NU100_YEAST - dbPTM
NU100_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NU100_YEAST
UniProt AC Q02629
Protein Name Nucleoporin NUP100/NSP100
Gene Name NUP100
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 959
Subcellular Localization Nucleus, nuclear pore complex. Nucleus membrane
Peripheral membrane protein
Cytoplasmic side. Nucleus membrane
Peripheral membrane protein
Nucleoplasmic side. Biased towards cytoplasmic 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). NUP100 plays an important role in several nuclear export and import pathways including poly(A)+ RNA and protein transport..
Protein Sequence MFGNNRPMFGGSNLSFGSNTSSFGGQQSQQPNSLFGNSNNNNNSTSNNAQSGFGGFTSAAGSNSNSLFGNNNTQNNGAFGQSMGATQNSPFGSLNSSNASNGNTFGGSSSMGSFGGNTNNAFNNNSNSTNSPFGFNKPNTGGTLFGSQNNNSAGTSSLFGGQSTSTTGTFGNTGSSFGTGLNGNGSNIFGAGNNSQSNTTGSLFGNQQSSAFGTNNQQGSLFGQQSQNTNNAFGNQNQLGGSSFGSKPVGSGSLFGQSNNTLGNTTNNRNGLFGQMNSSNQGSSNSGLFGQNSMNSSTQGVFGQNNNQMQINGNNNNSLFGKANTFSNSASGGLFGQNNQQQGSGLFGQNSQTSGSSGLFGQNNQKQPNTFTQSNTGIGLFGQNNNQQQQSTGLFGAKPAGTTGSLFGGNSSTQPNSLFGTTNVPTSNTQSQQGNSLFGATKLTNMPFGGNPTANQSGSGNSLFGTKPASTTGSLFGNNTASTTVPSTNGLFGNNANNSTSTTNTGLFGAKPDSQSKPALGGGLFGNSNSNSSTIGQNKPVFGGTTQNTGLFGATGTNSSAVGSTGKLFGQNNNTLNVGTQNVPPVNNTTQNALLGTTAVPSLQQAPVTNEQLFSKISIPNSITNPVKATTSKVNADMKRNSSLTSAYRLAPKPLFAPSSNGDAKFQKWGKTLERSDRGSSTSNSITDPESSYLNSNDLLFDPDRRYLKHLVIKNNKNLNVINHNDDEASKVKLVTFTTESASKDDQASSSIAASKLTEKAHSPQTDLKDDHDESTPDPQSKSPNGSTSIPMIENEKISSKVPGLLSNDVTFFKNNYYISPSIETLGNKSLIELRKINNLVIGHRNYGKVEFLEPVDLLNTPLDTLCGDLVTFGPKSCSIYENCSIKPEKGEGINVRCRVTLYSCFPIDKETRKPIKNITHPLLKRSIAKLKENPVYKFESYDPVTGTYSYTIDHPVLT
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
354PhosphorylationFGQNSQTSGSSGLFG
CCCCCCCCCCCCCCC		29.1030377154
457PhosphorylationGNPTANQSGSGNSLF
CCCCCCCCCCCCCCC		34.4328889911
459PhosphorylationPTANQSGSGNSLFGT
CCCCCCCCCCCCCCC		39.7921551504
462PhosphorylationNQSGSGNSLFGTKPA
CCCCCCCCCCCCCCC		28.7124961812
530PhosphorylationGLFGNSNSNSSTIGQ
CCCCCCCCCCCCCCC		37.6021551504
564PhosphorylationTNSSAVGSTGKLFGQ
CCCCCCCCCCEEECC		27.6424961812
565PhosphorylationNSSAVGSTGKLFGQN
CCCCCCCCCEEECCC		32.1924961812
642PhosphorylationNADMKRNSSLTSAYR
CHHHHCCCCCCCHHH		30.6622369663
643PhosphorylationADMKRNSSLTSAYRL
HHHHCCCCCCCHHHC		38.9322369663
645PhosphorylationMKRNSSLTSAYRLAP
HHCCCCCCCHHHCCC		17.1722369663
646PhosphorylationKRNSSLTSAYRLAPK
HCCCCCCCHHHCCCC		28.7022369663
648PhosphorylationNSSLTSAYRLAPKPL
CCCCCCHHHCCCCCC		13.1121440633
660PhosphorylationKPLFAPSSNGDAKFQ
CCCCCCCCCCCHHHH		43.7123749301
665AcetylationPSSNGDAKFQKWGKT
CCCCCCHHHHHHCCE		53.7424489116
676PhosphorylationWGKTLERSDRGSSTS
HCCEECCCCCCCCCC		23.4521440633
685PhosphorylationRGSSTSNSITDPESS
CCCCCCCCCCCCCHH		27.0023749301
714AcetylationYLKHLVIKNNKNLNV
HHHEEEEECCCCCCE		47.1625381059
730PhosphorylationNHNDDEASKVKLVTF
CCCCCHHHEEEEEEE		35.6121551504
736PhosphorylationASKVKLVTFTTESAS
HHEEEEEEEECCCCC		26.2123749301
738PhosphorylationKVKLVTFTTESASKD
EEEEEEEECCCCCCC		21.9329688323
739PhosphorylationVKLVTFTTESASKDD
EEEEEEECCCCCCCC		24.6124961812
741PhosphorylationLVTFTTESASKDDQA
EEEEECCCCCCCCHH		35.4329688323
743PhosphorylationTFTTESASKDDQASS
EEECCCCCCCCHHHH		45.9921551504
744AcetylationFTTESASKDDQASSS
EECCCCCCCCHHHHH		66.1124489116
749PhosphorylationASKDDQASSSIAASK
CCCCCHHHHHHHHHH		20.9821440633
763PhosphorylationKLTEKAHSPQTDLKD
HHHHCCCCCCCCCCC		24.4622369663
766PhosphorylationEKAHSPQTDLKDDHD
HCCCCCCCCCCCCCC		46.8425521595
775PhosphorylationLKDDHDESTPDPQSK
CCCCCCCCCCCCCCC		51.8322369663
776PhosphorylationKDDHDESTPDPQSKS
CCCCCCCCCCCCCCC		29.6620377248
781PhosphorylationESTPDPQSKSPNGST
CCCCCCCCCCCCCCC		40.2529136822
783PhosphorylationTPDPQSKSPNGSTSI
CCCCCCCCCCCCCCC		28.9222369663
787PhosphorylationQSKSPNGSTSIPMIE
CCCCCCCCCCCCEEE		26.1425521595
788PhosphorylationSKSPNGSTSIPMIEN
CCCCCCCCCCCEEEC		31.8822369663
789PhosphorylationKSPNGSTSIPMIENE
CCCCCCCCCCEEECC		26.7922369663
807PhosphorylationSKVPGLLSNDVTFFK
CCCCCHHCCCEEEEE		35.7122369663
811PhosphorylationGLLSNDVTFFKNNYY
CHHCCCEEEEECCEE		26.6422369663
910AcetylationYSCFPIDKETRKPIK
EECCCCCHHHCCCCC		62.8024489116
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 NU100_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NU100_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 NU100_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMB1_YEASTKAP95physical
9151683
RRP12_YEASTRRP12physical
14729571
NU188_YEASTNUP188physical
12543930
NU188_YEASTNUP188physical
11387327
MSN5_YEASTMSN5physical
12543930
MSN5_YEASTMSN5physical
11387327
NU133_YEASTNUP133physical
12543930
NU133_YEASTNUP133physical
11387327
IMB4_YEASTKAP123physical
12543930
IMB4_YEASTKAP123physical
11387327
XPO1_YEASTCRM1physical
12543930
XPO1_YEASTCRM1physical
11387327
TOF1_YEASTTOF1physical
12543930
TOF1_YEASTTOF1physical
11387327
SXM1_YEASTSXM1physical
12543930
SXM1_YEASTSXM1physical
11387327
NU120_YEASTNUP120physical
12543930
NU120_YEASTNUP120physical
11387327
NUP2_YEASTNUP2physical
12543930
NUP2_YEASTNUP2physical
11387327
IMB1_YEASTKAP95physical
12543930
IMB1_YEASTKAP95physical
11387327
NUP85_YEASTNUP85physical
12543930
NUP85_YEASTNUP85physical
11387327
NU145_YEASTNUP145physical
12543930
NU145_YEASTNUP145physical
11387327
HSP72_YEASTSSA2physical
12543930
HSP72_YEASTSSA2physical
11387327
PABP_YEASTPAB1physical
12543930
PABP_YEASTPAB1physical
11387327
MEX67_YEASTMEX67physical
12543930
MEX67_YEASTMEX67physical
11387327
IMA1_YEASTSRP1physical
12543930
IMA1_YEASTSRP1physical
11387327
IMB3_YEASTPSE1physical
12543930
IMB3_YEASTPSE1physical
11387327
TFC1_YEASTTFC1physical
12543930
TFC1_YEASTTFC1physical
11387327
IMB2_YEASTKAP104physical
12543930
IMB2_YEASTKAP104physical
11387327
SMC2_YEASTSMC2physical
12543930
SMC2_YEASTSMC2physical
11387327
NUP84_YEASTNUP84physical
12543930
NUP84_YEASTNUP84physical
11387327
HRP1_YEASTHRP1physical
12543930
HRP1_YEASTHRP1physical
11387327
ARX1_YEASTARX1physical
12543930
ARX1_YEASTARX1physical
11387327
RL2A_YEASTRPL2Aphysical
11387327
RL2B_YEASTRPL2Aphysical
11387327
MEX67_YEASTMEX67physical
11104765
NOG1_YEASTNOG1physical
11387327
NU170_YEASTNUP170physical
11387327
KA120_YEASTKAP120physical
11387327
GLE2_YEASTGLE2genetic
8970155
NU116_YEASTNUP116genetic
8970155
RMT2_YEASTRMT2physical
17448464
NU145_YEASTNUP145genetic
17875746
NUP57_YEASTNUP57genetic
17875746
IMB1_YEASTKAP95physical
17897934
NU116_YEASTNUP116physical
17897934
IMB1_YEASTKAP95physical
18467557
NU116_YEASTNUP116physical
18467557
NUP60_YEASTNUP60genetic
19061648
HPR1_YEASTHPR1genetic
19061648
SAC3_YEASTSAC3genetic
19061648
SEM1_YEASTSEM1genetic
19061648
ARC1_YEASTARC1genetic
19061648
NUP57_YEASTNUP57genetic
19061648
MOG1_YEASTMOG1genetic
19061648
UTP11_YEASTUTP11genetic
19061648
RRP6_YEASTRRP6genetic
19061648
NU188_YEASTNUP188genetic
19061648
LSM7_YEASTLSM7genetic
19061648
SYDM_YEASTMSD1genetic
19061648
THP2_YEASTTHP2genetic
19061648
GBP2_YEASTGBP2genetic
19061648
NU170_YEASTNUP170genetic
19061648
KA120_YEASTKAP120genetic
19061648
IF4B_YEASTTIF3genetic
19061648
NU100_YEASTNUP100physical
19345193
NUP49_YEASTNUP49genetic
19759143
NUP57_YEASTNUP57genetic
19759143
NSP1_YEASTNSP1genetic
19759143
NU145_YEASTNUP145genetic
19759143
MDV1_YEASTMDV1physical
19759143
NUP60_YEASTNUP60genetic
20093466
SAC3_YEASTSAC3genetic
20093466
THP2_YEASTTHP2genetic
20093466
NU133_YEASTNUP133genetic
20093466
NU188_YEASTNUP188genetic
20093466
YO13A_YEASTYOL013W-Agenetic
20093466
ARX1_YEASTARX1physical
17803941
NU192_YEASTNUP192physical
18046405
NU188_YEASTNUP188physical
18046405
NU170_YEASTNUP170physical
18046405
NU159_YEASTNUP159physical
18046405
PO152_YEASTPOM152physical
18046405
NU133_YEASTNUP133physical
18046405
NU120_YEASTNUP120physical
18046405
NU116_YEASTNUP116physical
18046405
NSP1_YEASTNSP1physical
18046405
NIC96_YEASTNIC96physical
18046405
NUP84_YEASTNUP84physical
18046405
NUP82_YEASTNUP82physical
18046405
NU145_YEASTNUP145physical
18046405
NUP59_YEASTASM4physical
18046405
MEX67_YEASTMEX67physical
18046405
IMB1_YEASTKAP95physical
22357553
IMB3_YEASTPSE1physical
22357553
IMB4_YEASTKAP123physical
22357553
NUP82_YEASTNUP82physical
22480613
GLE1_YEASTGLE1genetic
8970155
GSP1_YEASTGSP1genetic
25778920
MAK16_YEASTMAK16genetic
27708008
AAR2_YEASTAAR2genetic
27708008
ENP1_YEASTENP1genetic
27708008
NOP14_YEASTNOP14genetic
27708008
GLE1_YEASTGLE1genetic
27708008
NU145_YEASTNUP145genetic
27708008
RCC1_YEASTSRM1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
NUP57_YEASTNUP57genetic
27708008
XPO1_YEASTCRM1genetic
27708008
NU159_YEASTNUP159genetic
27708008
NU192_YEASTNUP192genetic
27708008
KTHY_YEASTCDC8genetic
27708008
NEP1_YEASTEMG1genetic
27708008
GSP1_YEASTGSP1genetic
27708008
MED4_YEASTMED4genetic
27708008
EI2BG_YEASTGCD1genetic
27708008
NUP60_YEASTNUP60genetic
27708008
SAC3_YEASTSAC3genetic
27708008
THP2_YEASTTHP2genetic
27708008
NU188_YEASTNUP188genetic
27708008
YO13A_YEASTYOL013W-Agenetic
27708008
HSP7F_YEASTSSE1genetic
27708008
RTP1_YEASTRTP1physical
23438601
RL36A_YEASTRPL36Agenetic
29158977
MTR2_YEASTMTR2physical
23212245
MEX67_YEASTMEX67physical
23212245
BUD20_YEASTBUD20physical
23212245
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NU100_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-643 AND SER-783, ANDMASS 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-763, AND MASSSPECTROMETRY.

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