P09651 (ROA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	372 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	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.24
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 SEPT6. Interacts with HCV NS5B and with the 5'-UTR and 3'-UTR of HCV RNA. Ref.24
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.24 Ref.25
Post-translational modification	Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine. Ref.9 Ref.16 Sumoylated. Ref.17
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	Host-virus interaction Transport mRNA processing mRNA splicing mRNA transport
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	RNA export from nucleus Inferred by curator Ref.13. Source: HGNC interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW nuclear import Inferred from direct assay Ref.13. Source: HGNC nuclear mRNA splicing, via spliceosome Inferred by curator Ref.15. Source: UniProtKB
Cellular component	catalytic step 2 spliceosome Inferred from direct assay Ref.15. Source: UniProtKB cytoplasm Inferred from direct assay Ref.13. Source: HGNC heterogeneous nuclear ribonucleoprotein complex Traceable author statement. Source: ProtInc nucleolus Inferred from direct assay. Source: HPA nucleoplasm Inferred from direct assay Ref.13. Source: HGNC
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro 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...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 372

371

Heterogeneous nuclear ribonucleoprotein A1

PRO_0000081828

Regions

Domain

14 – 97

84

RRM 1

Domain

105 – 184

80

RRM 2

Region

4 – 94

91

Globular A domain

Region

95 – 185

91

Globular B domain

Region

218 – 240

23

RNA-binding RGG-box

Region

320 – 357

38

Nuclear targeting sequence (M9)

Compositional bias

195 – 372

178

Gly-rich

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.9

Modified residue

3

1

N6-acetyllysine Ref.34

Modified residue

4

1

Phosphoserine Ref.21 Ref.29

Modified residue

6

1

Phosphoserine Ref.21 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31

Modified residue

91

1

Phosphoserine Ref.27

Modified residue

95

1

Phosphoserine Ref.27

Modified residue

113

1

N6-acetyllysine Ref.34

Modified residue

138

1

Phosphothreonine Ref.20

Modified residue

142

1

Phosphoserine Ref.31

Modified residue

167

1

Phosphotyrosine Ref.27

Modified residue

192

1

Phosphoserine; by MKNK2 Ref.18

Modified residue

194

1

Omega-N-methylated arginine Ref.16

Modified residue

206

1

Dimethylated arginine; alternate Ref.9 Ref.16

Modified residue

206

1

Omega-N-methylarginine; alternate Ref.9 Ref.16

Modified residue

225

1

Dimethylated arginine; alternate Ref.9 Ref.16

Modified residue

225

1

Omega-N-methylarginine; alternate Ref.9 Ref.16

Modified residue

311

1

Phosphoserine By similarity

Modified residue

338

1

Phosphoserine Ref.27

Modified residue

341

1

Phosphotyrosine Ref.33

Modified residue

347

1

Phosphotyrosine Ref.19 Ref.23

Modified residue

350

1

N6-acetyllysine Ref.22 Ref.34

Modified residue

357

1

Phosphotyrosine Ref.32 Ref.33

Modified residue

360

1

Phosphoserine Ref.32

Modified residue

361

1

Phosphoserine Ref.32

Modified residue

362

1

Phosphoserine; by MKNK2 Ref.18 Ref.32

Modified residue

363

1

Phosphoserine; by MKNK2 Ref.18 Ref.32

Modified residue

364

1

Phosphoserine; by MKNK2 Ref.18 Ref.32

Modified residue

365

1

Phosphoserine Ref.32

Modified residue

368

1

Phosphoserine Ref.31 Ref.32

Cross-link

113

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.17

Natural variations

Alternative sequence

203 – 307

105

Missing in isoform 2.

VSP_034076

Alternative sequence

252 – 303

52

Missing in isoform A1-A.

VSP_005824

Natural variant

73

1

N → S.
Corresponds to variant rs6533 [ dbSNP | Ensembl ].

VAR_014711

Experimental info

Mutagenesis

326

1

G → A: No nuclear import nor export. Ref.12

Mutagenesis

327

1

P → A: No nuclear import nor export. Ref.12

Mutagenesis

334 – 335

2

GG → LL: Normal nuclear import and export.

Sequence conflict

128

1

Y → F in CAA29922. Ref.2

Sequence conflict

140

1

R → P in CAA27874. Ref.8

Sequence conflict

146

1

R → K in CAA29922. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

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.

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.

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.

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.

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372

Helix Strand Turn

Details...

Helix

11 – 14

4

Beta strand

15 – 20

6

Helix

27 – 34

8

Helix

35 – 37

3

Beta strand

40 – 47

8

Turn

49 – 51

3

Beta strand

54 – 64

11

Helix

65 – 73

9

Beta strand

85 – 88

4

Beta strand

105 – 110

6

Turn

113 – 115

3

Helix

118 – 125

8

Turn

126 – 128

3

Beta strand

131 – 138

8

Turn

140 – 142

3

Beta strand

145 – 155

11

Helix

156 – 164

9

Beta strand

176 – 179

4

Helix

183 – 189

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform A1-B [UniParc]. Last modified February 9, 2010. Version 5. Checksum: A06683571C6C109F	FASTA	372	38,747
	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
	Isoform A1-A [UniParc]. Checksum: 59485C9FA1FF8AE1	FASTA	320	34,196
	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 GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR 310 320 NQGGYGGSSS SSSYGSGRRF
	Isoform 2 [UniParc]. Checksum: 2B492EF73FD41977	FASTA	267	29,386
	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 NFGGGSYNDF GNYNNQSSNF GPMKGGNFGG RSSGPYGGGG 250 260 QYFAKPRNQG GYGGSSSSSS YGSGRRF

References

	« Hide 'large scale' referencesShow '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: 2760922] [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: 2836799] [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. , 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: 14702039] [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. , 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: 16541075] [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. , 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: 15489334] [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: 3023065] [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, 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, 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: 1691095] [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: 7730395] [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: 8521471] [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: 7769000] [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: 11991638] [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: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-194; ARG-206 AND ARG-225, MASS SPECTROMETRY. 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: 15161980] [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: 16111636] [Abstract] Cited for: PHOSPHORYLATION AT SER-192; SER-362; SER-363 AND SER-364 BY MKNK2.
[19]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-347, MASS SPECTROMETRY.
[20]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138, MASS SPECTROMETRY. Tissue: Hepatoma.
[21]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-6, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-347, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[24]	"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: 17229681] [Abstract] Cited for: INTERACTION WITH SEPT6 AND HCV NS5B, FUNCTION, SUBCELLULAR LOCATION.
[25]	"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: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[26]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-91; SER-95; TYR-167 AND SER-338, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[28]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[31]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-142 AND SER-368, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[32]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-357; SER-360; SER-361; SER-362; SER-363; SER-364; SER-365 AND SER-368, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[33]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-341 AND TYR-357, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[34]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-113 AND LYS-350, MASS SPECTROMETRY.
[35]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]	"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: 2176620] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 107-190.
[37]	"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: 9164463] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 9-181.
[38]	"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: 9115444] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-182.
+	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.

IPI

IPI00215965.
IPI00465365.
IPI00797148.

PIR

S02061.
S12520.

RefSeq

NP_002127.1. NM_002136.2.
NP_112420.1. NM_031157.2.

UniGene

Hs.546261.
Hs.655424.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HA1	X-ray	1.75	A	1-184	[»]
1L3K	X-ray	1.10	A	1-196	[»]
1PGZ	X-ray	2.60	A	2-195	[»]
1PO6	X-ray	2.10	A	8-189	[»]
1U1K	X-ray	2.00	A	1-196	[»]
1U1L	X-ray	2.00	A	1-196	[»]
1U1M	X-ray	2.00	A	1-196	[»]
1U1N	X-ray	2.10	A	1-196	[»]
1U1O	X-ray	2.00	A	1-196	[»]
1U1P	X-ray	1.90	A	1-196	[»]
1U1Q	X-ray	1.80	A	1-196	[»]
1U1R	X-ray	1.80	A	1-196	[»]
1UP1	X-ray	1.90	A	3-184	[»]
2H4M	X-ray	3.05	C/D	309-357	[»]
2UP1	X-ray	2.10	A	8-190	[»]

ProteinModelPortal

P09651.

SMR

P09651. Positions 8-190.

DisProt

DP00324.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29338N.

IntAct

P09651. 51 interactions.

MINT

MINT-1035550.

STRING

P09651.

PTM databases

PhosphoSite

P09651.

Polymorphism databases

DMDM

288558857.

2D gel databases

SWISS-2DPAGE

P09651.

Aarhus/Ghent-2DPAGE

207. NEPHGE.
2114. NEPHGE.
3612. NEPHGE.

Proteomic databases

PRIDE

P09651.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000340913; ENSP00000341826; ENSG00000135486.
ENST00000420780; ENSP00000391986; ENSG00000135486.

GeneID

3178.

KEGG

hsa:3178.

UCSC

uc001sfl.1. human.
uc001sfn.1. human.
uc009zng.1. human.

Organism-specific databases

CTD

3178.

GeneCards

GC12P054674.

HGNC

HGNC:5031. HNRNPA1.

HPA

CAB010894.
HPA001666.

MIM

164017. gene.

neXtProt

NX_P09651.

PharmGKB

PA162391113.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15016.

GeneTree

ENSGT00550000074566.

HOGENOM

HBG756718.

HOVERGEN

HBG002295.

InParanoid

P09651.

OMA

IEVEIMT.

OrthoDB

EOG4HQDKF.

PhylomeDB

P09651.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P09651.

Bgee

P09651.

CleanEx

HS_HNRNPA1.

Genevestigator

P09651.

GermOnline

ENSG00000135486. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

KO

K12741.

Pfam

PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

12614.

SOURCE

Search...

Entry information

Entry name

ROA1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 168 of the entry and version 5 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.