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Protein

Heterogeneous nuclear ribonucleoprotein A/B

Gene

Hnrnpab

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

Functioni

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.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: MGI
  4. RNA binding Source: MGI

GO - Biological processi

  1. epithelial to mesenchymal transition Source: HGNC
  2. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  3. positive regulation of transcription, DNA-templated Source: HGNC
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein A/B
Short name:
hnRNP A/B
Alternative name(s):
CArG-binding factor-A
Short name:
CBF-A
Gene namesi
Name:Hnrnpab
Synonyms:Cbf-a, Cgbfa, Hnrpab
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1330294. Hnrnpab.

Subcellular locationi

  1. Nucleus Curated
  2. Cytoplasm By similarity

  3. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. nucleoplasm Source: MGI
  3. nucleus Source: HGNC
  4. ribonucleoprotein complex Source: UniProtKB
  5. RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Heterogeneous nuclear ribonucleoprotein A/BPRO_0000081493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871PhosphoserineBy similarity
Modified residuei220 – 2201N6-acetyllysine1 Publication
Modified residuei247 – 2471PhosphoserineBy similarity
Modified residuei250 – 2501Dimethylated arginine; alternateBy similarity
Modified residuei250 – 2501Omega-N-methylarginine; alternateBy similarity
Modified residuei271 – 2711N6-acetyllysine1 Publication
Modified residuei275 – 2751Dimethylated arginineBy similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ99020.
PaxDbiQ99020.
PRIDEiQ99020.

PTM databases

PhosphoSiteiQ99020.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ99020.
ExpressionAtlasiQ99020. baseline and differential.
GenevestigatoriQ99020.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi200358. 6 interactions.
DIPiDIP-31415N.
IntActiQ99020. 9 interactions.
MINTiMINT-4132837.

Structurei

3D structure databases

ProteinModelPortaliQ99020.
SMRiQ99020. Positions 70-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 15884RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini159 – 23880RRM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 4310Poly-Ala
Compositional biasi246 – 27732Gly-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234441.
HOVERGENiHBG002295.
InParanoidiQ99020.
KOiK13044.
OrthoDBiEOG715Q6V.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012956. CARG-binding_factor_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99020-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDAAEEQPM ETTGATENGH EAAPEGEAPV EPSAAAAAPA ASAGSGGGTT
60 70 80 90 100
TAPSGNQNGA EGDQINASKN EEDAGKMFVG GLSWDTSKKD LKDYFTKFGE
110 120 130 140 150
VVDCTIKMDP NTGRSRGFGF ILFKDSSSVE KVLDQKEHRL DGRVIDPKKA
160 170 180 190 200
MAMKKDPVKK IFVGGLNPEA TEEKIREYFG QFGEIEAIEL PIDPKLNKRR
210 220 230 240 250
GFVFITFKEE DPVKKVLEKK FHTVSGSKCE IKVAQPKEVY QQQQYGSGGR
260 270 280
GNRNRGNRGS GGGQGSTNYG KSQRRGGHQN NYKPY
Length:285
Mass (Da):30,831
Last modified:February 1, 1995 - v1
Checksum:i7881F34131160E0C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261G → S in BAC36208 (PubMed:16141072).Curated
Sequence conflicti41 – 411A → R in BAC36208 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90151 mRNA. Translation: BAA14181.1.
L36663 mRNA. Translation: AAA92146.1.
AK076132 mRNA. Translation: BAC36208.1.
CCDSiCCDS24654.1.
PIRiJQ0448.
RefSeqiNP_034578.1. NM_010448.3.
UniGeneiMm.256875.
Mm.280842.

Genome annotation databases

EnsembliENSMUST00000074669; ENSMUSP00000074238; ENSMUSG00000020358.
GeneIDi15384.
KEGGimmu:15384.
UCSCiuc007iua.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90151 mRNA. Translation: BAA14181.1.
L36663 mRNA. Translation: AAA92146.1.
AK076132 mRNA. Translation: BAC36208.1.
CCDSiCCDS24654.1.
PIRiJQ0448.
RefSeqiNP_034578.1. NM_010448.3.
UniGeneiMm.256875.
Mm.280842.

3D structure databases

ProteinModelPortaliQ99020.
SMRiQ99020. Positions 70-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200358. 6 interactions.
DIPiDIP-31415N.
IntActiQ99020. 9 interactions.
MINTiMINT-4132837.

PTM databases

PhosphoSiteiQ99020.

Proteomic databases

MaxQBiQ99020.
PaxDbiQ99020.
PRIDEiQ99020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074669; ENSMUSP00000074238; ENSMUSG00000020358.
GeneIDi15384.
KEGGimmu:15384.
UCSCiuc007iua.1. mouse.

Organism-specific databases

CTDi3182.
MGIiMGI:1330294. Hnrnpab.

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234441.
HOVERGENiHBG002295.
InParanoidiQ99020.
KOiK13044.
OrthoDBiEOG715Q6V.

Miscellaneous databases

ChiTaRSiHnrnpab. mouse.
NextBioi288056.
PROiQ99020.
SOURCEiSearch...

Gene expression databases

BgeeiQ99020.
ExpressionAtlasiQ99020. baseline and differential.
GenevestigatoriQ99020.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012956. CARG-binding_factor_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiROAA_MOUSE
AccessioniPrimary (citable) accession number: Q99020
Secondary accession number(s): Q8BPE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: March 4, 2015
This is version 134 of the entry and version 1 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

External Data

Dasty 3

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 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.