Q9NW64 (RBM22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Protein existence	Evidence 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.12 Ref.13
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.9 Ref.12
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 process	Transport mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to stress Inferred from direct assay Ref.12. Source: UniProtKB mRNA cis splicing, via spliceosome Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of RNA splicing Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of intracellular protein transport Inferred from direct assay Ref.12. Source: UniProtKB protein import into nucleus, translocation Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.7. Source: UniProtKB cytoplasm Inferred from direct assay Ref.12. Source: UniProtKB
Molecular_function	nucleocytoplasmic transporter activity Inferred from direct assay Ref.12. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro pre-mRNA binding Inferred from direct assay Ref.13. Source: UniProtKB snRNA binding Inferred from direct assay Ref.13. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRNP	P04156	1	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 420

420

Pre-mRNA-splicing factor RBM22

PRO_0000250546

Regions

Domain

232 – 305

74

RRM

Zinc finger

159 – 186

28

C3H1-type

Compositional bias

327 – 407

81

Pro-rich

Amino acid modifications

Modified residue

212

1

N6-acetyllysine Ref.10

Natural variations

Alternative sequence

43 – 91

49

Missing in isoform 2.

VSP_036832

Experimental info

Mutagenesis

170

1

K → R: Accumulates in speckle-like structures. Ref.9

Mutagenesis

324

1

K → R: Accumulates in speckle-like structures. Ref.9

Secondary structure

1

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420

Helix Strand Turn

Details...

Beta strand

234 – 237

4

Turn

240 – 242

3

Helix

245 – 253

9

Beta strand

258 – 264

7

Helix

265 – 267

3

Beta strand

269 – 276

8

Helix

277 – 285

9

Turn

286 – 290

5

Beta strand

300 – 302

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: A82549D8CC88C7D0	FASTA	420	46,896
	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
	Isoform 2 [UniParc]. Checksum: CD43CE9BAD03CE15	FASTA	371	41,152
	10 20 30 40 50 60 MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGLPIQVRDA GLSFKDDMPK 70 80 90 100 110 120 SDVNKEYYTQ NMEREISNSD GTRPVGMLGK ATSTSDMLLK LARTTPYYKR NRPHICSFWV 130 140 150 160 170 180 KGECKRGEEC PYRHEKPTDP DDPLADQNIK DRYYGINDPV ADKLLKRAST MPRLDPPEDK 190 200 210 220 230 240 TITTLYVGGL GDTITETDLR NHFYQFGEIR TITVVQRQQC AFIQFATRQA AEVAAEKSFN 250 260 270 280 290 300 KLIVNGRRLN VKWGRSQAAR GKEKEKDGTT DSGIKLEPVP GLPGALPPPP AAEEEASANY 310 320 330 340 350 360 FNLPPSGPPA VVNIALPPPP GIAPPPPPGF GPHMFHPMGP PPPFMRAPGP IHYPSQDPQR 370 MGAHAGKHSS P

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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]	"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.
[10]	"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, MASS SPECTROMETRY.
[11]	"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].
[12]	"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.
[13]	"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.
[14]	"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.

IPI

IPI00019046.
IPI00909290.

RefSeq

NP_060517.1. NM_018047.2.

UniGene

Hs.713564.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YTC	NMR	-	A	227-304	[»]

ProteinModelPortal

Q9NW64.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NW64. 4 interactions.

STRING

9606.ENSP00000199814.

PTM databases

PhosphoSite

Q9NW64.

Polymorphism databases

DMDM

74762758.

Proteomic databases

PaxDb

Q9NW64.

PRIDE

Q9NW64.

Protocols and materials databases

DNASU

55696.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000199814; ENSP00000199814; ENSG00000086589.
ENST00000447771; ENSP00000412118; ENSG00000086589.

GeneID

55696.

KEGG

hsa:55696.

UCSC

uc003lst.3. human.

Organism-specific databases

CTD

55696.

GeneCards

GC05M150050.

HGNC

HGNC:25503. RBM22.

HPA

HPA001634.

MIM

612430. gene.

neXtProt

NX_Q9NW64.

PharmGKB

PA134982384.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG277760.

HOGENOM

HOG000171086.

HOVERGEN

HBG083475.

InParanoid

Q9NW64.

KO

K12872.

OMA

ILADKAC.

OrthoDB

EOG40S0FW.

Gene expression databases

ArrayExpress

Q9NW64.

Bgee

Q9NW64.

CleanEx

HS_RBM22.

Genevestigator

Q9NW64.

GermOnline

ENSG00000086589. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
[Graphical view]

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9NW64.

GenomeRNAi

55696.

NextBio

60521.

SOURCE

Search...

Entry information

Entry name

RBM22_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.