NUP61_SCHPO - dbPTM
NUP61_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUP61_SCHPO
UniProt AC Q9USL4
Protein Name Nucleoporin nup61
Gene Name nup61
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 549
Subcellular Localization Nucleus, nuclear pore complex .
Protein Description Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. May play a role in mitotic spindle formation and/or function..
Protein Sequence MSKRGADHQLTKDQDDSDDDRHGPVEVPKEASADVMATRKIAKPKSRKRPTSGVSSPGIFANLAAKPVSLPASTTQFTFGKPAVTANNDSDIHLKKRGLNKSFIDAVIKSVDNNPFGNLSPLFDEYRQHFSSIEKKPAEEQPTSNAVVSEVNPQQQKSQDSSSFVTEKPASSEKEDKEKPLVPPGAPRFGFSAPALGSSFQFNSSAFTPKGSFGEKSATEAEAKEKETSSNQTATGTAATTTNQFSFNTAANPFAFAKKENEESKPLTPVFSFSTTMASADASKETKQTHETKDSKSEESKPSNNEKSENAVEPAKGNTMSFSWTPDKPIKFDTPEKKFTFTNPLSSKKLPASSDVKPPSAAAVGFSFGTTTNPFSFAAPKSSFPTSSTPASVGAEKSEETSNGNKSEQEEKENGNDETRSNDSLVSGKGKGEENEDSVFETRAKIYRFDATSKSYSDIGIGPLKINVDRDTGSARILARVEGSGKLLLNVRLCQDFEYSLAGKKDVKVPAASTDGKSIEMYLIRVKEPSTAEKLLAELNEKKVSKSEN
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
17PhosphorylationLTKDQDDSDDDRHGP
CCCCCCCCCCCCCCC		51.7528889911
51PhosphorylationPKSRKRPTSGVSSPG
CCCCCCCCCCCCCCC		41.9924763107
52PhosphorylationKSRKRPTSGVSSPGI
CCCCCCCCCCCCCCC		39.6221712547
55PhosphorylationKRPTSGVSSPGIFAN
CCCCCCCCCCCCHHH		34.0521712547
56PhosphorylationRPTSGVSSPGIFANL
CCCCCCCCCCCHHHH		25.4121712547
102PhosphorylationKKRGLNKSFIDAVIK
HHCCCCHHHHHHHHH		26.7625720772
162PhosphorylationQQKSQDSSSFVTEKP
HHHCCCCCCCCCCCC		35.7629996109
163PhosphorylationQKSQDSSSFVTEKPA
HHCCCCCCCCCCCCC		27.9129996109
166PhosphorylationQDSSSFVTEKPASSE
CCCCCCCCCCCCCCC		35.9621712547
171PhosphorylationFVTEKPASSEKEDKE
CCCCCCCCCCCCCCC		47.7821712547
172PhosphorylationVTEKPASSEKEDKEK
CCCCCCCCCCCCCCC		55.5929996109
268PhosphorylationNEESKPLTPVFSFST
CCCCCCCCCEEEEEC		26.4024763107
275PhosphorylationTPVFSFSTTMASADA
CCEEEEECCCCCCCC		20.6921712547
279PhosphorylationSFSTTMASADASKET
EEECCCCCCCCCHHH		18.8321712547
283PhosphorylationTMASADASKETKQTH
CCCCCCCCHHHHHHC		31.4121712547
295PhosphorylationQTHETKDSKSEESKP
HHCCCCCCCCCCCCC		39.3721712547
297PhosphorylationHETKDSKSEESKPSN
CCCCCCCCCCCCCCC		51.0121712547
303PhosphorylationKSEESKPSNNEKSEN
CCCCCCCCCCCCCCC		56.9025720772
308PhosphorylationKPSNNEKSENAVEPA
CCCCCCCCCCCCCCC		29.8825720772
319PhosphorylationVEPAKGNTMSFSWTP
CCCCCCCCCEEEECC		23.9021712547
321PhosphorylationPAKGNTMSFSWTPDK
CCCCCCCEEEECCCC		17.6821712547
323PhosphorylationKGNTMSFSWTPDKPI
CCCCCEEEECCCCCC		23.8021712547
325PhosphorylationNTMSFSWTPDKPIKF
CCCEEEECCCCCCCC		22.0221712547
334PhosphorylationDKPIKFDTPEKKFTF
CCCCCCCCCCCEEEE		36.1624763107
340PhosphorylationDTPEKKFTFTNPLSS
CCCCCEEEECCCCCC		38.1321712547
342PhosphorylationPEKKFTFTNPLSSKK
CCCEEEECCCCCCCC		32.6321712547
346PhosphorylationFTFTNPLSSKKLPAS
EEECCCCCCCCCCCC		41.1728889911
347PhosphorylationTFTNPLSSKKLPASS
EECCCCCCCCCCCCC		41.3028889911
387PhosphorylationPKSSFPTSSTPASVG
CCCCCCCCCCCCCCC		32.2424763107
388PhosphorylationKSSFPTSSTPASVGA
CCCCCCCCCCCCCCC		40.6729996109
389PhosphorylationSSFPTSSTPASVGAE
CCCCCCCCCCCCCCC		23.7329996109
392PhosphorylationPTSSTPASVGAEKSE
CCCCCCCCCCCCCCC		23.4524763107
402PhosphorylationAEKSEETSNGNKSEQ
CCCCCCCCCCCHHHH		46.1225720772
407PhosphorylationETSNGNKSEQEEKEN
CCCCCCHHHHHHHHH		48.8121712547
419PhosphorylationKENGNDETRSNDSLV
HHHCCCCCCCCCCCC		42.1124763107
421PhosphorylationNGNDETRSNDSLVSG
HCCCCCCCCCCCCCC		53.0324763107
424PhosphorylationDETRSNDSLVSGKGK
CCCCCCCCCCCCCCC		34.6221712547
457PhosphorylationDATSKSYSDIGIGPL
ECCCCCCCCCCCCCE		29.8225720772
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 NUP61_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUP61_SCHPO !!
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 NUP61_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU124_SCHPOnup124genetic
19547744
IMA2_SCHPOimp1genetic
19547744
RAF1_SCHPOraf1genetic
18818364
SFT1_SCHPOsft1genetic
22681890
PPK14_SCHPOppk14genetic
22681890
IMA3_SCHPOSPCC550.11genetic
22681890
REXO3_SCHPOrex3genetic
22681890
MGR2_SCHPOmgr2genetic
22681890
ALG9_SCHPOalg9genetic
22681890
CHP1_SCHPOchp1genetic
22681890
BCA1_SCHPOeca39genetic
22681890
SPN4_SCHPOspn4genetic
22681890
NU124_SCHPOnup124genetic
22681890
MMS19_SCHPOmms19genetic
22681890
YO48_SCHPOSPBC36B7.08cgenetic
22681890
ELP1_SCHPOelp1genetic
22681890
ATP11_SCHPOatp11genetic
22681890
PPME1_SCHPOSPBP4H10.17cgenetic
22681890
ALM1_SCHPOalm1genetic
22681890
IMA2_SCHPOimp1genetic
22681890
YQMA_SCHPOSPCP1E11.10genetic
22681890
YFE6_SCHPOgmh5genetic
22681890
CTU1_SCHPOctu1genetic
22681890
YBI8_SCHPOoga1genetic
22681890
NXT1_SCHPOnxt1genetic
22681890
SLX9_SCHPOslx9genetic
22681890
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NUP61_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-347, AND MASSSPECTROMETRY.

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