chao J.A., Patskovsky Y., Patel V., Levy M., Almo S.C., Singer R.H. Genes Dev. 24:148-158(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 404-566, FUNCTION, RNA-BINDING, DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF198254 mRNA. Translation: AAF37203.1.
DQ227344 mRNA. Translation: ABB46294.1.
AC091133 Genomic DNA. No translation available.
AC105030 Genomic DNA. No translation available.

IPI

IPI00008557.
IPI00930694.

RefSeq

NP_001153895.1. NM_001160423.1.
NP_006537.3. NM_006546.3.

UniGene

Hs.144936.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KRM	X-ray	2.75	A/B/C	404-566	[»]

ProteinModelPortal

Q9NZI8.

SMR

Q9NZI8. Positions 1-161, 198-349, 405-562.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38139N.

IntAct

Q9NZI8. 20 interactions.

STRING

9606.ENSP00000290341.

PTM databases

PhosphoSite

Q9NZI8.

Polymorphism databases

DMDM

296434536.

Proteomic databases

PaxDb

Q9NZI8.

PeptideAtlas

Q9NZI8.

PRIDE

Q9NZI8.

Protocols and materials databases

DNASU

10642.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000290341; ENSP00000290341; ENSG00000159217.
ENST00000431824; ENSP00000389135; ENSG00000159217.

GeneID

10642.

KEGG

hsa:10642.

UCSC

uc002iom.3. human.

Organism-specific databases

CTD

10642.

GeneCards

GC17P047074.

H-InvDB

HIX0013955.

HGNC

HGNC:28866. IGF2BP1.

HPA

HPA021367.

MIM

608288. gene.

neXtProt

NX_Q9NZI8.

PharmGKB

PA143485501.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG249985.

HOGENOM

HOG000000675.

HOVERGEN

HBG052725.

InParanoid

Q9NZI8.

OMA

EQETVHV.

OrthoDB

EOG405S0T.

PhylomeDB

Q9NZI8.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q9NZI8.

Bgee

Q9NZI8.

CleanEx

HS_IGF2BP1.
HS_ZBP1.

Genevestigator

Q9NZI8.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00013. KH_1. 4 hits.
PF00076. RRM_1. 1 hit.
[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

EvolutionaryTrace

Q9NZI8.

GenomeRNAi

10642.

NextBio

40447.

SOURCE

Search...

Entry information

Entry name

IF2B1_HUMAN

Accession

Primary (citable) accession number: Q9NZI8
Secondary accession number(s): C9JT33

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 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.