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O43390 (HNRPR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein R

Short name=hnRNP R
Gene names
Name:HNRNPR
Synonyms:HNRPR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length633 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 ribonucleosomes, which are complexes of at least 20 other different heterogenious nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus.

Subunit structure

Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with GTPBP1. Ref.7 Ref.8 Ref.12

Subcellular location

Nucleusnucleoplasm. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.8

Sequence similarities

Contains 3 RRM (RNA recognition motif) domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-713419,EBI-389883

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43390-1)

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: O43390-2)

The sequence of this isoform differs from the canonical sequence as follows:
     269-269: V → VTGL
Isoform 3 (identifier: O43390-3)

Also known as: hnRNP-R2;

The sequence of this isoform differs from the canonical sequence as follows:
     129-166: Missing.
Note: Expression is low and neural-specific.
Isoform 4 (identifier: O43390-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     269-269: V → VTGL
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 633632Heterogeneous nuclear ribonucleoprotein R
PRO_0000081870

Regions

Domain165 – 24480RRM 1
Domain246 – 32883RRM 2
Domain341 – 41171RRM 3
Repeat462 – 471101; approximate
Repeat472 – 482112
Repeat488 – 497103; approximate
Region447 – 567121RNA-binding RGG-box
Region462 – 497363 X 11 AA approximate repeats of D-D-Y-Y-G-Y-D-Y-H-D-Y
Motif412 – 4187Nuclear localization signal Potential
Compositional bias2 – 153152Asp/Glu-rich (acidic)
Compositional bias579 – 63355Asn/Gln-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.9 Ref.13
Modified residue3661N6-acetyllysine Ref.10

Natural variations

Alternative sequence1 – 101101Missing in isoform 4.
VSP_054703
Alternative sequence129 – 16638Missing in isoform 3.
VSP_047647
Alternative sequence2691V → VTGL in isoform 2 and isoform 4.
VSP_038360

Secondary structure

.............. 633
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 1998. Version 1.
Checksum: 088341F6465ED46F

FASTA63370,943
        10         20         30         40         50         60 
MANQVNGNAV QLKEEEEPMD TSSVTHTEHY KTLIEAGLPQ KVAERLDEIF QTGLVAYVDL 

        70         80         90        100        110        120 
DERAIDALRE FNEEGALSVL QQFKESDLSH VQNKSAFLCG VMKTYRQREK QGSKVQESTK 

       130        140        150        160        170        180 
GPDEAKIKAL LERTGYTLDV TTGQRKYGGP PPDSVYSGVQ PGIGTEVFVG KIPRDLYEDE 

       190        200        210        220        230        240 
LVPLFEKAGP IWDLRLMMDP LSGQNRGYAF ITFCGKEAAQ EAVKLCDSYE IRPGKHLGVC 

       250        260        270        280        290        300 
ISVANNRLFV GSIPKNKTKE NILEEFSKVT EGLVDVILYH QPDDKKKNRG FCFLEYEDHK 

       310        320        330        340        350        360 
SAAQARRRLM SGKVKVWGNV VTVEWADPVE EPDPEVMAKV KVLFVRNLAT TVTEEILEKS 

       370        380        390        400        410        420 
FSEFGKLERV KKLKDYAFVH FEDRGAAVKA MDEMNGKEIE GEEIEIVLAK PPDKKRKERQ 

       430        440        450        460        470        480 
AARQASRSTA YEDYYYHPPP RMPPPIRGRG RGGGRGGYGY PPDYYGYEDY YDDYYGYDYH 

       490        500        510        520        530        540 
DYRGGYEDPY YGYDDGYAVR GRGGGRGGRG APPPPRGRGA PPPRGRAGYS QRGAPLGPPR 

       550        560        570        580        590        600 
GSRGGRGGPA QQQRGRGSRG SRGNRGGNVG GKRKADGYNQ PDSKRRQTNN QQNWGSQPIA 

       610        620        630 
QQPLQQGGDY SGNYGYNNDN QEFYQDTYGQ QWK 

« Hide

Isoform 2 [UniParc].

Checksum: 4319EA79A1A6DED2
Show »

FASTA63671,214
Isoform 3 (hnRNP-R2) [UniParc].

Checksum: C9C67D917E7BCC44
Show »

FASTA59566,980
Isoform 4 [UniParc].

Checksum: EDEE799FB18DE444
Show »

FASTA53559,953

References

« Hide 'large scale' references
[1]"Molecular definition of heterogeneous nuclear ribonucleoprotein R (hnRNP R) using autoimmune antibody: immunological relationship with hnRNP P."
Hassfeld W., Chan E.K.L., Mathison D.A., Portman D., Dreyfuss G., Steiner G., Tan E.M.
Nucleic Acids Res. 26:439-445(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning and expression of a novel isoform of heterogeneous nuclear ribonucleoprotein-R."
Huang J., Chen X.H., Wu K., Xu P.
NeuroReport 16:727-730(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
Tissue: Brain.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 2).
Tissue: Placenta.
[5]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13; 32-41; 70-84; 95-103; 134-145; 175-216; 225-255; 258-285; 290-300; 347-366; 373-384; 398-414 AND 428-441, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[6]Lubec G., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 32-41 AND 347-359, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain.
[7]"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.
[8]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[9]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
[12]"Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs."
Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T.
FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GTPBP1.
[13]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Solution structure of RRM domain in heterogeneous nuclear ribonucleoprotein R (HNRNP R)."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 333-416.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF000364 mRNA. Translation: AAC39540.1.
DQ351905 mRNA. Translation: ABC73063.1.
AL109936 Genomic DNA. Translation: CAI19026.1.
AL109936 Genomic DNA. Translation: CAI19027.1.
BC001449 mRNA. Translation: AAH01449.1.
CCDSCCDS232.1. [O43390-1]
CCDS44085.1. [O43390-2]
PIRT02673.
RefSeqNP_001095867.1. NM_001102397.1.
NP_001095868.1. NM_001102398.1. [O43390-2]
NP_005817.1. NM_005826.3. [O43390-1]
XP_005245768.1. XM_005245711.2. [O43390-1]
XP_005245769.1. XM_005245712.2. [O43390-3]
XP_005245770.1. XM_005245713.2. [O43390-3]
UniGeneHs.373763.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK2NMR-A333-416[»]
ProteinModelPortalO43390.
SMRO43390. Positions 99-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115530. 161 interactions.
IntActO43390. 43 interactions.
MINTMINT-2796101.
STRING9606.ENSP00000363745.

PTM databases

PhosphoSiteO43390.

Proteomic databases

MaxQBO43390.
PaxDbO43390.
PeptideAtlasO43390.
PRIDEO43390.

Protocols and materials databases

DNASU10236.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302271; ENSP00000304405; ENSG00000125944. [O43390-1]
ENST00000374612; ENSP00000363741; ENSG00000125944. [O43390-1]
ENST00000374616; ENSP00000363745; ENSG00000125944. [O43390-2]
ENST00000427764; ENSP00000392799; ENSG00000125944. [O43390-3]
ENST00000478691; ENSP00000474437; ENSG00000125944.
GeneID10236.
KEGGhsa:10236.
UCSCuc001bgp.4. human. [O43390-2]
uc001bgr.4. human. [O43390-1]

Organism-specific databases

CTD10236.
GeneCardsGC01M023630.
HGNCHGNC:5047. HNRNPR.
HPACAB011687.
HPA026092.
MIM607201. gene.
neXtProtNX_O43390.
PharmGKBPA162391459.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258596.
HOGENOMHOG000186082.
HOVERGENHBG051917.
KOK13161.
OMAYYPPPRM.
OrthoDBEOG73JKW2.
PhylomeDBO43390.
TreeFamTF314932.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressO43390.
BgeeO43390.
CleanExHS_HNRNPR.
GenevestigatorO43390.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsTIGR01648. hnRNP-R-Q. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPR. human.
EvolutionaryTraceO43390.
GeneWikiHNRNPR.
GenomeRNAi10236.
NextBio38770.
PMAP-CutDBO43390.
PROO43390.
SOURCESearch...

Entry information

Entry nameHNRPR_HUMAN
AccessionPrimary (citable) accession number: O43390
Secondary accession number(s): Q2L7G6 expand/collapse secondary AC list , Q5TEH1, Q9BV64, S4R3J4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 148 of the entry and version 1 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM