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Q8BHS3 (RBM22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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:
Pre-mRNA-splicing factor RBM22
Alternative name(s):
RNA-binding motif protein 22
Gene names
Name:Rbm22
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses By similarity.

Subunit structure

Identified in the spliceosome C complex. Interacts with PDCD6; the interaction induces translocation of PDCD6 in the cytoplasm By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Note: Mainly located in the nucleus. Translocated from the nucleus to the cytoplasm after heat shock cell treatment. May be shuttling between the nucleus and the cytosol By similarity.

Domain

The C-terminus RRM domain and the zinc finger motif are necessary for RNA-binding By similarity.

Sequence similarities

Belongs to the SLT11 family.

Contains 1 C3H1-type zinc finger.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transport
   Cellular componentCytoplasm
Nucleus
Spliceosome
   DomainZinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA cis splicing, via spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of RNA splicing

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of intracellular protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

protein import into nucleus, translocation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcatalytic step 2 spliceosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleocytoplasmic transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

pre-mRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

snRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 420419Pre-mRNA-splicing factor RBM22
PRO_0000250548

Regions

Domain232 – 30574RRM
Zinc finger159 – 18628C3H1-type
Compositional bias327 – 40781Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2121N6-acetyllysine Ref.3

Experimental info

Sequence conflict1711G → R in BAE39585. Ref.1
Sequence conflict3391P → L in BAB31220. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BHS3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A82549D8CC88C7D0

FASTA42046,896
        10         20         30         40         50         60 
MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG 

        70         80         90        100        110        120 
VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG LSFKDDMPKS DVNKEYYTQN 

       130        140        150        160        170        180 
MEREISNSDG TRPVGMLGKA TSTSDMLLKL ARTTPYYKRN RPHICSFWVK GECKRGEECP 

       190        200        210        220        230        240 
YRHEKPTDPD DPLADQNIKD RYYGINDPVA DKLLKRASTM PRLDPPEDKT ITTLYVGGLG 

       250        260        270        280        290        300 
DTITETDLRN HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK LIVNGRRLNV 

       310        320        330        340        350        360 
KWGRSQAARG KEKEKDGTTD SGIKLEPVPG LPGALPPPPA AEEEASANYF NLPPSGPPAV 

       370        380        390        400        410        420 
VNIALPPPPG IAPPPPPGFG PHMFHPMGPP PPFMRAPGPI HYPSQDPQRM GAHAGKHSSP 

« Hide

References

[1]"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.
Tissue: Bone marrow, Heart, Lung and Placenta.
[2]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"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-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK018452 mRNA. Translation: BAB31220.1.
AK045116 mRNA. Translation: BAC32229.1.
AK150271 mRNA. Translation: BAE29427.1.
AK151758 mRNA. Translation: BAE30665.1.
AK152252 mRNA. Translation: BAE31073.1.
AK166600 mRNA. Translation: BAE38885.1.
AK167509 mRNA. Translation: BAE39585.1.
AK168919 mRNA. Translation: BAE40732.1.
BC080205 mRNA. Translation: AAH80205.1.
CCDSCCDS29272.1.
RefSeqNP_080052.1. NM_025776.2.
UniGeneMm.275106.

3D structure databases

ProteinModelPortalQ8BHS3.
SMRQ8BHS3. Positions 165-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BHS3. 1 interaction.
MINTMINT-4110604.
STRING10090.ENSMUSP00000025506.

PTM databases

PhosphoSiteQ8BHS3.

Proteomic databases

MaxQBQ8BHS3.
PaxDbQ8BHS3.
PRIDEQ8BHS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025506; ENSMUSP00000025506; ENSMUSG00000024604.
GeneID66810.
KEGGmmu:66810.
UCSCuc008fal.1. mouse.

Organism-specific databases

CTD55696.
MGIMGI:1914060. Rbm22.

Phylogenomic databases

eggNOGNOG277760.
GeneTreeENSGT00390000002792.
HOGENOMHOG000171086.
HOVERGENHBG083475.
InParanoidQ8BHS3.
KOK12872.
OMAHSRYGNG.
OrthoDBEOG7K0ZCH.
TreeFamTF314284.

Gene expression databases

BgeeQ8BHS3.
CleanExMM_RBM22.
GenevestigatorQ8BHS3.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBM22. mouse.
NextBio322703.
PROQ8BHS3.
SOURCESearch...

Entry information

Entry nameRBM22_MOUSE
AccessionPrimary (citable) accession number: Q8BHS3
Secondary accession number(s): Q3TJB0, Q9CXA0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 101 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