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Q9Y6M1 (IF2B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:IGF2BP2
Synonyms:IMP2, VICKZ2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.18

Subunit structure

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. Ref.6 Ref.9 Ref.18

Subcellular location

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. Ref.1 Ref.5 Ref.8 Ref.9 Ref.18

Tissue specificity

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. Ref.1 Ref.8

Domain

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. Ref.13 Ref.18

Miscellaneous

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

Sequence similarities

Belongs to the RRM IMP/VICKZ family.

Contains 4 KH domains.

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

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

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HNRNPDQ14103-44EBI-1024419,EBI-432545

Alternative products

This entry describes 6 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: Q9Y6M1-2)

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: Q9Y6M1-1)

The sequence of this isoform differs from the canonical sequence as follows:
     358-400: Missing.
Isoform 3 (identifier: Q9Y6M1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MMNKLYIGNL...VDYSVSKKLR → MFSCPGHYHVDGFLNPG
Isoform 4 (identifier: Q9Y6M1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MMNKLYIGNL...VDYSVSKKLR → MFSCPGHYHVDGFLNPG
     113-113: Q → QVFAFSL
Isoform 5 (identifier: Q9Y6M1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MMNKLYIGNL...VDYSVSKKLR → MFSCPGHYHVDGFLNPG
     358-400: Missing.
Isoform 6 (identifier: Q9Y6M1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.
Note: Generated by alternative initiation at Met-69.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 599599Insulin-like growth factor 2 mRNA-binding protein 2
PRO_0000244496

Regions

Domain3 – 7674RRM 1
Domain82 – 15776RRM 2
Domain193 – 25866KH 1
Domain274 – 34168KH 2
Domain427 – 49266KH 3
Domain509 – 57567KH 4

Amino acid modifications

Modified residue1621Phosphoserine Ref.10 Ref.15
Modified residue1641Phosphoserine Ref.10 Ref.12 Ref.15

Natural variations

Alternative sequence1 – 8080MMNKL…SKKLR → MFSCPGHYHVDGFLNPG in isoform 3, isoform 4 and isoform 5.
VSP_036550
Alternative sequence1 – 6868Missing in isoform 6.
VSP_043699
Alternative sequence1131Q → QVFAFSL in isoform 4.
VSP_036552
Alternative sequence358 – 40043Missing in isoform 2 and isoform 5.
VSP_036553

Experimental info

Mutagenesis2111K → 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. Ref.18
Mutagenesis2921K → 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. Ref.18
Mutagenesis445 – 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.
Mutagenesis527 – 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.

Secondary structure

.............. 599
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: EA656F8733BBB39A

FASTA59966,121
        10         20         30         40         50         60 
MMNKLYIGNL SPAVTADDLR QLFGDRKLPL AGQVLLKSGY AFVDYPDQNW AIRAIETLSG 

        70         80         90        100        110        120 
KVELHGKIME VDYSVSKKLR SRKIQIRNIP PHLQWEVLDG LLAQYGTVEN VEQVNTDTET 

       130        140        150        160        170        180 
AVVNVTYATR EEAKIAMEKL SGHQFENYSF KISYIPDEEV SSPSPPQRAQ RGDHSSREQG 

       190        200        210        220        230        240 
HAPGGTSQAR QIDFPLRILV PTQFVGAIIG KEGLTIKNIT KQTQSRVDIH RKENSGAAEK 

       250        260        270        280        290        300 
PVTIHATPEG TSEACRMILE IMQKEADETK LAEEIPLKIL AHNGLVGRLI GKEGRNLKKI 

       310        320        330        340        350        360 
EHETGTKITI SSLQDLSIYN PERTITVKGT VEACASAEIE IMKKLREAFE NDMLAVNQQA 

       370        380        390        400        410        420 
NLIPGLNLSA LGIFSTGLSV LSPPAGPRGA PPAAPYHPFT THSGYFSSLY PHHQFGPFPH 

       430        440        450        460        470        480 
HHSYPEQEIV NLFIPTQAVG AIIGKKGAHI KQLARFAGAS IKIAPAEGPD VSERMVIITG 

       490        500        510        520        530        540 
PPEAQFKAQG RIFGKLKEEN FFNPKEEVKL EAHIRVPSST AGRVIGKGGK TVNELQNLTS 

       550        560        570        580        590 
AEVIVPRDQT PDENEEVIVR IIGHFFASQT AQRKIREIVQ QVKQQEQKYP QGVASQRSK 

« Hide

Isoform 2 [UniParc].

Checksum: 1EDEFB100443DDC4
Show »

FASTA55661,842
Isoform 3 [UniParc].

Checksum: 733536C7BDAD8AF5
Show »

FASTA53659,001
Isoform 4 [UniParc].

Checksum: F1D98409DD8AE45D
Show »

FASTA54259,666
Isoform 5 [UniParc].

Checksum: 36BF971E2C4296F7
Show »

FASTA49354,722
Isoform 6 [UniParc].

Checksum: 1F5FD1AC97743530
Show »

FASTA53158,578

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"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: INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
[10]"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: 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]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001007226.1. NM_001007225.1.
NP_006539.3. NM_006548.4.
UniGeneHs.35354.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQHNMR-A2-81[»]
ProteinModelPortalQ9Y6M1.
SMRQ9Y6M1. Positions 2-158, 192-584.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115888. 24 interactions.
IntActQ9Y6M1. 21 interactions.
MINTMINT-6946387.
STRING9606.ENSP00000371634.

PTM databases

PhosphoSiteQ9Y6M1.

Polymorphism databases

DMDM224471831.

Proteomic databases

PaxDbQ9Y6M1.
PRIDEQ9Y6M1.

Protocols and materials databases

DNASU10644.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346192; ENSP00000320204; ENSG00000073792. [Q9Y6M1-1]
ENST00000382199; ENSP00000371634; ENSG00000073792. [Q9Y6M1-2]
ENST00000421047; ENSP00000413787; ENSG00000073792. [Q9Y6M1-4]
GeneID10644.
KEGGhsa:10644.
UCSCuc003fpo.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

CTD10644.
GeneCardsGC03M185361.
HGNCHGNC:28867. IGF2BP2.
HPACAB017126.
HPA035145.
MIM608289. gene.
neXtProtNX_Q9Y6M1.
PharmGKBPA128394577.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249985.
HOGENOMHOG000000675.
HOVERGENHBG052725.
KOK17392.
OrthoDBEOG7T7GSK.
PhylomeDBQ9Y6M1.
TreeFamTF320229.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9Y6M1.
BgeeQ9Y6M1.
CleanExHS_IGF2BP2.
GenevestigatorQ9Y6M1.

Family and domain databases

Gene3D3.30.1370.10. 4 hits.
3.30.70.330. 2 hits.
InterProIPR028743. IGF2BP2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERPTHR10288:SF93. PTHR10288:SF93. 1 hit.
PfamPF00013. KH_1. 4 hits.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00322. KH. 4 hits.
SM00360. RRM. 2 hits.
[Graphical view]
SUPFAMSSF54791. SSF54791. 4 hits.
PROSITEPS50084. KH_TYPE_1. 4 hits.
PS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIGF2BP2. human.
EvolutionaryTraceQ9Y6M1.
GeneWikiIGF2BP2.
GenomeRNAi10644.
NextBio40455.
PROQ9Y6M1.
SOURCESearch...

Entry information

Entry nameIF2B2_HUMAN
AccessionPrimary (citable) accession number: Q9Y6M1
Secondary accession number(s): A0A4Z0 expand/collapse secondary AC list , B3FTN2, B3FTN3, B3FTN4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM