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Q9NZI8

- IF2B1_HUMAN

UniProt

Q9NZI8 - IF2B1_HUMAN

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Protein

Insulin-like growth factor 2 mRNA-binding protein 1

Gene

IGF2BP1

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

Functioni

RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts.By similarity15 Publications

GO - Molecular functioni

  1. mRNA 3'-UTR binding Source: UniProtKB
  2. mRNA 5'-UTR binding Source: BHF-UCL
  3. mRNA binding Source: UniProtKB
  4. nucleotide binding Source: InterPro
  5. poly(A) RNA binding Source: UniProtKB
  6. translation regulator activity Source: BHF-UCL

GO - Biological processi

  1. CRD-mediated mRNA stabilization Source: UniProtKB
  2. gene expression Source: Reactome
  3. mRNA transport Source: UniProtKB-KW
  4. negative regulation of translation Source: BHF-UCL
  5. regulation of cytokine biosynthetic process Source: BHF-UCL
  6. regulation of mRNA stability involved in response to stress Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_22166. Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like growth factor 2 mRNA-binding protein 1
Short name:
IGF2 mRNA-binding protein 1
Short name:
IMP-1
Short name:
IMP1
Alternative name(s):
Coding region determinant-binding protein
Short name:
CRD-BP
IGF-II mRNA-binding protein 1
VICKZ family member 1
Zipcode-binding protein 1
Short name:
ZBP-1
Gene namesi
Name:IGF2BP1
Synonyms:CRDBP, VICKZ1, ZBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:28866. IGF2BP1.

Subcellular locationi

Nucleus. Cytoplasm. Cytoplasmperinuclear region. Cell projectionlamellipodium. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity. Cell projectiongrowth cone. Cell projectionfilopodium By similarity. Cell projectionaxon By similarity
Note: In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription (By similarity). In the cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with microtubules in growth cone filopodia and along neurites in neuronal cells (By similarity). Cytoplasmic colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript. In neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited (By similarity). In hippocampal neurons, predominantly located within dendrites, particularly at dendritic branching points in young cells, compared to axons (By similarity). In axons, predominantly found in axonal branches and their growth cones (By similarity). In motile cells, such as migrating fibroblasts, localizes to leading edges where it colocalizes with microtubules and microfilaments and to retracting tails (By similarity). Dendritic levels are regulated by neuronal activity and glutaminergic signals: they are increased by KCl-induced depolarization, which induces rapid efflux from the cell body into dendrites, and decreased by the NMDA receptor agonist (By similarity). In motile cells, transported towards the leading edge into the cortical region of the lamellipodia where it is connected to microfilaments (By similarity). In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules, but not to processing bodies.By similarity

GO - Cellular componenti

  1. CRD-mediated mRNA stability complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic stress granule Source: UniProtKB
  4. cytosol Source: Reactome
  5. dendrite Source: Ensembl
  6. nucleus Source: UniProtKB-KW
  7. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi213 – 2142KE → EL: 50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 294-E-L-295 and 423-E-L-424. 1 Publication
Mutagenesisi294 – 2952KE → EL: 50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 213-E-L-214 and 423-E-L-424. 1 Publication
Mutagenesisi423 – 4242KK → EL: 50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 213-E-L-214 and 294-E-L-295. 1 Publication

Organism-specific databases

PharmGKBiPA143485501.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 577577Insulin-like growth factor 2 mRNA-binding protein 1PRO_0000282533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811Phosphoserine4 Publications

Post-translational modificationi

Phosphorylated. Phosphorylation may impair association with ACTB mRNA and hence abolishes translational repression (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NZI8.
PaxDbiQ9NZI8.
PeptideAtlasiQ9NZI8.
PRIDEiQ9NZI8.

PTM databases

PhosphoSiteiQ9NZI8.

Expressioni

Tissue specificityi

Mainly expressed in the embryo, including in fetal liver, fetal lung, fetal kidney, fetal thymus (at protein level). Also expressed follicles of ovary, as well as in gonocytes of testis, spermatogonia, semen, oocytes and placenta (at protein level). Expressed in various cancers, including testis and lung cancers (at protein level), as well as kidney, prostate and trachea cancers.4 Publications

Inductioni

May be up-regulated in response to CTNNB1/beta-catenin activation.1 Publication

Gene expression databases

BgeeiQ9NZI8.
CleanExiHS_IGF2BP1.
HS_ZBP1.
ExpressionAtlasiQ9NZI8. baseline and differential.
GenevestigatoriQ9NZI8.

Organism-specific databases

HPAiHPA021367.

Interactioni

Subunit structurei

Can form homodimers and heterodimers with IGF2BP1 and IGF2BP3. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. During HCV infection, 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, composed of at least DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with DHX9, ELAVL2, HNRNPA2B1, HNRNPC, HNRNPH1, HNRNPU, IGF2BP2, ILF2, and YBX1. Interacts with FMR1. Component of a multisubunit autoregulatory RNP complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1/UNR. Directly interacts with PABPC1. Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP. Interacts with ELAVL4 in an RNA-dependent manner. Associates with microtubules and polysomes. Interacts with AGO1 and AGO2.10 Publications

Protein-protein interaction databases

BioGridi115886. 56 interactions.
DIPiDIP-38139N.
IntActiQ9NZI8. 25 interactions.
MINTiMINT-4998820.
STRINGi9606.ENSP00000290341.

Structurei

Secondary structure

1
577
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi406 – 4138Combined sources
Helixi414 – 4163Combined sources
Helixi417 – 4215Combined sources
Helixi423 – 4253Combined sources
Helixi426 – 43510Combined sources
Beta strandi438 – 4414Combined sources
Beta strandi450 – 4589Combined sources
Helixi460 – 47617Combined sources
Beta strandi488 – 4958Combined sources
Turni496 – 4983Combined sources
Helixi499 – 5035Combined sources
Helixi505 – 5073Combined sources
Helixi508 – 51710Combined sources
Beta strandi520 – 5223Combined sources
Beta strandi533 – 5419Combined sources
Helixi543 – 56018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KRMX-ray2.75A/B/C404-566[»]
ProteinModelPortaliQ9NZI8.
SMRiQ9NZI8. Positions 1-161, 198-349, 405-562.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZI8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7574RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini81 – 15676RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini195 – 26066KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini276 – 34368KH 2PROSITE-ProRule annotationAdd
BLAST
Domaini405 – 47066KH 3PROSITE-ProRule annotationAdd
BLAST
Domaini487 – 55367KH 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni187 – 570384Necessary for interaction with ELAVL4 and binding to TAU mRNABy similarityAdd
BLAST
Regioni310 – 32415Sufficient for nuclear exportAdd
BLAST
Regioni485 – 49511Sufficient for nuclear exportAdd
BLAST

Domaini

Domain KH3 and KH4 are the major RNA-binding modules, although KH1 and KH2 may also contribute. KH1 and KH2, and possibly KH3 and KH4, promote the formation of higher ordered protein-RNA complexes, which may be essential for IGF2BP1 cytoplasmic retention. KH domains are required for RNA-dependent homo- and heterooligomerization and for localization to stress granules. KH3 and KH4 mediate association with the cytoskeleton. Two nuclear export signals (NES) have been identified in KH2 and KH4 domains, respectively. Only KH2 NES is XPO1-dependent. Both NES may be redundant, since individual in vitro mutations do not affect subcellular location of the full length protein. The 4 KH domains are important to suppress HIV-1 infectivity.1 Publication

Sequence similaritiesi

Belongs to the RRM IMP/VICKZ family.Curated
Contains 4 KH domains.PROSITE-ProRule annotation
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG249985.
GeneTreeiENSGT00530000063171.
HOGENOMiHOG000000675.
HOVERGENiHBG052725.
InParanoidiQ9NZI8.
KOiK17391.
OMAiGSIENCC.
OrthoDBiEOG7T7GSK.
PhylomeDBiQ9NZI8.
TreeFamiTF320229.

Family and domain databases

Gene3Di3.30.1370.10. 4 hits.
3.30.70.330. 2 hits.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00013. KH_1. 4 hits.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 4 hits.
SM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 4 hits.
PROSITEiPS50084. KH_TYPE_1. 4 hits.
PS50102. RRM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NZI8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNKLYIGNLN ESVTPADLEK VFAEHKISYS GQFLVKSGYA FVDCPDEHWA
60 70 80 90 100
MKAIETFSGK VELQGKRLEI EHSVPKKQRS RKIQIRNIPP QLRWEVLDSL
110 120 130 140 150
LAQYGTVENC EQVNTESETA VVNVTYSNRE QTRQAIMKLN GHQLENHALK
160 170 180 190 200
VSYIPDEQIA QGPENGRRGG FGSRGQPRQG SPVAAGAPAK QQQVDIPLRL
210 220 230 240 250
LVPTQYVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA EKAISVHSTP
260 270 280 290 300
EGCSSACKMI LEIMHKEAKD TKTADEVPLK ILAHNNFVGR LIGKEGRNLK
310 320 330 340 350
KVEQDTETKI TISSLQDLTL YNPERTITVK GAIENCCRAE QEIMKKVREA
360 370 380 390 400
YENDVAAMSL QSHLIPGLNL AAVGLFPASS SAVPPPPSSV TGAAPYSSFM
410 420 430 440 450
QAPEQEMVQV FIPAQAVGAI IGKKGQHIKQ LSRFASASIK IAPPETPDSK
460 470 480 490 500
VRMVIITGPP EAQFKAQGRI YGKLKEENFF GPKEEVKLET HIRVPASAAG
510 520 530 540 550
RVIGKGGKTV NELQNLTAAE VVVPRDQTPD ENDQVIVKII GHFYASQMAQ
560 570
RKIRDILAQV KQQHQKGQSN QAQARRK
Length:577
Mass (Da):63,481
Last modified:May 18, 2010 - v2
Checksum:i1D036AE5388D05FA
GO
Isoform 2 (identifier: Q9NZI8-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:438
Mass (Da):48,598
Checksum:i2F615D03F5C00C1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101Missing AA sequence (PubMed:9891060)Curated
Sequence conflicti281 – 2811I → T in AAF37203. 1 PublicationCurated
Sequence conflicti320 – 3201Missing AA sequence (PubMed:9891060)Curated
Sequence conflicti365 – 3651I → T in AAF37203. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei135 – 273139Missing in isoform 2. 1 PublicationVSP_045366Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF198254 mRNA. Translation: AAF37203.1.
DQ227344 mRNA. Translation: ABB46294.1.
AC091133 Genomic DNA. No translation available.
AC105030 Genomic DNA. No translation available.
CCDSiCCDS11543.1. [Q9NZI8-1]
CCDS54138.1. [Q9NZI8-2]
RefSeqiNP_001153895.1. NM_001160423.1. [Q9NZI8-2]
NP_006537.3. NM_006546.3. [Q9NZI8-1]
UniGeneiHs.144936.

Genome annotation databases

EnsembliENST00000290341; ENSP00000290341; ENSG00000159217. [Q9NZI8-1]
ENST00000431824; ENSP00000389135; ENSG00000159217. [Q9NZI8-2]
GeneIDi10642.
KEGGihsa:10642.
UCSCiuc002iom.3. human. [Q9NZI8-1]

Polymorphism databases

DMDMi296434536.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF198254 mRNA. Translation: AAF37203.1 .
DQ227344 mRNA. Translation: ABB46294.1 .
AC091133 Genomic DNA. No translation available.
AC105030 Genomic DNA. No translation available.
CCDSi CCDS11543.1. [Q9NZI8-1 ]
CCDS54138.1. [Q9NZI8-2 ]
RefSeqi NP_001153895.1. NM_001160423.1. [Q9NZI8-2 ]
NP_006537.3. NM_006546.3. [Q9NZI8-1 ]
UniGenei Hs.144936.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3KRM X-ray 2.75 A/B/C 404-566 [» ]
ProteinModelPortali Q9NZI8.
SMRi Q9NZI8. Positions 1-161, 198-349, 405-562.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115886. 56 interactions.
DIPi DIP-38139N.
IntActi Q9NZI8. 25 interactions.
MINTi MINT-4998820.
STRINGi 9606.ENSP00000290341.

PTM databases

PhosphoSitei Q9NZI8.

Polymorphism databases

DMDMi 296434536.

Proteomic databases

MaxQBi Q9NZI8.
PaxDbi Q9NZI8.
PeptideAtlasi Q9NZI8.
PRIDEi Q9NZI8.

Protocols and materials databases

DNASUi 10642.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290341 ; ENSP00000290341 ; ENSG00000159217 . [Q9NZI8-1 ]
ENST00000431824 ; ENSP00000389135 ; ENSG00000159217 . [Q9NZI8-2 ]
GeneIDi 10642.
KEGGi hsa:10642.
UCSCi uc002iom.3. human. [Q9NZI8-1 ]

Organism-specific databases

CTDi 10642.
GeneCardsi GC17P047074.
H-InvDB HIX0013955.
HGNCi HGNC:28866. IGF2BP1.
HPAi HPA021367.
MIMi 608288. gene.
neXtProti NX_Q9NZI8.
PharmGKBi PA143485501.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249985.
GeneTreei ENSGT00530000063171.
HOGENOMi HOG000000675.
HOVERGENi HBG052725.
InParanoidi Q9NZI8.
KOi K17391.
OMAi GSIENCC.
OrthoDBi EOG7T7GSK.
PhylomeDBi Q9NZI8.
TreeFami TF320229.

Enzyme and pathway databases

Reactomei REACT_22166. Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.

Miscellaneous databases

ChiTaRSi IGF2BP1. human.
EvolutionaryTracei Q9NZI8.
GeneWikii IGF2BP1.
GenomeRNAii 10642.
NextBioi 40447.
PROi Q9NZI8.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZI8.
CleanExi HS_IGF2BP1.
HS_ZBP1.
ExpressionAtlasi Q9NZI8. baseline and differential.
Genevestigatori Q9NZI8.

Family and domain databases

Gene3Di 3.30.1370.10. 4 hits.
3.30.70.330. 2 hits.
InterProi IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00013. KH_1. 4 hits.
PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00322. KH. 4 hits.
SM00360. RRM. 2 hits.
[Graphical view ]
SUPFAMi SSF54791. SSF54791. 4 hits.
PROSITEi PS50084. KH_TYPE_1. 4 hits.
PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 213-LYS-GLU-214; 294-LYS-GLU-295 AND 423-LYS-LYS-424.
  10. "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: INTERACTION WITH FMR1, RNA-BINDING, SUBCELLULAR LOCATION.
  11. "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.
  12. 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, INTERACTION WITH PABPC1, RNA-BINDING.
  16. Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  20. "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.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. 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. "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.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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.
  27. "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.
  28. "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.
  29. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling."
    Stohr N., Kohn M., Lederer M., Glass M., Reinke C., Singer R.H., Huttelmaier S.
    Genes Dev. 26:176-189(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION.
  33. "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains."
    Wachter K., Kohn M., Stohr N., Huttelmaier S.
    Biol. Chem. 394:1077-1090(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELAVL1; DHX9 AND HNRNPU.
  34. "Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs): post-transcriptional drivers of cancer progression?"
    Bell J.L., Wachter K., Muhleck B., Pazaitis N., Kohn M., Lederer M., Huttelmaier S.
    Cell. Mol. Life Sci. 70:2657-2675(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  35. "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.

Entry informationi

Entry nameiIF2B1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZI8
Secondary accession number(s): C9JT33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 125 of the entry and version 2 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 17
    Human chromosome 17: 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