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P52597 (HNRPF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein F

Short name=hnRNP F
Alternative name(s):
Nucleolin-like protein mcs94-1
Gene names
Name:HNRNPF
Synonyms:HNRPF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.24

Subunit structure

Identified in the spliceosome C complex. Interacts with AGO1, AGO2, TBP and TXNL4/DIM1. Ref.9 Ref.10 Ref.13

Subcellular location

Nucleusnucleoplasm.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Heterogeneous nuclear ribonucleoprotein F
PRO_0000367114
Initiator methionine11Removed; alternate Ref.8
Chain2 – 415414Heterogeneous nuclear ribonucleoprotein F, N-terminally processed
PRO_0000081852

Regions

Domain13 – 8573RRM 1
Domain111 – 18878RRM 2
Domain289 – 36678RRM 3
Region81 – 866Interaction with RNA
Region179 – 1846Interaction with RNA
Region355 – 3606Interaction with RNA

Sites

Site161Interaction with RNA
Site201Interaction with RNA
Site521Interaction with RNA
Site751Interaction with RNA
Site1161Interaction with RNA
Site1201Interaction with RNA
Site1501Interaction with RNA
Site1731Interaction with RNA
Site2941Interaction with RNA
Site2981Interaction with RNA
Site3261Interaction with RNA
Site3491Interaction with RNA

Amino acid modifications

Modified residue11N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F; alternate Ref.8 Ref.16 Ref.22
Modified residue21N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F, N-terminally processed Ref.8 Ref.16 Ref.22
Modified residue1041Phosphoserine Ref.17 Ref.19 Ref.21
Modified residue1611Phosphoserine Ref.14
Modified residue1871Phosphoserine Ref.19
Modified residue2241N6-acetyllysine Ref.18
Cross-link72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Natural variations

Natural variant871K → R. Ref.7
Corresponds to variant rs17851426 [ dbSNP | Ensembl ].
VAR_027999

Experimental info

Mutagenesis201W → A: Loss of RNA-binding. Ref.24
Mutagenesis841E → A: Loss of RNA-binding. Ref.24
Mutagenesis1161R → A: Decreases affinity for RNA oligonucleotide 100-fold. Ref.24
Mutagenesis1201F → A: Little disruption of binding RNA. Decreases affinity for RNA oligonucleotide 100-fold. Abrogates RNA-binding; when associated with A-180. Ref.23 Ref.24
Mutagenesis1501K → A: No effect on affinity for RNA oligonucleotide. Ref.24
Mutagenesis1561F → A: Drastically effects folding of RRM2. Ref.23
Mutagenesis1731K → A: Minimal effect on affinity for RNA oligonucleotide. Ref.24
Mutagenesis1781H → A: Little disruption of binding RNA. Ref.23
Mutagenesis1791R → A: Decreases affinity for RNA oligonucleotide 100-fold. Ref.24
Mutagenesis1801Y → A: Decreases affinity for RNA oligonucleotide 10-fold. Abrogates RNA-binding; when associated with A-120. Ref.23 Ref.24
Mutagenesis1821E → A: Decreases affinity for RNA oligonucleotide 100-fold. Ref.24
Mutagenesis1841F → A: Minimal effect on affinity for RNA oligonucleotide. Ref.24

Secondary structure

.............................................................. 415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52597 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D14E170631FB1F31

FASTA41545,672
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, 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]"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, 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]"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, 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]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+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.
PIRS43484.
RefSeqNP_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.
UniGeneHs.712955.
Hs.808.

3D structure databases

PDBe
RCSB PDB
PDBj
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/F2-8[»]
ProteinModelPortalP52597.
SMRP52597. Positions 1-194, 277-381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109426. 115 interactions.
DIPDIP-33145N.
IntActP52597. 55 interactions.
MINTMINT-1157890.
STRING9606.ENSP00000338477.

PTM databases

PhosphoSiteP52597.

Polymorphism databases

DMDM1710628.

2D gel databases

OGPP52597.

Proteomic databases

PaxDbP52597.
PeptideAtlasP52597.
PRIDEP52597.

Protocols and materials databases

DNASU3185.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337970; ENSP00000338477; ENSG00000169813.
ENST00000356053; ENSP00000348345; ENSG00000169813.
ENST00000357065; ENSP00000349573; ENSG00000169813.
ENST00000443950; ENSP00000400433; ENSG00000169813.
ENST00000544000; ENSP00000438061; ENSG00000169813.
GeneID3185.
KEGGhsa:3185.
UCSCuc001jar.2. human.

Organism-specific databases

CTD3185.
GeneCardsGC10M043881.
HGNCHGNC:5039. HNRNPF.
HPAHPA001359.
HPA016884.
MIM601037. gene.
neXtProtNX_P52597.
PharmGKBPA162391271.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326351.
HOGENOMHOG000220896.
HOVERGENHBG055557.
InParanoidP52597.
KOK12898.
OMAEFAVQST.
OrthoDBEOG7BS4BZ.
PhylomeDBP52597.
TreeFamTF316157.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP52597.
BgeeP52597.
CleanExHS_HNRNPF.
GenevestigatorP52597.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR012996. Znf_CHHC.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
PF08080. zf-RNPHF. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPF. human.
EvolutionaryTraceP52597.
GeneWikiHNRPF.
GenomeRNAi3185.
NextBio12654.
PROP52597.
SOURCESearch...

Entry information

Entry nameHNRPF_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM