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Protein

Double-stranded RNA-binding protein Staufen homolog 1

Gene

STAU1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.

GO - Molecular functioni

  1. double-stranded RNA binding Source: ProtInc
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. intracellular mRNA localization Source: Ensembl
  2. positive regulation by virus of viral protein levels in host cell Source: AgBase
  3. positive regulation of viral genome replication Source: AgBase
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Double-stranded RNA-binding protein Staufen homolog 1
Gene namesi
Name:STAU1
Synonyms:STAU
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11370. STAU1.

Subcellular locationi

Cytoplasm 1 Publication. Rough endoplasmic reticulum 1 Publication
Note: Localizes exclusively with the rough reticulum endoplasmic (RER).

GO - Cellular componenti

  1. cell body Source: ParkinsonsUK-UCL
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  4. cytoplasmic stress granule Source: BHF-UCL
  5. dendrite Source: ParkinsonsUK-UCL
  6. endoplasmic reticulum Source: AgBase
  7. extracellular vesicular exosome Source: UniProtKB
  8. membrane Source: UniProtKB
  9. microtubule associated complex Source: ProtInc
  10. neuronal cell body Source: Ensembl
  11. rough endoplasmic reticulum Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36188.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 577576Double-stranded RNA-binding protein Staufen homolog 1PRO_0000072243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei390 – 3901Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95793.
PaxDbiO95793.
PRIDEiO95793.

PTM databases

PhosphoSiteiO95793.

Expressioni

Tissue specificityi

Widely expressed. Expressed in brain, pancreas, heart, skeletal muscles, liver, lung, kidney and placenta.

Gene expression databases

BgeeiO95793.
CleanExiHS_STAU1.
ExpressionAtlasiO95793. baseline and differential.
GenevestigatoriO95793.

Organism-specific databases

HPAiCAB020839.
HPA049892.

Interactioni

Subunit structurei

Binds tubulin. Binds with low affinity single-stranded RNA or DNA homopolymers. Interacts with CASC3 in an RNA-dependent manner (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 influenza virus nonstructural protein NS1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NSP034963EBI-358174,EBI-2547442From a different organism.
RPL7AP624242EBI-358174,EBI-354172
RPLP0P053884EBI-358174,EBI-354101
UPF1Q929005EBI-358174,EBI-373471

Protein-protein interaction databases

BioGridi112657. 297 interactions.
IntActiO95793. 59 interactions.
MINTiMINT-1160018.
STRINGi9606.ENSP00000360922.

Structurei

Secondary structure

1
577
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi448 – 46215Combined sources
Helixi466 – 4727Combined sources
Helixi489 – 50012Combined sources
Beta strandi504 – 5096Combined sources
Beta strandi517 – 5237Combined sources
Beta strandi525 – 5273Combined sources
Beta strandi529 – 5379Combined sources
Helixi538 – 55316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DKKX-ray1.70A448-557[»]
ProteinModelPortaliO95793.
SMRiO95793. Positions 123-164, 186-252, 287-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 16291DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini184 – 25168DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini286 – 35469DRBM 3PROSITE-ProRule annotationAdd
BLAST

Domaini

One of the DRDB could be involved in RER binding.
The C-terminal contains the tubulin binding domain (TBD).By similarity

Sequence similaritiesi

Contains 3 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG299502.
GeneTreeiENSGT00760000119275.
HOGENOMiHOG000231025.
HOVERGENiHBG005013.
InParanoidiO95793.
KOiK17597.
OMAiPIVKPQT.
OrthoDBiEOG7NGQCG.
PhylomeDBiO95793.
TreeFamiTF350296.

Family and domain databases

Gene3Di3.30.160.20. 3 hits.
InterProiIPR014720. dsRNA-bd_dom.
[Graphical view]
PfamiPF00035. dsrm. 3 hits.
[Graphical view]
SMARTiSM00358. DSRM. 3 hits.
[Graphical view]
PROSITEiPS50137. DS_RBD. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: O95793-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSQVQVQVQN PSAALSGSQI LNKNQSLLSQ PLMSIPSTTS SLPSENAGRP
60 70 80 90 100
IQNSALPSAS ITSTSAAAES ITPTVELNAL CMKLGKKPMY KPVDPYSRMQ
110 120 130 140 150
STYNYNMRGG AYPPRYFYPF PVPPLLYQVE LSVGGQQFNG KGKTRQAAKH
160 170 180 190 200
DAAAKALRIL QNEPLPERLE VNGRESEEEN LNKSEISQVF EIALKRNLPV
210 220 230 240 250
NFEVARESGP PHMKNFVTKV SVGEFVGEGE GKSKKISKKN AAIAVLEELK
260 270 280 290 300
KLPPLPAVER VKPRIKKKTK PIVKPQTSPE YGQGINPISR LAQIQQAKKE
310 320 330 340 350
KEPEYTLLTE RGLPRRREFV MQVKVGNHTA EGTGTNKKVA KRNAAENMLE
360 370 380 390 400
ILGFKVPQAQ PTKPALKSEE KTPIKKPGDG RKVTFFEPGS GDENGTSNKE
410 420 430 440 450
DEFRMPYLSH QQLPAGILPM VPEVAQAVGV SQGHHTKDFT RAAPNPAKAT
460 470 480 490 500
VTAMIARELL YGGTSPTAET ILKNNISSGH VPHGPLTRPS EQLDYLSRVQ
510 520 530 540 550
GFQVEYKDFP KNNKNEFVSL INCSSQPPLI SHGIGKDVES CHDMAALNIL
560 570
KLLSELDQQS TEMPRTGNGP MSVCGRC
Length:577
Mass (Da):63,182
Last modified:March 6, 2006 - v2
Checksum:i0977CEF40FD99517
GO
Isoform Short (identifier: O95793-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Show »
Length:496
Mass (Da):54,934
Checksum:i509B6CF2B928C02C
GO
Isoform 3 (identifier: O95793-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     203-203: E → ESFPLKQ

Show »
Length:502
Mass (Da):55,635
Checksum:i3AA2A672D9D87081
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti359 – 3591A → R (PubMed:10022909).Curated
Sequence conflicti359 – 3591A → R (PubMed:10325410).Curated
Sequence conflicti360 – 39233QPTKP…PGSGD → SHQTRTQVRGEDTHKETRGW KKSNLFLNLALGM (PubMed:10325410).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8181Missing in isoform Short and isoform 3. 5 PublicationsVSP_004434Add
BLAST
Alternative sequencei203 – 2031E → ESFPLKQ in isoform 3. 1 PublicationVSP_043701

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061939 mRNA. Translation: AAD17531.1.
AF061941 mRNA. Translation: AAD17533.1.
AF061938 mRNA. Translation: AAD17530.1.
AF061940 mRNA. Translation: AAD17532.1.
AJ132258 mRNA. Translation: CAB40082.1.
AY529074 mRNA. Translation: AAS76636.1.
AY546099 mRNA. Translation: AAS76637.1.
AL136601 mRNA. Translation: CAB66536.1.
AK292859 mRNA. Translation: BAF85548.1.
AL133174 Genomic DNA. Translation: CAC14084.1.
AL133174 Genomic DNA. Translation: CAC14085.1.
AL133174 Genomic DNA. Translation: CAI42820.1.
CH471077 Genomic DNA. Translation: EAW75669.1.
CH471077 Genomic DNA. Translation: EAW75671.1.
CH471077 Genomic DNA. Translation: EAW75672.1.
CH471077 Genomic DNA. Translation: EAW75673.1.
CH471077 Genomic DNA. Translation: EAW75674.1.
BC050432 mRNA. Translation: AAH50432.1.
BC095397 mRNA. Translation: AAH95397.1.
CCDSiCCDS13414.1. [O95793-1]
CCDS13415.1. [O95793-2]
CCDS33481.1. [O95793-3]
RefSeqiNP_001032405.1. NM_001037328.1. [O95793-3]
NP_004593.2. NM_004602.2. [O95793-2]
NP_059346.2. NM_017452.2. [O95793-2]
NP_059347.2. NM_017453.2. [O95793-1]
NP_059348.2. NM_017454.2. [O95793-2]
XP_005260583.1. XM_005260526.1. [O95793-3]
XP_005260584.1. XM_005260527.1. [O95793-3]
XP_005260585.1. XM_005260528.1. [O95793-3]
XP_005260586.1. XM_005260529.1. [O95793-2]
XP_006723930.1. XM_006723867.1. [O95793-1]
UniGeneiHs.596704.

Genome annotation databases

EnsembliENST00000340954; ENSP00000345425; ENSG00000124214. [O95793-2]
ENST00000347458; ENSP00000323443; ENSG00000124214. [O95793-2]
ENST00000360426; ENSP00000353604; ENSG00000124214. [O95793-2]
ENST00000371802; ENSP00000360867; ENSG00000124214. [O95793-3]
ENST00000371828; ENSP00000360893; ENSG00000124214. [O95793-3]
ENST00000371856; ENSP00000360922; ENSG00000124214. [O95793-1]
GeneIDi6780.
KEGGihsa:6780.
UCSCiuc002xua.3. human. [O95793-1]
uc002xub.3. human. [O95793-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061939 mRNA. Translation: AAD17531.1.
AF061941 mRNA. Translation: AAD17533.1.
AF061938 mRNA. Translation: AAD17530.1.
AF061940 mRNA. Translation: AAD17532.1.
AJ132258 mRNA. Translation: CAB40082.1.
AY529074 mRNA. Translation: AAS76636.1.
AY546099 mRNA. Translation: AAS76637.1.
AL136601 mRNA. Translation: CAB66536.1.
AK292859 mRNA. Translation: BAF85548.1.
AL133174 Genomic DNA. Translation: CAC14084.1.
AL133174 Genomic DNA. Translation: CAC14085.1.
AL133174 Genomic DNA. Translation: CAI42820.1.
CH471077 Genomic DNA. Translation: EAW75669.1.
CH471077 Genomic DNA. Translation: EAW75671.1.
CH471077 Genomic DNA. Translation: EAW75672.1.
CH471077 Genomic DNA. Translation: EAW75673.1.
CH471077 Genomic DNA. Translation: EAW75674.1.
BC050432 mRNA. Translation: AAH50432.1.
BC095397 mRNA. Translation: AAH95397.1.
CCDSiCCDS13414.1. [O95793-1]
CCDS13415.1. [O95793-2]
CCDS33481.1. [O95793-3]
RefSeqiNP_001032405.1. NM_001037328.1. [O95793-3]
NP_004593.2. NM_004602.2. [O95793-2]
NP_059346.2. NM_017452.2. [O95793-2]
NP_059347.2. NM_017453.2. [O95793-1]
NP_059348.2. NM_017454.2. [O95793-2]
XP_005260583.1. XM_005260526.1. [O95793-3]
XP_005260584.1. XM_005260527.1. [O95793-3]
XP_005260585.1. XM_005260528.1. [O95793-3]
XP_005260586.1. XM_005260529.1. [O95793-2]
XP_006723930.1. XM_006723867.1. [O95793-1]
UniGeneiHs.596704.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DKKX-ray1.70A448-557[»]
ProteinModelPortaliO95793.
SMRiO95793. Positions 123-164, 186-252, 287-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112657. 297 interactions.
IntActiO95793. 59 interactions.
MINTiMINT-1160018.
STRINGi9606.ENSP00000360922.

PTM databases

PhosphoSiteiO95793.

Proteomic databases

MaxQBiO95793.
PaxDbiO95793.
PRIDEiO95793.

Protocols and materials databases

DNASUi6780.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340954; ENSP00000345425; ENSG00000124214. [O95793-2]
ENST00000347458; ENSP00000323443; ENSG00000124214. [O95793-2]
ENST00000360426; ENSP00000353604; ENSG00000124214. [O95793-2]
ENST00000371802; ENSP00000360867; ENSG00000124214. [O95793-3]
ENST00000371828; ENSP00000360893; ENSG00000124214. [O95793-3]
ENST00000371856; ENSP00000360922; ENSG00000124214. [O95793-1]
GeneIDi6780.
KEGGihsa:6780.
UCSCiuc002xua.3. human. [O95793-1]
uc002xub.3. human. [O95793-3]

Organism-specific databases

CTDi6780.
GeneCardsiGC20M047729.
HGNCiHGNC:11370. STAU1.
HPAiCAB020839.
HPA049892.
MIMi601716. gene.
neXtProtiNX_O95793.
PharmGKBiPA36188.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG299502.
GeneTreeiENSGT00760000119275.
HOGENOMiHOG000231025.
HOVERGENiHBG005013.
InParanoidiO95793.
KOiK17597.
OMAiPIVKPQT.
OrthoDBiEOG7NGQCG.
PhylomeDBiO95793.
TreeFamiTF350296.

Miscellaneous databases

ChiTaRSiSTAU1. human.
GeneWikiiSTAU1.
GenomeRNAii6780.
NextBioi26468.
PROiO95793.
SOURCEiSearch...

Gene expression databases

BgeeiO95793.
CleanExiHS_STAU1.
ExpressionAtlasiO95793. baseline and differential.
GenevestigatoriO95793.

Family and domain databases

Gene3Di3.30.160.20. 3 hits.
InterProiIPR014720. dsRNA-bd_dom.
[Graphical view]
PfamiPF00035. dsrm. 3 hits.
[Graphical view]
SMARTiSM00358. DSRM. 3 hits.
[Graphical view]
PROSITEiPS50137. DS_RBD. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian Staufen is a double-stranded-RNA- and tubulin-binding protein which localizes to the rough endoplasmic reticulum."
    Wickham L., Duchaine T., Luo M., Nabi I.R., DesGroseillers L.
    Mol. Cell. Biol. 19:2220-2230(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Tissue: CNS.
  2. "Interaction of influenza virus NS1 protein and the human homologue of Staufen in vivo and in vitro."
    Falcon A.M., Fortes P., Marion R.M., Beloso A., Ortin J.
    Nucleic Acids Res. 27:2241-2247(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    Tissue: Kidney.
  3. "Cloning and characterization of a splicing variant of human staufen protein."
    Mao Y., Xie Y., Jin F.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
    Tissue: Brain.
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
    Tissue: Trachea.
  6. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
    Tissue: Placenta and Skin.
  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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTAU1_HUMAN
AccessioniPrimary (citable) accession number: O95793
Secondary accession number(s): A8K9Z4
, E1P5Y1, E1P608, Q5JW29, Q6GTM4, Q9H5B4, Q9H5B5, Q9Y3Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2000
Last sequence update: March 6, 2006
Last modified: March 3, 2015
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.