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P52597

- HNRPF_HUMAN

UniProt

P52597 - HNRPF_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein F

Gene

HNRNPF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei16 – 161Interaction with RNA
    Sitei20 – 201Interaction with RNA
    Sitei52 – 521Interaction with RNA
    Sitei75 – 751Interaction with RNA
    Sitei116 – 1161Interaction with RNA
    Sitei120 – 1201Interaction with RNA
    Sitei150 – 1501Interaction with RNA
    Sitei173 – 1731Interaction with RNA
    Sitei294 – 2941Interaction with RNA
    Sitei298 – 2981Interaction with RNA
    Sitei326 – 3261Interaction with RNA
    Sitei349 – 3491Interaction with RNA

    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 RNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA splicing, via spliceosome Source: UniProtKB
    3. regulation of RNA splicing Source: UniProtKB
    4. RNA processing Source: ProtInc
    5. 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 ribonucleoprotein F
    Short name:
    hnRNP F
    Alternative name(s):
    Nucleolin-like protein mcs94-1
    Cleaved into the following chain:
    Gene namesi
    Name:HNRNPF
    Synonyms:HNRPF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:5039. HNRNPF.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. membrane Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201W → A: Loss of RNA-binding. 1 Publication
    Mutagenesisi84 – 841E → A: Loss of RNA-binding. 1 Publication
    Mutagenesisi116 – 1161R → A: Decreases affinity for RNA oligonucleotide 100-fold. 1 Publication
    Mutagenesisi120 – 1201F → A: Little disruption of binding RNA. Decreases affinity for RNA oligonucleotide 100-fold. Abrogates RNA-binding; when associated with A-180. 2 Publications
    Mutagenesisi150 – 1501K → A: No effect on affinity for RNA oligonucleotide. 1 Publication
    Mutagenesisi156 – 1561F → A: Drastically effects folding of RRM2. 1 Publication
    Mutagenesisi173 – 1731K → A: Minimal effect on affinity for RNA oligonucleotide. 1 Publication
    Mutagenesisi178 – 1781H → A: Little disruption of binding RNA. 1 Publication
    Mutagenesisi179 – 1791R → A: Decreases affinity for RNA oligonucleotide 100-fold. 1 Publication
    Mutagenesisi180 – 1801Y → A: Decreases affinity for RNA oligonucleotide 10-fold. Abrogates RNA-binding; when associated with A-120. 2 Publications
    Mutagenesisi182 – 1821E → A: Decreases affinity for RNA oligonucleotide 100-fold. 1 Publication
    Mutagenesisi184 – 1841F → A: Minimal effect on affinity for RNA oligonucleotide. 1 Publication

    Organism-specific databases

    PharmGKBiPA162391271.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 415415Heterogeneous nuclear ribonucleoprotein FPRO_0000367114Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 415414Heterogeneous nuclear ribonucleoprotein F, N-terminally processedPRO_0000081852Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F; alternate3 Publications
    Modified residuei2 – 21N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F, N-terminally processed3 Publications
    Cross-linki72 – 72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei104 – 1041Phosphoserine3 Publications
    Modified residuei161 – 1611Phosphoserine1 Publication
    Modified residuei187 – 1871Phosphoserine1 Publication
    Modified residuei224 – 2241N6-acetyllysine1 Publication

    Post-translational modificationi

    Sumoylated.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP52597.
    PaxDbiP52597.
    PeptideAtlasiP52597.
    PRIDEiP52597.

    2D gel databases

    OGPiP52597.

    PTM databases

    PhosphoSiteiP52597.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously.

    Gene expression databases

    ArrayExpressiP52597.
    BgeeiP52597.
    CleanExiHS_HNRNPF.
    GenevestigatoriP52597.

    Organism-specific databases

    HPAiHPA001359.
    HPA016884.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Interacts with AGO1, AGO2, TBP and TXNL4/DIM1.4 Publications

    Protein-protein interaction databases

    BioGridi109426. 113 interactions.
    DIPiDIP-33145N.
    IntActiP52597. 55 interactions.
    MINTiMINT-1157890.
    STRINGi9606.ENSP00000338477.

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 176
    Helixi24 – 307
    Turni31 – 333
    Beta strandi37 – 404
    Beta strandi43 – 475
    Beta strandi49 – 513
    Beta strandi53 – 608
    Helixi64 – 718
    Turni72 – 743
    Beta strandi75 – 8713
    Helixi90 – 978
    Beta strandi107 – 1093
    Beta strandi112 – 1165
    Helixi124 – 1307
    Turni131 – 1333
    Beta strandi136 – 1427
    Beta strandi147 – 1515
    Beta strandi153 – 1619
    Helixi164 – 1696
    Turni170 – 1734
    Beta strandi175 – 1806
    Beta strandi184 – 1863
    Helixi188 – 1914
    Beta strandi284 – 29411
    Helixi302 – 3098
    Beta strandi315 – 3184
    Beta strandi322 – 3254
    Beta strandi332 – 3343
    Helixi337 – 3448
    Beta strandi351 – 3544
    Beta strandi358 – 3625
    Beta strandi368 – 3714
    Beta strandi377 – 3793

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HGLNMR-A1-102[»]
    2HGMNMR-A103-194[»]
    2HGNNMR-A277-381[»]
    2KFYNMR-A1-102[»]
    2KG0NMR-A103-194[»]
    2KG1NMR-A277-381[»]
    3TFYX-ray2.75D/E/F2-10[»]
    ProteinModelPortaliP52597.
    SMRiP52597. Positions 1-194, 277-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52597.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 8573RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini111 – 18878RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini289 – 36678RRM 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni81 – 866Interaction with RNA
    Regioni179 – 1846Interaction with RNA
    Regioni355 – 3606Interaction with RNA

    Domaini

    The N-terminal RRM domains are responsible for recognizing the G-tract of BCL-X RNA.

    Sequence similaritiesi

    Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG326351.
    HOGENOMiHOG000220896.
    HOVERGENiHBG055557.
    InParanoidiP52597.
    KOiK12898.
    OMAiEFAVQST.
    OrthoDBiEOG7BS4BZ.
    PhylomeDBiP52597.
    TreeFamiTF316157.

    Family and domain databases

    Gene3Di3.30.70.330. 3 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR012996. Znf_CHHC.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    PF08080. zf-RNPHF. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P52597-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMLGPEGGEG FVVKLRGLPW SCSVEDVQNF LSDCTIHDGA AGVHFIYTRE    50
    GRQSGEAFVE LGSEDDVKMA LKKDRESMGH RYIEVFKSHR TEMDWVLKHS 100
    GPNSADSAND GFVRLRGLPF GCTKEEIVQF FSGLEIVPNG ITLPVDPEGK 150
    ITGEAFVQFA SQELAEKALG KHKERIGHRY IEVFKSSQEE VRSYSDPPLK 200
    FMSVQRPGPY DRPGTARRYI GIVKQAGLER MRPGAYSTGY GGYEEYSGLS 250
    DGYGFTTDLF GRDLSYCLSG MYDHRYGDSE FTVQSTTGHC VHMRGLPYKA 300
    TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHEE AVAAMSKDRA 350
    NMQHRYIELF LNSTTGASNG AYSSQVMQGM GVSAAQATYS GLESQSVSGC 400
    YGAGYSGQNS MGGYD 415
    Length:415
    Mass (Da):45,672
    Last modified:January 23, 2007 - v3
    Checksum:iD14E170631FB1F31
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871K → R.1 Publication
    Corresponds to variant rs17851426 [ dbSNP | Ensembl ].
    VAR_027999

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L28010 mRNA. Translation: AAC37584.1.
    AL512654 Genomic DNA. Translation: CAI17066.1.
    AK001364 mRNA. Translation: BAG50896.1.
    CH471160 Genomic DNA. Translation: EAW86595.1.
    BC001432 mRNA. Translation: AAH01432.1.
    BC004254 mRNA. Translation: AAH04254.1.
    BC015580 mRNA. Translation: AAH15580.1.
    BC016736 mRNA. Translation: AAH16736.1.
    BC106008 mRNA. Translation: AAI06009.1.
    CCDSiCCDS7204.1.
    PIRiS43484.
    RefSeqiNP_001091674.1. NM_001098204.1.
    NP_001091675.1. NM_001098205.1.
    NP_001091676.1. NM_001098206.1.
    NP_001091677.1. NM_001098207.1.
    NP_001091678.1. NM_001098208.1.
    NP_004957.1. NM_004966.3.
    UniGeneiHs.712955.
    Hs.808.

    Genome annotation databases

    EnsembliENST00000337970; ENSP00000338477; ENSG00000169813.
    ENST00000356053; ENSP00000348345; ENSG00000169813.
    ENST00000357065; ENSP00000349573; ENSG00000169813.
    ENST00000443950; ENSP00000400433; ENSG00000169813.
    ENST00000544000; ENSP00000438061; ENSG00000169813.
    GeneIDi3185.
    KEGGihsa:3185.
    UCSCiuc001jar.2. human.

    Polymorphism databases

    DMDMi1710628.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L28010 mRNA. Translation: AAC37584.1 .
    AL512654 Genomic DNA. Translation: CAI17066.1 .
    AK001364 mRNA. Translation: BAG50896.1 .
    CH471160 Genomic DNA. Translation: EAW86595.1 .
    BC001432 mRNA. Translation: AAH01432.1 .
    BC004254 mRNA. Translation: AAH04254.1 .
    BC015580 mRNA. Translation: AAH15580.1 .
    BC016736 mRNA. Translation: AAH16736.1 .
    BC106008 mRNA. Translation: AAI06009.1 .
    CCDSi CCDS7204.1.
    PIRi S43484.
    RefSeqi NP_001091674.1. NM_001098204.1.
    NP_001091675.1. NM_001098205.1.
    NP_001091676.1. NM_001098206.1.
    NP_001091677.1. NM_001098207.1.
    NP_001091678.1. NM_001098208.1.
    NP_004957.1. NM_004966.3.
    UniGenei Hs.712955.
    Hs.808.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HGL NMR - A 1-102 [» ]
    2HGM NMR - A 103-194 [» ]
    2HGN NMR - A 277-381 [» ]
    2KFY NMR - A 1-102 [» ]
    2KG0 NMR - A 103-194 [» ]
    2KG1 NMR - A 277-381 [» ]
    3TFY X-ray 2.75 D/E/F 2-10 [» ]
    ProteinModelPortali P52597.
    SMRi P52597. Positions 1-194, 277-381.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109426. 113 interactions.
    DIPi DIP-33145N.
    IntActi P52597. 55 interactions.
    MINTi MINT-1157890.
    STRINGi 9606.ENSP00000338477.

    PTM databases

    PhosphoSitei P52597.

    Polymorphism databases

    DMDMi 1710628.

    2D gel databases

    OGPi P52597.

    Proteomic databases

    MaxQBi P52597.
    PaxDbi P52597.
    PeptideAtlasi P52597.
    PRIDEi P52597.

    Protocols and materials databases

    DNASUi 3185.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337970 ; ENSP00000338477 ; ENSG00000169813 .
    ENST00000356053 ; ENSP00000348345 ; ENSG00000169813 .
    ENST00000357065 ; ENSP00000349573 ; ENSG00000169813 .
    ENST00000443950 ; ENSP00000400433 ; ENSG00000169813 .
    ENST00000544000 ; ENSP00000438061 ; ENSG00000169813 .
    GeneIDi 3185.
    KEGGi hsa:3185.
    UCSCi uc001jar.2. human.

    Organism-specific databases

    CTDi 3185.
    GeneCardsi GC10M043881.
    HGNCi HGNC:5039. HNRNPF.
    HPAi HPA001359.
    HPA016884.
    MIMi 601037. gene.
    neXtProti NX_P52597.
    PharmGKBi PA162391271.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326351.
    HOGENOMi HOG000220896.
    HOVERGENi HBG055557.
    InParanoidi P52597.
    KOi K12898.
    OMAi EFAVQST.
    OrthoDBi EOG7BS4BZ.
    PhylomeDBi P52597.
    TreeFami TF316157.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi HNRNPF. human.
    EvolutionaryTracei P52597.
    GeneWikii HNRPF.
    GenomeRNAii 3185.
    NextBioi 12654.
    PROi P52597.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52597.
    Bgeei P52597.
    CleanExi HS_HNRNPF.
    Genevestigatori P52597.

    Family and domain databases

    Gene3Di 3.30.70.330. 3 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR012996. Znf_CHHC.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    PF08080. zf-RNPHF. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The hnRNP F protein: unique primary structure, nucleic acid-binding properties, and subcellular localization."
      Matunis M.J., Xing J., Dreyfuss G.
      Nucleic Acids Res. 22:1059-1067(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-61; 78-83 AND 128-136.
    2. "Heterogeneous nuclear ribonucleoproteins H, H', and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes."
      Honore B., Rasmussen H.H., Vorum H., Dejgaard K., Liu X., Gromov P., Madsen P., Gesser B., Tommerup N., Celis J.E.
      J. Biol. Chem. 270:28780-28789(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    3. "Identification and characterization of a gene at D10S94 in the MEN2A region."
      McDonald H., Smailus D., Jenkins H., Adams K., Simpson N.E., Goodfellow P.J.
      Genomics 13:344-348(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [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], VARIANT ARG-87.
      Tissue: Bone marrow, Lung, Ovary, Placenta and Uterus.
    8. Bienvenut W.V., Zebisch A., Kolch W.
      Submitted (OCT-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-14; 53-68; 82-87; 99-114; 151-167; 180-185 AND 300-347, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND MET-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma and Colon carcinoma.
    9. "Evidence that Dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for Dim1 interactions with hnRNP F and Npw38/PQBP-1."
      Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., Golemis E.A.
      Gene 257:33-43(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TXNL4.
    10. "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.
    11. "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-72.
    12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
      Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
      EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGO1 AND AGO2.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-104 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA recognition."
      Dominguez C., Allain F.H.
      Nucleic Acids Res. 34:3634-3645(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-102; 103-194 AND 277-381 IN COMPLEX WITH BCL-X RNA, MUTAGENESIS OF PHE-120; PHE-156; HIS-178 AND TYR-180.
    24. "Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs."
      Dominguez C., Fisette J.F., Chabot B., Allain F.H.
      Nat. Struct. Mol. Biol. 17:853-861(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-194 AND 277-381 IN COMPLEXES WITH AGGGAU RNA OLIGONUCLEOTIDE, FUNCTION, MUTAGENESIS OF TRP-20; GLU-84; ARG-116; PHE-120; LYS-150; LYS-173; ARG-179; TYR-180; GLU-182 AND PHE-184.

    Entry informationi

    Entry nameiHNRPF_HUMAN
    AccessioniPrimary (citable) accession number: P52597
    Secondary accession number(s): B3KM84, Q5T0N2, Q96AU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 163 of the entry and version 3 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 10
      Human chromosome 10: 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