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P09651

- ROA1_HUMAN

UniProt

P09651 - ROA1_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein A1

Gene

HNRNPA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 196 (01 Oct 2014)
      Sequence version 5 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication.1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. alternative mRNA splicing, via spliceosome Source: Ensembl
    2. cell death Source: UniProtKB-KW
    3. gene expression Source: Reactome
    4. mRNA processing Source: ProtInc
    5. mRNA splicing, via spliceosome Source: UniProtKB
    6. mRNA transport Source: UniProtKB-KW
    7. nuclear export Source: HGNC
    8. nuclear import Source: HGNC
    9. RNA export from nucleus Source: HGNC
    10. RNA splicing Source: Reactome
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    Host-virus interaction, mRNA processing, mRNA splicing, mRNA transport, Transport

    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 ribonucleoprotein A1
    Short name:
    hnRNP A1
    Alternative name(s):
    Helix-destabilizing protein
    Single-strand RNA-binding protein
    hnRNP core protein A1
    Cleaved into the following chain:
    Gene namesi
    Name:HNRNPA1
    Synonyms:HNRPA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:5031. HNRNPA1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. In the course of viral infection, colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV-replication dependent manner.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytoplasm Source: HGNC
    3. extracellular vesicular exosome Source: UniProt
    4. intermediate filament cytoskeleton Source: HPA
    5. membrane Source: UniProtKB
    6. nucleoplasm Source: HGNC
    7. nucleus Source: HPA
    8. ribonucleoprotein complex Source: UniProtKB
    9. 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 3 (IBMPFD3) [MIM:615424]: 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 varianti314 – 3141D → V in IBMPFD3. 1 Publication
    VAR_070589
    Amyotrophic lateral sclerosis 20 (ALS20) [MIM:615426]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti314 – 3141D → N in ALS20. 1 Publication
    VAR_070588
    Natural varianti319 – 3191N → S in ALS20. 1 Publication
    VAR_070590

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi326 – 3261G → A: No nuclear import nor export. 1 Publication
    Mutagenesisi327 – 3271P → A: No nuclear import nor export. 1 Publication
    Mutagenesisi334 – 3352GG → LL: Normal nuclear import and export.

    Keywords - Diseasei

    Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi615424. phenotype.
    615426. phenotype.
    Orphaneti803. Amyotrophic lateral sclerosis.
    52430. Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
    PharmGKBiPA162391113.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 372372Heterogeneous nuclear ribonucleoprotein A1PRO_0000424509Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate3 Publications
    Chaini2 – 372371Heterogeneous nuclear ribonucleoprotein A1, N-terminally processedPRO_0000081828Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylserine; in Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed4 Publications
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei3 – 31N6-acetyllysine1 Publication
    Modified residuei4 – 41Phosphoserine2 Publications
    Modified residuei6 – 61Phosphoserine3 Publications
    Cross-linki113 – 113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei192 – 1921Phosphoserine; by MKNK21 Publication
    Modified residuei194 – 1941Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei194 – 1941Dimethylated arginine; alternate1 Publication
    Modified residuei199 – 1991Phosphoserine1 Publication
    Modified residuei206 – 2061Dimethylated arginine; alternate2 Publications
    Modified residuei206 – 2061Omega-N-methylarginine; alternate2 Publications
    Modified residuei225 – 2251Dimethylated arginine; alternate2 Publications
    Modified residuei225 – 2251Omega-N-methylarginine; alternate2 Publications
    Modified residuei350 – 3501N6-acetyllysine1 Publication
    Modified residuei362 – 3621Phosphoserine; by MKNK21 Publication
    Modified residuei363 – 3631Phosphoserine; by MKNK21 Publication
    Modified residuei364 – 3641Phosphoserine; by MKNK21 Publication
    Modified residuei365 – 3651Phosphoserine1 Publication
    Modified residuei368 – 3681Phosphoserine2 Publications

    Post-translational modificationi

    Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine.
    Sumoylated.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP09651.
    PaxDbiP09651.
    PRIDEiP09651.

    2D gel databases

    SWISS-2DPAGEP09651.

    PTM databases

    PhosphoSiteiP09651.

    Expressioni

    Gene expression databases

    ArrayExpressiP09651.
    BgeeiP09651.
    CleanExiHS_HNRNPA1.
    GenevestigatoriP09651.

    Organism-specific databases

    HPAiCAB010894.
    HPA001609.
    HPA001666.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with SEPT6. Interacts with C9orf72. Interacts with HCV NS5B and with the 5'-UTR and 3'-UTR of HCV RNA.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279584EBI-352662,EBI-6904388From a different organism.
    KHDRBS1Q076662EBI-352662,EBI-1364
    SEPT6Q141413EBI-352662,EBI-745901

    Protein-protein interaction databases

    BioGridi109420. 244 interactions.
    DIPiDIP-29338N.
    IntActiP09651. 104 interactions.
    MINTiMINT-1035550.
    STRINGi9606.ENSP00000341826.

    Structurei

    Secondary structure

    1
    372
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 144
    Beta strandi15 – 206
    Helixi27 – 348
    Helixi35 – 373
    Beta strandi40 – 478
    Turni49 – 513
    Beta strandi54 – 6411
    Helixi65 – 739
    Beta strandi76 – 794
    Beta strandi85 – 884
    Helixi94 – 963
    Turni98 – 1014
    Beta strandi105 – 1106
    Turni113 – 1153
    Helixi118 – 1258
    Turni126 – 1283
    Beta strandi131 – 1388
    Turni140 – 1423
    Beta strandi145 – 15511
    Helixi156 – 1649
    Beta strandi168 – 1703
    Beta strandi176 – 1794
    Helixi183 – 1886

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HA1X-ray1.75A1-184[»]
    1L3KX-ray1.10A1-196[»]
    1PGZX-ray2.60A2-196[»]
    1PO6X-ray2.10A8-190[»]
    1U1KX-ray2.00A1-196[»]
    1U1LX-ray2.00A1-196[»]
    1U1MX-ray2.00A1-196[»]
    1U1NX-ray2.10A1-196[»]
    1U1OX-ray2.00A1-196[»]
    1U1PX-ray1.90A1-196[»]
    1U1QX-ray1.80A1-196[»]
    1U1RX-ray1.80A1-196[»]
    1UP1X-ray1.90A3-184[»]
    2H4MX-ray3.05C/D309-357[»]
    2LYVNMR-A2-196[»]
    2UP1X-ray2.10A8-190[»]
    DisProtiDP00324.
    ProteinModelPortaliP09651.
    SMRiP09651. Positions 8-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09651.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 9784RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini105 – 18480RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4 – 9491Globular A domainAdd
    BLAST
    Regioni95 – 18591Globular B domainAdd
    BLAST
    Regioni218 – 24023RNA-binding RGG-boxAdd
    BLAST
    Regioni320 – 35738Nuclear targeting sequence (M9)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi195 – 372178Gly-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000234442.
    HOVERGENiHBG002295.
    InParanoidiP09651.
    KOiK12741.
    OMAiKIVNIVQ.
    OrthoDBiEOG715Q6V.
    PhylomeDBiP09651.
    TreeFamiTF314808.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform A1-B (identifier: P09651-1) [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

    MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN    50
    TKRSRGFGFV TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA 100
    HLTVKKIFVG GIKEDTEEHH LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF 150
    VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA LSKQEMASAS SSQRGRSGSG 200
    NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS GDGYNGFGND 250
    GGYGGGGPGY SGGSRGYGSG GQGYGNQGSG YGGSGSYDSY NNGGGGGFGG 300
    GSGSNFGGGG SYNDFGNYNN QSSNFGPMKG GNFGGRSSGP YGGGGQYFAK 350
    PRNQGGYGGS SSSSSYGSGR RF 372
    Length:372
    Mass (Da):38,747
    Last modified:February 9, 2010 - v5
    Checksum:iA06683571C6C109F
    GO
    Isoform A1-A (identifier: P09651-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         252-303: Missing.

    Note: Is twenty times more abundant than isoform A1-B.

    Show »
    Length:320
    Mass (Da):34,196
    Checksum:i59485C9FA1FF8AE1
    GO
    Isoform 2 (identifier: P09651-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         203-307: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:267
    Mass (Da):29,386
    Checksum:i2B492EF73FD41977
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281Y → F in CAA29922. (PubMed:2836799)Curated
    Sequence conflicti140 – 1401R → P in CAA27874. (PubMed:3023065)Curated
    Sequence conflicti146 – 1461R → K in CAA29922. (PubMed:2836799)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti73 – 731N → S.
    Corresponds to variant rs6533 [ dbSNP | Ensembl ].
    VAR_014711
    Natural varianti314 – 3141D → N in ALS20. 1 Publication
    VAR_070588
    Natural varianti314 – 3141D → V in IBMPFD3. 1 Publication
    VAR_070589
    Natural varianti319 – 3191N → S in ALS20. 1 Publication
    VAR_070590

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei203 – 307105Missing in isoform 2. 1 PublicationVSP_034076Add
    BLAST
    Alternative sequencei252 – 30352Missing in isoform A1-A. 4 PublicationsVSP_005824Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12671 Genomic DNA. Translation: CAA31191.1.
    X06747 mRNA. Translation: CAA29922.1.
    X79536 mRNA. Translation: CAA56072.1.
    AK291113 mRNA. Translation: BAF83802.1.
    AC078778 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96761.1.
    BC002355 mRNA. Translation: AAH02355.1.
    BC009600 mRNA. Translation: AAH09600.1.
    BC012158 mRNA. Translation: AAH12158.1.
    BC033714 mRNA. Translation: AAH33714.1.
    BC052296 mRNA. Translation: AAH52296.1.
    BC070315 mRNA. Translation: AAH70315.1.
    BC074502 mRNA. Translation: AAH74502.1.
    BC103707 mRNA. Translation: AAI03708.1.
    X04347 mRNA. Translation: CAA27874.1.
    CCDSiCCDS41793.1. [P09651-2]
    CCDS44909.1. [P09651-1]
    PIRiS02061.
    S12520.
    RefSeqiNP_002127.1. NM_002136.2. [P09651-2]
    NP_112420.1. NM_031157.2. [P09651-1]
    XP_005268883.1. XM_005268826.1. [P09651-1]
    UniGeneiHs.546261.
    Hs.655424.

    Genome annotation databases

    EnsembliENST00000340913; ENSP00000341826; ENSG00000135486. [P09651-1]
    ENST00000546500; ENSP00000448617; ENSG00000135486. [P09651-2]
    ENST00000547276; ENSP00000447260; ENSG00000135486. [P09651-3]
    ENST00000547566; ENSP00000449913; ENSG00000135486. [P09651-2]
    GeneIDi3178.
    KEGGihsa:3178.
    UCSCiuc001sfl.3. human. [P09651-1]
    uc001sfm.3. human. [P09651-2]
    uc001sfn.3. human. [P09651-3]

    Polymorphism databases

    DMDMi288558857.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12671 Genomic DNA. Translation: CAA31191.1 .
    X06747 mRNA. Translation: CAA29922.1 .
    X79536 mRNA. Translation: CAA56072.1 .
    AK291113 mRNA. Translation: BAF83802.1 .
    AC078778 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96761.1 .
    BC002355 mRNA. Translation: AAH02355.1 .
    BC009600 mRNA. Translation: AAH09600.1 .
    BC012158 mRNA. Translation: AAH12158.1 .
    BC033714 mRNA. Translation: AAH33714.1 .
    BC052296 mRNA. Translation: AAH52296.1 .
    BC070315 mRNA. Translation: AAH70315.1 .
    BC074502 mRNA. Translation: AAH74502.1 .
    BC103707 mRNA. Translation: AAI03708.1 .
    X04347 mRNA. Translation: CAA27874.1 .
    CCDSi CCDS41793.1. [P09651-2 ]
    CCDS44909.1. [P09651-1 ]
    PIRi S02061.
    S12520.
    RefSeqi NP_002127.1. NM_002136.2. [P09651-2 ]
    NP_112420.1. NM_031157.2. [P09651-1 ]
    XP_005268883.1. XM_005268826.1. [P09651-1 ]
    UniGenei Hs.546261.
    Hs.655424.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HA1 X-ray 1.75 A 1-184 [» ]
    1L3K X-ray 1.10 A 1-196 [» ]
    1PGZ X-ray 2.60 A 2-196 [» ]
    1PO6 X-ray 2.10 A 8-190 [» ]
    1U1K X-ray 2.00 A 1-196 [» ]
    1U1L X-ray 2.00 A 1-196 [» ]
    1U1M X-ray 2.00 A 1-196 [» ]
    1U1N X-ray 2.10 A 1-196 [» ]
    1U1O X-ray 2.00 A 1-196 [» ]
    1U1P X-ray 1.90 A 1-196 [» ]
    1U1Q X-ray 1.80 A 1-196 [» ]
    1U1R X-ray 1.80 A 1-196 [» ]
    1UP1 X-ray 1.90 A 3-184 [» ]
    2H4M X-ray 3.05 C/D 309-357 [» ]
    2LYV NMR - A 2-196 [» ]
    2UP1 X-ray 2.10 A 8-190 [» ]
    DisProti DP00324.
    ProteinModelPortali P09651.
    SMRi P09651. Positions 8-190.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109420. 244 interactions.
    DIPi DIP-29338N.
    IntActi P09651. 104 interactions.
    MINTi MINT-1035550.
    STRINGi 9606.ENSP00000341826.

    Chemistry

    BindingDBi P09651.
    ChEMBLi CHEMBL1955709.

    PTM databases

    PhosphoSitei P09651.

    Polymorphism databases

    DMDMi 288558857.

    2D gel databases

    SWISS-2DPAGE P09651.

    Proteomic databases

    MaxQBi P09651.
    PaxDbi P09651.
    PRIDEi P09651.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340913 ; ENSP00000341826 ; ENSG00000135486 . [P09651-1 ]
    ENST00000546500 ; ENSP00000448617 ; ENSG00000135486 . [P09651-2 ]
    ENST00000547276 ; ENSP00000447260 ; ENSG00000135486 . [P09651-3 ]
    ENST00000547566 ; ENSP00000449913 ; ENSG00000135486 . [P09651-2 ]
    GeneIDi 3178.
    KEGGi hsa:3178.
    UCSCi uc001sfl.3. human. [P09651-1 ]
    uc001sfm.3. human. [P09651-2 ]
    uc001sfn.3. human. [P09651-3 ]

    Organism-specific databases

    CTDi 3178.
    GeneCardsi GC12P054674.
    H-InvDB HIX0032087.
    HIX0040127.
    HIX0202582.
    HGNCi HGNC:5031. HNRNPA1.
    HPAi CAB010894.
    HPA001609.
    HPA001666.
    MIMi 164017. gene.
    615424. phenotype.
    615426. phenotype.
    neXtProti NX_P09651.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    52430. Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
    PharmGKBi PA162391113.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000234442.
    HOVERGENi HBG002295.
    InParanoidi P09651.
    KOi K12741.
    OMAi KIVNIVQ.
    OrthoDBi EOG715Q6V.
    PhylomeDBi P09651.
    TreeFami TF314808.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi HNRNPA1. human.
    EvolutionaryTracei P09651.
    GeneWikii Heterogeneous_nuclear_ribonucleoprotein_A1.
    GenomeRNAii 3178.
    NextBioi 12614.
    PROi P09651.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09651.
    Bgeei P09651.
    CleanExi HS_HNRNPA1.
    Genevestigatori P09651.

    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. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of an active gene encoding human hnRNP protein A1. Evidence for alternative splicing."
      Biamonti G., Buvoli M., Bassi M.T., Morandi C., Cobianchi F., Riva S.
      J. Mol. Biol. 207:491-503(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A1-A).
      Tissue: Liver.
    2. "cDNA cloning of human hnRNP protein A1 reveals the existence of multiple mRNA isoforms."
      Buvoli M., Biamonti G., Ghetti A., Riva S., Bassi M.T., Horandi C.
      Nucleic Acids Res. 16:3751-3770(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1-A).
      Tissue: Fibroblast.
    3. Knudsen S.M., Leffers H.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1-A).
      Tissue: Lung.
    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 A1-A).
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS A1-A AND 2).
      Tissue: Bone marrow, Cervix, Eye, Kidney, Liver, Lung and Lymph.
    8. "Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1."
      Riva S., Morandi C., Tsoulfas P., Pandolfo M., Biamonti G., Merrill B., Williams K.R., Multhaup G., Beyreuther K., Werr H., Heinrich B., Schaefer K.P.
      EMBO J. 5:2267-2273(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    9. Cited for: PROTEIN SEQUENCE OF 2-47; 56-78; 93-140; 146-178; 197-232 AND 337-370, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-206 AND ARG-225, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma and Ovarian carcinoma.
    10. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 15-47; 147-161 AND 353-370, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    11. "Alternative splicing in the human gene for the core protein A1 generates another hnRNP protein."
      Buvoli M., Cobianchi F., Bestagno M.G., Mangiarotti A., Bassi M.T., Biamonti G., Riva S.
      EMBO J. 9:1229-1235(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 252-303 (ISOFORM A1-B).
    12. "A nuclear localization domain in the hnRNP A1 protein."
      Siomi H., Dreyfuss G.
      J. Cell Biol. 129:551-560(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF GLY-326; PRO-327 AND 334-GLY-GLY-335.
    13. "A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway."
      Michael W.M., Choi M., Dreyfuss G.
      Cell 83:415-422(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR LOCALIZATION SIGNAL, NUCLEAR EXPORT.
    14. "Nucleo-cytoplasmic distribution of human hnRNP proteins: a search for the targeting domains in hnRNP A1."
      Weighardt F., Biamonti G., Riva S.
      J. Cell Sci. 108:545-555(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR LOCALIZATION SIGNAL.
    15. "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.
    16. "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-194; ARG-206 AND ARG-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis."
      Li T., Evdokimov E., Shen R.F., Chao C.C., Tekle E., Wang T., Stadtman E.R., Yang D.C., Chock P.B.
      Proc. Natl. Acad. Sci. U.S.A. 101:8551-8556(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-113.
    18. "The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1."
      Buxade M., Parra J.L., Rousseau S., Shpiro N., Marquez R., Morrice N., Bain J., Espel E., Proud C.G.
      Immunity 23:177-189(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-192; SER-362; SER-363 AND SER-364 BY MKNK2.
    19. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication."
      Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.
      J. Virol. 81:3852-3865(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPT6 AND HCV NS5B, FUNCTION, SUBCELLULAR LOCATION.
    22. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    23. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "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].
    26. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    27. "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 SER-2; LYS-3 AND LYS-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4 AND SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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-4; SER-6; SER-199; SER-365 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "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.
    33. "Modeling by homology of RNA binding domain in A1 hnRNP protein."
      Ghetti A., Bolognesi M., Cobianchi F., Morandi C.
      FEBS Lett. 277:272-276(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 107-190.
    34. "Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75-A resolution."
      Shamoo Y., Krueger U., Rice L.M., Williams K.R., Steitz T.A.
      Nat. Struct. Biol. 4:215-222(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 9-181.
    35. "Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs."
      Xu R.M., Jokhan L., Cheng X., Mayeda A., Krainer A.R.
      Structure 5:559-570(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-182.
    36. Cited for: VARIANT IBMPFD3 VAL-314, VARIANTS ALS20 ASN-314 AND SER-319.

    Entry informationi

    Entry nameiROA1_HUMAN
    AccessioniPrimary (citable) accession number: P09651
    Secondary accession number(s): A8K4Z8, Q3MIB7, Q6PJZ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 196 of the entry and version 5 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 12
      Human chromosome 12: 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