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Q99020 (ROAA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
CArG-binding factor-A
Short name=CBF-A
Gene names
Name:Hnrnpab
Synonyms:Cbf-a, Cgbfa, Hnrpab
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor. Binds to CArG box motifs, single-stranded and double-stranded DNA, and RNA. It may be that repression by CBF-A is a result of competitive binding of CBF, a putative positive factor, and CBF-A to the same or overlapping motifs around the CArG boxes.

Subunit structure

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

Subcellular location

Nucleus Probable. Cytoplasm By similarity. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs By similarity.

Tissue specificity

Ubiquitous.

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Heterogeneous nuclear ribonucleoprotein A/B
PRO_0000081493

Regions

Domain75 – 15884RRM 1
Domain159 – 23880RRM 2
Compositional bias34 – 4310Poly-Ala
Compositional bias246 – 27732Gly-rich

Amino acid modifications

Modified residue2201N6-acetyllysine Ref.4
Modified residue2471Phosphoserine By similarity
Modified residue2501Dimethylated arginine; alternate By similarity
Modified residue2501Omega-N-methylarginine; alternate By similarity
Modified residue2711N6-acetyllysine Ref.4
Modified residue2751Dimethylated arginine By similarity

Experimental info

Sequence conflict261G → S in BAC36208. Ref.2
Sequence conflict411A → R in BAC36208. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99020 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 7881F34131160E0C

FASTA28530,831
        10         20         30         40         50         60 
MSDAAEEQPM ETTGATENGH EAAPEGEAPV EPSAAAAAPA ASAGSGGGTT TAPSGNQNGA 

        70         80         90        100        110        120 
EGDQINASKN EEDAGKMFVG GLSWDTSKKD LKDYFTKFGE VVDCTIKMDP NTGRSRGFGF 

       130        140        150        160        170        180 
ILFKDSSSVE KVLDQKEHRL DGRVIDPKKA MAMKKDPVKK IFVGGLNPEA TEEKIREYFG 

       190        200        210        220        230        240 
QFGEIEAIEL PIDPKLNKRR GFVFITFKEE DPVKKVLEKK FHTVSGSKCE IKVAQPKEVY 

       250        260        270        280 
QQQQYGSGGR GNRNRGNRGS GGGQGSTNYG KSQRRGGHQN NYKPY 

« Hide

References

« Hide 'large scale' references
[1]"A protein binding to CArG box motifs and to single-stranded DNA functions as a transcriptional repressor."
Kamada S., Miwa T.
Gene 119:229-236(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.
[2]"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. expand/collapse author list , 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.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 117-124; 161-174; 177-195 AND 201-208, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[4]"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-220 AND LYS-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90151 mRNA. Translation: BAA14181.1.
L36663 mRNA. Translation: AAA92146.1.
AK076132 mRNA. Translation: BAC36208.1.
CCDSCCDS24654.1.
PIRJQ0448.
RefSeqNP_034578.1. NM_010448.3.
UniGeneMm.256875.
Mm.280842.

3D structure databases

ProteinModelPortalQ99020.
SMRQ99020. Positions 70-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200358. 6 interactions.
DIPDIP-31415N.
IntActQ99020. 8 interactions.
MINTMINT-4132837.

PTM databases

PhosphoSiteQ99020.

Proteomic databases

MaxQBQ99020.
PaxDbQ99020.
PRIDEQ99020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000074669; ENSMUSP00000074238; ENSMUSG00000020358.
GeneID15384.
KEGGmmu:15384.
UCSCuc007iua.1. mouse.

Organism-specific databases

CTD3182.
MGIMGI:1330294. Hnrnpab.

Phylogenomic databases

eggNOGCOG0724.
GeneTreeENSGT00730000110184.
HOGENOMHOG000234441.
HOVERGENHBG002295.
KOK13044.
OrthoDBEOG715Q6V.

Gene expression databases

ArrayExpressQ99020.
BgeeQ99020.
GenevestigatorQ99020.

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. mouse.
NextBio288056.
PROQ99020.
SOURCESearch...

Entry information

Entry nameROAA_MOUSE
AccessionPrimary (citable) accession number: Q99020
Secondary accession number(s): Q8BPE0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot