O43390 (HNRPR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear ribonucleoprotein R
Short name=hnRNP R

Gene names

Name:	HNRNPR
Synonyms:	HNRPR

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	633 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 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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with GTPBP1. Ref.6 Ref.7 Ref.10
Subcellular location	Nucleus › nucleoplasm. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.7
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred by curator Ref.6. Source: UniProtKB
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.6. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	RNA binding Non-traceable author statement Ref.1. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	2	EBI-713419,EBI-389883

Alternative products

This entry describes 2 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 633

632

Heterogeneous nuclear ribonucleoprotein R

PRO_0000081870

Regions

Domain

165 – 244

80

RRM 1

Domain

246 – 328

83

RRM 2

Domain

341 – 411

71

RRM 3

Repeat

462 – 471

10

1; approximate

Repeat

472 – 482

11

2

Repeat

488 – 497

10

3; approximate

Region

447 – 567

121

RNA-binding RGG-box

Region

462 – 497

36

3 X 11 AA approximate repeats of D-D-Y-Y-G-Y-D-Y-H-D-Y

Motif

412 – 418

7

Nuclear localization signal Potential

Compositional bias

2 – 153

152

Asp/Glu-rich (acidic)

Compositional bias

579 – 633

55

Asn/Gln-rich

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.4

Modified residue

366

1

N6-acetyllysine Ref.8

Natural variations

Alternative sequence

269

1

V → VTGL in isoform 2.

VSP_038360

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

633

Helix Strand Turn

Details...

Helix

334 – 338

5

Beta strand

342 – 347

6

Helix

354 – 362

9

Beta strand

367 – 373

7

Beta strand

376 – 383

8

Helix

384 – 394

11

Beta strand

405 – 408

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 088341F6465ED46F	FASTA	633	70,943
	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
	Isoform 2 [UniParc]. Checksum: 4319EA79A1A6DED2	FASTA	636	71,214
	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 GLTEGLVDVI LYHQPDDKKK NRGFCFLEYE 310 320 330 340 350 360 DHKSAAQARR RLMSGKVKVW GNVVTVEWAD PVEEPDPEVM AKVKVLFVRN LATTVTEEIL 370 380 390 400 410 420 EKSFSEFGKL ERVKKLKDYA FVHFEDRGAA VKAMDEMNGK EIEGEEIEIV LAKPPDKKRK 430 440 450 460 470 480 ERQAARQASR STAYEDYYYH PPPRMPPPIR GRGRGGGRGG YGYPPDYYGY EDYYDDYYGY 490 500 510 520 530 540 DYHDYRGGYE DPYYGYDDGY AVRGRGGGRG GRGAPPPPRG RGAPPPRGRA GYSQRGAPLG 550 560 570 580 590 600 PPRGSRGGRG GPAQQQRGRG SRGSRGNRGG NVGGKRKADG YNQPDSKRRQ TNNQQNWGSQ 610 620 630 PIAQQPLQQG GDYSGNYGYN NDNQEFYQDT YGQQWK

References

	« Hide 'large scale' referencesShow '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]	"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].
[3]	"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.
[4]	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, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[5]	Lubec G., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 32-41 AND 347-359, MASS SPECTROMETRY. Tissue: Fetal brain.
[6]	"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.
[7]	"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.
[8]	"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, MASS SPECTROMETRY.
[9]	"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].
[10]	"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.
[11]	"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.
AL109936 Genomic DNA. Translation: CAI19026.1.
AL109936 Genomic DNA. Translation: CAI19027.1.
BC001449 mRNA. Translation: AAH01449.1.

IPI

IPI00012074.
IPI00941649.

PIR

T02673.

RefSeq

NP_001095867.1. NM_001102397.1.
NP_001095868.1. NM_001102398.1.
NP_005817.1. NM_005826.3.

UniGene

Hs.373763.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DK2	NMR	-	A	333-416	[»]

ProteinModelPortal

O43390.

ModBase

Search...

Protein-protein interaction databases

IntAct

O43390. 36 interactions.

MINT

MINT-2796101.

STRING

9606.ENSP00000363745.

PTM databases

PhosphoSite

O43390.

Proteomic databases

PaxDb

O43390.

PeptideAtlas

O43390.

PRIDE

O43390.

Protocols and materials databases

DNASU

10236.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302271; ENSP00000304405; ENSG00000125944.
ENST00000374612; ENSP00000363741; ENSG00000125944.
ENST00000374616; ENSP00000363745; ENSG00000125944.

GeneID

10236.

KEGG

hsa:10236.

UCSC

uc001bgp.4. human.
uc001bgr.4. human.

Organism-specific databases

CTD

10236.

GeneCards

GC01M023630.

HGNC

HGNC:5047. HNRNPR.

HPA

CAB011687.
HPA026092.

MIM

607201. gene.

neXtProt

NX_O43390.

PharmGKB

PA162391459.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG258596.

HOGENOM

HOG000186082.

HOVERGEN

HBG051917.

KO

K13161.

OMA

YYPPPRM.

PhylomeDB

O43390.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O43390.

Bgee

O43390.

CleanEx

HS_HNRNPR.

Genevestigator

O43390.

GermOnline

ENSG00000125944. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 3 hits.
[Graphical view]

SMART

SM00360. RRM. 3 hits.
[Graphical view]

TIGRFAMs

TIGR01648. hnRNP-R-Q. 1 hit.

PROSITE

PS50102. RRM. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HNRNPR. human.

EvolutionaryTrace

O43390.

GenomeRNAi

10236.

NextBio

38770.

PMAP-CutDB

O43390.

SOURCE

Search...

Entry information

Entry name

HNRPR_HUMAN

Accession

Primary (citable) accession number: O43390
Secondary accession number(s): Q5TEH1, Q9BV64

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 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.