Q8CJ67 (STAU2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Double-stranded RNA-binding protein Staufen homolog 2

Gene names

Name:

Stau2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of specific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell body By similarity.
Subunit structure	Interacts with microtubules. Isoform 2 and isoform 3 may also interact with ribosomes, and this association is independent of translation By similarity. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with the exportin XPO5. This requires RNA and RAN bound to GTP. Ref.5
Subcellular location	Cytoplasm. Nucleus. Nucleus › nucleolus. Endoplasmic reticulum. Note: Shuttles between the nucleolus, nucleus and the cytoplasm. Nuclear export of isoform 1 is independent of XPO1/CRM1 and requires the exportin XPO5. Nuclear export of isoform 2 and isoform 3 can occur by both XPO1/CRM1-dependent and XPO1/CRM1-independent pathways. May also be found in large cytoplasmic ribonucleoprotein (RNP) granules which are present in the actin rich regions of myelinating processes and associated with microtubules, polysomes and the endoplasmic reticulum. Also recruited to stress granules (SGs) upon inhibition of translation or oxidative stress. These structures are thought to harbor housekeeping mRNAs when translation is aborted. Ref.5
Tissue specificity	Expressed in brain and neurons, where isoform 2 and isoform 3 appear to be the most abundant. Expressed at the neuromuscular junction of the extensor digitorum longus, tibialis anterior and soleus muscles. Expression at neuromuscular junctions is most pronounced in slow-twitch muscle. Also weakly expressed in heart, kidney, ovary and testis. Ref.1 Ref.4
Induction	Expression in extrasynaptic regions of muscle is induced by denervation. Expression in myoblasts is induced during differentiation into myotubes and by treatment with nerve derived trophic factors such as AGRN (agrin) and NRG1 (neuregulin). Ref.4
Domain	The DRBM 3 domain appears to be the major RNA-binding determinant. This domain also mediates interaction with XPO5 and is required for XPO1/CRM1-independent nuclear export. Ref.1 Ref.5
Sequence similarities	Contains 4 DRBM (double-stranded RNA-binding) domains.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Endoplasmic reticulum Microtubule Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	double-stranded RNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8CJ67-1)

Also known as: Long;

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: Q8CJ67-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
     33-38: GPAHSK → MLQINQ

Isoform 3 (identifier: Q8CJ67-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
     33-38: GPAHSK → MLQINQ
     511-511: A → V
     512-570: Missing.

Isoform 4 (identifier: Q8CJ67-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-305: Missing.
     511-511: A → V
     512-570: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q8CJ67-5)

The sequence of this isoform differs from the canonical sequence as follows:
     92-125: GSITPTVELNGLAMKRGEPAIYRPLDPKPFPNYR → VGKLKETVLSPAHEVMIVGITHYSADNFFLHWCL
     126-570: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 570

570

Double-stranded RNA-binding protein Staufen homolog 2

PRO_0000072247

Regions

Domain

8 – 75

68

DRBM 1

Domain

95 – 181

87

DRBM 2

Domain

207 – 274

68

DRBM 3

Domain

307 – 375

69

DRBM 4

Region

381 – 570

190

Required for dendritic transport By similarity

Motif

273 – 291

19

Nuclear localization signal 1 Ref.5

Motif

373 – 412

40

Nuclear localization signal 2 By similarity

Amino acid modifications

Modified residue

188

1

Phosphoserine By similarity

Modified residue

416

1

Phosphoserine By similarity

Modified residue

440

1

Phosphoserine By similarity

Modified residue

455

1

Phosphoserine By similarity

Modified residue

485

1

Phosphoserine By similarity

Modified residue

486

1

Phosphoserine By similarity

Modified residue

488

1

Phosphothreonine By similarity

Modified residue

492

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 305

305

Missing in isoform 4.

VSP_015378

Alternative sequence

1 – 32

32

Missing in isoform 2 and isoform 3.

VSP_015379

Alternative sequence

33 – 38

6

GPAHSK → MLQINQ in isoform 2 and isoform 3.

VSP_015380

Alternative sequence

92 – 125

34

GSITP…FPNYR → VGKLKETVLSPAHEVMIVGI THYSADNFFLHWCL in isoform 5.

VSP_015381

Alternative sequence

126 – 570

445

Missing in isoform 5.

VSP_015382

Alternative sequence

511

1

A → V in isoform 3 and isoform 4.

VSP_015383

Alternative sequence

512 – 570

59

Missing in isoform 3 and isoform 4.

VSP_015384

Experimental info

Mutagenesis

235

1

H → A: Abrogates RNA-binding by DRBM 3 and interaction with XPO5 and nuclear export; when associated with A-237. Ref.5

Mutagenesis

237

1

K → A: Abrogates RNA-binding by DRBM 3 and interaction with XPO5 and nuclear export; when associated with A-235. Ref.5

Mutagenesis

273 – 274

2

KK → AA: Prevents nuclear localization of mutants lacking DRBM 3 function; when associated with 289-AAA-291.

Mutagenesis

289 – 291

3

KKR → AAA: Prevents nuclear localization of mutants lacking DRBM 3 function; when associated with 257-AA-258. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

570

Helix Strand Turn

Details...

Helix

308 – 318

11

Beta strand

325 – 333

9

Beta strand

339 – 346

8

Beta strand

349 – 357

9

Helix

358 – 373

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 3D7F2DA66B0B8D57	FASTA	570	62,535
	10 20 30 40 50 60 MANPKEKTPV CLVNELARFH SIQPQYKLLN ESGPAHSKMF SVQLSLGEQT WESEGSSIKK 70 80 90 100 110 120 AQQAVANKAL TESTLPKPVQ KPPKSNVNNN PGSITPTVEL NGLAMKRGEP AIYRPLDPKP 130 140 150 160 170 180 FPNYRANYNF RGMYNQRYHC PMPKIFYVQL TVGNNEFFGE GKTRQAARHN AAMKALQALQ 190 200 210 220 230 240 NEPIPEKSPQ NGESGKEMDD DKDANKSEIS LVFEIALKRN MPVSFEVIKE SGPPHMKSFV 250 260 270 280 290 300 TRVSVGEFSA EGEGNSKKLS KKRAATTVLQ ELKKLPPLPV VEKPKLFFKK RPKTIVKAGP 310 320 330 340 350 360 DYGQGMNPIS RLAQIQQARK EKEPDYILLS ERGMPRRREF VMQVKVGNEV ATGTGPNKKI 370 380 390 400 410 420 AKKNAAEAML LQLGYKASTS LQDPLDKTGE NKGWSGPKPG FPEPTNNTPK GILHLSPDVY 430 440 450 460 470 480 QEMEASRHRV TSGTTLSYLS PKDMNQPSSS FFSVSPSSTS SATVARELLM NGTSPTAEAI 490 500 510 520 530 540 GLKGSSPTSP CSSVQPSKQL EYLARIQGFQ AALSALKQFS EQGLESIDGA VNVEKGSLEK 550 560 570 QAKHLREKAD NNQAKPASIS QDCKKSKSAI
	Isoform 2 (Short) [UniParc]. Checksum: 6D746ED7D2A50F93	FASTA	538	59,004
	10 20 30 40 50 60 MLQINQMFSV QLSLGEQTWE SEGSSIKKAQ QAVANKALTE STLPKPVQKP PKSNVNNNPG 70 80 90 100 110 120 SITPTVELNG LAMKRGEPAI YRPLDPKPFP NYRANYNFRG MYNQRYHCPM PKIFYVQLTV 130 140 150 160 170 180 GNNEFFGEGK TRQAARHNAA MKALQALQNE PIPEKSPQNG ESGKEMDDDK DANKSEISLV 190 200 210 220 230 240 FEIALKRNMP VSFEVIKESG PPHMKSFVTR VSVGEFSAEG EGNSKKLSKK RAATTVLQEL 250 260 270 280 290 300 KKLPPLPVVE KPKLFFKKRP KTIVKAGPDY GQGMNPISRL AQIQQARKEK EPDYILLSER 310 320 330 340 350 360 GMPRRREFVM QVKVGNEVAT GTGPNKKIAK KNAAEAMLLQ LGYKASTSLQ DPLDKTGENK 370 380 390 400 410 420 GWSGPKPGFP EPTNNTPKGI LHLSPDVYQE MEASRHRVTS GTTLSYLSPK DMNQPSSSFF 430 440 450 460 470 480 SVSPSSTSSA TVARELLMNG TSPTAEAIGL KGSSPTSPCS SVQPSKQLEY LARIQGFQAA 490 500 510 520 530 LSALKQFSEQ GLESIDGAVN VEKGSLEKQA KHLREKADNN QAKPASISQD CKKSKSAI
	Isoform 3 [UniParc]. Checksum: FBADDEACE1F3E8EF	FASTA	479	52,724
	10 20 30 40 50 60 MLQINQMFSV QLSLGEQTWE SEGSSIKKAQ QAVANKALTE STLPKPVQKP PKSNVNNNPG 70 80 90 100 110 120 SITPTVELNG LAMKRGEPAI YRPLDPKPFP NYRANYNFRG MYNQRYHCPM PKIFYVQLTV 130 140 150 160 170 180 GNNEFFGEGK TRQAARHNAA MKALQALQNE PIPEKSPQNG ESGKEMDDDK DANKSEISLV 190 200 210 220 230 240 FEIALKRNMP VSFEVIKESG PPHMKSFVTR VSVGEFSAEG EGNSKKLSKK RAATTVLQEL 250 260 270 280 290 300 KKLPPLPVVE KPKLFFKKRP KTIVKAGPDY GQGMNPISRL AQIQQARKEK EPDYILLSER 310 320 330 340 350 360 GMPRRREFVM QVKVGNEVAT GTGPNKKIAK KNAAEAMLLQ LGYKASTSLQ DPLDKTGENK 370 380 390 400 410 420 GWSGPKPGFP EPTNNTPKGI LHLSPDVYQE MEASRHRVTS GTTLSYLSPK DMNQPSSSFF 430 440 450 460 470 SVSPSSTSSA TVARELLMNG TSPTAEAIGL KGSSPTSPCS SVQPSKQLEY LARIQGFQV
	Isoform 4 [UniParc]. Checksum: 05E34194CA94AB03	FASTA	206	22,340
	10 20 30 40 50 60 MNPISRLAQI QQARKEKEPD YILLSERGMP RRREFVMQVK VGNEVATGTG PNKKIAKKNA 70 80 90 100 110 120 AEAMLLQLGY KASTSLQDPL DKTGENKGWS GPKPGFPEPT NNTPKGILHL SPDVYQEMEA 130 140 150 160 170 180 SRHRVTSGTT LSYLSPKDMN QPSSSFFSVS PSSTSSATVA RELLMNGTSP TAEAIGLKGS 190 200 SPTSPCSSVQ PSKQLEYLAR IQGFQV
	Isoform 5 [UniParc]. Checksum: 8D678D8578C536E1	FASTA	125	13,836
	10 20 30 40 50 60 MANPKEKTPV CLVNELARFH SIQPQYKLLN ESGPAHSKMF SVQLSLGEQT WESEGSSIKK 70 80 90 100 110 120 AQQAVANKAL TESTLPKPVQ KPPKSNVNNN PVGKLKETVL SPAHEVMIVG ITHYSADNFF LHWCL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Staufen2 isoforms localize to the somatodendritic domain of neurons and interact with different organelles." Duchaine T.F., Hemraj I., Furic L., Deitinghoff A., Kiebler M.A., DesGroseillers L. J. Cell Sci. 115:3285-3295(2002) [PubMed: 12140260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), RNA-BINDING, DOMAIN, TISSUE SPECIFICITY. Strain: BALB/c.
[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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5). Strain: C57BL/6J. Tissue: Extraembryonic tissue, Placenta and Testis.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-570 (ISOFORMS 1/2). Strain: FVB/N. Tissue: Mammary tumor.
[4]	"Localization of the RNA-binding proteins Staufen1 and Staufen2 at the mammalian neuromuscular junction." Belanger G., Stocksley M.A., Vandromme M., Schaeffer L., Furic L., DesGroseillers L., Jasmin B.J. J. Neurochem. 86:669-677(2003) [PubMed: 12859680] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[5]	"The brain-specific double-stranded RNA-binding protein Staufen2: nucleolar accumulation and isoform-specific exportin-5-dependent export." Macchi P., Brownawell A.M., Grunewald B., DesGroseillers L., Macara I.G., Kiebler M.A. J. Biol. Chem. 279:31440-31444(2004) [PubMed: 15166236] [Abstract] Cited for: INTERACTION WITH XPO5, SUBCELLULAR LOCATION, DOMAIN NLS 1, MUTAGENESIS OF HIS-235; LYS-237; 273-LYS-LYS-274 AND 289-LYS--ARG-291.
[6]	"Solution structure of DSRNA binding domain in Staufen homolog 2." RIKEN structural genomics initiative (RSGI) Submitted (JUL-2003) to the PDB data bank Cited for: STRUCTURE BY NMR OF 308-383.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF459099 mRNA. Translation: AAN37928.1.
AF459100 mRNA. Translation: AAN37929.1.
AK015087 mRNA. Translation: BAB29708.1.
AK028390 mRNA. Translation: BAC25926.1.
BC010300 mRNA. Translation: AAH10300.1.
BC025118 mRNA. Translation: AAH25118.1.

IPI

IPI00404785.
IPI00407779.
IPI00621913.
IPI00649849.
IPI00989318.

RefSeq

NP_001104742.1. NM_001111272.1.
NP_079579.2. NM_025303.3.

UniGene

Mm.216257.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UHZ	NMR	-	A	308-383	[»]

ProteinModelPortal

Q8CJ67.

SMR

Q8CJ67. Positions 4-389.

ModBase

Search...

Protein-protein interaction databases

STRING

Q8CJ67.

PTM databases

PhosphoSite

Q8CJ67.

Proteomic databases

PRIDE

Q8CJ67.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000027052; ENSMUSP00000027052; ENSMUSG00000025920.
ENSMUST00000054668; ENSMUSP00000053190; ENSMUSG00000025920.
ENSMUST00000115359; ENSMUSP00000111016; ENSMUSG00000025920.
ENSMUST00000116646; ENSMUSP00000112345; ENSMUSG00000025920.
ENSMUST00000144138; ENSMUSP00000119130; ENSMUSG00000025920.
ENSMUST00000159558; ENSMUSP00000125726; ENSMUSG00000025920.
ENSMUST00000162007; ENSMUSP00000124303; ENSMUSG00000025920.
ENSMUST00000162435; ENSMUSP00000123827; ENSMUSG00000025920.
ENSMUST00000162627; ENSMUSP00000123781; ENSMUSG00000025920.
ENSMUST00000162751; ENSMUSP00000124505; ENSMUSG00000025920.

GeneID

29819.

KEGG

mmu:29819.

UCSC

uc007ajn.2. mouse.
uc007ajo.2. mouse.
uc007ajq.2. mouse.
uc007ajr.2. mouse.

Organism-specific databases

CTD

27067.

MGI

MGI:1352508. Stau2.

Phylogenomic databases

eggNOG

roNOG04720.

GeneTree

ENSGT00530000063014.

HOGENOM

HBG713249.

HOVERGEN

HBG005013.

InParanoid

Q8CJ67.

OMA

PIPEKSH.

OrthoDB

EOG44F68V.

PhylomeDB

Q8CJ67.

Gene expression databases

ArrayExpress

Q8CJ67.

Bgee

Q8CJ67.

Genevestigator

Q8CJ67.

GermOnline

ENSMUSG00000025920. Mus musculus.

Family and domain databases

InterPro

IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like.
[Graphical view]

Gene3D

G3DSA:3.30.160.20. dsRNA-bd-like. 4 hits.

Pfam

PF00035. dsrm. 4 hits.
[Graphical view]

SMART

SM00358. DSRM. 4 hits.
[Graphical view]

PROSITE

PS50137. DS_RBD. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

306990.

SOURCE

Search...

Entry information

Entry name

STAU2_MOUSE

Accession

Primary (citable) accession number: Q8CJ67
Secondary accession number(s): Q8BSY8 , Q8CJ66, Q8R175, Q91Z19, Q9D5N7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	March 1, 2003
Last modified:	November 16, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program