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Protein

Insulin-like growth factor 2 mRNA-binding protein 1

Gene

IGF2BP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • mRNA 3'-UTR binding Source: UniProtKB
  • mRNA 5'-UTR binding Source: BHF-UCL
  • mRNA binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • translation regulator activity Source: BHF-UCL

GO - Biological processi

  • CRD-mediated mRNA stabilization Source: UniProtKB
  • gene expression Source: Reactome
  • mRNA transport Source: UniProtKB-KW
  • negative regulation of translation Source: BHF-UCL
  • neuronal stem cell population maintenance Source: Ensembl
  • pallium cell proliferation in forebrain Source: Ensembl
  • regulation of cytokine biosynthetic process Source: BHF-UCL
  • 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

BioCyciZFISH:ENSG00000159217-MONOMER.
ReactomeiR-HSA-428359. Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.
R-HSA-5687128. MAPK6/MAPK4 signaling.

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
Proteomesi
  • UP000005640 Componenti: 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

  • axon Source: UniProtKB-SubCell
  • CRD-mediated mRNA stability complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic stress granule Source: UniProtKB
  • cytosol Source: Reactome
  • dendritic spine Source: UniProtKB-SubCell
  • filopodium Source: UniProtKB-SubCell
  • growth cone Source: UniProtKB-SubCell
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • lamellipodium Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi213 – 214KE → 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 Publication2
Mutagenesisi294 – 295KE → 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 Publication2
Mutagenesisi423 – 424KK → 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 Publication2

Organism-specific databases

DisGeNETi10642.
OpenTargetsiENSG00000159217.
PharmGKBiPA143485501.

Polymorphism and mutation databases

BioMutaiIGF2BP1.
DMDMi296434536.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002825331 – 577Insulin-like growth factor 2 mRNA-binding protein 1Add BLAST577

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12PhosphoserineCombined sources1
Modified residuei73PhosphoserineCombined sources1
Modified residuei181PhosphoserineCombined sources1
Cross-linki475Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei528PhosphothreonineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NZI8.
MaxQBiQ9NZI8.
PaxDbiQ9NZI8.
PeptideAtlasiQ9NZI8.
PRIDEiQ9NZI8.
TopDownProteomicsiQ9NZI8-1. [Q9NZI8-1]

PTM databases

iPTMnetiQ9NZI8.
PhosphoSitePlusiQ9NZI8.
SwissPalmiQ9NZI8.

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

BgeeiENSG00000159217.
CleanExiHS_IGF2BP1.
HS_ZBP1.
GenevisibleiQ9NZI8. HS.

Organism-specific databases

HPAiHPA021367.
HPA062273.

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. 76 interactors.
DIPiDIP-38139N.
IntActiQ9NZI8. 36 interactors.
MINTiMINT-4998820.
STRINGi9606.ENSP00000290341.

Structurei

Secondary structure

1577
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi406 – 413Combined sources8
Helixi414 – 416Combined sources3
Helixi417 – 421Combined sources5
Helixi423 – 425Combined sources3
Helixi426 – 435Combined sources10
Beta strandi438 – 441Combined sources4
Beta strandi450 – 458Combined sources9
Helixi460 – 476Combined sources17
Beta strandi488 – 495Combined sources8
Turni496 – 498Combined sources3
Helixi499 – 503Combined sources5
Helixi505 – 507Combined sources3
Helixi508 – 517Combined sources10
Beta strandi520 – 522Combined sources3
Beta strandi533 – 541Combined sources9
Helixi543 – 560Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KRMX-ray2.75A/B/C404-566[»]
ProteinModelPortaliQ9NZI8.
SMRiQ9NZI8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZI8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 75RRM 1PROSITE-ProRule annotationAdd BLAST74
Domaini81 – 156RRM 2PROSITE-ProRule annotationAdd BLAST76
Domaini195 – 260KH 1PROSITE-ProRule annotationAdd BLAST66
Domaini276 – 343KH 2PROSITE-ProRule annotationAdd BLAST68
Domaini405 – 470KH 3PROSITE-ProRule annotationAdd BLAST66
Domaini487 – 553KH 4PROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni187 – 570Necessary for interaction with ELAVL4 and binding to TAU mRNABy similarityAdd BLAST384
Regioni310 – 324Sufficient for nuclear exportAdd BLAST15
Regioni485 – 495Sufficient for nuclear exportAdd BLAST11

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

eggNOGiKOG2193. Eukaryota.
ENOG410ZKB4. LUCA.
GeneTreeiENSGT00530000063171.
HOGENOMiHOG000000675.
HOVERGENiHBG052725.
InParanoidiQ9NZI8.
KOiK17391.
OMAiSIENCCK.
OrthoDBiEOG091G17T1.
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. 2 hits.
[Graphical view]
SMARTiSM00322. KH. 4 hits.
SM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 4 hits.
SSF54928. SSF54928. 1 hit.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti10Missing AA sequence (PubMed:9891060).Curated1
Sequence conflicti281I → T in AAF37203 (Ref. 1) Curated1
Sequence conflicti320Missing AA sequence (PubMed:9891060).Curated1
Sequence conflicti365I → T in AAF37203 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_045366135 – 273Missing in isoform 2. 1 PublicationAdd BLAST139

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.4. human. [Q9NZI8-1]

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KRMX-ray2.75A/B/C404-566[»]
ProteinModelPortaliQ9NZI8.
SMRiQ9NZI8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115886. 76 interactors.
DIPiDIP-38139N.
IntActiQ9NZI8. 36 interactors.
MINTiMINT-4998820.
STRINGi9606.ENSP00000290341.

PTM databases

iPTMnetiQ9NZI8.
PhosphoSitePlusiQ9NZI8.
SwissPalmiQ9NZI8.

Polymorphism and mutation databases

BioMutaiIGF2BP1.
DMDMi296434536.

Proteomic databases

EPDiQ9NZI8.
MaxQBiQ9NZI8.
PaxDbiQ9NZI8.
PeptideAtlasiQ9NZI8.
PRIDEiQ9NZI8.
TopDownProteomicsiQ9NZI8-1. [Q9NZI8-1]

Protocols and materials databases

DNASUi10642.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290341; ENSP00000290341; ENSG00000159217. [Q9NZI8-1]
ENST00000431824; ENSP00000389135; ENSG00000159217. [Q9NZI8-2]
GeneIDi10642.
KEGGihsa:10642.
UCSCiuc002iom.4. human. [Q9NZI8-1]

Organism-specific databases

CTDi10642.
DisGeNETi10642.
GeneCardsiIGF2BP1.
H-InvDBHIX0013955.
HGNCiHGNC:28866. IGF2BP1.
HPAiHPA021367.
HPA062273.
MIMi608288. gene.
neXtProtiNX_Q9NZI8.
OpenTargetsiENSG00000159217.
PharmGKBiPA143485501.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2193. Eukaryota.
ENOG410ZKB4. LUCA.
GeneTreeiENSGT00530000063171.
HOGENOMiHOG000000675.
HOVERGENiHBG052725.
InParanoidiQ9NZI8.
KOiK17391.
OMAiSIENCCK.
OrthoDBiEOG091G17T1.
PhylomeDBiQ9NZI8.
TreeFamiTF320229.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000159217-MONOMER.
ReactomeiR-HSA-428359. Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.
R-HSA-5687128. MAPK6/MAPK4 signaling.

Miscellaneous databases

ChiTaRSiIGF2BP1. human.
EvolutionaryTraceiQ9NZI8.
GeneWikiiIGF2BP1.
GenomeRNAii10642.
PROiQ9NZI8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000159217.
CleanExiHS_IGF2BP1.
HS_ZBP1.
GenevisibleiQ9NZI8. HS.

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. 2 hits.
[Graphical view]
SMARTiSM00322. KH. 4 hits.
SM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 4 hits.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 4 hits.
PS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 145 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

Similar proteinsi

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