NU157_YEAST - dbPTM
NU157_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NU157_YEAST
UniProt AC P40064
Protein Name Nucleoporin NUP157
Gene Name NUP157
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1391
Subcellular Localization Nucleus, nuclear pore complex. Nucleus membrane
Peripheral membrane protein
Cytoplasmic side. Nucleus membrane
Peripheral membrane protein
Nucleoplasmic side. Symmetric distribution.
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..
Protein Sequence MYSTPLKKRIDYDRETFTASASLGGNRLRNRPRDDQNNGKPNLSSRSFLSERKTRKDVLNKYGEAGNTIESELRDVTTHVKISGLTSSEPLQLASEFVQDLSFRDRNTPILDNPDYYSKGLDYNFSDEVGGLGAFTPFQRQQVTNIPDEVLSQVSNTEIKSDMGIFLELNYCWITSDNKLILWNINNSSEYHCIDEIEHTILKVKLVKPSPNTFVSSVENLLIVATLFDIYILTISFNDRTHELNIFNTGLKVNVTGFNVSNIISYERTGQIFFTGATDGVNVWELQYNCSENLFNSKSNKICLTKSNLANLLPTKLIPSIPGGKLIQKVLEGDAGTEEETISQLEVDQSRGVLHTLSTKSIVRSYLITSNGLVGPVLIDAAHIRRGMNALGVKNSPLLSNRAFKIAKIVSISMCENNDLFLAVITTTGVRLYFKGSISRRSIGSLKLDSVKFPPTSISSSLEQNKSFIIGHHPLNTHDTGPLSTQKASSTYINTTCASTIISPGIYFTCVRKRANSGELSKGITNKALLENKEEHKLYVSAPDYGILKNYGKYVENTALLDTTDEIKEIVPLTRSFNYTSTPQGYANVFASQYSAEPLKVAVLTSNALEIYCYRTPDEVFESLIENPLPFIHSYGLSEACSTALYLACKFNKSEHIKSSALAFFSAGIPGVVEIKPKSSRESGSVPPISQNLFDKSGECDGIVLSPRFYGSALLITRLFSQIWEERVFVFKRASKTEKMDAFGISITRPQVEYYLSSISVLADFFNIHRPSFVSFVPPKGSNAITASDAESIAMNALILLINSIKDALSLINVFYEDIDAFKSLLNTLMGAGGVYDSKTREYFFDLKFHDLFTPNAKTKQLIKEILIEVVNANIASGTSADYIVNVLKERFGSFCHSADILCYRAGEHLEAAQKFEMIDSKISRNHLDTAIDLYERCAENIELCELRRVVDIMVKLNYQPKTVGFLLRFADKIDKGNQAQEYVSRGCNTADPRKVFYDKRINVYTLIFEIVKSVDDYTSIEQSPSIANISIFSPASSLKKRVYSVIMNSNNRFFHYCFYDWLVANKRQDYLLRLDSQFVLPYLKERAEKSLEISNLLWFYLFKEEHFLEAADVLYALASSDFDLKLSERIECLARANGLCDSSTSFDQKPALVQLSENIHELFDIASIQDDLLNLVRNETRIDEDYRKQLTLKLNGRVLPLSDLFNDCADPLDYYEIKLRIFKVSQFKDEKVIQGEWNRLLDSMKNAPSPDVGSVGQESFLSSISNTLIRIGKTTRDTDVVFPVHFLMNKILESFIDKSSAADGSVCSMFLLAGVSHLKLYYILSRIIENSEGNVELAKKEMVWLIKDWYQSDSDLRGSIAPEQIKKLEKYDPNTDPVQDYVKDRHHGLK
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
1Acetylation-------MYSTPLKK
-------CCCCCCCC		28.5922814378
3Phosphorylation-----MYSTPLKKRI
-----CCCCCCCCCC		35.0924603354
4Phosphorylation----MYSTPLKKRID
----CCCCCCCCCCC		31.5828152593
44PhosphorylationNNGKPNLSSRSFLSE
CCCCCCCCHHHHHCC		30.2823749301
50PhosphorylationLSSRSFLSERKTRKD
CCHHHHHCCCCCHHH		33.0927017623
171PhosphorylationGIFLELNYCWITSDN
EEEEEEEEEEEECCC		11.2027017623
175PhosphorylationELNYCWITSDNKLIL
EEEEEEEECCCCEEE		12.9127017623
176PhosphorylationLNYCWITSDNKLILW
EEEEEEECCCCEEEE		30.0127017623
337PhosphorylationVLEGDAGTEEETISQ
HHCCCCCCCCEEECC		41.7829688323
341PhosphorylationDAGTEEETISQLEVD
CCCCCCEEECCEEEC		29.2529688323
343PhosphorylationGTEEETISQLEVDQS
CCCCEEECCEEECCC		35.8129688323
350PhosphorylationSQLEVDQSRGVLHTL
CCEEECCCCCCCCCC		26.9129688323
447AcetylationRRSIGSLKLDSVKFP
CCEECCEEECCEECC		52.5324489116
456PhosphorylationDSVKFPPTSISSSLE
CCEECCCCCCCCCHH		38.6421126336
467PhosphorylationSSLEQNKSFIIGHHP
CCHHHCCCEEEEECC		29.2720377248
517PhosphorylationCVRKRANSGELSKGI
EEECCCCCCCCCCCC		32.4325521595
521PhosphorylationRANSGELSKGITNKA
CCCCCCCCCCCCCHH		25.2419823750
658UbiquitinationFNKSEHIKSSALAFF
CCCCHHHHHHHHHHH		40.0217644757
676UbiquitinationIPGVVEIKPKSSRES
CCCEEEECCCCCCCC		32.6517644757
678UbiquitinationGVVEIKPKSSRESGS
CEEEECCCCCCCCCC		56.9417644757
680PhosphorylationVEIKPKSSRESGSVP
EEECCCCCCCCCCCC		46.3121440633
683PhosphorylationKPKSSRESGSVPPIS
CCCCCCCCCCCCCCC		34.9529734811
685PhosphorylationKSSRESGSVPPISQN
CCCCCCCCCCCCCHH		40.5027214570
690PhosphorylationSGSVPPISQNLFDKS
CCCCCCCCHHCCCCC		20.8428889911
894PhosphorylationVLKERFGSFCHSADI
HHHHHHCHHHHHCCE		23.2223749301
962AcetylationVKLNYQPKTVGFLLR
HHCCCCCCCHHHHHH		40.0724489116
973AcetylationFLLRFADKIDKGNQA
HHHHHHHHHCCCCHH		49.7524489116
976AcetylationRFADKIDKGNQAQEY
HHHHHHCCCCHHHHH		64.3324489116
1024PhosphorylationDYTSIEQSPSIANIS
CCCCHHCCCCCEEEE		14.0721551504
1034PhosphorylationIANISIFSPASSLKK
CEEEEEECCCHHHCH		20.2028889911
1150UbiquitinationSSTSFDQKPALVQLS
CCCCCCCCCHHHHHC		33.8219722269
1189UbiquitinationRIDEDYRKQLTLKLN
CCCHHHHHHHHHHCC		43.3517644757
1194UbiquitinationYRKQLTLKLNGRVLP
HHHHHHHHCCCEEEE		34.3717644757
1216PhosphorylationCADPLDYYEIKLRIF
CCCCCCHHHEEEEEE		15.7328889911
1219UbiquitinationPLDYYEIKLRIFKVS
CCCHHHEEEEEEEHH		21.5517644757
1260PhosphorylationVGSVGQESFLSSISN
CCCCCHHHHHHHHHH		24.4930377154
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 NU157_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NU157_YEAST !!
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 NU157_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAD2_YEASTMAD2physical
10688190
NUP53_YEASTNUP53physical
10688190
EDC3_YEASTEDC3physical
10688190
NU170_YEASTNUP170genetic
8522578
NU188_YEASTNUP188genetic
8522578
NUP82_YEASTNUP82genetic
8628268
NU120_YEASTNUP120physical
15741174
NU145_YEASTNUP145physical
15741174
NUP85_YEASTNUP85physical
15741174
SEH1_YEASTSEH1physical
15741174
SEC13_YEASTSEC13physical
15741174
NUP84_YEASTNUP84physical
15741174
NU133_YEASTNUP133physical
15741174
NU100_YEASTNUP100physical
18467557
NU159_YEASTNUP159physical
18467557
LSM3_YEASTLSM3genetic
19061648
LTV1_YEASTLTV1genetic
19061648
DCPS_YEASTDCS1genetic
19061648
MYO4_YEASTMYO4genetic
19061648
POP8_YEASTPOP8genetic
19061648
NMD5_YEASTNMD5genetic
19061648
CBT1_YEASTCBT1genetic
19061648
RNA14_YEASTRNA14genetic
19061648
NUP53_YEASTNUP53physical
19414609
NU170_YEASTNUP170genetic
19414608
BUD31_YEASTBUD31genetic
20093466
NUP59_YEASTASM4genetic
20093466
ARX1_YEASTARX1genetic
20093466
RLA4_YEASTRPP2Bgenetic
20093466
SGF73_YEASTSGF73genetic
20093466
SLX9_YEASTSLX9genetic
20093466
DHOM_YEASTHOM6genetic
20093466
NU133_YEASTNUP133genetic
20093466
NU188_YEASTNUP188genetic
20093466
SRC1_YEASTSRC1genetic
20093466
NU170_YEASTNUP170genetic
20498018
PO152_YEASTPOM152physical
18046405
NU133_YEASTNUP133physical
18046405
NU120_YEASTNUP120physical
18046405
NIC96_YEASTNIC96physical
18046405
NUP85_YEASTNUP85physical
18046405
NUP84_YEASTNUP84physical
18046405
NU145_YEASTNUP145physical
18046405
SEH1_YEASTSEH1physical
18046405
SEC13_YEASTSEC13physical
18046405
LSP1_YEASTLSP1physical
18046405
SIR4_YEASTSIR4physical
23452847
SCC1_YEASTMCD1genetic
27708008
GLE1_YEASTGLE1genetic
27708008
RPN12_YEASTRPN12genetic
27708008
NU145_YEASTNUP145genetic
27708008
NUP57_YEASTNUP57genetic
27708008
XPO1_YEASTCRM1genetic
27708008
SYMC_YEASTMES1genetic
27708008
MOB1_YEASTMOB1genetic
27708008
NU159_YEASTNUP159genetic
27708008
STS1_YEASTSTS1genetic
27708008
NU192_YEASTNUP192genetic
27708008
EXO70_YEASTEXO70genetic
27708008
NUP85_YEASTNUP85genetic
27708008
NEP1_YEASTEMG1genetic
27708008
IMB1_YEASTKAP95genetic
27708008
GPI12_YEASTGPI12genetic
27708008
NU170_YEASTNUP170genetic
27708008
BUD31_YEASTBUD31genetic
27708008
MTU1_YEASTSLM3genetic
27708008
NUP59_YEASTASM4genetic
27708008
ARX1_YEASTARX1genetic
27708008
SGF73_YEASTSGF73genetic
27708008
MRM2_YEASTMRM2genetic
27708008
SLX9_YEASTSLX9genetic
27708008
DHOM_YEASTHOM6genetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
SAC1_YEASTSAC1genetic
27708008
NU133_YEASTNUP133genetic
27708008
SRC1_YEASTSRC1genetic
27708008
NU188_YEASTNUP188genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NU157_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; SER-685 ANDSER-1034, AND MASS SPECTROMETRY.

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