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Protein

Heterogeneous nuclear ribonucleoprotein A1

Gene

Hnrnpa1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection.

GO - Molecular functioni

GO - Biological processi

  • alternative mRNA splicing, via spliceosome Source: MGI
  • mRNA transport Source: UniProtKB-KW
  • nuclear export Source: HGNC
  • nuclear import Source: HGNC
  • RNA splicing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein A1
Short name:
hnRNP A1
Alternative name(s):
HDP-1
Helix-destabilizing protein
Single-strand-binding protein
Topoisomerase-inhibitor suppressed
hnRNP core protein A1
Cleaved into the following chain:
Gene namesi
Name:Hnrnpa1
Synonyms:Fli-2, Hnrpa1, Tis
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:104820. Hnrnpa1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Heterogeneous nuclear ribonucleoprotein A1PRO_0000081830Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 320319Heterogeneous nuclear ribonucleoprotein A1, N-terminally processedPRO_0000424511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylserine; in Heterogeneous nuclear ribonucleoprotein A1, N-terminally processedBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei3 – 31N6-acetyllysineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei6 – 61PhosphoserineCombined sources
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei22 – 221PhosphoserineCombined sources
Cross-linki113 – 113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei192 – 1921Phosphoserine; by MKNK2By similarity
Modified residuei194 – 1941Asymmetric dimethylarginine; alternateBy similarity
Modified residuei194 – 1941Dimethylated arginine; alternateBy similarity
Modified residuei199 – 1991PhosphoserineBy similarity
Modified residuei206 – 2061Asymmetric dimethylarginine; alternateBy similarity
Modified residuei206 – 2061Dimethylated arginine; alternateBy similarity
Modified residuei206 – 2061Omega-N-methylarginine; alternateBy similarity
Modified residuei218 – 2181Asymmetric dimethylarginineBy similarity
Modified residuei225 – 2251Asymmetric dimethylarginine; alternateBy similarity
Modified residuei225 – 2251Dimethylated arginine; alternateBy similarity
Modified residuei225 – 2251Omega-N-methylarginine; alternateBy similarity
Modified residuei232 – 2321Asymmetric dimethylarginineBy similarity
Modified residuei285 – 2851PhosphoserineBy similarity
Modified residuei298 – 2981N6-acetyllysineCombined sources
Modified residuei309 – 3091PhosphoserineBy similarity
Modified residuei310 – 3101Phosphoserine; by MKNK2By similarity
Modified residuei311 – 3111Phosphoserine; by MKNK2By similarity
Modified residuei312 – 3121Phosphoserine; by MKNK2By similarity
Modified residuei313 – 3131PhosphoserineBy similarity
Modified residuei316 – 3161PhosphoserineBy similarity

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49312.
MaxQBiP49312.
PaxDbiP49312.
PeptideAtlasiP49312.
PRIDEiP49312.
TopDownProteomicsiP49312-1. [P49312-1]

PTM databases

iPTMnetiP49312.
PhosphoSiteiP49312.

Expressioni

Gene expression databases

BgeeiP49312.
CleanExiMM_HNRNPA1.
ExpressionAtlasiP49312. baseline.
GenevisibleiP49312. MM.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with SEPT6. Interacts with C9orf72. Interacts with UBQLN2.By similarity

Protein-protein interaction databases

BioGridi200357. 6 interactions.
IntActiP49312. 7 interactions.
MINTiMINT-1744029.
STRINGi10090.ENSMUSP00000137406.

Structurei

3D structure databases

ProteinModelPortaliP49312.
SMRiP49312. Positions 8-190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 9784RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini105 – 18480RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 9491Globular A domainAdd
BLAST
Regioni95 – 18591Globular B domainAdd
BLAST
Regioni218 – 24023RNA-binding RGG-boxAdd
BLAST
Regioni268 – 30538Nuclear targeting sequenceBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi195 – 320126Gly-richAdd
BLAST
Compositional biasi308 – 3136Poly-Ser

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234442.
HOVERGENiHBG002295.
InParanoidiP49312.
KOiK12741.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR021662. HnRNPA1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF11627. HnRNPA1. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P49312-1) [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
MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN
60 70 80 90 100
TKRSRGFGFV TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA
110 120 130 140 150
HLTVKKIFVG GIKEDTEEHH LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF
160 170 180 190 200
VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA LSKQEMASAS SSQRGRSGSG
210 220 230 240 250
NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS GDGYNGFGND
260 270 280 290 300
GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR
310 320
NQGGYGGSSS SSSYGSGRRF
Length:320
Mass (Da):34,196
Last modified:January 23, 2007 - v2
Checksum:i59485C9FA1FF8AE1
GO
Isoform Short (identifier: P49312-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     252-303: Missing.

Show »
Length:268
Mass (Da):28,898
Checksum:i13A50CDCA6DFB3A2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei252 – 30352Missing in isoform Short. CuratedVSP_005825Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99167 mRNA. Translation: AAA37633.1.
D86729 mRNA. Translation: BAA13162.1.
D86728 mRNA. Translation: BAA13161.1.
AK007802 mRNA. Translation: BAB25267.1.
AK088308 mRNA. Translation: BAC40273.1.
AK131999 mRNA. Translation: BAE20929.1.
AK135391 mRNA. Translation: BAE22518.1.
AK161730 mRNA. Translation: BAE36552.1.
AK166901 mRNA. Translation: BAE39104.1.
AK167161 mRNA. Translation: BAE39302.1.
AK167810 mRNA. Translation: BAE39837.1.
AK167913 mRNA. Translation: BAE39920.1.
AK168420 mRNA. Translation: BAE40333.1.
AK168531 mRNA. Translation: BAE40409.1.
BC080675 mRNA. Translation: AAH80675.1.
BC083136 mRNA. Translation: AAH83136.1.
CCDSiCCDS37233.1. [P49312-1]
PIRiA44485.
RefSeqiNP_034577.1. NM_010447.5. [P49312-1]
UniGeneiMm.237064.
Mm.432031.

Genome annotation databases

EnsembliENSMUST00000087351; ENSMUSP00000084609; ENSMUSG00000046434. [P49312-1]
GeneIDi15382.
KEGGimmu:15382.
UCSCiuc007xxp.2. mouse. [P49312-1]
uc011zrp.1. mouse. [P49312-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99167 mRNA. Translation: AAA37633.1.
D86729 mRNA. Translation: BAA13162.1.
D86728 mRNA. Translation: BAA13161.1.
AK007802 mRNA. Translation: BAB25267.1.
AK088308 mRNA. Translation: BAC40273.1.
AK131999 mRNA. Translation: BAE20929.1.
AK135391 mRNA. Translation: BAE22518.1.
AK161730 mRNA. Translation: BAE36552.1.
AK166901 mRNA. Translation: BAE39104.1.
AK167161 mRNA. Translation: BAE39302.1.
AK167810 mRNA. Translation: BAE39837.1.
AK167913 mRNA. Translation: BAE39920.1.
AK168420 mRNA. Translation: BAE40333.1.
AK168531 mRNA. Translation: BAE40409.1.
BC080675 mRNA. Translation: AAH80675.1.
BC083136 mRNA. Translation: AAH83136.1.
CCDSiCCDS37233.1. [P49312-1]
PIRiA44485.
RefSeqiNP_034577.1. NM_010447.5. [P49312-1]
UniGeneiMm.237064.
Mm.432031.

3D structure databases

ProteinModelPortaliP49312.
SMRiP49312. Positions 8-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200357. 6 interactions.
IntActiP49312. 7 interactions.
MINTiMINT-1744029.
STRINGi10090.ENSMUSP00000137406.

PTM databases

iPTMnetiP49312.
PhosphoSiteiP49312.

Proteomic databases

EPDiP49312.
MaxQBiP49312.
PaxDbiP49312.
PeptideAtlasiP49312.
PRIDEiP49312.
TopDownProteomicsiP49312-1. [P49312-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087351; ENSMUSP00000084609; ENSMUSG00000046434. [P49312-1]
GeneIDi15382.
KEGGimmu:15382.
UCSCiuc007xxp.2. mouse. [P49312-1]
uc011zrp.1. mouse. [P49312-2]

Organism-specific databases

CTDi3178.
MGIiMGI:104820. Hnrnpa1.

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234442.
HOVERGENiHBG002295.
InParanoidiP49312.
KOiK12741.

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiHnrnpa1. mouse.
PROiP49312.
SOURCEiSearch...

Gene expression databases

BgeeiP49312.
CleanExiMM_HNRNPA1.
ExpressionAtlasiP49312. baseline.
GenevisibleiP49312. MM.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR021662. HnRNPA1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF11627. HnRNPA1. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Retroviral insertions downstream of the heterogeneous nuclear ribonucleoprotein A1 gene in erythroleukemia cells: evidence that A1 is not essential for cell growth."
    Ben-David Y., Bani M.R., Chabot B., de Koven A., Bernstein A.
    Mol. Cell. Biol. 12:4449-4455(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning of the genes suppressed in RVC lymphoma cells by topoisomerase inhibitors."
    Onishi Y., Kizaki H.
    Biochem. Biophys. Res. Commun. 228:7-13(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoma.
  3. "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.
    , 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].
    Strain: C57BL/6J and DBA/2.
    Tissue: Amnion, Liver, Muellerian duct, Pancreas and Thymus.
  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 LONG).
    Tissue: Limb and Olfactory epithelium.
  5. Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 107-113 AND 285-300.
    Strain: OF1.
    Tissue: Brain and Hippocampus.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiROA1_MOUSE
AccessioniPrimary (citable) accession number: P49312
Secondary accession number(s): P97312, Q3V269
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.