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Protein

Pre-mRNA-splicing factor RBM22

Gene

Rbm22

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri159 – 18628C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium-dependent protein binding Source: MGI
  2. metal ion binding Source: UniProtKB-KW
  3. nucleocytoplasmic transporter activity Source: UniProtKB
  4. nucleotide binding Source: InterPro
  5. poly(A) RNA binding Source: MGI
  6. pre-mRNA binding Source: UniProtKB
  7. snRNA binding Source: UniProtKB

GO - Biological processi

  1. cellular response to drug Source: UniProtKB
  2. mRNA cis splicing, via spliceosome Source: UniProtKB
  3. positive regulation of intracellular protein transport Source: UniProtKB
  4. positive regulation of RNA splicing Source: UniProtKB
  5. protein import into nucleus, translocation Source: MGI
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Transport

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor RBM22
Alternative name(s):
RNA-binding motif protein 22
Gene namesi
Name:Rbm22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1914060. Rbm22.

Subcellular locationi

  1. Nucleus By similarity
  2. Cytoplasm By similarity

  3. 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).By similarity

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: MGI
  2. cytoplasm Source: UniProtKB
  3. nucleoplasm Source: MGI
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 420419Pre-mRNA-splicing factor RBM22PRO_0000250548Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei212 – 2121N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BHS3.
PaxDbiQ8BHS3.
PRIDEiQ8BHS3.

PTM databases

PhosphoSiteiQ8BHS3.

Expressioni

Gene expression databases

BgeeiQ8BHS3.
CleanExiMM_RBM22.
GenevestigatoriQ8BHS3.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ8BHS3. 1 interaction.
MINTiMINT-4110604.
STRINGi10090.ENSMUSP00000025506.

Structurei

3D structure databases

ProteinModelPortaliQ8BHS3.
SMRiQ8BHS3. Positions 165-304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini232 – 30574RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi327 – 40781Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the SLT11 family.Curated
Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri159 – 18628C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG277760.
GeneTreeiENSGT00390000002792.
HOGENOMiHOG000171086.
HOVERGENiHBG083475.
InParanoidiQ8BHS3.
KOiK12872.
OMAiMPPQIKH.
OrthoDBiEOG7K0ZCH.
TreeFamiTF314284.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BHS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR
60 70 80 90 100
PFTVFRWCPG VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG
110 120 130 140 150
LSFKDDMPKS DVNKEYYTQN MEREISNSDG TRPVGMLGKA TSTSDMLLKL
160 170 180 190 200
ARTTPYYKRN RPHICSFWVK GECKRGEECP YRHEKPTDPD DPLADQNIKD
210 220 230 240 250
RYYGINDPVA DKLLKRASTM PRLDPPEDKT ITTLYVGGLG DTITETDLRN
260 270 280 290 300
HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK LIVNGRRLNV
310 320 330 340 350
KWGRSQAARG KEKEKDGTTD SGIKLEPVPG LPGALPPPPA AEEEASANYF
360 370 380 390 400
NLPPSGPPAV VNIALPPPPG IAPPPPPGFG PHMFHPMGPP PPFMRAPGPI
410 420
HYPSQDPQRM GAHAGKHSSP
Length:420
Mass (Da):46,896
Last modified:March 1, 2003 - v1
Checksum:iA82549D8CC88C7D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711G → R in BAE39585 (PubMed:16141072).Curated
Sequence conflicti339 – 3391P → L in BAB31220 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29272.1.
RefSeqiNP_080052.1. NM_025776.2.
UniGeneiMm.275106.

Genome annotation databases

EnsembliENSMUST00000025506; ENSMUSP00000025506; ENSMUSG00000024604.
GeneIDi66810.
KEGGimmu:66810.
UCSCiuc008fal.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29272.1.
RefSeqiNP_080052.1. NM_025776.2.
UniGeneiMm.275106.

3D structure databases

ProteinModelPortaliQ8BHS3.
SMRiQ8BHS3. Positions 165-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BHS3. 1 interaction.
MINTiMINT-4110604.
STRINGi10090.ENSMUSP00000025506.

PTM databases

PhosphoSiteiQ8BHS3.

Proteomic databases

MaxQBiQ8BHS3.
PaxDbiQ8BHS3.
PRIDEiQ8BHS3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025506; ENSMUSP00000025506; ENSMUSG00000024604.
GeneIDi66810.
KEGGimmu:66810.
UCSCiuc008fal.1. mouse.

Organism-specific databases

CTDi55696.
MGIiMGI:1914060. Rbm22.

Phylogenomic databases

eggNOGiNOG277760.
GeneTreeiENSGT00390000002792.
HOGENOMiHOG000171086.
HOVERGENiHBG083475.
InParanoidiQ8BHS3.
KOiK12872.
OMAiMPPQIKH.
OrthoDBiEOG7K0ZCH.
TreeFamiTF314284.

Miscellaneous databases

ChiTaRSiRbm22. mouse.
NextBioi322703.
PROiQ8BHS3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BHS3.
CleanExiMM_RBM22.
GenevestigatoriQ8BHS3.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiRBM22_MOUSE
AccessioniPrimary (citable) accession number: Q8BHS3
Secondary accession number(s): Q3TJB0, Q9CXA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2003
Last modified: March 4, 2015
This is version 107 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, 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.