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Protein

Heterogeneous nuclear ribonucleoprotein F

Gene

HNRNPF

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

  • RNA binding Source: UniProtKB
  • single-stranded RNA binding Source: UniProtKB
  • TBP-class protein binding Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, RNA-binding
Biological processmRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-HSA-6803529 FGFR2 alternative splicing
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72203 Processing of Capped Intron-Containing Pre-mRNA
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation

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

EuPathDBiHostDB:ENSG00000169813.16
HGNCiHGNC:5039 HNRNPF
MIMi601037 gene
neXtProtiNX_P52597

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
Cross-linki87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei104PhosphoserineCombined sources1
Modified residuei107PhosphoserineCombined sources1
Modified residuei161PhosphoserineCombined sources1
Cross-linki167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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-acetyllysine; alternateCombined sources1
Cross-linki224Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
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
HPA069667

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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109426, 185 interactors
CORUMiP52597
DIPiDIP-33145N
IntActiP52597, 120 interactors
MINTiP52597
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.

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
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
IPR012996 Znf_CHHC
PfamiView protein in Pfam
PF00076 RRM_1, 2 hits
PF08080 zf-RNPHF, 1 hit
SMARTiView protein in SMART
SM00360 RRM, 3 hits
SUPFAMiSSF54928 SSF54928, 3 hits
PROSITEiView protein in PROSITE
PS50102 RRM, 2 hits

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 → R1 PublicationCorresponds to variant dbSNP:rs17851426Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L28010 mRNA Translation: AAC37584.1
AL512654 Genomic DNA No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiHNRPF_HUMAN
AccessioniPrimary (citable) accession number: P52597
Secondary accession number(s): B3KM84, Q5T0N2, Q96AU2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 199 of the entry and version 3 of the sequence. See 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
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Main funding by: National Institutes of Health