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P22626 (ROA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Heterogeneous nuclear ribonucleoproteins A2/B1

Short name=hnRNP A2/B1
Gene names
Name:HNRNPA2B1
Synonyms:HNRPA2B1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus.

Subunit structure

Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1. Ref.11 Ref.14

Subcellular location

Nucleusnucleoplasm. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Predominantly nucleoplasmic, however isoform A2 is also found in the cytoplasm of cells in some tissues. Not found in the nucleolus. Ref.14

Involvement in disease

Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 2 (IBMPFD2) [MIM:615422]: An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.27

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainRepeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement. Source: Reactome

RNA transport

Inferred from direct assay PubMed 17004321. Source: HGNC

gene expression

Traceable author statement. Source: Reactome

mRNA processing

Inferred from direct assay Ref.1. Source: HGNC

mRNA splicing, via spliceosome

Inferred by curator Ref.11. Source: UniProtKB

negative regulation of mRNA splicing, via spliceosome

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.11. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

ribonucleoprotein complex

Inferred from direct assay Ref.14. Source: UniProtKB

spliceosomal complex

Inferred from direct assay PubMed 9731529. Source: HGNC

   Molecular_functionRNA binding

Inferred from direct assay PubMed 15659580. Source: HGNC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

pre-mRNA intronic binding

Inferred from electronic annotation. Source: Ensembl

single-stranded telomeric DNA binding

Inferred from direct assay PubMed 15659580. Source: HGNC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZMAT3Q9HA383EBI-299649,EBI-2548480

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B1 (identifier: P22626-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A2 (identifier: P22626-2)

The sequence of this isoform differs from the canonical sequence as follows:
     3-14: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 353353Heterogeneous nuclear ribonucleoproteins A2/B1
PRO_0000081836

Regions

Domain21 – 10484RRM 1
Domain112 – 19180RRM 2
Region308 – 34740Nuclear targeting sequence By similarity
Motif9 – 157Nuclear localization signal Potential
Compositional bias202 – 353152Gly-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5 Ref.25
Modified residue851Phosphoserine Ref.20 Ref.22
Modified residue1041N6,N6-dimethyllysine Ref.5
Modified residue1491Phosphoserine Ref.22
Modified residue1681N6-acetyllysine Ref.21
Modified residue1731N6-acetyllysine Ref.21
Modified residue2031Dimethylated arginine; alternate Ref.5 Ref.12
Modified residue2031Omega-N-methylarginine; alternate Ref.5 Ref.12
Modified residue2121Phosphoserine Ref.20 Ref.22 Ref.24
Modified residue2131Dimethylated arginine; alternate Ref.5
Modified residue2131Omega-N-methylarginine; alternate Ref.5
Modified residue2251Phosphoserine Ref.22 Ref.24
Modified residue2311Phosphoserine Ref.22 Ref.24
Modified residue2361Phosphoserine Ref.24
Modified residue2591Phosphoserine Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.24
Modified residue3241Phosphoserine Ref.24
Modified residue3311Phosphotyrosine Ref.24
Modified residue3411Phosphoserine Ref.13 Ref.15 Ref.17 Ref.22
Modified residue3441Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24

Natural variations

Alternative sequence3 – 1412Missing in isoform A2.
VSP_005830
Natural variant3021D → V in IBMPFD2. Ref.27
VAR_070591

Experimental info

Sequence conflict2051G → S in BAF82118. Ref.4

Secondary structure

................... 353
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform B1 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: 4C2560A3D8E99D62

FASTA35337,430
        10         20         30         40         50         60 
MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC VVMRDPASKR 

        70         80         90        100        110        120 
SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE ESGKPGAHVT VKKLFVGGIK 

       130        140        150        160        170        180 
EDTEEHHLRD YFEEYGKIDT IEIITDRQSG KKRGFGFVTF DDHDPVDKIV LQKYHTINGH 

       190        200        210        220        230        240 
NAEVRKALSR QEMQEVQSSR SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF 

       250        260        270        280        290        300 
GDGYNGYGGG PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGNY 

       310        320        330        340        350 
NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR SRY 

« Hide

Isoform A2 [UniParc].

Checksum: 39E8AB6ED874FA7C
Show »

FASTA34136,006

References

« Hide 'large scale' references
[1]"Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts."
Burd C.G., Swanson M.S., Goerlach M., Dreyfuss G.
Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B1 AND A2).
[2]"Two homologous genes, originated by duplication, encode the human hnRNP proteins A2 and A1."
Biamonti G., Ruggiu M., Saccone S., Della Valle G., Riva S.
Nucleic Acids Res. 22:1996-2002(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]"Structure and expression of the gene (HNRPA2B1) encoding the human hnRNP protein A2/B1."
Kozu T., Henrich B., Schaefer K.P.
Genomics 25:365-371(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B1).
Tissue: Glial tumor.
[5]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W., Dozynkiewicz M., Norman J.C.
Submitted (JUN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-12; 22-59; 63-89; 100-147; 153-185; 201-266 AND 326-350, ACETYLATION AT MET-1, METHYLATION AT LYS-104; ARG-203 AND ARG-213, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[6]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 22-38; 154-168; 174-185; 214-228 AND 326-350, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]"Purification and partial sequencing of the nuclear autoantigen RA33 shows that it is indistinguishable from the A2 protein of the heterogeneous nuclear ribonucleoprotein complex."
Steiner G., Hartmuth K., Skriner K., Maurer-Fogy I., Sinski A., Thalmann E., Hassfeld W., Barta A., Smolen J.S.
J. Clin. Invest. 90:1061-1066(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-46; 154-168; 204-228 AND 267-286.
Tissue: Cervix carcinoma.
[8]"ADP-ribosylation of heterogeneous ribonucleoproteins in HeLa cells."
Prasad S., Walent J., Dritschilo A.
Biochem. Biophys. Res. Commun. 204:772-779(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 80-100.
Tissue: Cervix carcinoma.
[9]"Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins."
Kumar A., Willams K.R., Szer W.
J. Biol. Chem. 261:11266-11273(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 100-107; 121-128 AND 174-180.
[10]"Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes."
Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 11:528-536(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 154-160; 204-212 AND 214-228.
[11]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[12]"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
Ong S.E., Mittler G., Mann M.
Nat. Methods 1:119-126(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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-259; SER-341 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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-85; SER-212; SER-259 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168 AND LYS-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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-85; SER-149; SER-212; SER-225; SER-231; SER-259; SER-341 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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].
[24]"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-212; SER-225; SER-231; SER-236; SER-259; SER-324; TYR-331 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Solution structure of RRM domain in heterogeneous nuclear ribonucleoproteins A2/B1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-103.
[27]"Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS."
Kim H.J., Kim N.C., Wang Y.D., Scarborough E.A., Moore J., Diaz Z., MacLea K.S., Freibaum B., Li S., Molliex A., Kanagaraj A.P., Carter R., Boylan K.B., Wojtas A.M., Rademakers R., Pinkus J.L., Greenberg S.A., Trojanowski J.Q. expand/collapse author list , Traynor B.J., Smith B.N., Topp S., Gkazi A.S., Miller J., Shaw C.E., Kottlors M., Kirschner J., Pestronk A., Li Y.R., Ford A.F., Gitler A.D., Benatar M., King O.D., Kimonis V.E., Ross E.D., Weihl C.C., Shorter J., Taylor J.P.
Nature 495:467-473(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IBMPFD2 VAL-302.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29064 mRNA. Translation: AAA60271.1.
M29065 mRNA. Translation: AAA36574.1.
U09123 expand/collapse EMBL AC list , U09120, U09121, U09122 Genomic DNA. Translation: AAB60650.1.
D28877 Genomic DNA. Translation: BAA06031.1.
D28877 Genomic DNA. Translation: BAA06032.1.
AK289429 mRNA. Translation: BAF82118.1.
PIRB34504. A56845.
RefSeqNP_002128.1. NM_002137.3.
NP_112533.1. NM_031243.2.
XP_005249786.1. XM_005249729.1.
UniGeneHs.487774.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4BNMR-A1-103[»]
ProteinModelPortalP22626.
SMRP22626. Positions 1-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109422. 139 interactions.
DIPDIP-32877N.
IntActP22626. 70 interactions.
MINTMINT-4998934.
STRING9606.ENSP00000346694.

PTM databases

PhosphoSiteP22626.

Polymorphism databases

DMDM133257.

2D gel databases

REPRODUCTION-2DPAGEIPI00396378.
IPI00414696.
P22626.
SWISS-2DPAGEP22626.
UCD-2DPAGEP22626.

Proteomic databases

PaxDbP22626.
PRIDEP22626.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354667; ENSP00000346694; ENSG00000122566. [P22626-1]
ENST00000356674; ENSP00000349101; ENSG00000122566. [P22626-2]
ENST00000360787; ENSP00000354021; ENSG00000122566. [P22626-1]
GeneID3181.
KEGGhsa:3181.
UCSCuc003sxr.4. human. [P22626-1]
uc003sxs.4. human. [P22626-2]

Organism-specific databases

CTD3181.
GeneCardsGC07M026229.
HGNCHGNC:5033. HNRNPA2B1.
HPACAB012403.
HPA001666.
MIM600124. gene.
615422. phenotype.
neXtProtNX_P22626.
Orphanet52430. Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
PharmGKBPA162391140.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000234442.
HOVERGENHBG002295.
KOK13158.
OMAYSARTSP.
OrthoDBEOG715Q6V.
PhylomeDBP22626.
TreeFamTF351342.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

BgeeP22626.
CleanExHS_HNRNPA2B1.
GenevestigatorP22626.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPA2B1. human.
EvolutionaryTraceP22626.
GeneWikiHNRPA2B1.
GenomeRNAi3181.
NextBio12622.
PMAP-CutDBP22626.
PROP22626.
SOURCESearch...

Entry information

Entry nameROA2_HUMAN
AccessionPrimary (citable) accession number: P22626
Secondary accession number(s): A8K064 expand/collapse secondary AC list , P22627, Q9UC98, Q9UDJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 160 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM