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Q9Y6M1

- IF2B2_HUMAN

UniProt

Q9Y6M1 - IF2B2_HUMAN

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Protein

Insulin-like growth factor 2 mRNA-binding protein 2

Gene
IGF2BP2, IMP2, VICKZ2
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 By similarity. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. Binds to beta-actin/ACTB and MYC transcripts.2 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  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
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 2
Short name:
IGF2 mRNA-binding protein 2
Short name:
IMP-2
Alternative name(s):
Hepatocellular carcinoma autoantigen p62
IGF-II mRNA-binding protein 2
VICKZ family member 2
Gene namesi
Name:IGF2BP2
Synonyms:IMP2, VICKZ2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:28867. IGF2BP2.

Subcellular locationi

Nucleus. Cytoplasm
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Localizes at the connecting piece and the tail of the spermatozoa. In response to cellular stress, such as oxidative stress, recruited to stress granules.5 Publications

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytoskeleton Source: BHF-UCL
  3. cytosol Source: Reactome
  4. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi211 – 2111K → E: Significantly impaired binding to ACTB transcript, but little effect on MYC transcript binding, accumulation in the nucleus; when associated with E-292. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-292; 445-E-E-446 and 526-E-E-527. 1 Publication
Mutagenesisi292 – 2921K → E: Significantly impaired binding to ACTB transcript, but little effect on MYC transcript binding, accumulation in the nucleus; when associated with E-211. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-211; 445-E-E-445 and 526-E-E-527. 1 Publication
Mutagenesisi445 – 4462KK → EE: Significantly impaired binding to ACTB and MYC transcripts; when associated with 527-E-E-528. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-211; E-292 and 527-E-E-528.
Mutagenesisi527 – 5282KG → EE: Significantly impaired binding to ACTB and MYC transcripts; when associated with 445-E-E-446. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-211; E-292 and 445-E-E-446.

Organism-specific databases

PharmGKBiPA128394577.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 599599Insulin-like growth factor 2 mRNA-binding protein 2PRO_0000244496Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621Phosphoserine2 Publications
Modified residuei164 – 1641Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y6M1.
PaxDbiQ9Y6M1.
PRIDEiQ9Y6M1.

PTM databases

PhosphoSiteiQ9Y6M1.

Expressioni

Tissue specificityi

Expressed in oocytes, granulosa cells of small and growing follicles, Leydig cells, spermatogonia and semen (at protein level). Expressed in testicular cancer (at protein level). Expressed weakly in heart, placenta, skeletal muscle, bone marrow, colon, kidney, salivary glands, testis and pancreas. Detected in fetal liver, fetal ovary, gonocytes and interstitial cells of the testis.2 Publications

Gene expression databases

ArrayExpressiQ9Y6M1.
BgeeiQ9Y6M1.
CleanExiHS_IGF2BP2.
GenevestigatoriQ9Y6M1.

Organism-specific databases

HPAiCAB017126.
HPA035145.

Interactioni

Subunit structurei

Can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. Interacts with HNRPD and IGF2BP1. Interacts with ELAVL1, DHX9 and HNRNPU.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HNRNPDQ14103-44EBI-1024419,EBI-432545

Protein-protein interaction databases

BioGridi115888. 25 interactions.
IntActiQ9Y6M1. 21 interactions.
MINTiMINT-6946387.
STRINGi9606.ENSP00000371634.

Structurei

Secondary structure

1
599
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84
Helixi16 – 2510
Beta strandi34 – 374
Beta strandi40 – 434
Helixi48 – 5811
Turni59 – 613
Beta strandi70 – 734

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQHNMR-A2-81[»]
ProteinModelPortaliQ9Y6M1.
SMRiQ9Y6M1. Positions 2-158, 198-337, 427-584.

Miscellaneous databases

EvolutionaryTraceiQ9Y6M1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7674RRM 1Add
BLAST
Domaini82 – 15776RRM 2Add
BLAST
Domaini193 – 25866KH 1Add
BLAST
Domaini274 – 34168KH 2Add
BLAST
Domaini427 – 49266KH 3Add
BLAST
Domaini509 – 57567KH 4Add
BLAST

Domaini

Domain KH3 and KH4 are the major RNA-binding modules, although KH1 and KH2 may also contribute. The contribution to RNA-binding of individual KH domains may be target-specific. 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.2 Publications

Sequence similaritiesi

Belongs to the RRM IMP/VICKZ family.
Contains 4 KH domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG249985.
HOGENOMiHOG000000675.
HOVERGENiHBG052725.
KOiK17392.
OrthoDBiEOG7T7GSK.
PhylomeDBiQ9Y6M1.
TreeFamiTF320229.

Family and domain databases

Gene3Di3.30.1370.10. 4 hits.
3.30.70.330. 2 hits.
InterProiIPR028743. IGF2BP2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR10288:SF93. PTHR10288:SF93. 1 hit.
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.
PROSITEiPS50084. KH_TYPE_1. 4 hits.
PS50102. RRM. 2 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform 1 (identifier: Q9Y6M1-2) [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

MMNKLYIGNL SPAVTADDLR QLFGDRKLPL AGQVLLKSGY AFVDYPDQNW    50
AIRAIETLSG KVELHGKIME VDYSVSKKLR SRKIQIRNIP PHLQWEVLDG 100
LLAQYGTVEN VEQVNTDTET AVVNVTYATR EEAKIAMEKL SGHQFENYSF 150
KISYIPDEEV SSPSPPQRAQ RGDHSSREQG HAPGGTSQAR QIDFPLRILV 200
PTQFVGAIIG KEGLTIKNIT KQTQSRVDIH RKENSGAAEK PVTIHATPEG 250
TSEACRMILE IMQKEADETK LAEEIPLKIL AHNGLVGRLI GKEGRNLKKI 300
EHETGTKITI SSLQDLSIYN PERTITVKGT VEACASAEIE IMKKLREAFE 350
NDMLAVNQQA NLIPGLNLSA LGIFSTGLSV LSPPAGPRGA PPAAPYHPFT 400
THSGYFSSLY PHHQFGPFPH HHSYPEQEIV NLFIPTQAVG AIIGKKGAHI 450
KQLARFAGAS IKIAPAEGPD VSERMVIITG PPEAQFKAQG RIFGKLKEEN 500
FFNPKEEVKL EAHIRVPSST AGRVIGKGGK TVNELQNLTS AEVIVPRDQT 550
PDENEEVIVR IIGHFFASQT AQRKIREIVQ QVKQQEQKYP QGVASQRSK 599
Length:599
Mass (Da):66,121
Last modified:March 3, 2009 - v2
Checksum:iEA656F8733BBB39A
GO
Isoform 2 (identifier: Q9Y6M1-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     358-400: Missing.

Show »
Length:556
Mass (Da):61,842
Checksum:i1EDEFB100443DDC4
GO
Isoform 3 (identifier: Q9Y6M1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MMNKLYIGNL...VDYSVSKKLR → MFSCPGHYHVDGFLNPG

Show »
Length:536
Mass (Da):59,001
Checksum:i733536C7BDAD8AF5
GO
Isoform 4 (identifier: Q9Y6M1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MMNKLYIGNL...VDYSVSKKLR → MFSCPGHYHVDGFLNPG
     113-113: Q → QVFAFSL

Show »
Length:542
Mass (Da):59,666
Checksum:iF1D98409DD8AE45D
GO
Isoform 5 (identifier: Q9Y6M1-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MMNKLYIGNL...VDYSVSKKLR → MFSCPGHYHVDGFLNPG
     358-400: Missing.

Show »
Length:493
Mass (Da):54,722
Checksum:i36BF971E2C4296F7
GO
Isoform 6 (identifier: Q9Y6M1-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.

Note: Generated by alternative initiation at Met-69.

Show »
Length:531
Mass (Da):58,578
Checksum:i1F5FD1AC97743530
GO

Sequence cautioni

The sequence AAH21290.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8080MMNKL…SKKLR → MFSCPGHYHVDGFLNPG in isoform 3, isoform 4 and isoform 5. VSP_036550Add
BLAST
Alternative sequencei1 – 6868Missing in isoform 6. VSP_043699Add
BLAST
Alternative sequencei113 – 1131Q → QVFAFSL in isoform 4. VSP_036552
Alternative sequencei358 – 40043Missing in isoform 2 and isoform 5. VSP_036553Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF057352 mRNA. Translation: AAD31596.1.
EU408701 mRNA. Translation: ACB86625.1.
EU408702 mRNA. Translation: ACB86626.1.
EU408703 mRNA. Translation: ACB86627.1.
AC016961 Genomic DNA. No translation available.
AC108670 Genomic DNA. No translation available.
BC021290 mRNA. Translation: AAH21290.1. Different initiation.
CCDSiCCDS3273.2. [Q9Y6M1-2]
CCDS33903.1. [Q9Y6M1-1]
RefSeqiNP_001007226.1. NM_001007225.1. [Q9Y6M1-1]
NP_001278798.1. NM_001291869.1.
NP_001278801.1. NM_001291872.1. [Q9Y6M1-4]
NP_001278802.1. NM_001291873.1. [Q9Y6M1-3]
NP_001278803.1. NM_001291874.1. [Q9Y6M1-5]
NP_001278804.1. NM_001291875.1.
NP_006539.3. NM_006548.4. [Q9Y6M1-2]
UniGeneiHs.35354.

Genome annotation databases

EnsembliENST00000346192; ENSP00000320204; ENSG00000073792. [Q9Y6M1-1]
ENST00000382199; ENSP00000371634; ENSG00000073792. [Q9Y6M1-2]
ENST00000421047; ENSP00000413787; ENSG00000073792. [Q9Y6M1-4]
GeneIDi10644.
KEGGihsa:10644.
UCSCiuc003fpo.3. human. [Q9Y6M1-2]
uc003fpp.3. human. [Q9Y6M1-1]
uc010hyi.3. human. [Q9Y6M1-4]
uc010hyj.3. human. [Q9Y6M1-3]
uc010hyl.3. human. [Q9Y6M1-5]

Polymorphism databases

DMDMi224471831.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF057352 mRNA. Translation: AAD31596.1 .
EU408701 mRNA. Translation: ACB86625.1 .
EU408702 mRNA. Translation: ACB86626.1 .
EU408703 mRNA. Translation: ACB86627.1 .
AC016961 Genomic DNA. No translation available.
AC108670 Genomic DNA. No translation available.
BC021290 mRNA. Translation: AAH21290.1 . Different initiation.
CCDSi CCDS3273.2. [Q9Y6M1-2 ]
CCDS33903.1. [Q9Y6M1-1 ]
RefSeqi NP_001007226.1. NM_001007225.1. [Q9Y6M1-1 ]
NP_001278798.1. NM_001291869.1.
NP_001278801.1. NM_001291872.1. [Q9Y6M1-4 ]
NP_001278802.1. NM_001291873.1. [Q9Y6M1-3 ]
NP_001278803.1. NM_001291874.1. [Q9Y6M1-5 ]
NP_001278804.1. NM_001291875.1.
NP_006539.3. NM_006548.4. [Q9Y6M1-2 ]
UniGenei Hs.35354.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CQH NMR - A 2-81 [» ]
ProteinModelPortali Q9Y6M1.
SMRi Q9Y6M1. Positions 2-158, 198-337, 427-584.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115888. 25 interactions.
IntActi Q9Y6M1. 21 interactions.
MINTi MINT-6946387.
STRINGi 9606.ENSP00000371634.

PTM databases

PhosphoSitei Q9Y6M1.

Polymorphism databases

DMDMi 224471831.

Proteomic databases

MaxQBi Q9Y6M1.
PaxDbi Q9Y6M1.
PRIDEi Q9Y6M1.

Protocols and materials databases

DNASUi 10644.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000346192 ; ENSP00000320204 ; ENSG00000073792 . [Q9Y6M1-1 ]
ENST00000382199 ; ENSP00000371634 ; ENSG00000073792 . [Q9Y6M1-2 ]
ENST00000421047 ; ENSP00000413787 ; ENSG00000073792 . [Q9Y6M1-4 ]
GeneIDi 10644.
KEGGi hsa:10644.
UCSCi uc003fpo.3. human. [Q9Y6M1-2 ]
uc003fpp.3. human. [Q9Y6M1-1 ]
uc010hyi.3. human. [Q9Y6M1-4 ]
uc010hyj.3. human. [Q9Y6M1-3 ]
uc010hyl.3. human. [Q9Y6M1-5 ]

Organism-specific databases

CTDi 10644.
GeneCardsi GC03M185361.
HGNCi HGNC:28867. IGF2BP2.
HPAi CAB017126.
HPA035145.
MIMi 608289. gene.
neXtProti NX_Q9Y6M1.
PharmGKBi PA128394577.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249985.
HOGENOMi HOG000000675.
HOVERGENi HBG052725.
KOi K17392.
OrthoDBi EOG7T7GSK.
PhylomeDBi Q9Y6M1.
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 IGF2BP2. human.
EvolutionaryTracei Q9Y6M1.
GeneWikii IGF2BP2.
GenomeRNAii 10644.
NextBioi 40455.
PROi Q9Y6M1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y6M1.
Bgeei Q9Y6M1.
CleanExi HS_IGF2BP2.
Genevestigatori Q9Y6M1.

Family and domain databases

Gene3Di 3.30.1370.10. 4 hits.
3.30.70.330. 2 hits.
InterProi IPR028743. IGF2BP2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
PANTHERi PTHR10288:SF93. PTHR10288:SF93. 1 hit.
Pfami PF00013. KH_1. 4 hits.
PF00076. RRM_1. 2 hits.
[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. "A novel cytoplasmic protein with RNA-binding motifs is an autoantigen in human hepatocellular carcinoma."
    Zhang J.-Y., Chan E.K.L., Peng X.-X., Tan E.M.
    J. Exp. Med. 189:1101-1110(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION AS A HEPATOCELLULAR CARCINOMA ANTIGEN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Colon adenocarcinoma.
  2. "A novel type 2 diabetes-associated variant of IGF2BP2 gene affects expression of a functional alternative splicing form."
    Prokunina-Olsson L., Hanisch J.J., Jackson A., Chines P.S., Erdos M.R., Bonnycastle L.L., Swift A., Narisu N., Scott L.J., Morken M., Mohlke K., Bergman R., Tuomilehto J., Boehnke M., Rotimi C.N., Watanabe R.N., Collins F.S.
    Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
    Tissue: Pancreatic islet.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Pancreas.
  5. "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: FUNCTION, SUBCELLULAR LOCATION.
  6. "Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D)."
    Moraes K.C., Quaresma A.J., Maehnss K., Kobarg J.
    Biol. Chem. 384:25-37(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRPD.
  7. "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.
  8. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. Cited for: INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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: RNA-BINDING, DOMAIN.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-162 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation."
    Le H.T., Sorrell A.M., Siddle K.
    PLoS ONE 7:E33140-E33140(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION (ISOFORM 6).
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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: FUNCTION, RNA-BINDING, OLIGOMERIZATION, INTERACTION WITH ELAVL1; DHX9 AND HNRNPU, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LYS-211; LYS-292; 445-LYS-LYS-446 AND 527-LYS-GLY-528.
  19. "Solution structure of the RNA binding domain of IGF-II mRNA-binding protein 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 2-81.

Entry informationi

Entry nameiIF2B2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6M1
Secondary accession number(s): A0A4Z0
, B3FTN2, B3FTN3, B3FTN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 3, 2009
Last modified: September 3, 2014
This is version 123 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

Miscellaneous

Autoantibodies against IGF2BP2 are detected in sera from some patients with hepatocellular carcinoma.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

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