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Q9NW64 (RBM22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
Zinc finger CCCH domain-containing protein 16
Gene names
Name:RBM22
Synonyms:ZC3H16
ORF Names:199G4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.8 Ref.13 Ref.14

Subunit structure

Identified in the spliceosome C complex. Interacts with PDCD6; the interaction induces translocation of PDCD6 in the cytoplasm. Ref.7 Ref.8

Subcellular location

Nucleus. Cytoplasm. 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. Ref.8 Ref.10 Ref.13

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.

Sequence caution

The sequence AAC99998.1 differs from that shown. Reason: Chimera.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transport
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to drug

Inferred from direct assay Ref.13. Source: UniProtKB

mRNA cis splicing, via spliceosome

Inferred from direct assay Ref.14. Source: UniProtKB

mRNA splicing, via spliceosome

Inferred by curator Ref.7. Source: UniProtKB

positive regulation of RNA splicing

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of intracellular protein transport

Inferred from direct assay Ref.13. Source: UniProtKB

protein import into nucleus, translocation

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.7. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.13. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11278427Ref.8Ref.13. Source: UniProtKB

   Molecular_functioncalcium-dependent protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleocytoplasmic transporter activity

Inferred from direct assay Ref.13. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

pre-mRNA binding

Inferred from direct assay Ref.14. Source: UniProtKB

snRNA binding

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRNPP041561EBI-2602260,EBI-977302

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NW64-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NW64-2)

The sequence of this isoform differs from the canonical sequence as follows:
     43-91: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 420419Pre-mRNA-splicing factor RBM22
PRO_0000250546

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.15 Ref.16
Modified residue2121N6-acetyllysine Ref.11

Natural variations

Alternative sequence43 – 9149Missing in isoform 2.
VSP_036832

Experimental info

Mutagenesis1701K → R: Accumulates in speckle-like structures. Ref.10
Mutagenesis3241K → R: Accumulates in speckle-like structures. Ref.10

Secondary structure

................ 420
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. 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

Isoform 2 [UniParc].

Checksum: CD43CE9BAD03CE15
Show »

FASTA37141,152

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Mammary gland and Umbilical cord blood.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Placenta.
[6]"Transcriptional map of the Treacher Collins candidate gene region."
Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J.
Genome Res. 6:26-34(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-420.
Tissue: Brain.
[7]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[8]"Nuclear translocation of the calcium-binding protein ALG-2 induced by the RNA-binding protein RBM22."
Montaville P., Dai Y., Cheung C.Y., Giller K., Becker S., Michalak M., Webb S.E., Miller A.L., Krebs J.
Biochim. Biophys. Acta 1763:1335-1343(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PDCD6.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"The influence of calcium signaling on the regulation of alternative splicing."
Krebs J.
Biochim. Biophys. Acta 1793:979-984(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-170 AND LYS-324.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7."
Janowicz A., Michalak M., Krebs J.
Biochim. Biophys. Acta 1813:1045-1049(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre."
Rasche N., Dybkov O., Schmitzova J., Akyildiz B., Fabrizio P., Luhrmann R.
EMBO J. 31:1591-1604(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[15]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Solution structure of RNA binding domain in pre-mRNA-splicing factor RBM22."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 227-304.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL136933 mRNA. Translation: CAB66867.1.
AK001152 mRNA. Translation: BAA91521.1.
AK297019 mRNA. Translation: BAG59551.1.
AC008453 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61711.1.
BC003402 mRNA. Translation: AAH03402.1.
U39402 mRNA. Translation: AAC99998.1. Sequence problems.
CCDSCCDS34278.1. [Q9NW64-1]
RefSeqNP_060517.1. NM_018047.2. [Q9NW64-1]
UniGeneHs.713564.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YTCNMR-A227-304[»]
ProteinModelPortalQ9NW64.
SMRQ9NW64. Positions 165-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120821. 15 interactions.
IntActQ9NW64. 11 interactions.
MINTMINT-2819539.
STRING9606.ENSP00000199814.

PTM databases

PhosphoSiteQ9NW64.

Polymorphism databases

DMDM74762758.

Proteomic databases

MaxQBQ9NW64.
PaxDbQ9NW64.
PRIDEQ9NW64.

Protocols and materials databases

DNASU55696.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000199814; ENSP00000199814; ENSG00000086589. [Q9NW64-1]
ENST00000447771; ENSP00000412118; ENSG00000086589. [Q9NW64-2]
GeneID55696.
KEGGhsa:55696.
UCSCuc003lst.3. human. [Q9NW64-1]

Organism-specific databases

CTD55696.
GeneCardsGC05M150050.
HGNCHGNC:25503. RBM22.
HPAHPA001634.
MIM612430. gene.
neXtProtNX_Q9NW64.
PharmGKBPA134982384.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277760.
HOGENOMHOG000171086.
HOVERGENHBG083475.
InParanoidQ9NW64.
KOK12872.
OMAHSRYGNG.
OrthoDBEOG7K0ZCH.
PhylomeDBQ9NW64.
TreeFamTF314284.

Gene expression databases

ArrayExpressQ9NW64.
BgeeQ9NW64.
CleanExHS_RBM22.
GenevestigatorQ9NW64.

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

EvolutionaryTraceQ9NW64.
GeneWikiRBM22.
GenomeRNAi55696.
NextBio60521.
PROQ9NW64.
SOURCESearch...

Entry information

Entry nameRBM22_HUMAN
AccessionPrimary (citable) accession number: Q9NW64
Secondary accession number(s): A6NDM5, B4DLI9, O95607
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM