P22626 (ROA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear ribonucleoproteins A2/B1
Short name=hnRNP A2/B1

Gene names

Name:	HNRNPA2B1
Synonyms:	HNRPA2B1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Protein existence	Evidence 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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with IGF2BP1. Ref.11 Ref.14
Subcellular location	Nucleus › nucleoplasm. 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
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA transport Inferred from direct assay PubMed 17004321. 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: Compara
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.11. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	RNA binding Inferred from direct assay PubMed 15659580. Source: HGNC nucleotide binding Inferred from electronic annotation. Source: InterPro pre-mRNA intronic binding Inferred from electronic annotation. Source: Compara single-stranded telomeric DNA binding Inferred from direct assay PubMed 15659580. Source: HGNC
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 353

353

Heterogeneous nuclear ribonucleoproteins A2/B1

PRO_0000081836

Regions

Domain

21 – 104

84

RRM 1

Domain

112 – 191

80

RRM 2

Region

308 – 347

40

Nuclear targeting sequence By similarity

Motif

9 – 15

7

Nuclear localization signal Potential

Compositional bias

202 – 353

152

Gly-rich

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.5

Modified residue

85

1

Phosphoserine Ref.19 Ref.21

Modified residue

104

1

N6,N6-dimethyllysine Ref.5

Modified residue

149

1

Phosphoserine Ref.21

Modified residue

168

1

N6-acetyllysine Ref.20

Modified residue

173

1

N6-acetyllysine Ref.20

Modified residue

203

1

Dimethylated arginine; alternate Ref.5 Ref.12

Modified residue

203

1

Omega-N-methylarginine; alternate Ref.5 Ref.12

Modified residue

212

1

Phosphoserine Ref.19 Ref.21 Ref.23

Modified residue

213

1

Dimethylated arginine; alternate Ref.5

Modified residue

213

1

Omega-N-methylarginine; alternate Ref.5

Modified residue

225

1

Phosphoserine Ref.21 Ref.23

Modified residue

231

1

Phosphoserine Ref.21 Ref.23

Modified residue

236

1

Phosphoserine Ref.23

Modified residue

259

1

Phosphoserine Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23

Modified residue

324

1

Phosphoserine Ref.23

Modified residue

331

1

Phosphotyrosine Ref.23

Modified residue

341

1

Phosphoserine Ref.13 Ref.15 Ref.17 Ref.21

Modified residue

344

1

Phosphoserine Ref.17 Ref.19 Ref.21 Ref.23

Natural variations

Alternative sequence

3 – 14

12

Missing in isoform A2.

VSP_005830

Experimental info

Sequence conflict

205

1

G → S in BAF82118. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

353

Helix Strand Turn

Details...

Helix

16 – 20

5

Beta strand

22 – 26

5

Helix

34 – 41

8

Beta strand

48 – 52

5

Turn

56 – 58

3

Beta strand

63 – 68

6

Helix

72 – 79

8

Beta strand

83 – 86

4

Beta strand

89 – 94

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform B1 [UniParc]. Last modified November 1, 1991. Version 2. Checksum: 4C2560A3D8E99D62	FASTA	353	37,430
	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
	Isoform A2 [UniParc]. Checksum: 39E8AB6ED874FA7C	FASTA	341	36,006
	10 20 30 40 50 60 MEREKEQFRK LFIGGLSFET TEESLRNYYE QWGKLTDCVV MRDPASKRSR GFGFVTFSSM 70 80 90 100 110 120 AEVDAAMAAR PHSIDGRVVE PKRAVAREES GKPGAHVTVK KLFVGGIKED TEEHHLRDYF 130 140 150 160 170 180 EEYGKIDTIE IITDRQSGKK RGFGFVTFDD HDPVDKIVLQ KYHTINGHNA EVRKALSRQE 190 200 210 220 230 240 MQEVQSSRSG RGGNFGFGDS RGGGGNFGPG PGSNFRGGSD GYGSGRGFGD GYNGYGGGPG 250 260 270 280 290 300 GGNFGGSPGY GGGRGGYGGG GPGYGNQGGG YGGGYDNYGG GNYGSGNYND FGNYNQQPSN 310 320 330 340 YGPMKSGNFG GSRNMGGPYG GGNYGPGGSG GSGGYGGRSR Y

References

	« Hide 'large scale' referencesShow '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. , 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, 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY.
[19]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"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, MASS SPECTROMETRY.
[21]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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].
[23]	"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, MASS SPECTROMETRY.
[24]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M29064 mRNA. Translation: AAA60271.1.
M29065 mRNA. Translation: AAA36574.1.
U09123 , 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.

IPI

IPI00396378.
IPI00414696.

PIR

B34504. A56845.

RefSeq

NP_002128.1. NM_002137.3.
NP_112533.1. NM_031243.2.

UniGene

Hs.487774.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X4B	NMR	-	A	1-103	[»]

ProteinModelPortal

P22626.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22626. 51 interactions.

MINT

MINT-4998934.

STRING

9606.ENSP00000346694.

PTM databases

PhosphoSite

P22626.

Polymorphism databases

DMDM

133257.

2D gel databases

REPRODUCTION-2DPAGE

IPI00396378.
IPI00414696.
P22626.

SWISS-2DPAGE

P22626.

UCD-2DPAGE

P22626.

Proteomic databases

PaxDb

P22626.

PRIDE

P22626.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354667; ENSP00000346694; ENSG00000122566.
ENST00000356674; ENSP00000349101; ENSG00000122566.
ENST00000360787; ENSP00000354021; ENSG00000122566.

GeneID

3181.

KEGG

hsa:3181.

UCSC

uc003sxr.4. human.
uc003sxs.4. human.

Organism-specific databases

CTD

3181.

GeneCards

GC07M026229.

HGNC

HGNC:5033. HNRNPA2B1.

HPA

CAB012403.
HPA001666.

MIM

600124. gene.

neXtProt

NX_P22626.

PharmGKB

PA162391140.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOGENOM

HOG000234442.

HOVERGEN

HBG002295.

KO

K13158.

OMA

HYSARTS.

OrthoDB

EOG4HQDKF.

PhylomeDB

P22626.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

Bgee

P22626.

CleanEx

HS_HNRNPA2B1.

Genevestigator

P22626.

GermOnline

ENSG00000122566. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HNRNPA2B1. human.

EvolutionaryTrace

P22626.

GenomeRNAi

3181.

NextBio

12622.

PMAP-CutDB

P22626.

SOURCE

Search...

Entry information

Entry name

ROA2_HUMAN

Accession

Primary (citable) accession number: P22626
Secondary accession number(s): A8K064 , P22627, Q9UC98, Q9UDJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 151 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.