NDC1_YEAST - dbPTM
NDC1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDC1_YEAST
UniProt AC P32500
Protein Name Nucleoporin NDC1
Gene Name NDC1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 655
Subcellular Localization Nucleus, nuclear pore complex. Nucleus membrane
Multi-pass membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Central core structure of the nuclear pore complex. Spindle pole body, central plaque.
Protein Description Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB), probably by playing a key role in de novo assembly and insertion of both structures in the nuclear envelope. In SPB duplication NDC1 is required for the insertion of the cytoplasmic side of the SPB in the nuclear envelope, thus allowing for the assembly of the nucleoplasmic SPB side. 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 MIQTPRELLNPRYTYHTIFSDVCKTRFNHLVTRLFFICSIIQTVVISLLALPHSPLWELALAFIPNILALNLVSLLIIVTRKNYMHVKNFGFANSLTFILGQLLSVKFLVYQGVYSMGSILLSFVLGVVFGRGGSGWKPYYKLFIWLVVPTIYNLQHHVTDADKLSFNCENFFQAPQDYVLERVKRIMEKSVILSVISMFVLPIFTTVFFSRQKSGLFDSFTNGVLAVTNLLIISCIIFITFEFINIAFDAHMSIGCLHKGKLISNLSSTPMETLLSGLSADKPFTRLTAYQELAYRATSLDPSLRAPIYHSKFRSSSGNTWSLILNECLKTIQINNEKVVQYLRSVQDLGGSATARHKKKVENLDYMYENGKLTSANERLFGNRPSMMAPLRDNGLLDESPNRLRVRTDDSVLLNRGNKKRHRSSYYDNDLDETTQTFNGSIFTHETTFMTAMRLMLKKLKNSIMSFIFPSYAERQSSDESDNYRLLPNGSNKAQISIIDIWSISKKRQAEKLVPLPICHANSVVALTGLLIRSKTEDPKGGIIASVGDILKTLERSICALGEFADWDPESMAYTAFQTQRTAQDRVQQDSEDEDSMKDTTDMISVLYQLSTSAFMEIVLEYNVALNDVYLDADVAKLANWFLEVYASGNPNAT
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
4Phosphorylation----MIQTPRELLNP
----CCCCHHHHHCC
17.2521440633
323PhosphorylationSSSGNTWSLILNECL
CCCCCHHHHHHHHHH
11.9525704821
353PhosphorylationSVQDLGGSATARHKK
HHHHHCCCCCHHHHH
22.2023749301
373AcetylationDYMYENGKLTSANER
HHHHHCCCCCCHHHH
61.2424489116
401PhosphorylationDNGLLDESPNRLRVR
CCCCCCCCCCCEEEC
27.4325533186
409PhosphorylationPNRLRVRTDDSVLLN
CCCEEECCCCCEEEC
41.1028889911
412PhosphorylationLRVRTDDSVLLNRGN
EEECCCCCEEECCCC
19.9225704821
464PhosphorylationMLKKLKNSIMSFIFP
HHHHHHHHHHHHHCH
20.3427017623
467PhosphorylationKLKNSIMSFIFPSYA
HHHHHHHHHHCHHHH
17.3327017623
541AcetylationRSKTEDPKGGIIASV
HCCCCCCCCCEEEEH
80.3224489116
592PhosphorylationQDRVQQDSEDEDSMK
HHHHHCCCCCCCHHH
42.4828889911

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 NDC1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDC1_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 NDC1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUP59_YEASTASM4physical
10688190
NUP53_YEASTNUP53physical
10688190
CUE1_YEASTCUE1genetic
12399372
DYHC_YEASTDYN1genetic
11071919
PO152_YEASTPOM152genetic
9864355
UBC6_YEASTUBC6genetic
12399372
UBC7_YEASTUBC7genetic
12399372
NIC96_YEASTNIC96genetic
15075274
MPS2_YEASTMPS2genetic
16436507
NBP1_YEASTNBP1genetic
16436507
NBP1_YEASTNBP1physical
16436507
POM34_YEASTPOM34genetic
16682526
NUP53_YEASTNUP53physical
11283351
UBI4P_YEASTUBI4genetic
12399372
IMB1_YEASTKAP95physical
17897934
PIS_YEASTPIS1physical
18467557
NU170_YEASTNUP170physical
19414609
NU157_YEASTNUP157physical
19414609
PO152_YEASTPOM152physical
19414609
NUP59_YEASTASM4physical
19414609
POM34_YEASTPOM34physical
19414609
MPS3_YEASTMPS3physical
19414609
NUP53_YEASTNUP53physical
19414609
POM34_YEASTPOM34genetic
19571182
AGC1_YEASTAGC1physical
16093310
POM33_YEASTPOM33genetic
20498018
PER33_YEASTPER33genetic
20498018
NU192_YEASTNUP192physical
18046405
NU170_YEASTNUP170physical
18046405
PO152_YEASTPOM152physical
18046405
NUP59_YEASTASM4physical
18046405
NU188_YEASTNUP188physical
18046405
NU159_YEASTNUP159physical
18046405
NSP1_YEASTNSP1physical
18046405
NIC96_YEASTNIC96physical
18046405
NUP82_YEASTNUP82physical
18046405
NUP84_YEASTNUP84physical
18046405
NUP53_YEASTNUP53physical
18046405
KPYK1_YEASTCDC19physical
18046405
EF3A_YEASTYEF3physical
18046405
RTN1_YEASTRTN1physical
22798490
SSB1_YEASTSSB1physical
22940862
NBP1_YEASTNBP1physical
24515347
PO152_YEASTPOM152physical
24515347
POM34_YEASTPOM34physical
24515347
MPS3_YEASTMPS3physical
24515347
PO152_YEASTPOM152genetic
24515347
YOP1_YEASTYOP1physical
26041935
RTN1_YEASTRTN1physical
26041935
BBP1_YEASTBBP1physical
28356353

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDC1_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-401, AND MASSSPECTROMETRY.
"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-401, AND MASSSPECTROMETRY.

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