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P07910

- HNRPC_HUMAN

UniProt

P07910 - HNRPC_HUMAN

Protein

Heterogeneous nuclear ribonucleoproteins C1/C2

Gene

HNRNPC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 186 (01 Oct 2014)
      Sequence version 4 (13 Jun 2006)
      Previous versions | rss
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    Functioni

    Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.4 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. mRNA 3'-UTR binding Source: UniProt
    3. nucleosomal DNA binding Source: UniProt
    4. nucleotide binding Source: InterPro
    5. poly(A) RNA binding Source: UniProtKB
    6. poly(U) RNA binding Source: UniProt
    7. protein binding Source: UniProtKB
    8. RNA binding Source: HGNC
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: UniProt
    10. RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProt

    GO - Biological processi

    1. 3'-UTR-mediated mRNA stabilization Source: UniProt
    2. ATP-dependent chromatin remodeling Source: UniProt
    3. gene expression Source: Reactome
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. osteoblast differentiation Source: UniProt
    6. RNA splicing Source: Reactome

    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 C1/C2
    Short name:
    hnRNP C1/C2
    Gene namesi
    Name:HNRNPC
    Synonyms:HNRPC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:5035. HNRNPC.

    Subcellular locationi

    Nucleus
    Note: Component of ribonucleosomes.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytosol Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProt
    5. nuclear chromatin Source: UniProt
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProt
    8. protein complex Source: UniProt
    9. spliceosomal complex Source: HGNC

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi197 – 1971K → R: No effect on sumoylation. 1 Publication
    Mutagenesisi250 – 2501K → R: Loss of sumoylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA162391217.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 306305Heterogeneous nuclear ribonucleoproteins C1/C2PRO_0000081844Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei109 – 1091Phosphothreonine1 Publication
    Modified residuei113 – 1131Phosphoserine2 Publications
    Modified residuei115 – 1151Phosphoserine1 Publication
    Modified residuei162 – 1621Phosphoserine2 Publications
    Modified residuei166 – 1661Phosphoserine1 Publication
    Modified residuei176 – 1761N6-acetyllysineBy similarity
    Modified residuei233 – 2331Phosphoserine6 Publications
    Modified residuei241 – 2411Phosphoserine2 Publications
    Cross-linki250 – 250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei253 – 2531Phosphoserine6 Publications
    Modified residuei260 – 2601Phosphoserine8 Publications
    Modified residuei299 – 2991Phosphoserine6 Publications
    Modified residuei306 – 3061Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated on Ser-260 and Ser-299 in resting cells. Phosphorylated on Ser-253 and on 1 serine residue in the poly-Ser stretch at position 238 in response to hydrogen peroxide.11 Publications
    Sumoylated. Sumoylation reduces affinity for mRNA.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP07910.
    PaxDbiP07910.
    PRIDEiP07910.

    2D gel databases

    SWISS-2DPAGEP07910.

    PTM databases

    PhosphoSiteiP07910.

    Expressioni

    Gene expression databases

    ArrayExpressiP07910.
    BgeeiP07910.
    GenevestigatoriP07910.

    Organism-specific databases

    HPAiCAB005223.
    HPA051075.

    Interactioni

    Subunit structurei

    Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise to a 19S complex that interacts with HNRNPA2B1 tetramers. Component of the 40S hnRNP particle. Identified in the spliceosome C complex. Interacts with IGF2BP1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-357966,EBI-357966
    SRPK2P783622EBI-357966,EBI-593303
    YWHAZP631042EBI-357966,EBI-347088

    Protein-protein interaction databases

    BioGridi109424. 134 interactions.
    DIPiDIP-29854N.
    IntActiP07910. 71 interactions.
    MINTiMINT-4999718.

    Structurei

    Secondary structure

    1
    306
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 236
    Turni25 – 273
    Helixi30 – 356
    Beta strandi43 – 497
    Beta strandi51 – 599
    Helixi60 – 689
    Turni69 – 724
    Beta strandi81 – 844
    Helixi194 – 21623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TXPNMR-A/B/C/D194-220[»]
    1WF2NMR-A8-92[»]
    3LN4X-ray1.30C102-117[»]
    ProteinModelPortaliP07910.
    SMRiP07910. Positions 2-92.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07910.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 8772RRMPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili190 – 23849Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi155 – 1617Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi181 – 303123Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the RRM HNRPC family. RALY subfamily.Curated
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG311712.
    HOVERGENiHBG002302.
    InParanoidiP07910.
    KOiK12884.
    OMAiFSSPVEM.
    OrthoDBiEOG7KWSK9.
    PhylomeDBiP07910.
    TreeFamiTF330974.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR017347. hnRNP_C_Raly.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037992. hnRNP-C_Raly. 1 hit.
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform C2 (identifier: P07910-1) [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

    MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK    50
    GFAFVQYVNE RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS 100
    AAEMYGSVTE HPSPSPLLSS SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA 150
    RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR GSSKSGKLKG DDLQAIKKEL 200
    TQIKQKVDSL LENLEKIEKE QSKQAVEMKN DKSEEEQSSS SVKKDETNVK 250
    MESEGGADDS AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA 300
    NGEDDS 306
    Length:306
    Mass (Da):33,670
    Last modified:June 13, 2006 - v4
    Checksum:i17BBC78690C69C5C
    GO
    Isoform C1 (identifier: P07910-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         108-120: Missing.

    Note: Contains a phosphoserine at position 107. Contains a phosphoserine at position 108.

    Show »
    Length:293
    Mass (Da):32,338
    Checksum:iB90DDFD06A77FEE8
    GO
    Isoform 3 (identifier: P07910-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         39-119: KYGKIVGCSV...EHPSPSPLLS → N

    Show »
    Length:226
    Mass (Da):25,230
    Checksum:iBE6EC8C7A9FD7114
    GO
    Isoform 4 (identifier: P07910-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         108-120: Missing.
         153-195: Missing.

    Note: Contains a phosphoserine at position 107. Contains a phosphoserine at position 108.

    Show »
    Length:250
    Mass (Da):27,822
    Checksum:i543388C3EC431836
    GO

    Sequence cautioni

    The sequence BAD92764.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1101E → G in AAH08423. (PubMed:15489334)Curated
    Sequence conflicti217 – 2171I → M(PubMed:2557628)Curated
    Sequence conflicti217 – 2171I → M(PubMed:3110598)Curated
    Sequence conflicti224 – 2241Q → R in AAH08364. (PubMed:15489334)Curated
    Sequence conflicti244 – 2441K → R in AAH08364. (PubMed:15489334)Curated
    Sequence conflicti254 – 2541E → G in AAH07052. (PubMed:15489334)Curated
    Sequence conflicti303 – 3064EDDS → G(PubMed:2557628)Curated
    Sequence conflicti303 – 3064EDDS → G(PubMed:3110598)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671R → Q.
    Corresponds to variant rs3272 [ dbSNP | Ensembl ].
    VAR_052224

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei39 – 11981KYGKI…SPLLS → N in isoform 3. 1 PublicationVSP_019225Add
    BLAST
    Alternative sequencei108 – 12013Missing in isoform C1 and isoform 4. 3 PublicationsVSP_005831Add
    BLAST
    Alternative sequencei153 – 19543Missing in isoform 4. 1 PublicationVSP_019226Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29063 mRNA. Translation: AAA36576.1.
    M16342 mRNA. Translation: AAA52680.1.
    BX161480 mRNA. Translation: CAD61934.1.
    BX247961 mRNA. Translation: CAD62300.1.
    BX247992 mRNA. Translation: CAD62326.1.
    AB209527 mRNA. Translation: BAD92764.1. Different initiation.
    AK223517 mRNA. Translation: BAD97237.1.
    CH471078 Genomic DNA. Translation: EAW66392.1.
    CH471078 Genomic DNA. Translation: EAW66393.1.
    CH471078 Genomic DNA. Translation: EAW66394.1.
    CH471078 Genomic DNA. Translation: EAW66395.1.
    CH471078 Genomic DNA. Translation: EAW66396.1.
    CH471078 Genomic DNA. Translation: EAW66399.1.
    CH471078 Genomic DNA. Translation: EAW66400.1.
    BC003394 mRNA. Translation: AAH03394.1.
    BC007052 mRNA. Translation: AAH07052.1.
    BC008364 mRNA. Translation: AAH08364.1.
    BC008423 mRNA. Translation: AAH08423.1.
    BC066932 mRNA. Translation: AAH66932.1.
    BC089438 mRNA. Translation: AAH89438.1.
    BC108658 mRNA. Translation: AAI08659.1.
    BC103758 mRNA. Translation: AAI03759.1.
    CCDSiCCDS41915.1. [P07910-1]
    CCDS45079.1. [P07910-2]
    PIRiA26885.
    C34504.
    RefSeqiNP_001070910.1. NM_001077442.1. [P07910-1]
    NP_001070911.1. NM_001077443.1. [P07910-2]
    NP_004491.2. NM_004500.3. [P07910-2]
    NP_112604.2. NM_031314.2. [P07910-1]
    XP_006720188.1. XM_006720125.1. [P07910-2]
    XP_006720189.1. XM_006720126.1. [P07910-2]
    UniGeneiHs.508848.
    Hs.675546.

    Genome annotation databases

    EnsembliENST00000420743; ENSP00000404848; ENSG00000092199. [P07910-1]
    ENST00000430246; ENSP00000442816; ENSG00000092199. [P07910-2]
    ENST00000449098; ENSP00000404559; ENSG00000092199. [P07910-2]
    ENST00000553300; ENSP00000450544; ENSG00000092199. [P07910-2]
    ENST00000554455; ENSP00000451291; ENSG00000092199. [P07910-1]
    ENST00000554969; ENSP00000450725; ENSG00000092199. [P07910-2]
    ENST00000555883; ENSP00000450629; ENSG00000092199. [P07910-4]
    ENST00000556628; ENSP00000451652; ENSG00000092199. [P07910-3]
    ENST00000556897; ENSP00000451176; ENSG00000092199. [P07910-2]
    ENST00000557201; ENSP00000452276; ENSG00000092199. [P07910-1]
    GeneIDi3183.
    KEGGihsa:3183.
    UCSCiuc001vzw.3. human. [P07910-2]
    uc001vzy.3. human. [P07910-1]
    uc001wac.3. human. [P07910-4]
    uc001wad.3. human. [P07910-3]

    Polymorphism databases

    DMDMi108935845.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29063 mRNA. Translation: AAA36576.1 .
    M16342 mRNA. Translation: AAA52680.1 .
    BX161480 mRNA. Translation: CAD61934.1 .
    BX247961 mRNA. Translation: CAD62300.1 .
    BX247992 mRNA. Translation: CAD62326.1 .
    AB209527 mRNA. Translation: BAD92764.1 . Different initiation.
    AK223517 mRNA. Translation: BAD97237.1 .
    CH471078 Genomic DNA. Translation: EAW66392.1 .
    CH471078 Genomic DNA. Translation: EAW66393.1 .
    CH471078 Genomic DNA. Translation: EAW66394.1 .
    CH471078 Genomic DNA. Translation: EAW66395.1 .
    CH471078 Genomic DNA. Translation: EAW66396.1 .
    CH471078 Genomic DNA. Translation: EAW66399.1 .
    CH471078 Genomic DNA. Translation: EAW66400.1 .
    BC003394 mRNA. Translation: AAH03394.1 .
    BC007052 mRNA. Translation: AAH07052.1 .
    BC008364 mRNA. Translation: AAH08364.1 .
    BC008423 mRNA. Translation: AAH08423.1 .
    BC066932 mRNA. Translation: AAH66932.1 .
    BC089438 mRNA. Translation: AAH89438.1 .
    BC108658 mRNA. Translation: AAI08659.1 .
    BC103758 mRNA. Translation: AAI03759.1 .
    CCDSi CCDS41915.1. [P07910-1 ]
    CCDS45079.1. [P07910-2 ]
    PIRi A26885.
    C34504.
    RefSeqi NP_001070910.1. NM_001077442.1. [P07910-1 ]
    NP_001070911.1. NM_001077443.1. [P07910-2 ]
    NP_004491.2. NM_004500.3. [P07910-2 ]
    NP_112604.2. NM_031314.2. [P07910-1 ]
    XP_006720188.1. XM_006720125.1. [P07910-2 ]
    XP_006720189.1. XM_006720126.1. [P07910-2 ]
    UniGenei Hs.508848.
    Hs.675546.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TXP NMR - A/B/C/D 194-220 [» ]
    1WF2 NMR - A 8-92 [» ]
    3LN4 X-ray 1.30 C 102-117 [» ]
    ProteinModelPortali P07910.
    SMRi P07910. Positions 2-92.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109424. 134 interactions.
    DIPi DIP-29854N.
    IntActi P07910. 71 interactions.
    MINTi MINT-4999718.

    Chemistry

    ChEMBLi CHEMBL2216742.

    PTM databases

    PhosphoSitei P07910.

    Polymorphism databases

    DMDMi 108935845.

    2D gel databases

    SWISS-2DPAGE P07910.

    Proteomic databases

    MaxQBi P07910.
    PaxDbi P07910.
    PRIDEi P07910.

    Protocols and materials databases

    DNASUi 3183.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000420743 ; ENSP00000404848 ; ENSG00000092199 . [P07910-1 ]
    ENST00000430246 ; ENSP00000442816 ; ENSG00000092199 . [P07910-2 ]
    ENST00000449098 ; ENSP00000404559 ; ENSG00000092199 . [P07910-2 ]
    ENST00000553300 ; ENSP00000450544 ; ENSG00000092199 . [P07910-2 ]
    ENST00000554455 ; ENSP00000451291 ; ENSG00000092199 . [P07910-1 ]
    ENST00000554969 ; ENSP00000450725 ; ENSG00000092199 . [P07910-2 ]
    ENST00000555883 ; ENSP00000450629 ; ENSG00000092199 . [P07910-4 ]
    ENST00000556628 ; ENSP00000451652 ; ENSG00000092199 . [P07910-3 ]
    ENST00000556897 ; ENSP00000451176 ; ENSG00000092199 . [P07910-2 ]
    ENST00000557201 ; ENSP00000452276 ; ENSG00000092199 . [P07910-1 ]
    GeneIDi 3183.
    KEGGi hsa:3183.
    UCSCi uc001vzw.3. human. [P07910-2 ]
    uc001vzy.3. human. [P07910-1 ]
    uc001wac.3. human. [P07910-4 ]
    uc001wad.3. human. [P07910-3 ]

    Organism-specific databases

    CTDi 3183.
    GeneCardsi GC14M021677.
    HGNCi HGNC:5035. HNRNPC.
    HPAi CAB005223.
    HPA051075.
    MIMi 164020. gene.
    neXtProti NX_P07910.
    PharmGKBi PA162391217.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG311712.
    HOVERGENi HBG002302.
    InParanoidi P07910.
    KOi K12884.
    OMAi FSSPVEM.
    OrthoDBi EOG7KWSK9.
    PhylomeDBi P07910.
    TreeFami TF330974.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi HNRNPC. human.
    EvolutionaryTracei P07910.
    GeneWikii HNRNPC.
    GenomeRNAii 3183.
    NextBioi 12634.
    PROi P07910.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07910.
    Bgeei P07910.
    Genevestigatori P07910.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR017347. hnRNP_C_Raly.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037992. hnRNP-C_Raly. 1 hit.
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [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] (ISOFORM C2).
    2. "Primary structure of human nuclear ribonucleoprotein particle C proteins: conservation of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins."
      Swanson M.S., Nakagawa T.Y., Levan K., Dreyfuss G.
      Mol. Cell. Biol. 7:1731-1739(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C1).
    3. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1 AND 3).
      Tissue: Neuroblastoma and Placenta.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C2).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 C1; C2 AND 4).
      Tissue: Bone marrow, Brain, Chondrosarcoma, Eye and Placenta.
    7. Bienvenut W.V., Matallanas D., Cooper W.N., Calvo F., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 18-39; 43-61; 74-89; 143-151; 188-198 AND 205-216, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma and Mammary carcinoma.
    8. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 18-39; 51-61; 74-89 AND 207-216, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    9. "Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles."
      Merrill B.M., Barnett S.F., Lestourgeon W.M., Williams K.R.
      Nucleic Acids Res. 17:8441-8449(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, CHARACTERIZATION.
    10. "The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein particles."
      Huang M., Rech J.E., Northington S.J., Flicker P.F., Mayeda A., Krainer A.R., LeStourgeon W.M.
      Mol. Cell. Biol. 14:518-533(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    11. "A T to G mutation in the polypyrimidine tract of the second intron of the human beta-globin gene reduces in vitro splicing efficiency: evidence for an increased hnRNP C interaction."
      Sebillon P., Beldjord C., Kaplan J.-C., Brody E., Marie J.
      Nucleic Acids Res. 23:3419-3425(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "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.
    13. "Basal and hydrogen peroxide stimulated sites of phosphorylation in heterogeneous nuclear ribonucleoprotein C1/C2."
      Stone J.R., Maki J.L., Collins T.
      Biochemistry 42:1301-1308(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-253; SER-260 AND SER-299, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner."
      Kim J.H., Paek K.Y., Choi K., Kim T.-D., Hahm B., Kim K.-T., Jang S.K.
      Mol. Cell. Biol. 23:708-720(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "SUMO modification of heterogeneous nuclear ribonucleoproteins."
      Vassileva M.T., Matunis M.J.
      Mol. Cell. Biol. 24:3623-3632(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-197 AND LYS-250, SUMOYLATION AT LYS-250.
    16. "Regulation of urokinase receptor mRNA stability by hnRNP C in lung epithelial cells."
      Shetty S.
      Mol. Cell. Biochem. 272:107-118(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-233; SER-253 AND SER-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    19. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    20. Cited for: INTERACTION WITH IGF2BP1.
    21. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    22. "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-253 AND SER-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-233 AND SER-241, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-108 (ISOFORMS 4 AND C1), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-253; SER-260; SER-299 AND SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109; SER-113; SER-115; SER-233; SER-253 AND SER-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    27. "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-233; SER-260 AND SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-166; SER-233; SER-241; SER-253; SER-260; SER-299 AND SER-306, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 (ISOFORMS 4 AND C1), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "1H, 13C, and 15N NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteins."
      Witteking M., Goerlach M., Friedrichs M., Dreyfuss G., Mueller L.
      Biochemistry 31:6254-6265(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-94.
    32. "Interaction of the RNA-binding domain of the hnRNP C proteins with RNA."
      Goerlach M., Witteking M., Beckman R.A., Mueller L., Dreyfuss G.
      EMBO J. 11:3289-3295(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-94.
    33. "An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: a mechanism for RNA chaperonin activity."
      Shahied L., Braswell E.H., LeStourgeon W.M., Krezel A.M.
      J. Mol. Biol. 305:817-828(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 193-220, SUBUNIT.
    34. "Solution structure of RRM domain in HNRPC protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 8-92.
    35. "Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: implications for biological function."
      Whitson S.R., LeStourgeon W.M., Krezel A.M.
      J. Mol. Biol. 350:319-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 193-220, SUBUNIT.

    Entry informationi

    Entry nameiHNRPC_HUMAN
    AccessioniPrimary (citable) accession number: P07910
    Secondary accession number(s): D3DS19
    , D3DS22, P22628, Q53EX2, Q59FD3, Q5FWE8, Q86SF8, Q86U45, Q96HK7, Q96HM4, Q96IY5, Q9BTS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 186 of the entry and version 4 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 14
      Human chromosome 14: 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