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Protein

Heterogeneous nuclear ribonucleoprotein F

Gene

HNRNPF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • single-stranded RNA binding Source: UniProtKB

GO - Biological processi

  • fibroblast growth factor receptor signaling pathway Source: Reactome
  • gene expression Source: Reactome
  • mRNA splicing, via spliceosome Source: UniProtKB
  • regulation of RNA splicing Source: UniProtKB
  • RNA processing Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169813-MONOMER.
ReactomeiR-HSA-6803529. FGFR2 alternative splicing.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:5039. HNRNPF.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytoplasm Source: HPA
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20W → A: Loss of RNA-binding. 1 Publication1
Mutagenesisi84E → A: Loss of RNA-binding. 1 Publication1
Mutagenesisi116R → A: Decreases affinity for RNA oligonucleotide 100-fold. 1 Publication1
Mutagenesisi120F → A: Little disruption of binding RNA. Decreases affinity for RNA oligonucleotide 100-fold. Abrogates RNA-binding; when associated with A-180. 2 Publications1
Mutagenesisi150K → A: No effect on affinity for RNA oligonucleotide. 1 Publication1
Mutagenesisi156F → A: Drastically effects folding of RRM2. 1 Publication1
Mutagenesisi173K → A: Minimal effect on affinity for RNA oligonucleotide. 1 Publication1
Mutagenesisi178H → A: Little disruption of binding RNA. 1 Publication1
Mutagenesisi179R → A: Decreases affinity for RNA oligonucleotide 100-fold. 1 Publication1
Mutagenesisi180Y → A: Decreases affinity for RNA oligonucleotide 10-fold. Abrogates RNA-binding; when associated with A-120. 2 Publications1
Mutagenesisi182E → A: Decreases affinity for RNA oligonucleotide 100-fold. 1 Publication1
Mutagenesisi184F → A: Minimal effect on affinity for RNA oligonucleotide. 1 Publication1

Organism-specific databases

DisGeNETi3185.
OpenTargetsiENSG00000169813.
PharmGKBiPA162391271.

Polymorphism and mutation databases

BioMutaiHNRNPF.
DMDMi1710628.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003671141 – 415Heterogeneous nuclear ribonucleoprotein FAdd BLAST415
Initiator methionineiRemoved; alternateCombined sources1 Publication
ChainiPRO_00000818522 – 415Heterogeneous nuclear ribonucleoprotein F, N-terminally processedAdd BLAST414

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F; alternateCombined sources1 Publication1
Modified residuei2N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F, N-terminally processedCombined sources1 Publication1
Cross-linki72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei104PhosphoserineCombined sources1
Modified residuei107PhosphoserineCombined sources1
Modified residuei161PhosphoserineCombined sources1
Modified residuei187PhosphoserineCombined sources1
Modified residuei193PhosphoserineCombined sources1
Modified residuei195PhosphoserineBy similarity1
Modified residuei200N6-acetyllysine; alternateBy similarity1
Cross-linki200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei215PhosphothreonineCombined sources1
Modified residuei224N6-acetyllysineCombined sources1
Modified residuei265PhosphoserineCombined sources1

Post-translational modificationi

Sumoylated.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP52597.
MaxQBiP52597.
PaxDbiP52597.
PeptideAtlasiP52597.
PRIDEiP52597.

2D gel databases

OGPiP52597.

PTM databases

iPTMnetiP52597.
PhosphoSitePlusiP52597.
SwissPalmiP52597.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Gene expression databases

BgeeiENSG00000169813.
CleanExiHS_HNRNPF.
ExpressionAtlasiP52597. baseline and differential.
GenevisibleiP52597. HS.

Organism-specific databases

HPAiHPA016884.

Interactioni

Subunit structurei

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei16Interaction with RNA1
Sitei20Interaction with RNA1
Sitei52Interaction with RNA1
Sitei75Interaction with RNA1
Sitei116Interaction with RNA1
Sitei120Interaction with RNA1
Sitei150Interaction with RNA1
Sitei173Interaction with RNA1
Sitei294Interaction with RNA1
Sitei298Interaction with RNA1
Sitei326Interaction with RNA1
Sitei349Interaction with RNA1

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-352986,EBI-717810
C1orf94Q6P1W55EBI-352986,EBI-946029
DZIP3Q86Y135EBI-352986,EBI-948630
EIF4ENIF1Q9NRA83EBI-352986,EBI-301024
HNRNPMP522723EBI-352986,EBI-486809
HNRNPUL1Q9BUJ24EBI-352986,EBI-1018153
HSFY2Q96LI63EBI-352986,EBI-3957665
IKZF3Q9UKT93EBI-352986,EBI-747204
RBFOX2O432514EBI-352986,EBI-746056
TFGQ927343EBI-352986,EBI-357061

Protein-protein interaction databases

BioGridi109426. 173 interactors.
DIPiDIP-33145N.
IntActiP52597. 84 interactors.
MINTiMINT-1157890.
STRINGi9606.ENSP00000338477.

Structurei

Secondary structure

1415
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 17Combined sources6
Helixi24 – 30Combined sources7
Turni31 – 33Combined sources3
Beta strandi37 – 40Combined sources4
Beta strandi43 – 47Combined sources5
Beta strandi49 – 51Combined sources3
Beta strandi53 – 60Combined sources8
Helixi64 – 71Combined sources8
Turni72 – 74Combined sources3
Beta strandi75 – 87Combined sources13
Helixi90 – 97Combined sources8
Beta strandi107 – 109Combined sources3
Beta strandi112 – 116Combined sources5
Helixi124 – 130Combined sources7
Turni131 – 133Combined sources3
Beta strandi136 – 142Combined sources7
Beta strandi147 – 151Combined sources5
Beta strandi153 – 161Combined sources9
Helixi164 – 169Combined sources6
Turni170 – 173Combined sources4
Beta strandi175 – 180Combined sources6
Beta strandi184 – 186Combined sources3
Helixi188 – 191Combined sources4
Beta strandi284 – 294Combined sources11
Helixi302 – 309Combined sources8
Beta strandi315 – 318Combined sources4
Beta strandi322 – 325Combined sources4
Beta strandi332 – 334Combined sources3
Helixi337 – 344Combined sources8
Beta strandi351 – 354Combined sources4
Beta strandi358 – 362Combined sources5
Beta strandi368 – 371Combined sources4
Beta strandi377 – 379Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52597.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 85RRM 1PROSITE-ProRule annotationAdd BLAST73
Domaini111 – 188RRM 2PROSITE-ProRule annotationAdd BLAST78
Domaini289 – 366RRM 3PROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni81 – 86Interaction with RNA6
Regioni179 – 184Interaction with RNA6
Regioni355 – 360Interaction with RNA6

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

eggNOGiKOG4211. Eukaryota.
ENOG410Z6M0. LUCA.
GeneTreeiENSGT00760000119102.
HOGENOMiHOG000220896.
HOVERGENiHBG055557.
InParanoidiP52597.
KOiK12898.
OMAiFLSECKI.
OrthoDBiEOG091G0CTJ.
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. 2 hits.
PF08080. zf-RNPHF. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
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

        10         20         30         40         50
MMLGPEGGEG FVVKLRGLPW SCSVEDVQNF LSDCTIHDGA AGVHFIYTRE
60 70 80 90 100
GRQSGEAFVE LGSEDDVKMA LKKDRESMGH RYIEVFKSHR TEMDWVLKHS
110 120 130 140 150
GPNSADSAND GFVRLRGLPF GCTKEEIVQF FSGLEIVPNG ITLPVDPEGK
160 170 180 190 200
ITGEAFVQFA SQELAEKALG KHKERIGHRY IEVFKSSQEE VRSYSDPPLK
210 220 230 240 250
FMSVQRPGPY DRPGTARRYI GIVKQAGLER MRPGAYSTGY GGYEEYSGLS
260 270 280 290 300
DGYGFTTDLF GRDLSYCLSG MYDHRYGDSE FTVQSTTGHC VHMRGLPYKA
310 320 330 340 350
TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHEE AVAAMSKDRA
360 370 380 390 400
NMQHRYIELF LNSTTGASNG AYSSQVMQGM GVSAAQATYS GLESQSVSGC
410
YGAGYSGQNS MGGYD
Length:415
Mass (Da):45,672
Last modified:January 23, 2007 - v3
Checksum:iD14E170631FB1F31
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02799987K → R.1 PublicationCorresponds to variant rs17851426dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109426. 173 interactors.
DIPiDIP-33145N.
IntActiP52597. 84 interactors.
MINTiMINT-1157890.
STRINGi9606.ENSP00000338477.

PTM databases

iPTMnetiP52597.
PhosphoSitePlusiP52597.
SwissPalmiP52597.

Polymorphism and mutation databases

BioMutaiHNRNPF.
DMDMi1710628.

2D gel databases

OGPiP52597.

Proteomic databases

EPDiP52597.
MaxQBiP52597.
PaxDbiP52597.
PeptideAtlasiP52597.
PRIDEiP52597.

Protocols and materials databases

DNASUi3185.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3185.
DisGeNETi3185.
GeneCardsiHNRNPF.
HGNCiHGNC:5039. HNRNPF.
HPAiHPA016884.
MIMi601037. gene.
neXtProtiNX_P52597.
OpenTargetsiENSG00000169813.
PharmGKBiPA162391271.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4211. Eukaryota.
ENOG410Z6M0. LUCA.
GeneTreeiENSGT00760000119102.
HOGENOMiHOG000220896.
HOVERGENiHBG055557.
InParanoidiP52597.
KOiK12898.
OMAiFLSECKI.
OrthoDBiEOG091G0CTJ.
PhylomeDBiP52597.
TreeFamiTF316157.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169813-MONOMER.
ReactomeiR-HSA-6803529. FGFR2 alternative splicing.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.

Miscellaneous databases

ChiTaRSiHNRNPF. human.
EvolutionaryTraceiP52597.
GeneWikiiHNRPF.
GenomeRNAii3185.
PROiP52597.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000169813.
CleanExiHS_HNRNPF.
ExpressionAtlasiP52597. baseline and differential.
GenevisibleiP52597. HS.

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. 2 hits.
PF08080. zf-RNPHF. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 187 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.