SPC34_YEAST - dbPTM
SPC34_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPC34_YEAST
UniProt AC P36131
Protein Name DASH complex subunit SPC34
Gene Name SPC34
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 295
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . Associates with the mitotic spindle and the kinetochore.
Protein Description Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids..
Protein Sequence MGESLDRCIDDINRAVDSMSTLYFKPPGIFHNAILQGASNKASIRKDITRLIKDCNHDEAYLLFKVNPEKQSVSRRDGKEGVFDYVIKRDTDMKRNRRLGRPGEKPIIHVPKEVYLNKDRLDLNNKRRRTATTSGGGLNGFIFDTDLIGSSVISNSSSGTFKALSAVFKDDPQIQRLLYALENGSVLMEEESNNQRRKTIFVEDFPTDLILKVMAEVTDLWPLTEFKQDYDQLYHNYEQLSSKLRFIKKEVLLQDDRLKTMSQYHPSSSHDVAKIIRKEKDEIRRLEMEIANLQE
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
112AcetylationKPIIHVPKEVYLNKD
CCCEECCCEEECCCC		59.7422865919
199PhosphorylationSNNQRRKTIFVEDFP
CCCCCCEEEEECCCC		20.1717330950
274AcetylationSSSHDVAKIIRKEKD
CCCHHHHHHHHHHHH		38.2224489116
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
199TPhosphorylationKinaseIPL1P38991
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPC34_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 SPC34_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JSN1_YEASTJSN1physical
10688190
SPC19_YEASTSPC19physical
10688190
SPC19_YEASTSPC19physical
11782438
DUO1_YEASTDUO1physical
11799062
DAM1_YEASTDAM1physical
12925767
DUO1_YEASTDUO1physical
12925767
SPC19_YEASTSPC19physical
12925767
SPC34_YEASTSPC34physical
12925767
DAD1_YEASTDAD1physical
14627828
DAM1_YEASTDAM1physical
14627828
DUO1_YEASTDUO1physical
14627828
SPC19_YEASTSPC19physical
14627828
DAM1_YEASTDAM1physical
14633972
IPL1_YEASTIPL1genetic
12408861
APQ12_YEASTAPQ12genetic
15998715
CTF3_YEASTCTF3genetic
15998715
RFT1_YEASTRFT1genetic
15998715
PFD2_YEASTGIM4genetic
15998715
CTF4_YEASTCTF4genetic
15998715
SST2_YEASTSST2genetic
15998715
PALH_YEASTRIM21genetic
15998715
VPS71_YEASTVPS71genetic
15998715
KAR3_YEASTKAR3genetic
15998715
BIM1_YEASTBIM1genetic
15998715
CTF19_YEASTCTF19genetic
15998715
MCM21_YEASTMCM21genetic
15998715
PFD6_YEASTYKE2genetic
15998715
CIK1_YEASTCIK1genetic
15998715
MAD2_YEASTMAD2genetic
15998715
MAD1_YEASTMAD1genetic
15998715
CTK2_YEASTCTK2genetic
15998715
YRA1_YEASTYRA1physical
16554755
GCN1_YEASTGCN1physical
16554755
HSK3_YEASTHSK3physical
16554755
ASK1_YEASTASK1physical
15640796
DAM1_YEASTDAM1physical
15640796
DUO1_YEASTDUO1physical
15640796
SPC19_YEASTSPC19physical
15640796
DAD2_YEASTDAD2physical
15640796
DAD1_YEASTDAD1physical
15640796
DAD3_YEASTDAD3physical
15640796
DAD4_YEASTDAD4physical
15640796
HSK3_YEASTHSK3physical
15640796
DAD1_YEASTDAD1physical
11283351
SPC19_YEASTSPC19physical
11283351
DUO1_YEASTDUO1physical
11283351
ATG17_YEASTATG17physical
11283351
SHE1_YEASTSHE1physical
17634282
SLI15_YEASTSLI15physical
17634282
DAD1_YEASTDAD1physical
17634282
SPC19_YEASTSPC19physical
17634282
BIM1_YEASTBIM1physical
17634282
SPC25_YEASTSPC25physical
17634282
DUO1_YEASTDUO1physical
17634282
DAM1_YEASTDAM1physical
17634282
DAD2_YEASTDAD2physical
17634282
STU2_YEASTSTU2physical
17634282
ASK1_YEASTASK1physical
18364702
DAD1_YEASTDAD1physical
18364702
DAM1_YEASTDAM1physical
18364702
DUO1_YEASTDUO1physical
18364702
SPC19_YEASTSPC19physical
18364702
DAD2_YEASTDAD2physical
18364702
DAD3_YEASTDAD3physical
18364702
DAD4_YEASTDAD4physical
18364702
HSK3_YEASTHSK3physical
18364702
ASK1_YEASTASK1physical
17460120
DAM1_YEASTDAM1physical
17460120
DUO1_YEASTDUO1physical
17460120
SPC19_YEASTSPC19physical
17460120
DAD2_YEASTDAD2physical
17460120
DAD1_YEASTDAD1physical
17460120
DAD3_YEASTDAD3physical
17460120
HSK3_YEASTHSK3physical
17460120
DUO1_YEASTDUO1physical
20730753
DAM1_YEASTDAM1physical
20730753
SPC19_YEASTSPC19physical
20730753
HSK3_YEASTHSK3physical
25382489
DAD2_YEASTDAD2physical
25382489
DAD3_YEASTDAD3physical
25382489
DAD4_YEASTDAD4physical
25382489
SPC19_YEASTSPC19physical
25382489
DUO1_YEASTDUO1physical
25382489
DAM1_YEASTDAM1physical
25382489
DAD1_YEASTDAD1physical
25382489
ASK1_YEASTASK1physical
25382489
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPC34_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-199, AND MASSSPECTROMETRY.
"Phospho-regulation of kinetochore-microtubule attachments by theAurora kinase Ipl1p.";
Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S.,Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.;
Cell 111:163-172(2002).
Cited for: PHOSPHORYLATION AT THR-199.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory