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Q9Z2X1 (HNRPF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein F
Short name=hnRNP F

Cleaved into the following chain:

  1. Heterogeneous nuclear ribonucleoprotein F, N-terminally processed
Gene names
Name:Hnrnpf
Synonyms:Hnrpf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 By similarity.

Subunit structure

Identified in the spliceosome C complex. Interacts with EIF2C1, EIF2C2, TBP and TXNL4/DIM1 By similarity.

Subcellular location

Nucleus › nucleoplasm By similarity.

Domain

The N-terminal RRM domains are responsible for recognizing the G-tract of BCL-X RNA By similarity.

Post-translational modification

Sumoylated By similarity.

Sequence similarities

Contains 3 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAH27003.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH29764.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC36361.1 differs from that shown. Reason: Erroneous termination at position 416. Translated as stop.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Z2X1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Z2X1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MMLGPEGGEGYVVKLRGLPWSC → MW

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Heterogeneous nuclear ribonucleoprotein F
PRO_0000367116
Initiator methionine11Removed; alternate By similarity
Chain2 – 415414Heterogeneous nuclear ribonucleoprotein F, N-terminally processed
PRO_0000253053

Regions

Domain11 – 9080RRM 1
Domain111 – 18878RRM 2
Domain289 – 36678RRM 3
Region81 – 866Interaction with RNA By similarity
Region179 – 1846Interaction with RNA By similarity
Region355 – 3606Interaction with RNA By similarity

Sites

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

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F, N-terminally processed By similarity
Modified residue1041Phosphoserine By similarity
Modified residue1611Phosphoserine By similarity
Modified residue1871Phosphoserine By similarity
Modified residue2241N6-acetyllysine By similarity
Cross-link72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 2222MMLGP…LPWSC → MW in isoform 2.
VSP_021004

Experimental info

Sequence conflict2721Y → C in AAH27003. Ref.2

Secondary structure

1 ....................... 415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 31E1C9C90A8E051F

FASTA41545,730
        10         20         30         40         50         60 
MMLGPEGGEG YVVKLRGLPW SCSIEDVQNF LSDCTIHDGV AGVHFIYTRE GRQSGEAFVE 

        70         80         90        100        110        120 
LESEDDVKLA 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 GIVKQAGLDR MRSGAYSAGY 

       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

Isoform 2 [UniParc].

Checksum: 2EC531A33BA024CF
Show »

FASTA39543,685

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Head.
[2]"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] (ISOFORMS 1 AND 2).
Strain: C57BL/6, Czech II and FVB/N.
Tissue: Eye, Fetal brain, Mammary gland and Mammary tumor.
[3]"Solution structure of the RNA binding domain in heterogeneous nuclear ribonucleoprotein F homolog."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-105.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK076478 mRNA. Translation: BAC36361.1. Sequence problems.
BC018185 mRNA. Translation: AAH18185.1.
BC025481 mRNA. Translation: AAH25481.1.
BC027003 mRNA. Translation: AAH27003.1. Different initiation.
BC029163 mRNA. Translation: AAH29163.1.
BC029764 mRNA. Translation: AAH29764.1. Different initiation.
BC033483 mRNA. Translation: AAH33483.1.
BC089313 mRNA. Translation: AAH89313.1.
IPIIPI00226073.
IPI00798511.
RefSeqNP_001159899.1. NM_001166427.1.
NP_001159900.1. NM_001166428.1.
NP_001159901.1. NM_001166429.1.
NP_001159902.1. NM_001166430.1.
NP_001159903.1. NM_001166431.1.
NP_001159904.1. NM_001166432.1.
NP_598595.1. NM_133834.2.
UniGeneMm.422979.
Mm.476420.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DB1NMR-A1-105[»]
ProteinModelPortalQ9Z2X1.
SMRQ9Z2X1. Positions 1-194, 277-381.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Z2X1. 3 interactions.

PTM databases

PhosphoSiteQ9Z2X1.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2X1.

Proteomic databases

PaxDbQ9Z2X1.
PRIDEQ9Z2X1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035493; ENSMUSP00000045048; ENSMUSG00000042079.
ENSMUST00000163168; ENSMUSP00000130023; ENSMUSG00000042079.
ENSMUST00000167182; ENSMUSP00000126817; ENSMUSG00000042079.
ENSMUST00000167657; ENSMUSP00000125911; ENSMUSG00000042079.
ENSMUST00000170346; ENSMUSP00000130844; ENSMUSG00000042079.
ENSMUST00000180020; ENSMUSP00000137632; ENSMUSG00000042079.
ENSMUST00000180341; ENSMUSP00000136700; ENSMUSG00000042079.
GeneID98758.
KEGGmmu:98758.
UCSCuc009dle.2. mouse.

Organism-specific databases

CTD3185.
MGIMGI:2138741. Hnrnpf.

Phylogenomic databases

eggNOGNOG326351.
GeneTreeENSGT00620000087736.
HOGENOMHOG000220896.
HOVERGENHBG055557.
InParanoidQ9Z2X1.
KOK12898.
OMASDCTIRD.
OrthoDBEOG4CRM03.

Gene expression databases

ArrayExpressQ9Z2X1.
BgeeQ9Z2X1.
GenevestigatorQ9Z2X1.
GermOnlineENSMUSG00000042079. Mus musculus.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR012996. Znf_CHHC.
[Graphical view]
PfamPF08080. zf-RNPHF. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPF. mouse.
EvolutionaryTraceQ9Z2X1.
NextBio353639.
SOURCESearch...

Entry information

Entry nameHNRPF_MOUSE
AccessionPrimary (citable) accession number: Q9Z2X1
Secondary accession number(s): Q5FWK2 expand/collapse secondary AC list , Q8BVU8, Q8K2U9, Q8R0E7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents