Reviewed, UniProtKB/Swiss-Prot P52597 (HNRPF_HUMAN)

Names and origin

Protein names

Recommended name:
    Heterogeneous nuclear ribonucleoprotein F
      Short name=hnRNP F
Alternative name(s):
    Nucleolin-like protein mcs94-1
Cleaved into the following chain:
    1- Recommended name:
            Heterogeneous nuclear ribonucleoprotein F, N-terminally processed

Gene names

Name:	HNRNPF
Synonyms:	HNRPF

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Probably binds G-rich sequences in pre-mRNAs.
Subunit structure	Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRNPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Interacts with TBP and TXNL4/DIM1. Ref.7
Subcellular location	Nucleus › nucleoplasm.
Tissue specificity	Expressed ubiquitously.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome regulation of RNA splicing Inferred from mutant phenotype. Source: UniProtKB
Cellular component	heterogeneous nuclear ribonucleoprotein complex Ref.2 Traceable author statement. Source: ProtInc nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Ref.2 Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NDRG1	Q92597	1	EBI-352986,EBI-716486
TOB1	P50616	1	EBI-352986,EBI-723281

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 415

415

Heterogeneous nuclear ribonucleoprotein F

PRO_0000367114

Initiator methionine

1

1

Removed; alternate Ref.6

Chain

2 – 415

414

Heterogeneous nuclear ribonucleoprotein F, N-terminally processed

PRO_0000081852

Regions

Domain

13 – 85

73

RRM 1

Domain

111 – 188

78

RRM 2

Domain

289 – 366

78

RRM 3

Amino acid modifications

Modified residue

1

1

N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F; alternate Ref.6

Modified residue

2

1

N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F, N-terminally processed Ref.6

Modified residue

161

1

Phosphoserine Ref.12

Modified residue

187

1

Phosphoserine Ref.14

Modified residue

246

1

Phosphotyrosine Ref.10

Modified residue

310

1

Phosphoserine Ref.9 Ref.11 Ref.13 Ref.14

Natural variations

Natural variant

87

1

K → R: dbSNP rs17851426. Ref.5

VAR_027999

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

415

Helix Strand Turn

Details...

Beta strand

107 – 109

3

Beta strand

112 – 116

5

Helix

124 – 130

7

Turn

131 – 133

3

Beta strand

136 – 142

7

Beta strand

147 – 151

5

Beta strand

153 – 161

9

Helix

164 – 169

6

Turn

170 – 173

4

Beta strand

184 – 186

3

Helix

188 – 191

4

Helix

302 – 309

8

Beta strand

315 – 318

4

Beta strand

322 – 325

4

Beta strand

332 – 334

3

Helix

337 – 344

8

Beta strand

351 – 354

4

Sequences

	Sequence		Length	Mass (Da)
	P52597-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D14E170631FB1F31	FASTA	415	45,672
	10 20 30 40 50 60 MMLGPEGGEG FVVKLRGLPW SCSVEDVQNF LSDCTIHDGA AGVHFIYTRE GRQSGEAFVE 70 80 90 100 110 120 LGSEDDVKMA LKKDRESMGH RYIEVFKSHR TEMDWVLKHS GPNSADSAND GFVRLRGLPF 130 140 150 160 170 180 GCTKEEIVQF FSGLEIVPNG ITLPVDPEGK ITGEAFVQFA SQELAEKALG KHKERIGHRY 190 200 210 220 230 240 IEVFKSSQEE VRSYSDPPLK FMSVQRPGPY DRPGTARRYI GIVKQAGLER MRPGAYSTGY 250 260 270 280 290 300 GGYEEYSGLS DGYGFTTDLF GRDLSYCLSG MYDHRYGDSE FTVQSTTGHC VHMRGLPYKA 310 320 330 340 350 360 TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHEE AVAAMSKDRA NMQHRYIELF 370 380 390 400 410 LNSTTGASNG AYSSQVMQGM GVSAAQATYS GLESQSVSGC YGAGYSGQNS MGGYD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7512260] [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: 7499401] [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: 1351868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-87. Tissue: Bone marrow, Lung, Ovary, Placenta and Uterus.
[6]	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, MASS SPECTROMETRY. Tissue: B-cell lymphoma and Colon carcinoma.
[7]	"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: 11054566] [Abstract] Cited for: INTERACTION WITH TXNL4.
[8]	"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: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, MASS SPECTROMETRY.
[11]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, MASS SPECTROMETRY.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY.
[14]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-310, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L28010 mRNA. Translation: AAC37584.1.
AL512654 Genomic DNA. Translation: CAI17066.1.
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.

IPI

IPI00003881.

PIR

S43484.

RefSeq

NP_001091674.1.
NP_001091675.1.
NP_001091676.1.
NP_001091677.1.
NP_001091678.1.
NP_004957.1.

UniGene

Hs.712955
Hs.808

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HGL	NMR	-	A	1-102	[»]
2HGM	NMR	-	A	103-194	[»]
2HGN	NMR	-	A	277-381	[»]

SMR

P52597. Positions 1-102, 102-193, 103-194.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52597. 8 interactions.

PTM databases

PhosphoSite

P52597.

2-D gel databases

Aarhus/Ghent-2DPAGE

6304. IEF.
7312. IEF.

OGP

P52597.

Proteomic databases

PeptideAtlas

P52597.

PRIDE

P52597.

Genome annotation databases

Ensembl

ENSG00000169813. Homo sapiens. [Contig view]

GeneID

3185.

KEGG

hsa:3185.

Organism-specific databases

GeneCards

GC10M043202.

H-InvDB

HIX0008779.

HGNC

HGNC:5039. HNRNPF.

HPA

HPA016884.

MIM

601037. gene.

PharmGKB

PA29364.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P52597.

HOVERGEN

P52597.

OMA

P52597. SADTAND.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P52597.

Bgee

P52597.

CleanEx

HS_HNRNPF.

GermOnline

ENSG00000169813. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
IPR012996. Znf_CHHC.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.

Pfam

PF00076. RRM_1. 2 hits.
PF08080. zf-RNPHF. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 3 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

12654.

SOURCE

Search...

Entry information

Entry name

HNRPF_HUMAN

Accession

Primary (citable) accession number: P52597
Secondary accession number(s): Q5T0N2, Q96AU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)