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P22626

- ROA2_HUMAN

UniProt

P22626 - ROA2_HUMAN

Protein

Heterogeneous nuclear ribonucleoproteins A2/B1

Gene

HNRNPA2B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. pre-mRNA intronic binding Source: Ensembl
    4. protein binding Source: HGNC
    5. RNA binding Source: HGNC
    6. single-stranded telomeric DNA binding Source: HGNC

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA processing Source: HGNC
    3. mRNA splicing, via spliceosome Source: UniProtKB
    4. negative regulation of mRNA splicing, via spliceosome Source: Ensembl
    5. RNA splicing Source: Reactome
    6. RNA transport Source: HGNC

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heterogeneous nuclear ribonucleoproteins A2/B1
    Short name:
    hnRNP A2/B1
    Gene namesi
    Name:HNRNPA2B1
    Synonyms:HNRPA2B1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:5033. HNRNPA2B1.

    Subcellular locationi

    Nucleusnucleoplasm 1 Publication. Cytoplasm 1 Publication
    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.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProt
    6. ribonucleoprotein complex Source: UniProtKB
    7. spliceosomal complex Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti302 – 3021D → V in IBMPFD2. 1 Publication
    VAR_070591

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615422. phenotype.
    Orphaneti52430. Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
    PharmGKBiPA162391140.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 353353Heterogeneous nuclear ribonucleoproteins A2/B1PRO_0000081836Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei85 – 851Phosphoserine2 Publications
    Modified residuei104 – 1041N6,N6-dimethyllysine1 Publication
    Modified residuei149 – 1491Phosphoserine1 Publication
    Modified residuei168 – 1681N6-acetyllysine1 Publication
    Modified residuei173 – 1731N6-acetyllysine1 Publication
    Modified residuei203 – 2031Dimethylated arginine; alternate2 Publications
    Modified residuei203 – 2031Omega-N-methylarginine; alternate2 Publications
    Modified residuei212 – 2121Phosphoserine3 Publications
    Modified residuei213 – 2131Dimethylated arginine; alternate1 Publication
    Modified residuei213 – 2131Omega-N-methylarginine; alternate1 Publication
    Modified residuei225 – 2251Phosphoserine2 Publications
    Modified residuei231 – 2311Phosphoserine2 Publications
    Modified residuei236 – 2361Phosphoserine1 Publication
    Modified residuei259 – 2591Phosphoserine8 Publications
    Modified residuei324 – 3241Phosphoserine1 Publication
    Modified residuei331 – 3311Phosphotyrosine1 Publication
    Modified residuei341 – 3411Phosphoserine4 Publications
    Modified residuei344 – 3441Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP22626.
    PaxDbiP22626.
    PRIDEiP22626.

    2D gel databases

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

    PTM databases

    PhosphoSiteiP22626.

    Miscellaneous databases

    PMAP-CutDBP22626.

    Expressioni

    Gene expression databases

    BgeeiP22626.
    CleanExiHS_HNRNPA2B1.
    GenevestigatoriP22626.

    Organism-specific databases

    HPAiCAB012403.
    HPA001666.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1. Interacts with C9orf72.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ZMAT3Q9HA383EBI-299649,EBI-2548480

    Protein-protein interaction databases

    BioGridi109422. 137 interactions.
    DIPiDIP-32877N.
    IntActiP22626. 70 interactions.
    MINTiMINT-4998934.
    STRINGi9606.ENSP00000346694.

    Structurei

    Secondary structure

    1
    353
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 205
    Beta strandi22 – 265
    Helixi34 – 418
    Beta strandi48 – 525
    Turni56 – 583
    Beta strandi63 – 686
    Helixi72 – 798
    Beta strandi83 – 864
    Beta strandi89 – 946

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X4BNMR-A1-103[»]
    ProteinModelPortaliP22626.
    SMRiP22626. Positions 1-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22626.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 10484RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini112 – 19180RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni308 – 34740Nuclear targeting sequenceBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 157Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi202 – 353152Gly-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000234442.
    HOVERGENiHBG002295.
    KOiK13158.
    OMAiYSARTSP.
    OrthoDBiEOG715Q6V.
    PhylomeDBiP22626.
    TreeFamiTF351342.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform B1 (identifier: P22626-1) [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

    MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC    50
    VVMRDPASKR SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE 100
    ESGKPGAHVT VKKLFVGGIK EDTEEHHLRD YFEEYGKIDT IEIITDRQSG 150
    KKRGFGFVTF DDHDPVDKIV LQKYHTINGH NAEVRKALSR QEMQEVQSSR 200
    SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF GDGYNGYGGG 250
    PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGNY 300
    NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR 350
    SRY 353
    Length:353
    Mass (Da):37,430
    Last modified:November 1, 1991 - v2
    Checksum:i4C2560A3D8E99D62
    GO
    Isoform A2 (identifier: P22626-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:341
    Mass (Da):36,006
    Checksum:i39E8AB6ED874FA7C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti205 – 2051G → S in BAF82118. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti302 – 3021D → V in IBMPFD2. 1 Publication
    VAR_070591

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei3 – 1412Missing in isoform A2. 1 PublicationVSP_005830Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS43557.1. [P22626-1]
    CCDS5397.1. [P22626-2]
    PIRiA56845. B34504.
    RefSeqiNP_002128.1. NM_002137.3. [P22626-2]
    NP_112533.1. NM_031243.2. [P22626-1]
    XP_005249786.1. XM_005249729.1. [P22626-1]
    UniGeneiHs.487774.

    Genome annotation databases

    EnsembliENST00000354667; ENSP00000346694; ENSG00000122566. [P22626-1]
    ENST00000356674; ENSP00000349101; ENSG00000122566. [P22626-2]
    ENST00000360787; ENSP00000354021; ENSG00000122566. [P22626-1]
    GeneIDi3181.
    KEGGihsa:3181.
    UCSCiuc003sxr.4. human. [P22626-1]
    uc003sxs.4. human. [P22626-2]

    Polymorphism databases

    DMDMi133257.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS43557.1. [P22626-1 ]
    CCDS5397.1. [P22626-2 ]
    PIRi A56845. B34504.
    RefSeqi NP_002128.1. NM_002137.3. [P22626-2 ]
    NP_112533.1. NM_031243.2. [P22626-1 ]
    XP_005249786.1. XM_005249729.1. [P22626-1 ]
    UniGenei Hs.487774.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X4B NMR - A 1-103 [» ]
    ProteinModelPortali P22626.
    SMRi P22626. Positions 1-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109422. 137 interactions.
    DIPi DIP-32877N.
    IntActi P22626. 70 interactions.
    MINTi MINT-4998934.
    STRINGi 9606.ENSP00000346694.

    PTM databases

    PhosphoSitei P22626.

    Polymorphism databases

    DMDMi 133257.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00396378.
    IPI00414696.
    P22626.
    SWISS-2DPAGE P22626.
    UCD-2DPAGE P22626.

    Proteomic databases

    MaxQBi P22626.
    PaxDbi P22626.
    PRIDEi P22626.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354667 ; ENSP00000346694 ; ENSG00000122566 . [P22626-1 ]
    ENST00000356674 ; ENSP00000349101 ; ENSG00000122566 . [P22626-2 ]
    ENST00000360787 ; ENSP00000354021 ; ENSG00000122566 . [P22626-1 ]
    GeneIDi 3181.
    KEGGi hsa:3181.
    UCSCi uc003sxr.4. human. [P22626-1 ]
    uc003sxs.4. human. [P22626-2 ]

    Organism-specific databases

    CTDi 3181.
    GeneCardsi GC07M026229.
    HGNCi HGNC:5033. HNRNPA2B1.
    HPAi CAB012403.
    HPA001666.
    MIMi 600124. gene.
    615422. phenotype.
    neXtProti NX_P22626.
    Orphaneti 52430. Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
    PharmGKBi PA162391140.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000234442.
    HOVERGENi HBG002295.
    KOi K13158.
    OMAi YSARTSP.
    OrthoDBi EOG715Q6V.
    PhylomeDBi P22626.
    TreeFami TF351342.

    Enzyme and pathway databases

    Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi HNRNPA2B1. human.
    EvolutionaryTracei P22626.
    GeneWikii HNRPA2B1.
    GenomeRNAii 3181.
    NextBioi 12622.
    PMAP-CutDB P22626.
    PROi P22626.
    SOURCEi Search...

    Gene expression databases

    Bgeei P22626.
    CleanExi HS_HNRNPA2B1.
    Genevestigatori P22626.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking."
      Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A., Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E., Atkin J.D.
      Hum. Mol. Genet. 23:3579-3595(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH C9ORF72.
    27. "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.
    28. Cited for: VARIANT IBMPFD2 VAL-302.

    Entry informationi

    Entry nameiROA2_HUMAN
    AccessioniPrimary (citable) accession number: P22626
    Secondary accession number(s): A8K064
    , P22627, Q9UC98, Q9UDJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 165 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 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3