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Q99020

- ROAA_MOUSE

UniProt

Q99020 - ROAA_MOUSE

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Protein

Heterogeneous nuclear ribonucleoprotein A/B

Gene

Hnrnpab

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. 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: Chromosome 11

Organism-specific databases

MGIiMGI:1330294. Hnrnpab.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. nucleus Source: HGNC
  3. ribonucleoprotein complex Source: UniProtKB
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 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 .
CCDSi CCDS24654.1.
PIRi JQ0448.
RefSeqi NP_034578.1. NM_010448.3.
UniGenei Mm.256875.
Mm.280842.

3D structure databases

ProteinModelPortali Q99020.
SMRi Q99020. Positions 70-237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200358. 6 interactions.
DIPi DIP-31415N.
IntActi Q99020. 9 interactions.
MINTi MINT-4132837.

PTM databases

PhosphoSitei Q99020.

Proteomic databases

MaxQBi Q99020.
PaxDbi Q99020.
PRIDEi Q99020.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000074669 ; ENSMUSP00000074238 ; ENSMUSG00000020358 .
GeneIDi 15384.
KEGGi mmu:15384.
UCSCi uc007iua.1. mouse.

Organism-specific databases

CTDi 3182.
MGIi MGI:1330294. Hnrnpab.

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00760000118873.
HOGENOMi HOG000234441.
HOVERGENi HBG002295.
InParanoidi Q99020.
KOi K13044.
OrthoDBi EOG715Q6V.

Miscellaneous databases

ChiTaRSi Hnrnpab. mouse.
NextBioi 288056.
PROi Q99020.
SOURCEi Search...

Gene expression databases

Bgeei Q99020.
ExpressionAtlasi Q99020. baseline and differential.
Genevestigatori Q99020.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR012956. CARG-binding_factor_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 131 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