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Q99729 (ROAA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein A/B

Short name=hnRNP A/B
Alternative name(s):
APOBEC1-binding protein 1
Short name=ABBP-1
Gene names
Name:HNRNPAB
Synonyms:ABBP1, HNRPAB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds single-stranded RNA. Has a high affinity for G-rich and U-rich regions of hnRNA. Also binds to APOB mRNA transcripts around the RNA editing site.

Subunit structure

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with APOBEC1. Ref.9

Subcellular location

Nucleus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.9

Tissue specificity

Ubiquitous.

Post-translational modification

Dimethylation at Arg-322 is probably asymmetric.

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAC50956.1 differs from that shown. Reason: Frameshift at positions 296, 307 and 330.

Isoform 4: The sequence AAA36575.1 differs from that shown. Reason: Frameshift at several positions.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99729-1)

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: Q99729-2)

The sequence of this isoform differs from the canonical sequence as follows:
     26-32: ASRGRGW → GESPAGAG
     164-165: SP → A
Isoform 3 (identifier: Q99729-3)

The sequence of this isoform differs from the canonical sequence as follows:
     26-32: ASRGRGW → GESPAGAG
     164-165: SP → A
     264-310: Missing.
Note: Contains a N6-acetyllysine at position 271. Contains a phosphoserine at position 255.
Isoform 4 (identifier: Q99729-4)

The sequence of this isoform differs from the canonical sequence as follows:
     26-32: ASRGRGW → GESPAGAG
     264-310: Missing.
Note: Contains a N6-acetyllysine at position 272. Contains a phosphoserine at position 256.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Heterogeneous nuclear ribonucleoprotein A/B
PRO_0000081492

Regions

Domain69 – 15486RRM 1
Domain153 – 23381RRM 2
Compositional bias241 – 32484Gly-rich

Amino acid modifications

Modified residue2151N6-acetyllysine By similarity
Modified residue2421Phosphoserine Ref.8 Ref.11 Ref.14 Ref.16
Modified residue2451Dimethylated arginine; alternate Ref.6
Modified residue2451Omega-N-methylarginine; alternate Ref.6
Modified residue3181N6-acetyllysine By similarity
Modified residue3221Dimethylated arginine Ref.7

Natural variations

Alternative sequence26 – 327ASRGRGW → GESPAGAG in isoform 2, isoform 3 and isoform 4.
VSP_007826
Alternative sequence164 – 1652SP → A in isoform 2 and isoform 3.
VSP_007828
Alternative sequence264 – 31047Missing in isoform 3 and isoform 4.
VSP_007829

Secondary structure

.................. 332
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: F824A7E08D15268A

FASTA33236,225
        10         20         30         40         50         60 
MSEAGEEQPM ETTGATENGH EAVPEASRGR GWTGAAAGAG GATAAPPSGN QNGAEGDQIN 

        70         80         90        100        110        120 
ASKNEEDAGK MFVGGLSWDT SKKDLKDYFT KFGEVVDCTI KMDPNTGRSR GFGFILFKDA 

       130        140        150        160        170        180 
ASVEKVLDQK EHRLDGRVID PKKAMAMKKD PVKKIFVGGL NPESPTEEKI REYFGEFGEI 

       190        200        210        220        230        240 
EAIELPMDPK LNKRRGFVFI TFKEEEPVKK VLEKKFHTVS GSKCEIKVAQ PKEVYQQQQY 

       250        260        270        280        290        300 
GSGGRGNRNR GNRGSGGGGG GGGQSQSWNQ GYGNYWNQGY GYQQGYGPGY GGYDYSPYGY 

       310        320        330 
YGYGPGYDYS QGSTNYGKSQ RRGGHQNNYK PY 

« Hide

Isoform 2 [UniParc].

Checksum: F710B690D495500D
Show »

FASTA33235,968
Isoform 3 [UniParc].

Checksum: 3E4F386C2F5B9705
Show »

FASTA28530,588
Isoform 4 [UniParc].

Checksum: AA24BA3F6A0BAD62
Show »

FASTA28630,701

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of a human type A/B hnRNP protein."
Khan F., Jaiswal A.K., Szer W.
FEBS Lett. 290:159-161(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[2]"Cloning of an Apobec-1-binding protein that also interacts with apolipoprotein B mRNA and evidence for its involvement in RNA editing."
Lau P.P., Zhu H.J., Nakamuta M., Chan L.
J. Biol. Chem. 272:1452-1455(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"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] (ISOFORMS 2 AND 3).
Tissue: Testis.
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 2 AND 3).
Tissue: Placenta, Skin and Uterus.
[6]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 71-101; 111-118; 170-190; 196-203 AND 233-248, METHYLATION AT ARG-245, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[7]"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-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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-271 (ISOFORM 3), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"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-242, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65028 mRNA. Translation: AAA36575.1. Frameshift.
U76713 mRNA. Translation: AAC50956.1. Frameshift.
AK054600 mRNA. Translation: BAG51397.1.
AK097657 mRNA. Translation: BAC05134.1.
CH471165 Genomic DNA. Translation: EAW53843.1.
CH471165 Genomic DNA. Translation: EAW53844.1.
CH471165 Genomic DNA. Translation: EAW53845.1.
BC001616 mRNA. Translation: AAH01616.1.
BC002625 mRNA. Translation: AAH02625.1.
BC004561 mRNA. Translation: AAH04561.1.
BC009359 mRNA. Translation: AAH09359.1.
BC036708 mRNA. Translation: AAH36708.1.
PIRS17563.
RefSeqNP_004490.2. NM_004499.3.
NP_112556.2. NM_031266.2.
UniGeneHs.591731.
Hs.715055.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S7RX-ray2.15A/B59-144[»]
ProteinModelPortalQ99729.
SMRQ99729. Positions 24-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109423. 60 interactions.
IntActQ99729. 32 interactions.
MINTMINT-4537784.
STRING9606.ENSP00000351108.

PTM databases

PhosphoSiteQ99729.

Polymorphism databases

DMDM158523286.

2D gel databases

SWISS-2DPAGEQ99729.

Proteomic databases

PaxDbQ99729.
PRIDEQ99729.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355836; ENSP00000348093; ENSG00000197451. [Q99729-3]
ENST00000358344; ENSP00000351108; ENSG00000197451. [Q99729-2]
ENST00000504898; ENSP00000425031; ENSG00000197451. [Q99729-2]
ENST00000506259; ENSP00000427465; ENSG00000197451. [Q99729-3]
GeneID3182.
KEGGhsa:3182.
UCSCuc003miu.3. human. [Q99729-2]
uc003miv.3. human. [Q99729-3]

Organism-specific databases

CTD3182.
GeneCardsGC05P177631.
HGNCHGNC:5034. HNRNPAB.
HPAHPA046688.
MIM602688. gene.
neXtProtNX_Q99729.
PharmGKBPA162391196.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000234441.
HOVERGENHBG002295.
InParanoidQ99729.
KOK13044.
OMAFIFITYK.
OrthoDBEOG715Q6V.
PhylomeDBQ99729.
TreeFamTF314808.

Gene expression databases

ArrayExpressQ99729.
BgeeQ99729.
CleanExHS_HNRNPAB.
GenevestigatorQ99729.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012956. CARG-binding_factor_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPAB. human.
EvolutionaryTraceQ99729.
GeneWikiHNRPAB.
GenomeRNAi3182.
NextBio12628.
PROQ99729.
SOURCESearch...

Entry information

Entry nameROAA_HUMAN
AccessionPrimary (citable) accession number: Q99729
Secondary accession number(s): B3KNN5 expand/collapse secondary AC list , D3DWP7, Q04150, Q8N7U3, Q9BQ99
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 131 of the entry and version 2 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 chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM