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P09651 (ROA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 191. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 A1

Short name=hnRNP A1
Alternative name(s):
Helix-destabilizing protein
Single-strand RNA-binding protein
hnRNP core protein A1
Gene names
Name:HNRNPA1
Synonyms:HNRPA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. May play a role in HCV RNA replication. Ref.21

Subunit structure

Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with SEPT6. Interacts with HCV NS5B and with the 5'-UTR and 3'-UTR of HCV RNA. Ref.15 Ref.21 Ref.22

Subcellular location

Nucleus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. In the course of viral infection, colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV-replication dependent manner. Ref.21 Ref.22

Post-translational modification

Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine. Ref.9

Sumoylated. Ref.17

Involvement in disease

Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 3 (IBMPFD3) [MIM:615424]: An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35

Amyotrophic lateral sclerosis 20 (ALS20) [MIM:615426]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA processing
mRNA splicing
mRNA transport
Transport
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Neurodegeneration
   DomainRepeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA export from nucleus

Inferred by curator Ref.13. Source: HGNC

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA processing

Traceable author statement Ref.13. Source: ProtInc

mRNA splicing, via spliceosome

Inferred by curator Ref.15. Source: UniProtKB

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear export

Inferred from direct assay Ref.13. Source: HGNC

nuclear import

Inferred from direct assay Ref.13. Source: HGNC

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.15. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.13. Source: HGNC

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

nucleoplasm

Inferred from direct assay Ref.13. Source: HGNC

nucleus

Inferred from direct assay. Source: HPA

ribonucleoprotein complex

Inferred from direct assay Ref.22. Source: UniProtKB

spliceosomal complex

Inferred from direct assay PubMed 9731529. Source: HGNC

   Molecular_functionRNA binding

Traceable author statement Ref.13. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

single-stranded DNA binding

Inferred from direct assay Ref.13. Source: HGNC

single-stranded RNA binding

Inferred by curator Ref.13. Source: HGNC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KHDRBS1Q076662EBI-352662,EBI-1364

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A1-B (identifier: P09651-1)

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 A1-A (identifier: P09651-2)

The sequence of this isoform differs from the canonical sequence as follows:
     252-303: Missing.
Note: Is twenty times more abundant than isoform A1-B.
Isoform 2 (identifier: P09651-3)

The sequence of this isoform differs from the canonical sequence as follows:
     203-307: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Heterogeneous nuclear ribonucleoprotein A1
PRO_0000424509
Initiator methionine11Removed; alternate Ref.9
Chain2 – 372371Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed
PRO_0000081828

Regions

Domain14 – 9784RRM 1
Domain105 – 18480RRM 2
Region4 – 9491Globular A domain
Region95 – 18591Globular B domain
Region218 – 24023RNA-binding RGG-box
Region320 – 35738Nuclear targeting sequence (M9)
Compositional bias195 – 372178Gly-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.31
Modified residue21N-acetylserine; in Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed Ref.9 Ref.27 Ref.28 Ref.31
Modified residue21Phosphoserine Ref.28
Modified residue31N6-acetyllysine Ref.27
Modified residue41Phosphoserine Ref.28 Ref.30
Modified residue61Phosphoserine Ref.24 Ref.28 Ref.30
Modified residue1921Phosphoserine; by MKNK2 Ref.18
Modified residue1941Asymmetric dimethylarginine; alternate By similarity
Modified residue1941Dimethylated arginine; alternate Ref.16
Modified residue1991Phosphoserine Ref.30
Modified residue2061Dimethylated arginine; alternate Ref.9 Ref.16
Modified residue2061Omega-N-methylarginine; alternate Ref.9 Ref.16
Modified residue2251Dimethylated arginine; alternate Ref.9 Ref.16
Modified residue2251Omega-N-methylarginine; alternate Ref.9 Ref.16
Modified residue3501N6-acetyllysine Ref.27
Modified residue3621Phosphoserine; by MKNK2 Ref.18
Modified residue3631Phosphoserine; by MKNK2 Ref.18
Modified residue3641Phosphoserine; by MKNK2 Ref.18
Modified residue3651Phosphoserine Ref.30
Modified residue3681Phosphoserine Ref.24 Ref.30
Cross-link113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.17

Natural variations

Alternative sequence203 – 307105Missing in isoform 2.
VSP_034076
Alternative sequence252 – 30352Missing in isoform A1-A.
VSP_005824
Natural variant731N → S.
Corresponds to variant rs6533 [ dbSNP | Ensembl ].
VAR_014711
Natural variant3141D → N in ALS20. Ref.35
VAR_070588
Natural variant3141D → V in IBMPFD3. Ref.35
VAR_070589
Natural variant3191N → S in ALS20. Ref.35
VAR_070590

Experimental info

Mutagenesis3261G → A: No nuclear import nor export. Ref.12
Mutagenesis3271P → A: No nuclear import nor export. Ref.12
Mutagenesis334 – 3352GG → LL: Normal nuclear import and export.
Sequence conflict1281Y → F in CAA29922. Ref.2
Sequence conflict1401R → P in CAA27874. Ref.8
Sequence conflict1461R → K in CAA29922. Ref.2

Secondary structure

.......................................... 372
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A1-B [UniParc].

Last modified February 9, 2010. Version 5.
Checksum: A06683571C6C109F

FASTA37238,747
        10         20         30         40         50         60 
MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV 

        70         80         90        100        110        120 
TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH 

       130        140        150        160        170        180 
LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA 

       190        200        210        220        230        240 
LSKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS 

       250        260        270        280        290        300 
GDGYNGFGND GGYGGGGPGY SGGSRGYGSG GQGYGNQGSG YGGSGSYDSY NNGGGGGFGG 

       310        320        330        340        350        360 
GSGSNFGGGG SYNDFGNYNN QSSNFGPMKG GNFGGRSSGP YGGGGQYFAK PRNQGGYGGS 

       370 
SSSSSYGSGR RF 

« Hide

Isoform A1-A [UniParc].

Checksum: 59485C9FA1FF8AE1
Show »

FASTA32034,196
Isoform 2 [UniParc].

Checksum: 2B492EF73FD41977
Show »

FASTA26729,386

References

« Hide 'large scale' references
[1]"Isolation of an active gene encoding human hnRNP protein A1. Evidence for alternative splicing."
Biamonti G., Buvoli M., Bassi M.T., Morandi C., Cobianchi F., Riva S.
J. Mol. Biol. 207:491-503(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A1-A).
Tissue: Liver.
[2]"cDNA cloning of human hnRNP protein A1 reveals the existence of multiple mRNA isoforms."
Buvoli M., Biamonti G., Ghetti A., Riva S., Bassi M.T., Horandi C.
Nucleic Acids Res. 16:3751-3770(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1-A).
Tissue: Fibroblast.
[3]Knudsen S.M., Leffers H.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1-A).
Tissue: Lung.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A1-A).
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 A1-A AND 2).
Tissue: Bone marrow, Cervix, Eye, Kidney, Liver, Lung and Lymph.
[8]"Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1."
Riva S., Morandi C., Tsoulfas P., Pandolfo M., Biamonti G., Merrill B., Williams K.R., Multhaup G., Beyreuther K., Werr H., Heinrich B., Schaefer K.P.
EMBO J. 5:2267-2273(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[9]Bienvenut W.V., Calvo F., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-47; 56-78; 93-140; 146-178; 197-232 AND 337-370, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-206 AND ARG-225, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma and Ovarian carcinoma.
[10]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 15-47; 147-161 AND 353-370, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[11]"Alternative splicing in the human gene for the core protein A1 generates another hnRNP protein."
Buvoli M., Cobianchi F., Bestagno M.G., Mangiarotti A., Bassi M.T., Biamonti G., Riva S.
EMBO J. 9:1229-1235(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 252-303 (ISOFORM A1-B).
[12]"A nuclear localization domain in the hnRNP A1 protein."
Siomi H., Dreyfuss G.
J. Cell Biol. 129:551-560(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF GLY-326; PRO-327 AND 334-GLY-GLY-335.
[13]"A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway."
Michael W.M., Choi M., Dreyfuss G.
Cell 83:415-422(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL, NUCLEAR EXPORT.
[14]"Nucleo-cytoplasmic distribution of human hnRNP proteins: a search for the targeting domains in hnRNP A1."
Weighardt F., Biamonti G., Riva S.
J. Cell Sci. 108:545-555(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL.
[15]"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.
[16]"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
Ong S.E., Mittler G., Mann M.
Nat. Methods 1:119-126(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-194; ARG-206 AND ARG-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis."
Li T., Evdokimov E., Shen R.F., Chao C.C., Tekle E., Wang T., Stadtman E.R., Yang D.C., Chock P.B.
Proc. Natl. Acad. Sci. U.S.A. 101:8551-8556(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-113.
[18]"The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1."
Buxade M., Parra J.L., Rousseau S., Shpiro N., Marquez R., Morrice N., Bain J., Espel E., Proud C.G.
Immunity 23:177-189(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-192; SER-362; SER-363 AND SER-364 BY MKNK2.
[19]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication."
Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.
J. Virol. 81:3852-3865(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPT6 AND HCV NS5B, FUNCTION, SUBCELLULAR LOCATION.
[22]"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.
[23]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[24]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[27]"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 SER-2; LYS-3 AND LYS-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4 AND SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"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].
[30]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-6; SER-199; SER-365 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Modeling by homology of RNA binding domain in A1 hnRNP protein."
Ghetti A., Bolognesi M., Cobianchi F., Morandi C.
FEBS Lett. 277:272-276(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 107-190.
[33]"Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75-A resolution."
Shamoo Y., Krueger U., Rice L.M., Williams K.R., Steitz T.A.
Nat. Struct. Biol. 4:215-222(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 9-181.
[34]"Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs."
Xu R.M., Jokhan L., Cheng X., Mayeda A., Krainer A.R.
Structure 5:559-570(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-182.
[35]"Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS."
Kim H.J., Kim N.C., Wang Y.D., Scarborough E.A., Moore J., Diaz Z., MacLea K.S., Freibaum B., Li S., Molliex A., Kanagaraj A.P., Carter R., Boylan K.B., Wojtas A.M., Rademakers R., Pinkus J.L., Greenberg S.A., Trojanowski J.Q. expand/collapse author list , Traynor B.J., Smith B.N., Topp S., Gkazi A.S., Miller J., Shaw C.E., Kottlors M., Kirschner J., Pestronk A., Li Y.R., Ford A.F., Gitler A.D., Benatar M., King O.D., Kimonis V.E., Ross E.D., Weihl C.C., Shorter J., Taylor J.P.
Nature 495:467-473(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IBMPFD3 VAL-314, VARIANTS ALS20 ASN-314 AND SER-319.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12671 Genomic DNA. Translation: CAA31191.1.
X06747 mRNA. Translation: CAA29922.1.
X79536 mRNA. Translation: CAA56072.1.
AK291113 mRNA. Translation: BAF83802.1.
AC078778 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96761.1.
BC002355 mRNA. Translation: AAH02355.1.
BC009600 mRNA. Translation: AAH09600.1.
BC012158 mRNA. Translation: AAH12158.1.
BC033714 mRNA. Translation: AAH33714.1.
BC052296 mRNA. Translation: AAH52296.1.
BC070315 mRNA. Translation: AAH70315.1.
BC074502 mRNA. Translation: AAH74502.1.
BC103707 mRNA. Translation: AAI03708.1.
X04347 mRNA. Translation: CAA27874.1.
PIRS02061.
S12520.
RefSeqNP_002127.1. NM_002136.2.
NP_112420.1. NM_031157.2.
XP_005268883.1. XM_005268826.1.
UniGeneHs.546261.
Hs.655424.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HA1X-ray1.75A1-184[»]
1L3KX-ray1.10A1-196[»]
1PGZX-ray2.60A2-195[»]
1PO6X-ray2.10A8-189[»]
1U1KX-ray2.00A1-196[»]
1U1LX-ray2.00A1-196[»]
1U1MX-ray2.00A1-196[»]
1U1NX-ray2.10A1-196[»]
1U1OX-ray2.00A1-196[»]
1U1PX-ray1.90A1-196[»]
1U1QX-ray1.80A1-196[»]
1U1RX-ray1.80A1-196[»]
1UP1X-ray1.90A3-184[»]
2H4MX-ray3.05C/D309-357[»]
2LYVNMR-A2-196[»]
2UP1X-ray2.10A8-190[»]
DisProtDP00324.
ProteinModelPortalP09651.
SMRP09651. Positions 8-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109420. 235 interactions.
DIPDIP-29338N.
IntActP09651. 101 interactions.
MINTMINT-1035550.
STRING9606.ENSP00000341826.

Chemistry

BindingDBP09651.
ChEMBLCHEMBL1955709.

PTM databases

PhosphoSiteP09651.

Polymorphism databases

DMDM288558857.

2D gel databases

SWISS-2DPAGEP09651.

Proteomic databases

PaxDbP09651.
PRIDEP09651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340913; ENSP00000341826; ENSG00000135486. [P09651-1]
ENST00000546500; ENSP00000448617; ENSG00000135486. [P09651-2]
ENST00000547276; ENSP00000447260; ENSG00000135486. [P09651-3]
ENST00000547566; ENSP00000449913; ENSG00000135486. [P09651-2]
GeneID3178.
KEGGhsa:3178.
UCSCuc001sfl.3. human. [P09651-1]
uc001sfm.3. human. [P09651-2]
uc001sfn.3. human. [P09651-3]

Organism-specific databases

CTD3178.
GeneCardsGC12P054674.
H-InvDBHIX0032087.
HIX0040127.
HIX0202582.
HGNCHGNC:5031. HNRNPA1.
HPACAB010894.
HPA001609.
HPA001666.
MIM164017. gene.
615424. phenotype.
615426. phenotype.
neXtProtNX_P09651.
Orphanet803. Amyotrophic lateral sclerosis.
52430. Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
PharmGKBPA162391113.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000234442.
HOVERGENHBG002295.
InParanoidP09651.
KOK12741.
OMAKIVNIVQ.
OrthoDBEOG715Q6V.
PhylomeDBP09651.
TreeFamTF314808.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP09651.
BgeeP09651.
CleanExHS_HNRNPA1.
GenevestigatorP09651.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPA1. human.
EvolutionaryTraceP09651.
GeneWikiHeterogeneous_nuclear_ribonucleoprotein_A1.
GenomeRNAi3178.
NextBio12614.
PROP09651.
SOURCESearch...

Entry information

Entry nameROA1_HUMAN
AccessionPrimary (citable) accession number: P09651
Secondary accession number(s): A8K4Z8, Q3MIB7, Q6PJZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 9, 2010
Last modified: April 16, 2014
This is version 191 of the entry and version 5 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM