Q9NUL3 (STAU2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

STAU2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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 the exportin XPO5. This requires RNA and RAN bound to GTP. 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.
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. 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 By similarity.
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 By similarity.
Sequence similarities	Contains 4 DRBM (double-stranded RNA-binding) domains.
Sequence caution	The sequence BAA91766.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB14522.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Endoplasmic reticulum Microtubule Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	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 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9NUL3-1)

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: Q9NUL3-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MANPKEKTAMCLVNELARFNRVQPQYKLLNERGPAHSK → MLQINQ

Isoform 3 (identifier: Q9NUL3-3)

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

Isoform 4 (identifier: Q9NUL3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-197: Missing.
     511-511: A → V
     512-570: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q9NUL3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MANPKEKTAMCLVNELARFNRVQPQYKLLNERGPAHSK → MLQINQ
     138-570: 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_0000072246
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 By similarity
	Motif	373 – 412	40	Nuclear localization signal 2 By similarity
Amino acid modifications
	Modified residue	188	1	Phosphoserine Ref.9
	Modified residue	416	1	Phosphoserine Ref.8 Ref.9 Ref.10
	Modified residue	440	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.13
	Modified residue	455	1	Phosphoserine Ref.9 Ref.10
	Modified residue	485	1	Phosphoserine Ref.11
	Modified residue	486	1	Phosphoserine Ref.10 Ref.11
	Modified residue	488	1	Phosphothreonine Ref.10 Ref.11
	Modified residue	492	1	Phosphoserine Ref.10 Ref.11 Ref.13
Natural variations
	Alternative sequence	1 – 197	197	Missing in isoform 4.		VSP_015373
	Alternative sequence	1 – 38	38	MANPK…PAHSK → MLQINQ in isoform 2, isoform 3 and isoform 5.		VSP_015374
	Alternative sequence	138 – 570	433	Missing in isoform 5.		VSP_015375
	Alternative sequence	511	1	A → V in isoform 3 and isoform 4.		VSP_015376
	Alternative sequence	512 – 570	59	Missing in isoform 3 and isoform 4.		VSP_015377
	Natural variant	198	1	M → V. Ref.5 Corresponds to variant rs949493 [ dbSNP | Ensembl ].		VAR_023394
Experimental info
	Sequence conflict	433	1	G → D in CAH10527. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 09B0BC7A96B1D2FA	FASTA	570	62,641
	10 20 30 40 50 60 MANPKEKTAM CLVNELARFN RVQPQYKLLN ERGPAHSKMF SVQLSLGEQT WESEGSSIKK 70 80 90 100 110 120 AQQAVANKAL TESTLPKPVQ KPPKSNVNNN PGSITPTVEL NGLAMKRGEP AIYRPLDPKP 130 140 150 160 170 180 FPNYRANYNF RGMYNQRYHC PVPKIFYVQL TVGNNEFFGE GKTRQAARHN AAMKALQALQ 190 200 210 220 230 240 NEPIPERSPQ NGESGKDMDD DKDANKSEIS LVFEIALKRN MPVSFEVIKE SGPPHMKSFV 250 260 270 280 290 300 TRVSVGEFSA EGEGNSKKLS KKRAATTVLQ ELKKLPPLPV VEKPKLFFKK RPKTIVKAGP 310 320 330 340 350 360 EYGQGMNPIS RLAQIQQAKK EKEPDYVLLS ERGMPRRREF VMQVKVGNEV ATGTGPNKKI 370 380 390 400 410 420 AKKNAAEAML LQLGYKASTN LQDQLEKTGE NKGWSGPKPG FPEPTNNTPK GILHLSPDVY 430 440 450 460 470 480 QEMEASRHKV ISGTTLGYLS PKDMNQPSSS FFSISPTSNS SATIARELLM NGTSSTAEAI 490 500 510 520 530 540 GLKGSSPTPP CSPVQPSKQL EYLARIQGFQ AALSALKQFS EQGLDPIDGA MNIEKGSLEK 550 560 570 QAKHLREKAD NNQAPPGSIA QDCKKSNSAV
	Isoform 2 (Short) [UniParc]. Checksum: 25AC7A3A8A787A11	FASTA	538	59,002
	10 20 30 40 50 60 MLQINQMFSV QLSLGEQTWE SEGSSIKKAQ QAVANKALTE STLPKPVQKP PKSNVNNNPG 70 80 90 100 110 120 SITPTVELNG LAMKRGEPAI YRPLDPKPFP NYRANYNFRG MYNQRYHCPV PKIFYVQLTV 130 140 150 160 170 180 GNNEFFGEGK TRQAARHNAA MKALQALQNE PIPERSPQNG ESGKDMDDDK DANKSEISLV 190 200 210 220 230 240 FEIALKRNMP VSFEVIKESG PPHMKSFVTR VSVGEFSAEG EGNSKKLSKK RAATTVLQEL 250 260 270 280 290 300 KKLPPLPVVE KPKLFFKKRP KTIVKAGPEY GQGMNPISRL AQIQQAKKEK EPDYVLLSER 310 320 330 340 350 360 GMPRRREFVM QVKVGNEVAT GTGPNKKIAK KNAAEAMLLQ LGYKASTNLQ DQLEKTGENK 370 380 390 400 410 420 GWSGPKPGFP EPTNNTPKGI LHLSPDVYQE MEASRHKVIS GTTLGYLSPK DMNQPSSSFF 430 440 450 460 470 480 SISPTSNSSA TIARELLMNG TSSTAEAIGL KGSSPTPPCS PVQPSKQLEY LARIQGFQAA 490 500 510 520 530 LSALKQFSEQ GLDPIDGAMN IEKGSLEKQA KHLREKADNN QAPPGSIAQD CKKSNSAV
	Isoform 3 [UniParc]. Checksum: A799D1C30D1DF8B9	FASTA	479	52,769
	10 20 30 40 50 60 MLQINQMFSV QLSLGEQTWE SEGSSIKKAQ QAVANKALTE STLPKPVQKP PKSNVNNNPG 70 80 90 100 110 120 SITPTVELNG LAMKRGEPAI YRPLDPKPFP NYRANYNFRG MYNQRYHCPV PKIFYVQLTV 130 140 150 160 170 180 GNNEFFGEGK TRQAARHNAA MKALQALQNE PIPERSPQNG ESGKDMDDDK DANKSEISLV 190 200 210 220 230 240 FEIALKRNMP VSFEVIKESG PPHMKSFVTR VSVGEFSAEG EGNSKKLSKK RAATTVLQEL 250 260 270 280 290 300 KKLPPLPVVE KPKLFFKKRP KTIVKAGPEY GQGMNPISRL AQIQQAKKEK EPDYVLLSER 310 320 330 340 350 360 GMPRRREFVM QVKVGNEVAT GTGPNKKIAK KNAAEAMLLQ LGYKASTNLQ DQLEKTGENK 370 380 390 400 410 420 GWSGPKPGFP EPTNNTPKGI LHLSPDVYQE MEASRHKVIS GTTLGYLSPK DMNQPSSSFF 430 440 450 460 470 SISPTSNSSA TIARELLMNG TSSTAEAIGL KGSSPTPPCS PVQPSKQLEY LARIQGFQV
	Isoform 4 [UniParc]. Checksum: 3693E8AC06717D95	FASTA	314	34,357
	10 20 30 40 50 60 MDDDKDANKS EISLVFEIAL KRNMPVSFEV IKESGPPHMK SFVTRVSVGE FSAEGEGNSK 70 80 90 100 110 120 KLSKKRAATT VLQELKKLPP LPVVEKPKLF FKKRPKTIVK AGPEYGQGMN PISRLAQIQQ 130 140 150 160 170 180 AKKEKEPDYV LLSERGMPRR REFVMQVKVG NEVATGTGPN KKIAKKNAAE AMLLQLGYKA 190 200 210 220 230 240 STNLQDQLEK TGENKGWSGP KPGFPEPTNN TPKGILHLSP DVYQEMEASR HKVISGTTLG 250 260 270 280 290 300 YLSPKDMNQP SSSFFSISPT SNSSATIARE LLMNGTSSTA EAIGLKGSSP TPPCSPVQPS 310 KQLEYLARIQ GFQV
	Isoform 5 [UniParc]. Checksum: 581E40C45AE59FDC	FASTA	105	11,763
	10 20 30 40 50 60 MLQINQMFSV QLSLGEQTWE SEGSSIKKAQ QAVANKALTE STLPKPVQKP PKSNVNNNPG 70 80 90 100 SITPTVELNG LAMKRGEPAI YRPLDPKPFP NYRANYNFRG MYNQR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel homolog of the Drosophila staufen protein in the chromosome 8q13-q21.1 region." Buchner G., Bassi M.T., Andolfi G., Ballabio A., Franco B. Genomics 62:113-118(1999) [PubMed: 10585778] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[2]	"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).
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-570 (ISOFORMS 3/4). Tissue: Ovary, Placenta and Teratocarcinoma.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Retina.
[5]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed: 16421571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-198.
[6]	"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] (ISOFORMS 2 AND 5). Tissue: Urinary bladder carcinoma.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-416; SER-440 AND SER-455, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-440; SER-455; SER-486; THR-488 AND SER-492, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485; SER-486; THR-488 AND SER-492, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs." Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S. RNA 15:104-115(2009) [PubMed: 19029303] [Abstract] Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440 AND SER-492, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y19062 mRNA. Translation: CAB64341.1. AF459097 mRNA. Translation: AAN37926.1. AF459098 mRNA. Translation: AAN37927.1. AK001576 mRNA. Translation: BAA91766.1. Different initiation. AK002152 mRNA. Translation: BAA92111.1. AK023314 mRNA. Translation: BAB14522.1. Different initiation. CR627442 mRNA. Translation: CAH10527.1. AC027018 Genomic DNA. No translation available. AC100784 Genomic DNA. No translation available. BC008369 mRNA. Translation: AAH08369.1. BC008370 mRNA. Translation: AAH08370.1.
IPI	IPI00164481. IPI00300789. IPI00644696. IPI01009003. IPI01009624.
RefSeq	NP_001157852.1. NM_001164380.1. NP_001157853.1. NM_001164381.1. NP_001157854.1. NM_001164382.1. NP_001157855.1. NM_001164383.1. NP_001157856.1. NM_001164384.1. NP_001157857.1. NM_001164385.1. NP_055208.2. NM_014393.2.
UniGene	Hs.561815.
3D structure databases
ProteinModelPortal	Q9NUL3.
SMR	Q9NUL3. Positions 4-78, 95-181, 203-389.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NUL3. 3 interactions.
MINT	MINT-1426106.
STRING	Q9NUL3.
PTM databases
PhosphoSite	Q9NUL3.
Polymorphism databases
DMDM	73919458.
Proteomic databases
PRIDE	Q9NUL3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000418363; ENSP00000389932; ENSG00000040341.
GeneID	27067.
KEGG	hsa:27067.
UCSC	uc003xzm.2. human. uc003xzr.2. human.
Organism-specific databases
CTD	27067.
GeneCards	GC08M074332.
H-InvDB	HIX0007585.
HGNC	HGNC:11371. STAU2.
HPA	CAB020836. HPA019155.
MIM	605920. gene.
neXtProt	NX_Q9NUL3.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00530000063014.
HOGENOM	HBG713249.
HOVERGEN	HBG005013.
InParanoid	Q9NUL3.
OrthoDB	EOG44F68V.
Gene expression databases
ArrayExpress	Q9NUL3.
CleanEx	HS_STAU2.
Genevestigator	Q9NUL3.
GermOnline	ENSG00000040341. Homo sapiens.
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	49639.
SOURCE	Search...

Entry information

Entry name

STAU2_HUMAN

Accession

Primary (citable) accession number: Q9NUL3
Secondary accession number(s): Q6AHY7 , Q96HM0, Q96HM1, Q9NVI5, Q9UGG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 91 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.