P52597 (HNRPF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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. Heterogeneous nuclear ribonucleoprotein F, N-terminally processed

Gene names

Name:	HNRNPF
Synonyms:	HNRPF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. 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. Ref.22
Subunit structure	Identified in the spliceosome C complex. Interacts with EIF2C1, EIF2C2, TBP and TXNL4/DIM1. Ref.9 Ref.10 Ref.13
Subcellular location	Nucleus › nucleoplasm.
Tissue specificity	Expressed ubiquitously.
Domain	The N-terminal RRM domains are responsible for recognizing the G-tract of BCL-X RNA.
Post-translational modification	Sumoylated. Ref.11
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 Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred by curator Ref.10. Source: UniProtKB regulation of RNA splicing Inferred from direct assay Ref.22. Source: UniProtKB
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.10. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro single-stranded RNA binding Inferred from direct assay Ref.22. Source: UniProtKB
Complete GO annotation...

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.8

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

Region

81 – 86

6

Interaction with RNA

Region

179 – 184

6

Interaction with RNA

Region

355 – 360

6

Interaction with RNA

Sites

Site

16

1

Interaction with RNA

Site

20

1

Interaction with RNA

Site

52

1

Interaction with RNA

Site

75

1

Interaction with RNA

Site

116

1

Interaction with RNA

Site

120

1

Interaction with RNA

Site

150

1

Interaction with RNA

Site

173

1

Interaction with RNA

Site

294

1

Interaction with RNA

Site

298

1

Interaction with RNA

Site

326

1

Interaction with RNA

Site

349

1

Interaction with RNA

Amino acid modifications

Modified residue

1

1

N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F; alternate Ref.8

Modified residue

2

1

N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F, N-terminally processed Ref.8

Modified residue

104

1

Phosphoserine Ref.16 Ref.18 Ref.20

Modified residue

161

1

Phosphoserine Ref.14

Modified residue

187

1

Phosphoserine Ref.18

Modified residue

224

1

N6-acetyllysine Ref.17

Cross-link

72

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Natural variations

Natural variant

87

1

K → R. Ref.7
Corresponds to variant rs17851426 [ dbSNP | Ensembl ].

VAR_027999

Experimental info

Mutagenesis

20

1

W → A: Loss of RNA-binding. Ref.22

Mutagenesis

84

1

E → A: Loss of RNA-binding. Ref.22

Mutagenesis

116

1

R → A: Decreases affinity for RNA oligonucleotide 100-fold. Ref.22

Mutagenesis

120

1

F → A: Little disruption of binding RNA. Decreases affinity for RNA oligonucleotide 100-fold. Abrogates RNA-binding; when associated with A-180. Ref.21 Ref.22

Mutagenesis

150

1

K → A: No effect on affinity for RNA oligonucleotide. Ref.22

Mutagenesis

156

1

F → A: Drastically effects folding of RRM2. Ref.21

Mutagenesis

173

1

K → A: Minimal effect on affinity for RNA oligonucleotide. Ref.22

Mutagenesis

178

1

H → A: Little disruption of binding RNA. Ref.21

Mutagenesis

179

1

R → A: Decreases affinity for RNA oligonucleotide 100-fold. Ref.22

Mutagenesis

180

1

Y → A: Decreases affinity for RNA oligonucleotide 10-fold. Abrogates RNA-binding; when associated with A-120. Ref.21 Ref.22

Mutagenesis

182

1

E → A: Decreases affinity for RNA oligonucleotide 100-fold. Ref.22

Mutagenesis

184

1

F → A: Minimal effect on affinity for RNA oligonucleotide. Ref.22

Secondary structure

1

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415

Helix Strand Turn

Details...

Beta strand

12 – 17

6

Helix

24 – 30

7

Turn

31 – 33

3

Beta strand

37 – 40

4

Beta strand

43 – 47

5

Beta strand

49 – 51

3

Beta strand

53 – 60

8

Helix

64 – 71

8

Turn

72 – 74

3

Beta strand

75 – 87

13

Helix

90 – 97

8

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

175 – 180

6

Beta strand

184 – 186

3

Helix

188 – 191

4

Beta strand

284 – 294

11

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

Beta strand

358 – 362

5

Beta strand

368 – 371

4

Beta strand

377 – 379

3

Sequences

	Sequence		Length	Mass (Da)
	P52597 [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] [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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, 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 EIF2C1 AND EIF2C2.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, MASS SPECTROMETRY. 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]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY.
[17]	"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, MASS SPECTROMETRY.
[18]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"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, MASS SPECTROMETRY.
[21]	"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.
[22]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00003881.

PIR

S43484.

RefSeq

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.

UniGene

Hs.712955.
Hs.808.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-8	[»]

ProteinModelPortal

P52597.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52597. 36 interactions.

MINT

MINT-1157890.

STRING

9606.ENSP00000338477.

PTM databases

PhosphoSite

P52597.

Polymorphism databases

DMDM

1710628.

2D gel databases

OGP

P52597.

Proteomic databases

PaxDb

P52597.

PeptideAtlas

P52597.

PRIDE

P52597.

Protocols and materials databases

DNASU

3185.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337970; ENSP00000338477; ENSG00000169813.
ENST00000356053; ENSP00000348345; ENSG00000169813.
ENST00000357065; ENSP00000349573; ENSG00000169813.
ENST00000443950; ENSP00000400433; ENSG00000169813.
ENST00000544000; ENSP00000438061; ENSG00000169813.

GeneID

3185.

KEGG

hsa:3185.

UCSC

uc001jar.2. human.

Organism-specific databases

CTD

3185.

GeneCards

GC10M043881.

HGNC

HGNC:5039. HNRNPF.

HPA

HPA001359.
HPA016884.

MIM

601037. gene.

neXtProt

NX_P52597.

PharmGKB

PA162391271.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG326351.

HOGENOM

HOG000220896.

HOVERGEN

HBG055557.

InParanoid

P52597.

KO

K12898.

OMA

SDCTIRD.

OrthoDB

EOG4CRM03.

PhylomeDB

P52597.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P52597.

Bgee

P52597.

CleanEx

HS_HNRNPF.

Genevestigator

P52597.

GermOnline

ENSG00000169813. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 3 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR012996. Znf_CHHC.
[Graphical view]

Pfam

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

SMART

SM00360. RRM. 3 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HNRNPF. human.

EvolutionaryTrace

P52597.

GenomeRNAi

3185.

NextBio

12654.

SOURCE

Search...

Entry information

Entry name

HNRPF_HUMAN

Accession

Primary (citable) accession number: P52597
Secondary accession number(s): B3KM84, Q5T0N2, Q96AU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 149 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.