NUP2_YEAST - dbPTM
NUP2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUP2_YEAST
UniProt AC P32499
Protein Name Nucleoporin NUP2
Gene Name NUP2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 720
Subcellular Localization Nucleus, nuclear pore complex. Nucleus membrane
Peripheral membrane protein
Nucleoplasmic side.
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 (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP2 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP1 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading..
Protein Sequence MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTFGSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQEDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINTNTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKGSQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKKDDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK
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
14PhosphorylationDAQIQRETYDSNESD
HHHHHHHHCCCCCCC		34.5122369663
15PhosphorylationAQIQRETYDSNESDD
HHHHHHHCCCCCCCC		16.7825521595
17PhosphorylationIQRETYDSNESDDDV
HHHHHCCCCCCCCCC		31.8922369663
20PhosphorylationETYDSNESDDDVTPS
HHCCCCCCCCCCCCC		51.0622369663
25PhosphorylationNESDDDVTPSTKVAS
CCCCCCCCCCHHHHH		20.6522890988
27PhosphorylationSDDDVTPSTKVASSA
CCCCCCCCHHHHHHH		31.3422890988
28PhosphorylationDDDVTPSTKVASSAV
CCCCCCCHHHHHHHH		30.6422890988
32PhosphorylationTPSTKVASSAVMNRR
CCCHHHHHHHHHCHH		23.0922369663
33PhosphorylationPSTKVASSAVMNRRK
CCHHHHHHHHHCHHC		18.3622369663
51AcetylationPKRRMAFKPFGSAKS
CCCCCCCCCCCCCCC		29.8724489116
55PhosphorylationMAFKPFGSAKSDETK
CCCCCCCCCCCCCCC		32.6630377154
57AcetylationFKPFGSAKSDETKQA
CCCCCCCCCCCCCCC		61.2024489116
58PhosphorylationKPFGSAKSDETKQAS
CCCCCCCCCCCCCCC		40.1628889911
62AcetylationSAKSDETKQASSFSF
CCCCCCCCCCCCCCC		41.6524489116
65PhosphorylationSDETKQASSFSFLNR
CCCCCCCCCCCCCCC		29.4422369663
66PhosphorylationDETKQASSFSFLNRA
CCCCCCCCCCCCCCC		28.1122369663
68PhosphorylationTKQASSFSFLNRADG
CCCCCCCCCCCCCCC		30.6722369663
76PhosphorylationFLNRADGTGEAQVDN
CCCCCCCCCCCCCCC		32.1822369663
84PhosphorylationGEAQVDNSPTTESNS
CCCCCCCCCCCCCCH		21.1122369663
86PhosphorylationAQVDNSPTTESNSRL
CCCCCCCCCCCCHHH		42.9122369663
87PhosphorylationQVDNSPTTESNSRLK
CCCCCCCCCCCHHHH		40.5822369663
89PhosphorylationDNSPTTESNSRLKAL
CCCCCCCCCHHHHHH		37.7022369663
91PhosphorylationSPTTESNSRLKALNL
CCCCCCCHHHHHHCC		48.5522369663
103AcetylationLNLQFKAKVDDLVLG
HCCEEEEECCHHCCC		46.9524489116
123PhosphorylationLRPLFTRYELYIKNI
HHHHHHHHHHHHHHH		13.7625533186
136AcetylationNILEAPVKSIENPTQ
HHHHCCCEECCCCCC		44.6624489116
137PhosphorylationILEAPVKSIENPTQT
HHHCCCEECCCCCCC		35.0625752575
142PhosphorylationVKSIENPTQTKGNDA
CEECCCCCCCCCCCC		61.5217563356
144PhosphorylationSIENPTQTKGNDAKP
ECCCCCCCCCCCCCC		43.3227017623
160PhosphorylationKVEDVQKSSDSSSED
CHHHHHHCCCCCCCC		23.4522369663
161PhosphorylationVEDVQKSSDSSSEDE
HHHHHHCCCCCCCCC		48.8525521595
163PhosphorylationDVQKSSDSSSEDEVK
HHHHCCCCCCCCCEE		37.4022369663
164PhosphorylationVQKSSDSSSEDEVKV
HHHCCCCCCCCCEEE		42.6122369663
165PhosphorylationQKSSDSSSEDEVKVE
HHCCCCCCCCCEEEE		53.6825521595
181AcetylationPKFTIDAKPPISDSV
CCEEECCCCCCCCCC		47.8024489116
185PhosphorylationIDAKPPISDSVFSFG
ECCCCCCCCCCCCCC		29.6130377154
187PhosphorylationAKPPISDSVFSFGPK
CCCCCCCCCCCCCCC		20.4730377154
190PhosphorylationPISDSVFSFGPKKEN
CCCCCCCCCCCCHHC		27.4317563356
203PhosphorylationENRKKDESDSENDIE
HCCCCCCCCCCCCCE		57.4822369663
205PhosphorylationRKKDESDSENDIEIK
CCCCCCCCCCCCEEE		47.8022369663
219PhosphorylationKGPEFKFSGTVSSDV
ECCCCEEEEEECCCE		33.8617563356
221PhosphorylationPEFKFSGTVSSDVFK
CCCEEEEEECCCEEE		18.9330377154
223PhosphorylationFKFSGTVSSDVFKLN
CEEEEEECCCEEECC		22.2122369663
224PhosphorylationKFSGTVSSDVFKLNP
EEEEEECCCEEECCC		33.2022369663
228AcetylationTVSSDVFKLNPSTDK
EECCCEEECCCCCCC		47.4024489116
232PhosphorylationDVFKLNPSTDKNEKK
CEEECCCCCCCCCCC		48.4430377154
239AcetylationSTDKNEKKTETNAKP
CCCCCCCCCCCCCCC		45.4724489116
245AcetylationKKTETNAKPFSFSSA
CCCCCCCCCCCCCCC		48.9824489116
248PhosphorylationETNAKPFSFSSATST
CCCCCCCCCCCCCCC		32.5217563356
250PhosphorylationNAKPFSFSSATSTTE
CCCCCCCCCCCCCCC		20.1924961812
251PhosphorylationAKPFSFSSATSTTEQ
CCCCCCCCCCCCCCC		33.2928889911
253PhosphorylationPFSFSSATSTTEQTK
CCCCCCCCCCCCCCC		28.6730377154
254PhosphorylationFSFSSATSTTEQTKS
CCCCCCCCCCCCCCC		32.8030377154
255PhosphorylationSFSSATSTTEQTKSK
CCCCCCCCCCCCCCC		29.9630377154
261PhosphorylationSTTEQTKSKNPLSLT
CCCCCCCCCCCCCCC		40.8422369663
262AcetylationTTEQTKSKNPLSLTE
CCCCCCCCCCCCCCC		65.2324489116
266PhosphorylationTKSKNPLSLTEATKT
CCCCCCCCCCCCEEC		34.2123749301
268PhosphorylationSKNPLSLTEATKTNV
CCCCCCCCCCEECCC		21.8730377154
271PhosphorylationPLSLTEATKTNVDNN
CCCCCCCEECCCCCC		31.9730377154
272AcetylationLSLTEATKTNVDNNS
CCCCCCEECCCCCCC		45.1924489116
273PhosphorylationSLTEATKTNVDNNSK
CCCCCEECCCCCCCC		35.8030377154
279PhosphorylationKTNVDNNSKAEASFT
ECCCCCCCCEEEEEE		39.2230377154
280AcetylationTNVDNNSKAEASFTF
CCCCCCCCEEEEEEE		52.9822865919
284PhosphorylationNNSKAEASFTFGTKH
CCCCEEEEEEECCCC		19.1422369663
286PhosphorylationSKAEASFTFGTKHAA
CCEEEEEEECCCCCC		20.7522369663
289PhosphorylationEASFTFGTKHAADSQ
EEEEEECCCCCCCCC		18.5722369663
295PhosphorylationGTKHAADSQNNKPSF
CCCCCCCCCCCCCCE		30.0422369663
299AcetylationAADSQNNKPSFVFGQ
CCCCCCCCCCEEEEE		49.9824489116
301PhosphorylationDSQNNKPSFVFGQAA
CCCCCCCCEEEEECC		35.3322369663
310AcetylationVFGQAAAKPSLEKSS
EEEECCCCCCCCCCE		30.3424489116
312PhosphorylationGQAAAKPSLEKSSFT
EECCCCCCCCCCEEE		48.7522369663
315AcetylationAAKPSLEKSSFTFGS
CCCCCCCCCEEEECC		57.6125381059
316PhosphorylationAKPSLEKSSFTFGST
CCCCCCCCEEEECCE		22.7025521595
317PhosphorylationKPSLEKSSFTFGSTT
CCCCCCCEEEECCEE		39.1025521595
319PhosphorylationSLEKSSFTFGSTTIE
CCCCCEEEECCEEEE		29.0922369663
322PhosphorylationKSSFTFGSTTIEKKN
CCEEEECCEEEEEEC		20.4122369663
323PhosphorylationSSFTFGSTTIEKKND
CEEEECCEEEEEECC		31.9722369663
324PhosphorylationSFTFGSTTIEKKNDE
EEEECCEEEEEECCC		28.9222369663
327AcetylationFGSTTIEKKNDENST
ECCEEEEEECCCCCC		53.6924489116
337PhosphorylationDENSTSNSKPEKSSD
CCCCCCCCCCCCCCC		49.7219779198
338AcetylationENSTSNSKPEKSSDS
CCCCCCCCCCCCCCC		62.5424489116
342PhosphorylationSNSKPEKSSDSNDSN
CCCCCCCCCCCCCCC		37.4020377248
343PhosphorylationNSKPEKSSDSNDSNP
CCCCCCCCCCCCCCC		57.0120377248
345PhosphorylationKPEKSSDSNDSNPSF
CCCCCCCCCCCCCCC		44.4720377248
348PhosphorylationKSSDSNDSNPSFSFS
CCCCCCCCCCCCCEE		55.6922369663
351PhosphorylationDSNDSNPSFSFSIPS
CCCCCCCCCCEECCC		37.4622369663
353PhosphorylationNDSNPSFSFSIPSKN
CCCCCCCCEECCCCC		23.5620377248
355PhosphorylationSNPSFSFSIPSKNTP
CCCCCCEECCCCCCC		32.1824961812
358PhosphorylationSFSFSIPSKNTPDAS
CCCEECCCCCCCCCC		36.5520377248
359AcetylationFSFSIPSKNTPDASK
CCEECCCCCCCCCCC		60.5324489116
361PhosphorylationFSIPSKNTPDASKPS
EECCCCCCCCCCCCC		26.7029136822
365PhosphorylationSKNTPDASKPSFSFG
CCCCCCCCCCCEECC		53.1029136822
368PhosphorylationTPDASKPSFSFGVPN
CCCCCCCCEECCCCC		36.9421551504
370PhosphorylationDASKPSFSFGVPNSS
CCCCCCEECCCCCCC		25.9829136822
377PhosphorylationSFGVPNSSKNETSKP
ECCCCCCCCCCCCCC		46.2530377154
378AcetylationFGVPNSSKNETSKPV
CCCCCCCCCCCCCCE		59.6322865919
381PhosphorylationPNSSKNETSKPVFSF
CCCCCCCCCCCEEEE		51.9830377154
382PhosphorylationNSSKNETSKPVFSFG
CCCCCCCCCCEEEEC		28.8730377154
383AcetylationSSKNETSKPVFSFGA
CCCCCCCCCEEEECC		53.2524489116
387PhosphorylationETSKPVFSFGAATPS
CCCCCEEEECCCCCC		24.0117563356
392PhosphorylationVFSFGAATPSAKEAS
EEEECCCCCCHHHHC		19.7622369663
394PhosphorylationSFGAATPSAKEASQE
EECCCCCCHHHHCCC		47.8422369663
399PhosphorylationTPSAKEASQEDDNNN
CCCHHHHCCCCCCCC		34.8822369663
409AcetylationDDNNNVEKPSSKPAF
CCCCCCCCCCCCHHH		46.0122865919
411PhosphorylationNNNVEKPSSKPAFNL
CCCCCCCCCCHHHHH		63.1622369663
412PhosphorylationNNVEKPSSKPAFNLI
CCCCCCCCCHHHHHH		51.7022369663
420PhosphorylationKPAFNLISNAGTEKE
CHHHHHHHCCCCHHH		24.6421551504
424PhosphorylationNLISNAGTEKEKESK
HHHHCCCCHHHHHCC		41.2822369663
439PhosphorylationKDSKPAFSFGISNGS
CCCCCCEEECCCCCC		25.3517563356
443PhosphorylationPAFSFGISNGSESKD
CCEEECCCCCCCCCC		35.2022369663
446PhosphorylationSFGISNGSESKDSDK
EECCCCCCCCCCCCC		42.8422369663
448PhosphorylationGISNGSESKDSDKPS
CCCCCCCCCCCCCCC		43.3822369663
453AcetylationSESKDSDKPSLPSAV
CCCCCCCCCCCCCCC		40.2224489116
455PhosphorylationSKDSDKPSLPSAVDG
CCCCCCCCCCCCCCC		59.6619795423
458PhosphorylationSDKPSLPSAVDGEND
CCCCCCCCCCCCCCC		46.3319795423
471AcetylationNDKKEATKPAFSFGI
CCCCCCCCCCEEEEC		41.2024489116
475PhosphorylationEATKPAFSFGINTNT
CCCCCCEEEECCCCC		25.3530377154
489AcetylationTTKTADTKAPTFTFG
CCCCCCCCCCEEECC		53.5724489116
492PhosphorylationTADTKAPTFTFGSSA
CCCCCCCEEECCCCH		39.9222369663
494PhosphorylationDTKAPTFTFGSSALA
CCCCCEEECCCCHHC		29.5722369663
497PhosphorylationAPTFTFGSSALADNK
CCEEECCCCHHCCCH		14.3022369663
498PhosphorylationPTFTFGSSALADNKE
CEEECCCCHHCCCHH		27.9022369663
509AcetylationDNKEDVKKPFSFGTS
CCHHHCCCCCCCCCC		51.6624489116
512PhosphorylationEDVKKPFSFGTSQPN
HHCCCCCCCCCCCCC		31.1517563356
515PhosphorylationKKPFSFGTSQPNNTP
CCCCCCCCCCCCCCC		23.3730377154
516PhosphorylationKPFSFGTSQPNNTPS
CCCCCCCCCCCCCCC		43.9817563356
521PhosphorylationGTSQPNNTPSFSFGK
CCCCCCCCCCCCCCC		27.2730377154
523PhosphorylationSQPNNTPSFSFGKTT
CCCCCCCCCCCCCCC		31.3324909858
525PhosphorylationPNNTPSFSFGKTTAN
CCCCCCCCCCCCCCC		37.1117563356
528AcetylationTPSFSFGKTTANLPA
CCCCCCCCCCCCCCC		40.4624489116
529PhosphorylationPSFSFGKTTANLPAN
CCCCCCCCCCCCCCC		31.3622369663
530PhosphorylationSFSFGKTTANLPANS
CCCCCCCCCCCCCCC		19.6222369663
537PhosphorylationTANLPANSSTSPAPS
CCCCCCCCCCCCCCC		36.7822369663
538PhosphorylationANLPANSSTSPAPSI
CCCCCCCCCCCCCCC		32.4825521595
539PhosphorylationNLPANSSTSPAPSIP
CCCCCCCCCCCCCCC		38.2522369663
540PhosphorylationLPANSSTSPAPSIPS
CCCCCCCCCCCCCCC		22.4725521595
544PhosphorylationSSTSPAPSIPSTGFK
CCCCCCCCCCCCCEE		49.6022369663
547PhosphorylationSPAPSIPSTGFKFSL
CCCCCCCCCCEEEEE		39.2222369663
548PhosphorylationPAPSIPSTGFKFSLP
CCCCCCCCCEEEEEC		41.0822369663
551AcetylationSIPSTGFKFSLPFEQ
CCCCCCEEEEECCCC		35.0724489116
553PhosphorylationPSTGFKFSLPFEQKG
CCCCEEEEECCCCCC		35.4130377154
561PhosphorylationLPFEQKGSQTTTNDS
ECCCCCCCCCCCCCC		31.2422890988
563PhosphorylationFEQKGSQTTTNDSKE
CCCCCCCCCCCCCCC		36.9722890988
564PhosphorylationEQKGSQTTTNDSKEE
CCCCCCCCCCCCCCC		18.9022890988
565PhosphorylationQKGSQTTTNDSKEES
CCCCCCCCCCCCCCC		40.1822890988
568PhosphorylationSQTTTNDSKEESTTE
CCCCCCCCCCCCCCC		44.0022890988
569UbiquitinationQTTTNDSKEESTTEA
CCCCCCCCCCCCCCC		69.2523749301
572PhosphorylationTNDSKEESTTEATGN
CCCCCCCCCCCCCCC		41.5422369663
573PhosphorylationNDSKEESTTEATGNE
CCCCCCCCCCCCCCC		31.7522890988
574PhosphorylationDSKEESTTEATGNES
CCCCCCCCCCCCCCC		32.6622890988
577PhosphorylationEESTTEATGNESQDA
CCCCCCCCCCCCCCC		34.0222890988
581PhosphorylationTEATGNESQDATKVD
CCCCCCCCCCCCCCC		37.0422369663
585PhosphorylationGNESQDATKVDATPE
CCCCCCCCCCCCCCC		39.6322890988
590PhosphorylationDATKVDATPEESKPI
CCCCCCCCCCCCCCC		27.1122369663
594PhosphorylationVDATPEESKPINLQN
CCCCCCCCCCCCCCC		41.9122369663
595AcetylationDATPEESKPINLQNG
CCCCCCCCCCCCCCC		53.8724489116
611PhosphorylationEDEVALFSQKAKLMT
CCHHHEEEHHEEEEE		31.4622369663
615AcetylationALFSQKAKLMTFNAE
HEEEHHEEEEEEECC		45.9124489116
618PhosphorylationSQKAKLMTFNAETKS
EHHEEEEEEECCCCC		24.9517563356
624AcetylationMTFNAETKSYDSRGV
EEEECCCCCCCCCCC		38.2224489116
624SuccinylationMTFNAETKSYDSRGV
EEEECCCCCCCCCCC		38.2223954790
698AcetylationKLVTYIVKFKQKEEG
CEEEEEEEECCHHHC		36.9724489116
707PhosphorylationKQKEEGRSFTKAIED
CCHHHCCCHHHHHHH		48.3930377154
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
68SPhosphorylationKinaseCHEK2-GPS
284SPhosphorylationKinaseCHEK2-GPS
317SPhosphorylationKinaseCHEK2-GPS
351SPhosphorylationKinaseCHEK2-GPS
368SPhosphorylationKinaseCHEK2-GPS
399SPhosphorylationKinaseATM/ATR-GPS
512SPhosphorylationKinaseCHEK2-GPS
523SPhosphorylationKinaseCHEK2-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUP2_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 NUP2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CH10_YEASTHSP10physical
10688190
IMA1_YEASTSRP1physical
8045927
IMA1_YEASTSRP1physical
11425876
IMB1_YEASTKAP95physical
11425876
NUP60_YEASTNUP60physical
11425876
IMA1_YEASTSRP1physical
10725229
IMA1_YEASTSRP1physical
14532109
IMB1_YEASTKAP95physical
11046143
IMA1_YEASTSRP1physical
11046143
IMA1_YEASTSRP1physical
10542277
IMA1_YEASTSRP1physical
14514698
IMB1_YEASTKAP95physical
12543930
IMA1_YEASTSRP1physical
12543930
NU100_YEASTNUP100physical
12543930
IMA1_YEASTSRP1physical
11387327
IMB1_YEASTKAP95physical
11387327
HSP71_YEASTSSA1physical
11387327
SSB1_YEASTSSB1physical
11387327
PABP_YEASTPAB1physical
11387327
IMB1_YEASTKAP95physical
10725229
NUP60_YEASTNUP60genetic
11425876
RCC1_YEASTSRM1genetic
10542277
RNA1_YEASTRNA1genetic
10542277
IMA1_YEASTSRP1genetic
10542277
NUP1_YEASTNUP1genetic
8443417
IMB1_YEASTKAP95physical
16554755
IMA1_YEASTSRP1physical
16554755
IMB1_YEASTKAP95physical
16429126
METK1_YEASTSAM1physical
16429126
IMB4_YEASTKAP123physical
16429126
NUP60_YEASTNUP60physical
16429126
IMA1_YEASTSRP1physical
16429126
RCC1_YEASTSRM1physical
16365162
NUP60_YEASTNUP60physical
16365162
IMA1_YEASTSRP1physical
16365162
IMB1_YEASTKAP95physical
16365162
NUP1_YEASTNUP1physical
16365162
IMB4_YEASTKAP123physical
16365162
ACT_YEASTACT1physical
16365162
RUVB1_YEASTRVB1physical
16365162
RUVB2_YEASTRVB2physical
16365162
NUP60_YEASTNUP60physical
15741174
IMB4_YEASTKAP123physical
15741174
IMB1_YEASTKAP95physical
15741174
IMA1_YEASTSRP1physical
15741174
POM34_YEASTPOM34genetic
19061648
YPT6_YEASTYPT6genetic
19061648
CDC73_YEASTCDC73genetic
19061648
RPB1_YEASTRPO21genetic
19061648
NU170_YEASTNUP170genetic
19061648
CSE1_YEASTCSE1genetic
19061648
MED31_YEASTSOH1genetic
19061648
CGR1_YEASTCGR1genetic
19061648
NUP57_YEASTNUP57genetic
19061648
MOG1_YEASTMOG1genetic
19061648
NU120_YEASTNUP120genetic
19061648
APQ12_YEASTAPQ12genetic
19061648
NU188_YEASTNUP188genetic
19061648
IMA1_YEASTSRP1genetic
19061648
NOP13_YEASTNOP13genetic
19061648
MEX67_YEASTMEX67genetic
19061648
TSR2_YEASTTSR2genetic
19061648
PAP2_YEASTPAP2genetic
19061648
SMT3_YEASTSMT3physical
18719252
SSB1_YEASTSSB1physical
19536198
YPT6_YEASTYPT6genetic
19547744
SLX9_YEASTSLX9genetic
19547744
POM34_YEASTPOM34genetic
19547744
NOP13_YEASTNOP13genetic
19547744
DPB4_YEASTDPB4genetic
20093466
SGF73_YEASTSGF73genetic
20093466
SLX9_YEASTSLX9genetic
20093466
APQ12_YEASTAPQ12genetic
20093466
MOG1_YEASTMOG1genetic
20093466
FRMSR_YEASTYKL069Wgenetic
20093466
NU133_YEASTNUP133genetic
20093466
NU188_YEASTNUP188genetic
20093466
MSB4_YEASTMSB4genetic
20093466
ECM1_YEASTECM1genetic
20348449
HOG1_YEASTHOG1physical
23645671
DPOD_YEASTPOL3genetic
27708008
VMA21_YEASTVMA21genetic
27708008
ORC2_YEASTORC2genetic
27708008
POP7_YEASTPOP7genetic
27708008
PRP5_YEASTPRP5genetic
27708008
RPB1_YEASTRPO21genetic
27708008
NOP14_YEASTNOP14genetic
27708008
DBF4_YEASTDBF4genetic
27708008
TAF12_YEASTTAF12genetic
27708008
TRS23_YEASTTRS23genetic
27708008
RPN12_YEASTRPN12genetic
27708008
NU145_YEASTNUP145genetic
27708008
SP105_YEASTSPC105genetic
27708008
RCC1_YEASTSRM1genetic
27708008
PRP43_YEASTPRP43genetic
27708008
BRR6_YEASTBRR6genetic
27708008
CBF3A_YEASTCBF2genetic
27708008
BRL1_YEASTBRL1genetic
27708008
UTP9_YEASTUTP9genetic
27708008
DSN1_YEASTDSN1genetic
27708008
STS1_YEASTSTS1genetic
27708008
NU192_YEASTNUP192genetic
27708008
NUP85_YEASTNUP85genetic
27708008
STU2_YEASTSTU2genetic
27708008
CFT2_YEASTCFT2genetic
27708008
BET5_YEASTBET5genetic
27708008
GPI12_YEASTGPI12genetic
27708008
HAS1_YEASTHAS1genetic
27708008
TRM6_YEASTGCD10genetic
27708008
RPC6_YEASTRPC34genetic
27708008
EI2BG_YEASTGCD1genetic
27708008
NU170_YEASTNUP170genetic
27708008
ARX1_YEASTARX1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
SGF73_YEASTSGF73genetic
27708008
SLX9_YEASTSLX9genetic
27708008
HTD2_YEASTHTD2genetic
27708008
LPLA_YEASTAIM22genetic
27708008
MOG1_YEASTMOG1genetic
27708008
FABG_YEASTOAR1genetic
27708008
NU133_YEASTNUP133genetic
27708008
NU188_YEASTNUP188genetic
27708008
MSB4_YEASTMSB4genetic
27708008
SPO11_YEASTSPO11genetic
28455351
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NUP2_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 TYR-15; SER-17; SER-20;SER-66; SER-68; SER-84; SER-137; SER-160; SER-163; SER-165; SER-203;SER-205; SER-224; SER-248; SER-251; SER-284; SER-317; SER-342;SER-351; SER-353; SER-368; SER-370; SER-455; SER-516; SER-538; SER-540AND THR-590, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-68; SER-84;THR-142; SER-163; SER-165; SER-190; SER-203; SER-205; SER-219;SER-248; SER-284; SER-317; SER-351; SER-368; SER-387; SER-399;SER-439; THR-494; SER-512; SER-516; SER-523; SER-525; SER-540;SER-561; SER-572; SER-581; THR-590 AND THR-618, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-203 ANDSER-205, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-165;SER-203 AND SER-205, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-17 AND SER-20,AND MASS SPECTROMETRY.

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