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O43390

- HNRPR_HUMAN

UniProt

O43390 - HNRPR_HUMAN

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Protein

Heterogeneous nuclear ribonucleoprotein R

Gene

HNRNPR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA processing Source: UniProtKB
  3. mRNA splicing, via spliceosome Source: UniProtKB
  4. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein R
Short name:
hnRNP R
Gene namesi
Name:HNRNPR
Synonyms:HNRPR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:5047. HNRNPR.

Subcellular locationi

Nucleusnucleoplasm 1 Publication. Cytoplasm 1 Publication
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. nucleoplasm Source: UniProtKB
  4. nucleus Source: HPA
  5. ribonucleoprotein complex Source: UniProtKB
  6. spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162391459.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 633632Heterogeneous nuclear ribonucleoprotein RPRO_0000081870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei366 – 3661N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO43390.
PaxDbiO43390.
PeptideAtlasiO43390.
PRIDEiO43390.

PTM databases

PhosphoSiteiO43390.

Miscellaneous databases

PMAP-CutDBO43390.

Expressioni

Gene expression databases

BgeeiO43390.
CleanExiHS_HNRNPR.
ExpressionAtlasiO43390. baseline and differential.
GenevestigatoriO43390.

Organism-specific databases

HPAiCAB011687.
HPA026092.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with GTPBP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-713419,EBI-389883

Protein-protein interaction databases

BioGridi115530. 159 interactions.
IntActiO43390. 44 interactions.
MINTiMINT-2796101.
STRINGi9606.ENSP00000363745.

Structurei

Secondary structure

1
633
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi334 – 3385
Beta strandi342 – 3476
Helixi354 – 3629
Beta strandi367 – 3737
Beta strandi376 – 3838
Helixi384 – 39411
Beta strandi405 – 4084

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK2NMR-A333-416[»]
ProteinModelPortaliO43390.
SMRiO43390. Positions 99-416.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43390.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini165 – 24480RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini246 – 32883RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini341 – 41171RRM 3PROSITE-ProRule annotationAdd
BLAST
Repeati462 – 471101; approximate
Repeati472 – 482112Add
BLAST
Repeati488 – 497103; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni447 – 567121RNA-binding RGG-boxAdd
BLAST
Regioni462 – 497363 X 11 AA approximate repeats of D-D-Y-Y-G-Y-D-Y-H-D-YAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi412 – 4187Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 153152Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi579 – 63355Asn/Gln-richAdd
BLAST

Sequence similaritiesi

Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG258596.
GeneTreeiENSGT00550000074366.
HOGENOMiHOG000186082.
HOVERGENiHBG051917.
InParanoidiO43390.
KOiK13161.
OMAiYYPPPRM.
OrthoDBiEOG73JKW2.
PhylomeDBiO43390.
TreeFamiTF314932.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsiTIGR01648. hnRNP-R-Q. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43390-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MANQVNGNAV QLKEEEEPMD TSSVTHTEHY KTLIEAGLPQ KVAERLDEIF
60 70 80 90 100
QTGLVAYVDL DERAIDALRE FNEEGALSVL QQFKESDLSH VQNKSAFLCG
110 120 130 140 150
VMKTYRQREK QGSKVQESTK GPDEAKIKAL LERTGYTLDV TTGQRKYGGP
160 170 180 190 200
PPDSVYSGVQ PGIGTEVFVG KIPRDLYEDE LVPLFEKAGP IWDLRLMMDP
210 220 230 240 250
LSGQNRGYAF ITFCGKEAAQ EAVKLCDSYE IRPGKHLGVC ISVANNRLFV
260 270 280 290 300
GSIPKNKTKE NILEEFSKVT EGLVDVILYH QPDDKKKNRG FCFLEYEDHK
310 320 330 340 350
SAAQARRRLM SGKVKVWGNV VTVEWADPVE EPDPEVMAKV KVLFVRNLAT
360 370 380 390 400
TVTEEILEKS FSEFGKLERV KKLKDYAFVH FEDRGAAVKA MDEMNGKEIE
410 420 430 440 450
GEEIEIVLAK PPDKKRKERQ AARQASRSTA YEDYYYHPPP RMPPPIRGRG
460 470 480 490 500
RGGGRGGYGY PPDYYGYEDY YDDYYGYDYH DYRGGYEDPY YGYDDGYAVR
510 520 530 540 550
GRGGGRGGRG APPPPRGRGA PPPRGRAGYS QRGAPLGPPR GSRGGRGGPA
560 570 580 590 600
QQQRGRGSRG SRGNRGGNVG GKRKADGYNQ PDSKRRQTNN QQNWGSQPIA
610 620 630
QQPLQQGGDY SGNYGYNNDN QEFYQDTYGQ QWK
Length:633
Mass (Da):70,943
Last modified:June 1, 1998 - v1
Checksum:i088341F6465ED46F
GO
Isoform 2 (identifier: O43390-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     269-269: V → VTGL

Show »
Length:636
Mass (Da):71,214
Checksum:i4319EA79A1A6DED2
GO
Isoform 3 (identifier: O43390-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:595
Mass (Da):66,980
Checksum:iC9C67D917E7BCC44
GO
Isoform 4 (identifier: O43390-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:535
Mass (Da):59,953
Checksum:iEDEE799FB18DE444
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 101101Missing in isoform 4. CuratedVSP_054703Add
BLAST
Alternative sequencei129 – 16638Missing in isoform 3. 1 PublicationVSP_047647Add
BLAST
Alternative sequencei269 – 2691V → VTGL in isoform 2 and isoform 4. 1 PublicationVSP_038360

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS232.1. [O43390-1]
CCDS44085.1. [O43390-2]
CCDS60020.1. [O43390-4]
CCDS72727.1. [O43390-3]
PIRiT02673.
RefSeqiNP_001095868.1. NM_001102398.2. [O43390-2]
NP_001284549.1. NM_001297620.1. [O43390-3]
NP_005817.1. NM_005826.4. [O43390-1]
XP_005245768.1. XM_005245711.2. [O43390-1]
XP_005245770.1. XM_005245713.2. [O43390-3]
UniGeneiHs.373763.

Genome annotation databases

EnsembliENST00000302271; ENSP00000304405; ENSG00000125944. [O43390-1]
ENST00000374612; ENSP00000363741; ENSG00000125944. [O43390-1]
ENST00000374616; ENSP00000363745; ENSG00000125944. [O43390-2]
ENST00000427764; ENSP00000392799; ENSG00000125944. [O43390-3]
ENST00000478691; ENSP00000474437; ENSG00000125944. [O43390-4]
GeneIDi10236.
KEGGihsa:10236.
UCSCiuc001bgp.4. human. [O43390-2]
uc001bgr.4. human. [O43390-1]
uc010odw.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS232.1. [O43390-1 ]
CCDS44085.1. [O43390-2 ]
CCDS60020.1. [O43390-4 ]
CCDS72727.1. [O43390-3 ]
PIRi T02673.
RefSeqi NP_001095868.1. NM_001102398.2. [O43390-2 ]
NP_001284549.1. NM_001297620.1. [O43390-3 ]
NP_005817.1. NM_005826.4. [O43390-1 ]
XP_005245768.1. XM_005245711.2. [O43390-1 ]
XP_005245770.1. XM_005245713.2. [O43390-3 ]
UniGenei Hs.373763.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DK2 NMR - A 333-416 [» ]
ProteinModelPortali O43390.
SMRi O43390. Positions 99-416.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115530. 159 interactions.
IntActi O43390. 44 interactions.
MINTi MINT-2796101.
STRINGi 9606.ENSP00000363745.

PTM databases

PhosphoSitei O43390.

Proteomic databases

MaxQBi O43390.
PaxDbi O43390.
PeptideAtlasi O43390.
PRIDEi O43390.

Protocols and materials databases

DNASUi 10236.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302271 ; ENSP00000304405 ; ENSG00000125944 . [O43390-1 ]
ENST00000374612 ; ENSP00000363741 ; ENSG00000125944 . [O43390-1 ]
ENST00000374616 ; ENSP00000363745 ; ENSG00000125944 . [O43390-2 ]
ENST00000427764 ; ENSP00000392799 ; ENSG00000125944 . [O43390-3 ]
ENST00000478691 ; ENSP00000474437 ; ENSG00000125944 . [O43390-4 ]
GeneIDi 10236.
KEGGi hsa:10236.
UCSCi uc001bgp.4. human. [O43390-2 ]
uc001bgr.4. human. [O43390-1 ]
uc010odw.2. human.

Organism-specific databases

CTDi 10236.
GeneCardsi GC01M023630.
HGNCi HGNC:5047. HNRNPR.
HPAi CAB011687.
HPA026092.
MIMi 607201. gene.
neXtProti NX_O43390.
PharmGKBi PA162391459.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258596.
GeneTreei ENSGT00550000074366.
HOGENOMi HOG000186082.
HOVERGENi HBG051917.
InParanoidi O43390.
KOi K13161.
OMAi YYPPPRM.
OrthoDBi EOG73JKW2.
PhylomeDBi O43390.
TreeFami TF314932.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi HNRNPR. human.
EvolutionaryTracei O43390.
GeneWikii HNRNPR.
GenomeRNAii 10236.
NextBioi 38770.
PMAP-CutDB O43390.
PROi O43390.
SOURCEi Search...

Gene expression databases

Bgeei O43390.
CleanExi HS_HNRNPR.
ExpressionAtlasi O43390. baseline and differential.
Genevestigatori O43390.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 3 hits.
[Graphical view ]
SMARTi SM00360. RRM. 3 hits.
[Graphical view ]
TIGRFAMsi TIGR01648. hnRNP-R-Q. 1 hit.
PROSITEi PS50102. RRM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiHNRPR_HUMAN
AccessioniPrimary (citable) accession number: O43390
Secondary accession number(s): Q2L7G6
, Q5TEH1, Q9BV64, S4R3J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 1, 1998
Last modified: October 29, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3