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Protein

Double-stranded RNA-binding protein Staufen homolog 2

Gene

STAU2

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

Functioni

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).By similarity

GO - Molecular functioni

  • double-stranded RNA binding Source: MGI
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Double-stranded RNA-binding protein Staufen homolog 2
Gene namesi
Name:STAU2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:11371. STAU2.

Subcellular locationi

  • Cytoplasm
  • Nucleus
  • Nucleusnucleolus
  • 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).By similarity

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36189.

Polymorphism and mutation databases

BioMutaiSTAU2.
DMDMi73919458.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 570570Double-stranded RNA-binding protein Staufen homolog 2PRO_0000072246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881PhosphoserineCombined sources
Modified residuei395 – 3951PhosphoserineCombined sources
Modified residuei405 – 4051PhosphothreonineCombined sources
Modified residuei416 – 4161PhosphoserineCombined sources
Modified residuei426 – 4261PhosphoserineCombined sources
Modified residuei440 – 4401PhosphoserineCombined sources
Modified residuei455 – 4551PhosphoserineCombined sources
Modified residuei492 – 4921PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NUL3.
MaxQBiQ9NUL3.
PaxDbiQ9NUL3.
PRIDEiQ9NUL3.

PTM databases

iPTMnetiQ9NUL3.
PhosphoSiteiQ9NUL3.

Expressioni

Gene expression databases

BgeeiQ9NUL3.
CleanExiHS_STAU2.
ExpressionAtlasiQ9NUL3. baseline and differential.
GenevisibleiQ9NUL3. HS.

Organism-specific databases

HPAiCAB020836.
HPA019155.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX58Q96C102EBI-722938,EBI-744193
EIF2AK2P195252EBI-722938,EBI-640775

Protein-protein interaction databases

BioGridi117978. 47 interactions.
IntActiQ9NUL3. 17 interactions.
MINTiMINT-1426106.
STRINGi9606.ENSP00000428756.

Structurei

3D structure databases

ProteinModelPortaliQ9NUL3.
SMRiQ9NUL3. Positions 6-76, 209-275, 308-389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 7568DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini95 – 18187DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini207 – 27468DRBM 3PROSITE-ProRule annotationAdd
BLAST
Domaini307 – 37569DRBM 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni381 – 570190Required for dendritic transportBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi273 – 29119Nuclear localization signal 1By similarityAdd
BLAST
Motifi373 – 41240Nuclear localization signal 2By similarityAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Contains 4 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3732. Eukaryota.
ENOG410XSCK. LUCA.
GeneTreeiENSGT00830000128290.
HOGENOMiHOG000231025.
HOVERGENiHBG005013.
InParanoidiQ9NUL3.
KOiK17597.
OrthoDBiEOG7NGQCG.
PhylomeDBiQ9NUL3.
TreeFamiTF350296.

Family and domain databases

Gene3Di3.30.160.20. 4 hits.
InterProiIPR014720. dsRBD_dom.
IPR032478. Staufen_C.
[Graphical view]
PfamiPF00035. dsrm. 4 hits.
PF16482. Staufen_C. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 4 hits.
[Graphical view]
PROSITEiPS50137. DS_RBD. 4 hits.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NUL3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MANPKEKTAM CLVNELARFN RVQPQYKLLN ERGPAHSKMF SVQLSLGEQT
60 70 80 90 100
WESEGSSIKK AQQAVANKAL TESTLPKPVQ KPPKSNVNNN PGSITPTVEL
110 120 130 140 150
NGLAMKRGEP AIYRPLDPKP FPNYRANYNF RGMYNQRYHC PVPKIFYVQL
160 170 180 190 200
TVGNNEFFGE GKTRQAARHN AAMKALQALQ NEPIPERSPQ NGESGKDMDD
210 220 230 240 250
DKDANKSEIS LVFEIALKRN MPVSFEVIKE SGPPHMKSFV TRVSVGEFSA
260 270 280 290 300
EGEGNSKKLS KKRAATTVLQ ELKKLPPLPV VEKPKLFFKK RPKTIVKAGP
310 320 330 340 350
EYGQGMNPIS RLAQIQQAKK EKEPDYVLLS ERGMPRRREF VMQVKVGNEV
360 370 380 390 400
ATGTGPNKKI AKKNAAEAML LQLGYKASTN LQDQLEKTGE NKGWSGPKPG
410 420 430 440 450
FPEPTNNTPK GILHLSPDVY QEMEASRHKV ISGTTLGYLS PKDMNQPSSS
460 470 480 490 500
FFSISPTSNS SATIARELLM NGTSSTAEAI GLKGSSPTPP CSPVQPSKQL
510 520 530 540 550
EYLARIQGFQ AALSALKQFS EQGLDPIDGA MNIEKGSLEK QAKHLREKAD
560 570
NNQAPPGSIA QDCKKSNSAV
Length:570
Mass (Da):62,641
Last modified:October 1, 2000 - v1
Checksum:i09B0BC7A96B1D2FA
GO
Isoform 2 (identifier: Q9NUL3-2) [UniParc]FASTAAdd to basket

Also known as: Short

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

Show »
Length:538
Mass (Da):59,002
Checksum:i25AC7A3A8A787A11
GO
Isoform 3 (identifier: Q9NUL3-3) [UniParc]FASTAAdd to basket

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

Show »
Length:479
Mass (Da):52,769
Checksum:iA799D1C30D1DF8B9
GO
Isoform 4 (identifier: Q9NUL3-4) [UniParc]FASTAAdd to basket

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.
Show »
Length:314
Mass (Da):34,357
Checksum:i3693E8AC06717D95
GO
Isoform 5 (identifier: Q9NUL3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MANPKEKTAMCLVNELARFNRVQPQYKLLNERGPAHSK → MLQINQ
     138-570: Missing.

Show »
Length:105
Mass (Da):11,763
Checksum:i581E40C45AE59FDC
GO
Isoform 6 (identifier: Q9NUL3-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-172: Missing.

Note: No experimental confirmation available.
Show »
Length:398
Mass (Da):43,310
Checksum:iD5EE6567A238F902
GO
Isoform 7 (identifier: Q9NUL3-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.
     509-509: F → FQVHYCDRQSGKECVTCLTLAPVQMTFHAIGSSIEASHD

Note: No experimental confirmation available.
Show »
Length:504
Mass (Da):55,446
Checksum:iD705A2812D5F4CB6
GO
Isoform 8 (identifier: Q9NUL3-8) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:473
Mass (Da):52,041
Checksum:i75978FFF1EFE2B05
GO

Sequence cautioni

The sequence BAA91766.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14522.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451K → T in BAH11778 (PubMed:14702039).Curated
Sequence conflicti433 – 4331G → D in CAH10527 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti198 – 1981M → V.2 Publications
Corresponds to variant rs949493 [ dbSNP | Ensembl ].
VAR_023394

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 197197Missing in isoform 4. 1 PublicationVSP_015373Add
BLAST
Alternative sequencei1 – 172172Missing in isoform 6. 1 PublicationVSP_046138Add
BLAST
Alternative sequencei1 – 104104Missing in isoform 7. 1 PublicationVSP_046139Add
BLAST
Alternative sequencei1 – 3838MANPK…PAHSK → MLQINQ in isoform 2, isoform 3 and isoform 5. 3 PublicationsVSP_015374Add
BLAST
Alternative sequencei1 – 3838Missing in isoform 8. 1 PublicationVSP_046140Add
BLAST
Alternative sequencei138 – 570433Missing in isoform 5. 1 PublicationVSP_015375Add
BLAST
Alternative sequencei509 – 5091F → FQVHYCDRQSGKECVTCLTL APVQMTFHAIGSSIEASHD in isoform 7. 1 PublicationVSP_046141
Alternative sequencei511 – 57060AALSA…SNSAV → V in isoform 8. 1 PublicationVSP_046142Add
BLAST
Alternative sequencei511 – 5111A → V in isoform 3 and isoform 4. 2 PublicationsVSP_015376
Alternative sequencei512 – 57059Missing in isoform 3 and isoform 4. 2 PublicationsVSP_015377Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK293496 mRNA. Translation: BAH11522.1.
AK294466 mRNA. Translation: BAH11778.1.
AK303104 mRNA. Translation: BAH13900.1.
CR627442 mRNA. Translation: CAH10527.1.
AC018620 Genomic DNA. No translation available.
AC027018 Genomic DNA. No translation available.
AC100784 Genomic DNA. No translation available.
BC008369 mRNA. Translation: AAH08369.1.
BC008370 mRNA. Translation: AAH08370.1.
CCDSiCCDS55244.1. [Q9NUL3-6]
CCDS55245.1. [Q9NUL3-7]
CCDS55246.1. [Q9NUL3-8]
CCDS55247.1. [Q9NUL3-1]
CCDS55248.1. [Q9NUL3-2]
CCDS6214.1. [Q9NUL3-3]
RefSeqiNP_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.
UniGeneiHs.561815.

Genome annotation databases

EnsembliENST00000524104; ENSP00000430611; ENSG00000040341. [Q9NUL3-5]
GeneIDi27067.
KEGGihsa:27067.
UCSCiuc003xzs.5. human. [Q9NUL3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK293496 mRNA. Translation: BAH11522.1.
AK294466 mRNA. Translation: BAH11778.1.
AK303104 mRNA. Translation: BAH13900.1.
CR627442 mRNA. Translation: CAH10527.1.
AC018620 Genomic DNA. No translation available.
AC027018 Genomic DNA. No translation available.
AC100784 Genomic DNA. No translation available.
BC008369 mRNA. Translation: AAH08369.1.
BC008370 mRNA. Translation: AAH08370.1.
CCDSiCCDS55244.1. [Q9NUL3-6]
CCDS55245.1. [Q9NUL3-7]
CCDS55246.1. [Q9NUL3-8]
CCDS55247.1. [Q9NUL3-1]
CCDS55248.1. [Q9NUL3-2]
CCDS6214.1. [Q9NUL3-3]
RefSeqiNP_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.
UniGeneiHs.561815.

3D structure databases

ProteinModelPortaliQ9NUL3.
SMRiQ9NUL3. Positions 6-76, 209-275, 308-389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117978. 47 interactions.
IntActiQ9NUL3. 17 interactions.
MINTiMINT-1426106.
STRINGi9606.ENSP00000428756.

PTM databases

iPTMnetiQ9NUL3.
PhosphoSiteiQ9NUL3.

Polymorphism and mutation databases

BioMutaiSTAU2.
DMDMi73919458.

Proteomic databases

EPDiQ9NUL3.
MaxQBiQ9NUL3.
PaxDbiQ9NUL3.
PRIDEiQ9NUL3.

Protocols and materials databases

DNASUi27067.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000524104; ENSP00000430611; ENSG00000040341. [Q9NUL3-5]
GeneIDi27067.
KEGGihsa:27067.
UCSCiuc003xzs.5. human. [Q9NUL3-1]

Organism-specific databases

CTDi27067.
GeneCardsiSTAU2.
H-InvDBHIX0007585.
HGNCiHGNC:11371. STAU2.
HPAiCAB020836.
HPA019155.
MIMi605920. gene.
neXtProtiNX_Q9NUL3.
PharmGKBiPA36189.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3732. Eukaryota.
ENOG410XSCK. LUCA.
GeneTreeiENSGT00830000128290.
HOGENOMiHOG000231025.
HOVERGENiHBG005013.
InParanoidiQ9NUL3.
KOiK17597.
OrthoDBiEOG7NGQCG.
PhylomeDBiQ9NUL3.
TreeFamiTF350296.

Miscellaneous databases

ChiTaRSiSTAU2. human.
GeneWikiiSTAU2.
GenomeRNAii27067.
NextBioi49639.
PROiQ9NUL3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NUL3.
CleanExiHS_STAU2.
ExpressionAtlasiQ9NUL3. baseline and differential.
GenevisibleiQ9NUL3. HS.

Family and domain databases

Gene3Di3.30.160.20. 4 hits.
InterProiIPR014720. dsRBD_dom.
IPR032478. Staufen_C.
[Graphical view]
PfamiPF00035. dsrm. 4 hits.
PF16482. Staufen_C. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 4 hits.
[Graphical view]
PROSITEiPS50137. DS_RBD. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 6; 7 AND 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-570 (ISOFORMS 3/4), VARIANT VAL-198.
    Tissue: Amygdala, Cerebellum, Ovary, Placenta, Teratocarcinoma and Thymus.
  4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-416, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-440; SER-455 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; THR-405; SER-416; SER-426; SER-440 AND SER-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTAU2_HUMAN
AccessioniPrimary (citable) accession number: Q9NUL3
Secondary accession number(s): B7Z1I6
, B7Z292, B7Z8B4, E7ER74, E9PEI3, E9PF26, E9PF50, Q6AHY7, Q96HM0, Q96HM1, Q9NVI5, Q9UGG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 1, 2000
Last modified: April 13, 2016
This is version 133 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.