FIN1_YEAST - dbPTM
FIN1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIN1_YEAST
UniProt AC Q03898
Protein Name Filament protein FIN1
Gene Name FIN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 291
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, spindle pole . Nuclear during early bud formation, located at the spindle poles during late mitosis, very low abundance in resting cells.
Protein Description Forms cell-cycle specific filaments between the spindle pole bodies of dividing yeast cells..
Protein Sequence MSNKSNRRSLRDIGNTIGRNNIPSDKDNVFVRLSMSPLRTTSQKEFLKPPMRISPNKTDGMKHSIQVTPRRIMSPECLKGYVSKETQSLDRPQFKNSNKNVKIQNSDHITNIIFPTSPTKLTFSNENKIGGDGSLTRIRARFKNGLMSPERIQQQQQQHILPSDAKSNTDLCSNTELKDAPFENDLPRAKLKGKNLLVELKKEEEDVGNGIESLTKSNTKLNSMLANEGKIHKASFQKSVKFKLPDNIVTEETVELKEIKDLLLQMLRRQREIESRLSNIELQLTEIPKHK
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
26UbiquitinationRNNIPSDKDNVFVRL
CCCCCCCCCCEEEEE
56.3823749301
34PhosphorylationDNVFVRLSMSPLRTT
CCEEEEECCCCCCCC
13.4722369663
36PhosphorylationVFVRLSMSPLRTTSQ
EEEEECCCCCCCCCH
19.8722369663
40PhosphorylationLSMSPLRTTSQKEFL
ECCCCCCCCCHHHHC
38.1824961812
41PhosphorylationSMSPLRTTSQKEFLK
CCCCCCCCCHHHHCC
23.7924961812
42PhosphorylationMSPLRTTSQKEFLKP
CCCCCCCCHHHHCCC
38.3524961812
54PhosphorylationLKPPMRISPNKTDGM
CCCCCEECCCCCCCC
16.4417173039
68PhosphorylationMKHSIQVTPRRIMSP
CCCCCEECCCEECCH
8.4917173039
74PhosphorylationVTPRRIMSPECLKGY
ECCCEECCHHHHHHH
18.3821082442
86PhosphorylationKGYVSKETQSLDRPQ
HHHCCHHHCCCCCHH
27.4825752575
88PhosphorylationYVSKETQSLDRPQFK
HCCHHHCCCCCHHHC
39.3919823750
102UbiquitinationKNSNKNVKIQNSDHI
CCCCCCCEECCCCCC
48.2217644757
116PhosphorylationITNIIFPTSPTKLTF
CEEEEECCCCCEEEE
36.2722369663
117PhosphorylationTNIIFPTSPTKLTFS
EEEEECCCCCEEEEC
30.7022369663
119PhosphorylationIIFPTSPTKLTFSNE
EEECCCCCEEEECCC
38.1520377248
120UbiquitinationIFPTSPTKLTFSNEN
EECCCCCEEEECCCC
49.2517644757
134PhosphorylationNKIGGDGSLTRIRAR
CCCCCCCCCHHHHHH
31.1627214570
148PhosphorylationRFKNGLMSPERIQQQ
HHHCCCCCHHHHHHH
28.7522369663
163PhosphorylationQQQHILPSDAKSNTD
HHHCCCCCCCCCCCC
46.9120377248
166UbiquitinationHILPSDAKSNTDLCS
CCCCCCCCCCCCCCC
49.5917644757
194UbiquitinationPRAKLKGKNLLVELK
CHHHHCCCEEEEEEH
42.7217644757
201UbiquitinationKNLLVELKKEEEDVG
CEEEEEEHHHHHHHH
44.6317644757
202UbiquitinationNLLVELKKEEEDVGN
EEEEEEHHHHHHHHC
80.9217644757
216UbiquitinationNGIESLTKSNTKLNS
CHHHHHHHCCHHHHH
47.1817644757
235PhosphorylationEGKIHKASFQKSVKF
CCCCCHHHHHCCCCE
32.7721126336

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
-KUbiquitinationE3 ubiquitin ligaseCDH1P53197
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIN1_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 FIN1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BMH1_YEASTBMH1physical
12551942
BMH2_YEASTBMH2physical
12551942
FIN1_YEASTFIN1physical
11967834
FIN1_YEASTFIN1physical
11931638
FIN1_YEASTFIN1physical
17804403
BMH1_YEASTBMH1physical
19948764
BMH2_YEASTBMH2physical
19948764
NDC80_YEASTNDC80physical
19948764
DSN1_YEASTDSN1physical
19948764
NUF2_YEASTNUF2physical
19948764
ASK1_YEASTASK1physical
19948764
SPC19_YEASTSPC19physical
19948764
MCM21_YEASTMCM21physical
19948764
DAM1_YEASTDAM1physical
19948764
SP105_YEASTSPC105physical
19948764
PP12_YEASTGLC7physical
19948764
IPL1_YEASTIPL1genetic
19948764
SSB1_YEASTSSB1physical
19948764
EF1A_YEASTTEF2physical
19948764
AKL1_YEASTAKL1physical
19948764
RS14A_YEASTRPS14Aphysical
19948764
YI002_YEASTYIL002W-Aphysical
19948764
NSR1_YEASTNSR1physical
19948764
DEF1_YEASTDEF1physical
19948764
HSP72_YEASTSSA2physical
19948764
RL23A_YEASTRPL23Aphysical
19948764
RL23B_YEASTRPL23Aphysical
19948764
RL6B_YEASTRPL6Bphysical
19948764
IF4B_YEASTTIF3physical
19948764
RS3_YEASTRPS3physical
19948764
RL25_YEASTRPL25physical
19948764
RL4A_YEASTRPL4Aphysical
19948764
RPA2_YEASTRPA135physical
19948764
RL11B_YEASTRPL11Bphysical
19948764
YD12B_YEASTYDR210C-Dphysical
19948764
KPYK1_YEASTCDC19physical
19948764
RL21A_YEASTRPL21Aphysical
19948764
RL16B_YEASTRPL16Bphysical
19948764
PABP_YEASTPAB1physical
19948764
SPT5_YEASTSPT5physical
19948764
PHO84_YEASTPHO84physical
19948764
MLF3_YEASTMLF3physical
19948764
DED1_YEASTDED1physical
19948764
NEW1_YEASTNEW1physical
19948764
RL19A_YEASTRPL19Bphysical
19948764
RL19B_YEASTRPL19Bphysical
19948764
RS6A_YEASTRPS6Bphysical
19948764
RS6B_YEASTRPS6Bphysical
19948764
RS9B_YEASTRPS9Bphysical
19948764
RS26B_YEASTRPS26Bphysical
19948764
RS20_YEASTRPS20physical
19948764
TOD6_YEASTTOD6physical
19948764
IF4F1_YEASTTIF4631physical
19948764
RS13_YEASTRPS13physical
19948764
IF2G_YEASTGCD11physical
19948764
G3P3_YEASTTDH3physical
19948764
STM1_YEASTSTM1physical
19948764
RLA0_YEASTRPP0physical
19948764
SUB1_YEASTSUB1physical
19948764
RL26B_YEASTRPL26Bphysical
19948764
RL17B_YEASTRPL17Bphysical
19948764
NOG2_YEASTNOG2physical
19948764
FBRL_YEASTNOP1physical
19948764
RL15A_YEASTRPL15Aphysical
19948764
RL36A_YEASTRPL36Aphysical
19948764
SSB2_YEASTSSB2physical
19948764
EIF3B_YEASTPRT1physical
19948764
RL12A_YEASTRPL12Bphysical
19948764
RL12B_YEASTRPL12Bphysical
19948764
RS7B_YEASTRPS7Bphysical
19948764
SEA4_YEASTSEA4physical
19948764
BEM2_YEASTBEM2physical
19948764
YHI0_YEASTYHR020Wphysical
19948764
CBK1_YEASTCBK1physical
19948764
REXO4_YEASTREX4physical
19948764
RL1A_YEASTRPL1Bphysical
19948764
RL1B_YEASTRPL1Bphysical
19948764
PMA1_YEASTPMA1physical
19948764
RL13A_YEASTRPL13Aphysical
19948764
RL8A_YEASTRPL8Aphysical
19948764
FET4_YEASTFET4physical
19948764
RS15_YEASTRPS15physical
19948764
TRM6_YEASTGCD10physical
19948764
RS17B_YEASTRPS17Bphysical
19948764
RL7A_YEASTRPL7Aphysical
19948764
LSB3_YEASTLSB3physical
19948764
RL10_YEASTRPL10physical
19948764
YD15B_YEASTYDR365W-Bphysical
19948764
YE11B_YEASTYER138Cphysical
19948764
SSBP1_YEASTSBP1physical
19948764
RS16A_YEASTRPS16Bphysical
19948764
RS16B_YEASTRPS16Bphysical
19948764
RL31A_YEASTRPL31Aphysical
19948764
SEC66_YEASTSEC66genetic
20093466
SWD3_YEASTSWD3genetic
20093466
MCFS2_YEASTEHT1genetic
20093466
MBA1_YEASTMBA1genetic
20093466
CLPX_YEASTMCX1genetic
20093466
THRC_YEASTTHR4genetic
20093466
CYPD_YEASTCPR5genetic
20093466
OMS1_YEASTOMS1genetic
20093466
MCM21_YEASTMCM21genetic
20093466
BCS1_YEASTBCS1genetic
20093466
RTG2_YEASTRTG2genetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
UBCX_YEASTPEX4genetic
20093466
MEH1_YEASTMEH1genetic
20093466
SRL3_YEASTSRL3genetic
20093466
COX8_YEASTCOX8genetic
20093466
SMA2_YEASTSMA2genetic
20093466
NPL4_YEASTNPL4genetic
27708008
SEC66_YEASTSEC66genetic
27708008
MCFS2_YEASTEHT1genetic
27708008
MBA1_YEASTMBA1genetic
27708008
CLPX_YEASTMCX1genetic
27708008
MGR1_YEASTMGR1genetic
27708008
RV161_YEASTRVS161genetic
27708008
RIM1_YEASTRIM1genetic
27708008
IMG2_YEASTIMG2genetic
27708008
MCM21_YEASTMCM21genetic
27708008
BCS1_YEASTBCS1genetic
27708008
MMS2_YEASTMMS2genetic
27708008
MRM2_YEASTMRM2genetic
27708008
RTG2_YEASTRTG2genetic
27708008
COX23_YEASTCOX23genetic
27708008
ICE2_YEASTICE2genetic
27708008
YJ24_YEASTKCH1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
SRL3_YEASTSRL3genetic
27708008
SRN2_YEASTSRN2genetic
27708008
ARV1_YEASTARV1genetic
27708008
ATP10_YEASTATP10genetic
27708008
COX8_YEASTCOX8genetic
27708008
UBX2_YEASTUBX2genetic
27708008
GTR1_YEASTGTR1genetic
27708008
MSS1_YEASTMSS1genetic
27708008
ASE1_YEASTASE1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
HCM1_YEASTHCM1genetic
29674565
BOI2_YEASTBOI2genetic
29674565
SCS2_YEASTSCS2genetic
29674565
RL2A_YEASTRPL2Agenetic
29674565
RL2B_YEASTRPL2Agenetic
29674565
SYMC_YEASTMES1genetic
29674565
ATC7_YEASTNEO1genetic
29674565
EAF6_YEASTEAF6genetic
29674565
SRP40_YEASTSRP40genetic
29674565
RL40A_YEASTRPL40Bgenetic
29674565
RL40B_YEASTRPL40Bgenetic
29674565
PPID_YEASTCPR6genetic
29674565
GAS1_YEASTGAS1genetic
29674565
AF9_YEASTYAF9genetic
29674565
NOP12_YEASTNOP12genetic
29674565
MYO2_YEASTMYO2genetic
29674565
TBCC_YEASTCIN2genetic
29674565
BRR1_YEASTBRR1genetic
29674565
ORC4_YEASTORC4genetic
29674565
NAB3_YEASTNAB3genetic
29674565
ARP1_YEASTARP1genetic
29674565
ICE2_YEASTICE2genetic
29674565
PFD6_YEASTYKE2genetic
29674565
TAD3_YEASTTAD3genetic
29674565
CSK2C_YEASTCKB2genetic
29674565
ASE1_YEASTASE1genetic
29674565
NCBP2_YEASTCBC2genetic
29674565
KAR3_YEASTKAR3genetic
29674565
KPC1_YEASTPKC1genetic
29674565
RAD51_YEASTRAD51genetic
29674565
UBP3_YEASTUBP3genetic
29674565
SEC15_YEASTSEC15genetic
29674565
TIM16_YEASTPAM16genetic
29674565
VPS35_YEASTVPS35genetic
29674565
YET1_YEASTYET1genetic
29674565
VPS51_YEASTVPS51genetic
29674565
SEC10_YEASTSEC10genetic
29674565
FKS1_YEASTFKS1genetic
29674565
SRC1_YEASTSRC1genetic
29674565
ERG5_YEASTERG5genetic
29674565
SCS7_YEASTSCS7genetic
29674565
RL9B_YEASTRPL9Bgenetic
29674565
ATG3_YEASTATG3genetic
29674565
DCAM_YEASTSPE2genetic
29674565
MET22_YEASTMET22genetic
29674565
RFM1_YEASTRFM1genetic
29674565
CSR2_YEASTCSR2genetic
29674565
MMS1_YEASTMMS1genetic
29674565

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FIN1_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-74, 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-88 AND SER-117, 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-54; THR-68; SER-74;SER-88 AND SER-148, AND MASS SPECTROMETRY.

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