S7A6O_HUMAN - dbPTM
S7A6O_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S7A6O_HUMAN
UniProt AC Q96CW6
Protein Name Probable RNA polymerase II nuclear localization protein SLC7A6OS
Gene Name SLC7A6OS
Organism Homo sapiens (Human).
Sequence Length 309
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Directs RNA polymerase II nuclear import..
Protein Sequence MEAARTAVLRVKRKRSAEPAEALVLACKRLRSDAVESAAQKTSEGLERAAENNVFHLVATVCSQEEPVQPLLREVLRPSRDSQQRVRRNLRASAREVRQEGRYRVLSSRRSLGTTSSGQESEYTPGNPEAAGNSGFQLLDLVHEEGEPEAASAGSCKTSDPDVILCNSVELIRERLTVSEDGPGVRRQEEQKHDDYVYDIYYLETATPGWIENILSVQPYSQEWELVNDDQEPEDIYDDEDDENSENNWRNEYPEEESSDGDEDSRGSADYNSLSEEERGSSRQRMWSKYPLDVQKEFGYDSPHDLDSD
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
6Phosphorylation--MEAARTAVLRVKR
--CHHHHHHHHHHHH		19.1822912867
16PhosphorylationLRVKRKRSAEPAEAL
HHHHHCCCCCHHHHH		39.7623401153
28UbiquitinationEALVLACKRLRSDAV
HHHHHHHHHHCHHHH		49.1932015554
28AcetylationEALVLACKRLRSDAV
HHHHHHHHHHCHHHH		49.1925953088
32PhosphorylationLACKRLRSDAVESAA
HHHHHHCHHHHHHHH		34.2228555341
41UbiquitinationAVESAAQKTSEGLER
HHHHHHHHHHHHHHH		49.6621906983
79PhosphorylationLREVLRPSRDSQQRV
HHHHHCCCHHHHHHH		42.1424719451
82PhosphorylationVLRPSRDSQQRVRRN
HHCCCHHHHHHHHHH		27.4028674419
108PhosphorylationGRYRVLSSRRSLGTT
HCEEEEECCCCCCCC		27.7924719451
111PhosphorylationRVLSSRRSLGTTSSG
EEEECCCCCCCCCCC		30.0028348404
114PhosphorylationSSRRSLGTTSSGQES
ECCCCCCCCCCCCCC		28.8828348404
115PhosphorylationSRRSLGTTSSGQESE
CCCCCCCCCCCCCCC		21.0628348404
116PhosphorylationRRSLGTTSSGQESEY
CCCCCCCCCCCCCCC		32.1028348404
117PhosphorylationRSLGTTSSGQESEYT
CCCCCCCCCCCCCCC		42.2628348404
123PhosphorylationSSGQESEYTPGNPEA
CCCCCCCCCCCCHHH		27.7522210691
159PhosphorylationSAGSCKTSDPDVILC
CCCCCCCCCCCEEEE		32.4224719451
168PhosphorylationPDVILCNSVELIRER
CCEEEECCHHHHHHH		18.9029507054
237PhosphorylationDQEPEDIYDDEDDEN
CCCCHHCCCCCCCCC		29.6626657352
258PhosphorylationNEYPEEESSDGDEDS
CCCCHHHCCCCCCCC		36.6920873877
259PhosphorylationEYPEEESSDGDEDSR
CCCHHHCCCCCCCCC		49.2221815630
265PhosphorylationSSDGDEDSRGSADYN
CCCCCCCCCCCCCHH		36.1725841592
268PhosphorylationGDEDSRGSADYNSLS
CCCCCCCCCCHHHCC		19.5024461736
271PhosphorylationDSRGSADYNSLSEEE
CCCCCCCHHHCCHHH		13.3323186163
273PhosphorylationRGSADYNSLSEEERG
CCCCCHHHCCHHHHC		27.3523663014
275PhosphorylationSADYNSLSEEERGSS
CCCHHHCCHHHHCCH		42.6623663014
281PhosphorylationLSEEERGSSRQRMWS
CCHHHHCCHHHCHHH		28.68-
282PhosphorylationSEEERGSSRQRMWSK
CHHHHCCHHHCHHHC		34.94-
288PhosphorylationSSRQRMWSKYPLDVQ
CHHHCHHHCCCCHHH		16.9929083192
290PhosphorylationRQRMWSKYPLDVQKE
HHCHHHCCCCHHHHH		11.9628176443
300PhosphorylationDVQKEFGYDSPHDLD
HHHHHHCCCCCCCCC		20.6923927012
302PhosphorylationQKEFGYDSPHDLDSD
HHHHCCCCCCCCCCC		18.6923927012
308PhosphorylationDSPHDLDSD------
CCCCCCCCC------		53.1423927012
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 S7A6O_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S7A6O_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 S7A6O_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AAR2_HUMANAAR2physical
28561026
ACD11_HUMANACAD11physical
28561026
ASPH_HUMANASPHphysical
28561026
PRP16_HUMANDHX38physical
28561026
EAPP_HUMANEAPPphysical
28561026
ECD_HUMANECDphysical
28561026
U5S1_HUMANEFTUD2physical
28561026
ECHP_HUMANEHHADHphysical
28561026
TBA8_HUMANEHHADHphysical
28561026
C1TC_HUMANMTHFD1physical
28561026
OBSL1_HUMANOBSL1physical
28561026
RPC1_HUMANPOLR3Aphysical
28561026
PRP19_HUMANPRPF19physical
28561026
PRP8_HUMANPRPF8physical
28561026
S7A6O_HUMANSLC7A6OSphysical
28561026
U520_HUMANSNRNP200physical
28561026
RSMB_HUMANSNRPBphysical
28561026
SMD3_HUMANSNRPD3physical
28561026
RUXG_HUMANSNRPGphysical
28561026
TSSC4_HUMANTSSC4physical
28561026
WDR5_HUMANWDR5physical
28561026
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 S7A6O_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-302 AND SER-308, 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-302 AND SER-308, ANDMASS 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-302 AND SER-308, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-308, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6, AND MASSSPECTROMETRY.

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