STAU2_HUMAN - dbPTM
STAU2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAU2_HUMAN
UniProt AC Q9NUL3
Protein Name Double-stranded RNA-binding protein Staufen homolog 2
Gene Name STAU2
Organism Homo sapiens (Human).
Sequence Length 570
Subcellular Localization Cytoplasm. Nucleus. Nucleus, nucleolus. Endoplasmic reticulum. 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
Protein Description 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)..
Protein Sequence MANPKEKTAMCLVNELARFNRVQPQYKLLNERGPAHSKMFSVQLSLGEQTWESEGSSIKKAQQAVANKALTESTLPKPVQKPPKSNVNNNPGSITPTVELNGLAMKRGEPAIYRPLDPKPFPNYRANYNFRGMYNQRYHCPVPKIFYVQLTVGNNEFFGEGKTRQAARHNAAMKALQALQNEPIPERSPQNGESGKDVDDDKDANKSEISLVFEIALKRNMPVSFEVIKESGPPHMKSFVTRVSVGEFSAEGEGNSKKLSKKRAATTVLQELKKLPPLPVVEKPKLFFKKRPKTIVKAGPEYGQGMNPISRLAQIQQAKKEKEPDYVLLSERGMPRRREFVMQVKVGNEVATGTGPNKKIAKKNAAEAMLLQLGYKASTNLQDQLEKTGENKGWSGPKPGFPEPTNNTPKGILHLSPDVYQEMEASRHKVISGTTLGYLSPKDMNQPSSSFFSISPTSNSSATIARELLMNGTSSTAEAIGLKGSSPTPPCSPVQPSKQLEYLARIQGFQAALSALKQFSEQGLDPIDGAMNIEKGSLEKQAKHLREKADNNQAPPGSIAQDCKKSNSAV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
9 (in isoform 2)Phosphorylation-9.5824043423
9 (in isoform 3)Phosphorylation-9.5824043423
9 (in isoform 5)Phosphorylation-9.5824043423
13 (in isoform 2)Phosphorylation-4.4424043423
13 (in isoform 3)Phosphorylation-4.4424043423
13 (in isoform 5)Phosphorylation-4.4424043423
18 (in isoform 2)Phosphorylation-41.8324043423
18 (in isoform 3)Phosphorylation-41.8324043423
18 (in isoform 5)Phosphorylation-41.8324043423
21 (in isoform 2)Phosphorylation-26.2424043423
21 (in isoform 3)Phosphorylation-26.2424043423
21 (in isoform 5)Phosphorylation-26.2424043423
24 (in isoform 2)Phosphorylation-36.2924043423
24 (in isoform 3)Phosphorylation-36.2924043423
24 (in isoform 5)Phosphorylation-36.2924043423
25 (in isoform 2)Phosphorylation-30.7924043423
25 (in isoform 3)Phosphorylation-30.7924043423
25 (in isoform 5)Phosphorylation-30.7924043423
28 (in isoform 2)Ubiquitination-5.4521906983
28 (in isoform 3)Ubiquitination-5.4521906983
28 (in isoform 5)Ubiquitination-5.4521906983
60UbiquitinationSEGSSIKKAQQAVAN
CCCHHHHHHHHHHHH		50.1621906983
60 (in isoform 1)Ubiquitination-50.1621906983
68UbiquitinationAQQAVANKALTESTL
HHHHHHHHHHCCCCC		34.73-
71PhosphorylationAVANKALTESTLPKP
HHHHHHHCCCCCCCC		32.5221406692
73PhosphorylationANKALTESTLPKPVQ
HHHHHCCCCCCCCCC		29.9721406692
74PhosphorylationNKALTESTLPKPVQK
HHHHCCCCCCCCCCC		40.6321406692
74 (in isoform 2)Ubiquitination-40.6321906983
74 (in isoform 3)Ubiquitination-40.6321906983
74 (in isoform 5)Ubiquitination-40.6321906983
81UbiquitinationTLPKPVQKPPKSNVN
CCCCCCCCCCCCCCC		64.62-
85PhosphorylationPVQKPPKSNVNNNPG
CCCCCCCCCCCCCCC		52.3528450419
93PhosphorylationNVNNNPGSITPTVEL
CCCCCCCCCCCCEEE		25.2528450419
95PhosphorylationNNNPGSITPTVELNG
CCCCCCCCCCEEECC		18.0128450419
97PhosphorylationNPGSITPTVELNGLA
CCCCCCCCEEECCEE		20.2628450419
106UbiquitinationELNGLAMKRGEPAIY
EECCEEECCCCCCCC		52.2021906983
106 (in isoform 1)Ubiquitination-52.2021906983
107MethylationLNGLAMKRGEPAIYR
ECCEEECCCCCCCCC		41.44115917921
113PhosphorylationKRGEPAIYRPLDPKP
CCCCCCCCCCCCCCC		14.32-
114MethylationRGEPAIYRPLDPKPF
CCCCCCCCCCCCCCC		21.13115917925
119UbiquitinationIYRPLDPKPFPNYRA
CCCCCCCCCCCCCCC		59.98-
131MethylationYRANYNFRGMYNQRY
CCCCCEECCCCCCCC		25.9030761269
137DimethylationFRGMYNQRYHCPVPK
ECCCCCCCCCCCCCE		21.37-
137MethylationFRGMYNQRYHCPVPK
ECCCCCCCCCCCCCE		21.3754549533
138PhosphorylationRGMYNQRYHCPVPKI
CCCCCCCCCCCCCEE		9.6727642862
142 (in isoform 2)Ubiquitination-10.31-
153 (in isoform 4)Ubiquitination-26.4721906983
162UbiquitinationNEFFGEGKTRQAARH
CCCCCCCHHHHHHHH		35.91-
174UbiquitinationARHNAAMKALQALQN
HHHHHHHHHHHHHHC		41.02-
188PhosphorylationNEPIPERSPQNGESG
CCCCCCCCCCCCCCC		29.2219651622
188PhosphorylationNEPIPERSPQNGESG
CCCCCCCCCCCCCCC		29.2230266825
193 (in isoform 4)Ubiquitination-64.9621906983
194PhosphorylationRSPQNGESGKDVDDD
CCCCCCCCCCCCCCC		53.1725850435
194PhosphorylationRSPQNGESGKDVDDD
CCCCCCCCCCCCCCC		53.1730266825
221SulfoxidationEIALKRNMPVSFEVI
HHHHHCCCCEEEEEH		3.9421406390
225 (in isoform 2)Ubiquitination-9.8921906983
225 (in isoform 3)Ubiquitination-9.8921906983
238PhosphorylationSGPPHMKSFVTRVSV
HCCCCCCEEEEEEEC		19.8524706070
241PhosphorylationPHMKSFVTRVSVGEF
CCCCEEEEEEECCCC		24.2824719451
254 (in isoform 4)Ubiquitination-55.3521906983
256PhosphorylationSAEGEGNSKKLSKKR
CCCCCCCCHHHCHHH		41.8623401153
257UbiquitinationAEGEGNSKKLSKKRA
CCCCCCCHHHCHHHH		62.8321906983
257 (in isoform 1)Ubiquitination-62.8321906983
265 (in isoform 2)Ubiquitination-14.0821906983
265 (in isoform 3)Ubiquitination-14.0821906983
267PhosphorylationSKKRAATTVLQELKK
CHHHHHHHHHHHHHC		17.94-
283UbiquitinationPPLPVVEKPKLFFKK
CCCCCCCCCCCCCCC		35.52-
294PhosphorylationFFKKRPKTIVKAGPE
CCCCCCCEEEECCCC		33.4120068231
297UbiquitinationKRPKTIVKAGPEYGQ
CCCCEEEECCCCCCC		43.7221906983
297 (in isoform 1)Ubiquitination-43.7221906983
302PhosphorylationIVKAGPEYGQGMNPI
EEECCCCCCCCCCHH		20.2020068231
319UbiquitinationLAQIQQAKKEKEPDY
HHHHHHHHHHCCCCE		58.07-
322UbiquitinationIQQAKKEKEPDYVLL
HHHHHHHCCCCEEEE		81.22-
326PhosphorylationKKEKEPDYVLLSERG
HHHCCCCEEEEECCC		12.06-
326 (in isoform 2)Ubiquitination-12.0621906983
326 (in isoform 3)Ubiquitination-12.0621906983
358UbiquitinationATGTGPNKKIAKKNA
CCCCCCCHHHHHHCH		49.002190698
358 (in isoform 1)Ubiquitination-49.0021906983
359UbiquitinationTGTGPNKKIAKKNAA
CCCCCCHHHHHHCHH		55.31-
387UbiquitinationNLQDQLEKTGENKGW
CHHHHHHHHCCCCCC		71.12-
392UbiquitinationLEKTGENKGWSGPKP
HHHHCCCCCCCCCCC		58.41-
395PhosphorylationTGENKGWSGPKPGFP
HCCCCCCCCCCCCCC		54.6120068231
398UbiquitinationNKGWSGPKPGFPEPT
CCCCCCCCCCCCCCC		62.39-
405PhosphorylationKPGFPEPTNNTPKGI
CCCCCCCCCCCCCEE		39.1622167270
408PhosphorylationFPEPTNNTPKGILHL
CCCCCCCCCCEEEEC		28.5722167270
410UbiquitinationEPTNNTPKGILHLSP
CCCCCCCCEEEECCH		57.45-
416PhosphorylationPKGILHLSPDVYQEM
CCEEEECCHHHHHHH		14.3322167270
420PhosphorylationLHLSPDVYQEMEASR
EECCHHHHHHHHHHH		13.2128176443
426PhosphorylationVYQEMEASRHKVISG
HHHHHHHHHCCCCCC		22.9325159151
429UbiquitinationEMEASRHKVISGTTL
HHHHHHCCCCCCCCC		39.90-
432PhosphorylationASRHKVISGTTLGYL
HHHCCCCCCCCCEEC		32.8321945579
434O-linked_GlycosylationRHKVISGTTLGYLSP
HCCCCCCCCCEECCH		16.4423301498
434PhosphorylationRHKVISGTTLGYLSP
HCCCCCCCCCEECCH		16.4421945579
435PhosphorylationHKVISGTTLGYLSPK
CCCCCCCCCEECCHH		23.0121945579
438PhosphorylationISGTTLGYLSPKDMN
CCCCCCEECCHHHCC		13.7121945579
440PhosphorylationGTTLGYLSPKDMNQP
CCCCEECCHHHCCCC		22.7819664994
448PhosphorylationPKDMNQPSSSFFSIS
HHHCCCCCCCCCCCC		28.9327174698
449PhosphorylationKDMNQPSSSFFSISP
HHCCCCCCCCCCCCC		37.5427174698
450PhosphorylationDMNQPSSSFFSISPT
HCCCCCCCCCCCCCC		34.3520068231
453PhosphorylationQPSSSFFSISPTSNS
CCCCCCCCCCCCCCC		21.8325850435
455PhosphorylationSSSFFSISPTSNSSA
CCCCCCCCCCCCCHH		22.4128355574
457PhosphorylationSFFSISPTSNSSATI
CCCCCCCCCCCHHHH		33.4830278072
458PhosphorylationFFSISPTSNSSATIA
CCCCCCCCCCHHHHH		37.7930278072
460PhosphorylationSISPTSNSSATIARE
CCCCCCCCHHHHHHH		22.5521712546
461PhosphorylationISPTSNSSATIAREL
CCCCCCCHHHHHHHH		33.4125850435
463PhosphorylationPTSNSSATIARELLM
CCCCCHHHHHHHHHH		19.6725850435
470SulfoxidationTIARELLMNGTSSTA
HHHHHHHHCCCCCHH		7.3121406390
473PhosphorylationRELLMNGTSSTAEAI
HHHHHCCCCCHHHHH		17.9428555341
474PhosphorylationELLMNGTSSTAEAIG
HHHHCCCCCHHHHHC		27.3921712546
475PhosphorylationLLMNGTSSTAEAIGL
HHHCCCCCHHHHHCC		31.3221712546
485PhosphorylationEAIGLKGSSPTPPCS
HHHCCCCCCCCCCCC		31.4025159151
486PhosphorylationAIGLKGSSPTPPCSP
HHCCCCCCCCCCCCC		41.2725159151
488PhosphorylationGLKGSSPTPPCSPVQ
CCCCCCCCCCCCCCC		41.6425159151
492PhosphorylationSSPTPPCSPVQPSKQ
CCCCCCCCCCCCHHH		33.6023927012
497PhosphorylationPCSPVQPSKQLEYLA
CCCCCCCHHHHHHHH		18.8830266825
498UbiquitinationCSPVQPSKQLEYLAR
CCCCCCHHHHHHHHH		66.63-
502PhosphorylationQPSKQLEYLARIQGF
CCHHHHHHHHHHHHH		17.7926074081
514PhosphorylationQGFQAALSALKQFSE
HHHHHHHHHHHHHHH		27.1628555341
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of STAU2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAU2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of STAU2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CE126_HUMANKIAA1377physical
16169070
DICER_HUMANDICER1physical
24778252
PRKRA_HUMANPRKRAphysical
24778252
RENT1_HUMANUPF1physical
24778252
E2AK2_HUMANEIF2AK2physical
24778252
ZN346_HUMANZNF346physical
24778252
DSRAD_HUMANADARphysical
24778252
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STAU2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440 AND SER-492, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485; SER-486; THR-488AND SER-492, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-440; SER-455;SER-486; THR-488 AND SER-492, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-416; SER-440AND SER-455, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND MASSSPECTROMETRY.

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