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P52597

- HNRPF_HUMAN

UniProt

P52597 - HNRPF_HUMAN

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Protein
Heterogeneous nuclear ribonucleoprotein F
Gene
HNRNPF, HNRPF
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. RNA binding Source: ProtInc
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. single-stranded RNA binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. RNA processing Source: ProtInc
  2. RNA splicing Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA splicing, via spliceosome Source: UniProtKB
  5. regulation of RNA splicing Source: UniProtKB
Complete GO annotation...

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. nucleoplasm Source: Reactome
  3. nucleus Source: ProtInc
Complete GO annotation...

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 F
PRO_0000367114Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 415414Heterogeneous nuclear ribonucleoprotein F, N-terminally processed
PRO_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)1 Publication
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/DIM1.3 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP52597.

Family & Domainsi

Domains and Repeats

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

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 162 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

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