PO152_YEAST - dbPTM
PO152_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PO152_YEAST
UniProt AC P39685
Protein Name Nucleoporin POM152
Gene Name POM152
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1337
Subcellular Localization Nucleus, nuclear pore complex. Nucleus membrane
Multi-pass membrane protein. Central core structure of the 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. POM152 is important for the de novo assembly of NPCs..
Protein Sequence MEHRYNVFNDTPRGNHWMGSSVSGSPRPSYSSRPNVNTTRRFQYSDDEPAEKIRPLRSRSFKSTESNISDEKSRISERDSKDRYINGDKKVDIYSLPLISTDVLEISKQRTFAVILFLIIQCYKIYDLVILKSGLPLSGLLFKNYRFNFISKYFIIDSFFLYVLPSFNIPRLTFKPWVVYLQILAMLLLNIFISSDHEFVLISLIMTTWRKLYTKELSVTGSAINHHRIFDSSAHFKGALTIKILPENTAMFNPLHESYCLPMDTNLFKINSIDVPIRINSTEEIEYIELEYRDLYTNSVELRSLSKKDFKIIDNPKSFLKKDQSVLKSHSNDFEEGSTIRYLAVTLQDIGFYQIKKIVDSKKLNLKIHQSHLVVPYCPIASITGTGSNDRCIGDSDNVSFEIQGVPPMKLAYSKIVNGQTFSYVDSSLQPEYFESPLQSSKSKQSFTQGELNDLKWGRNQPVNINLDSSITQDGKFAYKIDKITDGLGNVVDFTSLPEELKKRYDLSYNFNVHEVPRAALEERFDPKSPTKRSIAIVFEEIKNWISDIPYVISLSYTDAQDKSKKIMNVTTDSLTKVLQADLPGSYNLEYIESKFCPGEIVGKSNVLVTMPVAPTMEVKSFPILDQCVGQVGLNFELSFTGAPPYYYNTKIYKLENGERKLYDAKRYTSEGTRNRFSYSPPKEGNYEIVFDTVSNKLFTEPIKLEPVKEYTFKTSMRVKPSASLKLHHDLKLCLGDHSSVPVALKGQGPFTLTYDIIETFSSKRKTFEIKEIKTNEYVIKTPVFTTGGDYILSLVSIKDSTGCVVGLSQPDAKIQVRRDIPSAAFNFFEPIKEAKIKHGSVTEIPLKLSGEGPFTVKFKHMDYDGNIVKEFENKFQNSYKPALKVSKEGLYQLVDIRDSSCQGNVIYRNSLYKVSFLEKPKFAIQDNHHITKVTENLFSKEEVCQGMEGTVDLALFGSPPFILEYDLMAPNGHISTKKIQVATKYASLKLPNQIPGEYITTIKAIFDGNYGESDIHFREHQSELIIKQTVHPIPDVAFADGGKTLRACAANVDQISFLEPINLKFLQGESPFSITFSVYHESTSRTDQYTIDNIDSENFSFEKLYEGMKLGNHAITIDSVVDANGCVNSLISGPRNQILVSITDAPKIHILDPSTEYCVGDYVAYQLNGVAPFMIKYEFNGIPLKSKERSSQFVRLASEPGIISITSLQDSSSQCIVDFTNPKLKSEFDDLSLNIHPIPSVTVSQGNYVTEDIREGDQAEVIFSFEGTPPFSLTYVRTEETDGKHGKRRSQVVETHKVTDIYSHEYKVITSLQGTYEAIEITDAYCFAKNDLFFNN
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
11PhosphorylationRYNVFNDTPRGNHWM
CCCCCCCCCCCCCCC		18.9122369663
23PhosphorylationHWMGSSVSGSPRPSY
CCCCCCCCCCCCCCC		35.1928889911
25PhosphorylationMGSSVSGSPRPSYSS
CCCCCCCCCCCCCCC		15.3825704821
31PhosphorylationGSPRPSYSSRPNVNT
CCCCCCCCCCCCCCC		24.9819779198
44PhosphorylationNTTRRFQYSDDEPAE
CCCCCEECCCCCCHH		16.0327214570
45PhosphorylationTTRRFQYSDDEPAEK
CCCCEECCCCCCHHH		28.0017330950
52AcetylationSDDEPAEKIRPLRSR
CCCCCHHHHHCCCCC		46.2324489116
58PhosphorylationEKIRPLRSRSFKSTE
HHHHCCCCCCCCCCC		39.7019795423
60PhosphorylationIRPLRSRSFKSTESN
HHCCCCCCCCCCCCC		37.9717287358
63PhosphorylationLRSRSFKSTESNISD
CCCCCCCCCCCCCCC		35.0823749301
64PhosphorylationRSRSFKSTESNISDE
CCCCCCCCCCCCCCH		43.9824961812
66PhosphorylationRSFKSTESNISDEKS
CCCCCCCCCCCCHHH		39.2823749301
69PhosphorylationKSTESNISDEKSRIS
CCCCCCCCCHHHHHC		43.9223749301
73PhosphorylationSNISDEKSRISERDS
CCCCCHHHHHCCCCC		32.5730377154
76PhosphorylationSDEKSRISERDSKDR
CCHHHHHCCCCCCCC		26.0127717283
80PhosphorylationSRISERDSKDRYING
HHHCCCCCCCCCCCC		42.5527717283
280N-linked_GlycosylationIDVPIRINSTEEIEY
EECCEECCCCCEEEE		32.798138573
356UbiquitinationDIGFYQIKKIVDSKK
HHEEEEEEEECCCCC		22.4117644757
357UbiquitinationIGFYQIKKIVDSKKL
HEEEEEEEECCCCCC		49.9817644757
505PhosphorylationPEELKKRYDLSYNFN
CHHHHHHHCCCCCCC		30.0728889911
508PhosphorylationLKKRYDLSYNFNVHE
HHHHHCCCCCCCCCC		18.3521082442
509PhosphorylationKKRYDLSYNFNVHEV
HHHHCCCCCCCCCCC		30.9428889911
577UbiquitinationVTTDSLTKVLQADLP
ECHHHHHHHHHCCCC		46.3617644757
595UbiquitinationNLEYIESKFCPGEIV
CCCEEECCCCCCCEE		37.8917644757
697UbiquitinationVFDTVSNKLFTEPIK
EEEECCCCCCCCCEE		37.1517644757
704UbiquitinationKLFTEPIKLEPVKEY
CCCCCCEECEECCEE		58.4717644757
709UbiquitinationPIKLEPVKEYTFKTS
CEECEECCEEEEEEE		56.5717644757
709AcetylationPIKLEPVKEYTFKTS
CEECEECCEEEEEEE		56.5724489116
714UbiquitinationPVKEYTFKTSMRVKP
ECCEEEEEEECCCCC		31.7117644757
746UbiquitinationSSVPVALKGQGPFTL
CCCCEEECCCCCEEE		39.1817644757
752PhosphorylationLKGQGPFTLTYDIIE
ECCCCCEEEEEEHHH		22.7127017623
754PhosphorylationGQGPFTLTYDIIETF
CCCCEEEEEEHHHHH		18.9827017623
762PhosphorylationYDIIETFSSKRKTFE
EEHHHHHCCCCCEEE		42.2328889911
763PhosphorylationDIIETFSSKRKTFEI
EHHHHHCCCCCEEEE		32.0828889911
764UbiquitinationIIETFSSKRKTFEIK
HHHHHCCCCCEEEEE		57.6317644757
771AcetylationKRKTFEIKEIKTNEY
CCCEEEEEECCCCCE		46.3024489116
781UbiquitinationKTNEYVIKTPVFTTG
CCCCEEEECCEEECC		36.4117644757
787PhosphorylationIKTPVFTTGGDYILS
EECCEEECCCCEEEE		27.9228889911
797PhosphorylationDYILSLVSIKDSTGC
CEEEEEEEEECCCCC		29.2528889911
799UbiquitinationILSLVSIKDSTGCVV
EEEEEEEECCCCCEE		37.8117644757
814UbiquitinationGLSQPDAKIQVRRDI
EECCCCCEEEEECCC		40.8417644757
833UbiquitinationFNFFEPIKEAKIKHG
HHCCCCCCCCCCCCC		63.4317644757
836UbiquitinationFEPIKEAKIKHGSVT
CCCCCCCCCCCCCEE		54.0717644757
838UbiquitinationPIKEAKIKHGSVTEI
CCCCCCCCCCCEEEE		41.0017644757
848UbiquitinationSVTEIPLKLSGEGPF
CEEEEEEEECCCCCE		34.9417644757
848AcetylationSVTEIPLKLSGEGPF
CEEEEEEEECCCCCE		34.9424489116
870AcetylationDYDGNIVKEFENKFQ
CCCCCHHHHHHHHCC		53.5424489116
875AcetylationIVKEFENKFQNSYKP
HHHHHHHHCCCCCCC		40.9224489116
888AcetylationKPALKVSKEGLYQLV
CCCEECCCCCEEEEE		59.8124489116
914UbiquitinationIYRNSLYKVSFLEKP
EECCCEEEEEEECCC		36.3717644757
920AcetylationYKVSFLEKPKFAIQD
EEEEEECCCCEEEEC		56.5124489116
920UbiquitinationYKVSFLEKPKFAIQD
EEEEEECCCCEEEEC		56.5117644757
922UbiquitinationVSFLEKPKFAIQDNH
EEEECCCCEEEECCC		59.5017644757
933UbiquitinationQDNHHITKVTENLFS
ECCCCCCHHHHCCCC		46.7017644757
1130PhosphorylationDANGCVNSLISGPRN
ECCCHHHHHHCCCCC		13.4930377154
1133PhosphorylationGCVNSLISGPRNQIL
CHHHHHHCCCCCEEE		48.3030377154
1249PhosphorylationVTVSQGNYVTEDIRE
EEECCCCEEECCCCC		18.6428132839
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 PO152_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PO152_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 PO152_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IKS1_YEASTIKS1physical
10688190
NUP53_YEASTNUP53physical
10688190
SMC3_YEASTSMC3physical
11087867
NIC96_YEASTNIC96physical
8682855
NDC1_YEASTNDC1physical
9864355
NU188_YEASTNUP188genetic
8682855
NIC96_YEASTNIC96genetic
8522578
NU157_YEASTNUP157genetic
8522578
NU170_YEASTNUP170genetic
8522578
NU188_YEASTNUP188genetic
8522578
NU188_YEASTNUP188genetic
9988776
NUP59_YEASTASM4genetic
9988776
NU170_YEASTNUP170genetic
9988776
NIC96_YEASTNIC96genetic
9988776
UTP8_YEASTUTP8physical
17634288
SAC3_YEASTSAC3genetic
19061648
NUP57_YEASTNUP57genetic
19061648
NMD5_YEASTNMD5genetic
19061648
NU120_YEASTNUP120genetic
19061648
APQ12_YEASTAPQ12genetic
19061648
SRC1_YEASTSRC1genetic
19061648
RNA14_YEASTRNA14genetic
19061648
MEX67_YEASTMEX67genetic
19061648
KA120_YEASTKAP120genetic
19061648
THP2_YEASTTHP2genetic
19061648
KRR1_YEASTKRR1genetic
19061648
SAP30_YEASTSAP30genetic
19061648
NDC1_YEASTNDC1physical
19414609
POM34_YEASTPOM34physical
19414609
HSP72_YEASTSSA2physical
19536198
HSP7F_YEASTSSE1physical
19536198
GDIR_YEASTRDI1genetic
20093466
NUP59_YEASTASM4genetic
20093466
ARX1_YEASTARX1genetic
20093466
PEX3_YEASTPEX3genetic
20093466
SLX9_YEASTSLX9genetic
20093466
THP2_YEASTTHP2genetic
20093466
FRMSR_YEASTYKL069Wgenetic
20093466
VPS24_YEASTVPS24genetic
20093466
NU133_YEASTNUP133genetic
20093466
NU188_YEASTNUP188genetic
20093466
SRC1_YEASTSRC1genetic
20093466
EOS1_YEASTEOS1genetic
20093466
NU170_YEASTNUP170physical
18046405
NU157_YEASTNUP157physical
18046405
NIC96_YEASTNIC96physical
18046405
NUP59_YEASTASM4physical
18046405
NDC1_YEASTNDC1physical
18046405
NUP57_YEASTNUP57physical
18046405
NUP49_YEASTNUP49physical
18046405
NU192_YEASTNUP192physical
18046405
NU116_YEASTNUP116physical
18046405
NSP1_YEASTNSP1physical
18046405
NUP82_YEASTNUP82physical
18046405
POM34_YEASTPOM34physical
18046405
SLA1_YEASTSLA1genetic
21987634
LONM_YEASTPIM1genetic
21987634
VATB_YEASTVMA2genetic
21987634
THRC_YEASTTHR4genetic
21987634
UBP4_YEASTDOA4genetic
21987634
APQ12_YEASTAPQ12genetic
21987634
MMM1_YEASTMMM1genetic
21987634
MFT1_YEASTMFT1genetic
21987634
UBX4_YEASTUBX4genetic
21987634
VPS4_YEASTVPS4genetic
21987634
LCF3_YEASTFAA3genetic
22125491
HSP72_YEASTSSA2physical
22940862
DED1_YEASTDED1physical
22940862
PO152_YEASTPOM152physical
22940862
HSP71_YEASTSSA1physical
22940862
NOP14_YEASTNOP14genetic
27708008
GLE1_YEASTGLE1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
NU145_YEASTNUP145genetic
27708008
CDC20_YEASTCDC20genetic
27708008
BRL1_YEASTBRL1genetic
27708008
NU159_YEASTNUP159genetic
27708008
STS1_YEASTSTS1genetic
27708008
NU192_YEASTNUP192genetic
27708008
NUP85_YEASTNUP85genetic
27708008
NEP1_YEASTEMG1genetic
27708008
IMB1_YEASTKAP95genetic
27708008
MEX67_YEASTMEX67genetic
27708008
NU170_YEASTNUP170genetic
27708008
NUP59_YEASTASM4genetic
27708008
ARX1_YEASTARX1genetic
27708008
SAC3_YEASTSAC3genetic
27708008
SLX9_YEASTSLX9genetic
27708008
THP2_YEASTTHP2genetic
27708008
VPS24_YEASTVPS24genetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
NU133_YEASTNUP133genetic
27708008
ORM2_YEASTORM2genetic
27708008
SRC1_YEASTSRC1genetic
27708008
NU188_YEASTNUP188genetic
27708008
EOS1_YEASTEOS1genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
VPS4_YEASTVPS4genetic
27708008
YJE9_YEASTYJL049Wgenetic
27733427
CALM_YEASTCMD1genetic
29674565
SSH1_YEASTSSH1genetic
29674565
SAC7_YEASTSAC7genetic
29674565
HAC1_YEASTHAC1genetic
29674565
IRE1_YEASTIRE1genetic
29674565
OST3_YEASTOST3genetic
29674565
KRE5_YEASTKRE5genetic
29674565
ECM1_YEASTECM1genetic
29674565
CND2_YEASTBRN1genetic
29674565
KPC1_YEASTPKC1genetic
29674565
SLX5_YEASTSLX5genetic
29674565
NUP59_YEASTASM4genetic
29674565
ARX1_YEASTARX1genetic
29674565
SAC3_YEASTSAC3genetic
29674565
NU145_YEASTNUP145genetic
29674565
SLX9_YEASTSLX9genetic
29674565
APQ12_YEASTAPQ12genetic
29674565
VPS24_YEASTVPS24genetic
29674565
FRMSR_YEASTYKL069Wgenetic
29674565
NU133_YEASTNUP133genetic
29674565
IMB1_YEASTKAP95genetic
29674565
SRC1_YEASTSRC1genetic
29674565
NU188_YEASTNUP188genetic
29674565
SCS7_YEASTSCS7genetic
29674565
BUB3_YEASTBUB3genetic
29674565
VPS5_YEASTVPS5genetic
29674565
KEX1_YEASTKEX1genetic
29674565
BRL1_YEASTBRL1genetic
29674565
NMD2_YEASTNMD2genetic
29674565
OST1_YEASTOST1genetic
29674565
YJY1_YEASTYJR011Cgenetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PO152_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-45; THR-787 AND SER-797,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-45, AND MASSSPECTROMETRY.
"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-60, AND MASSSPECTROMETRY.
"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-45, AND MASSSPECTROMETRY.

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