SA185_YEAST - dbPTM
SA185_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SA185_YEAST
UniProt AC P40856
Protein Name SIT4-associating protein SAP185
Gene Name SAP185
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1058
Subcellular Localization
Protein Description Associates with the SIT4 phosphatase in a cell cycle dependent manner. May be directly or indirectly involved in SIT4-dependent functions in budding and in normal G1 cyclin expression..
Protein Sequence MSGSFWKFGQDFGSQSPLAKLLNRAFIKIDDKPTSTEAGKIDSNSTDESLESNSFKSEDEEEEYELPNREEDYKAYKPNLSLLNDLLDDEELYTELMCSNFKLLVYLKYPEVLSKLIDYVRNSTILESNIDRVTSEDRDLVRGEDKDTTEDFENAKADKKNIDGTFEEKERTRSGEEEELENEENDSASEDTRVTLPHELEEHDDTRRARIAAEILSADVWPISSALIENEGLLAKLWSILRLPSPLSIEASTYFMKINERLLDMNMDGIIEFILKKEHIVDDFLAHIDNPPLMDFLLKVISTDKPEISNGVIQLFKKQNLVPKLIHLLDPVFDSCTQSAAGDFLKALVTISGNCPNEITSSIGPNELTRQLVSPNMMKQLMDIMLKGGNSLNNGVGIIIELIRKNNSDYDTIQTNYTTIESHPPTDRDPIYLGYLVKMFSEHMADFNKILTEKKIPLLQTSYGTIEPLGFERFKICELIAELLHCSNMTLLNEPSAYDIVRERDAERERIFNSQNYVDSNDRSELKENEDDNTGDADDEVEDDTNQVESANTSIDGEEVIDKLNSLQIETNKVNQNMNNEEQHSLMPDFNNGDFKDEEDENPFEPQYSDVILDSSDIEKNFRVSPNVGDQLKISLQDTRVIDTMLEMFFHFQWNNFLHNVVYDVVQQIFNGPLKIGYNRFLLDDLLINIRLTDMIINGNNECIEYEKGHDTRLGYMGHLTLIAEEVTKFTAYIEEMNITFENTEVMSSLFESKWIAYTEDVLEDLKEKYNAILGDIAEEGDMLQDEEEDAVYDKGERTMGTVDDYINDIMQMDNVRCQEEEEDEGEGYVSFDEDEPQEYRNGDSVRSKESNSSEGKRDQEQLYYEYVNEDGTKTRLNFNPDSDATEQVPGEVNRDHKIPLKLKRSFTDACKSETIPNNTVNAKEESVFQFSNELSDGWESSPSNSIPKRASPSKNGMNSPMFQHQFELHSPTDEFGGHKDEILSAEGHDYDIDEYDELSDDSDEEYDNCEDEDSLDYADSAAYALCRSKSKDKISWDEEEQARLMGVVKFNSEHYRD
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
2Phosphorylation------MSGSFWKFG
------CCCCCCCCC		55.2227717283
4Phosphorylation----MSGSFWKFGQD
----CCCCCCCCCCC		36.9115665377
14PhosphorylationKFGQDFGSQSPLAKL
CCCCCCCCCCHHHHH		27.7220190278
20UbiquitinationGSQSPLAKLLNRAFI
CCCCHHHHHHHHHHC		62.2823749301
28AcetylationLLNRAFIKIDDKPTS
HHHHHHCEECCCCCC		33.3624489116
32UbiquitinationAFIKIDDKPTSTEAG
HHCEECCCCCCCCCC		46.5823749301
34PhosphorylationIKIDDKPTSTEAGKI
CEECCCCCCCCCCCC		54.7621551504
35PhosphorylationKIDDKPTSTEAGKID
EECCCCCCCCCCCCC		32.5527717283
36PhosphorylationIDDKPTSTEAGKIDS
ECCCCCCCCCCCCCC		32.1227717283
43PhosphorylationTEAGKIDSNSTDESL
CCCCCCCCCCCCHHH		35.8328889911
45PhosphorylationAGKIDSNSTDESLES
CCCCCCCCCCHHHHH		40.9828889911
46PhosphorylationGKIDSNSTDESLESN
CCCCCCCCCHHHHHC		48.3028889911
52PhosphorylationSTDESLESNSFKSED
CCCHHHHHCCCCCCC		42.9619779198
54PhosphorylationDESLESNSFKSEDEE
CHHHHHCCCCCCCHH		43.2428889911
57PhosphorylationLESNSFKSEDEEEEY
HHHCCCCCCCHHHHC		48.5528889911
64PhosphorylationSEDEEEEYELPNREE
CCCHHHHCCCCCHHH		26.5019779198
128PhosphorylationRNSTILESNIDRVTS
HHCCHHHHCCCCCCC		35.3221551504
135PhosphorylationSNIDRVTSEDRDLVR
HCCCCCCCCCCCHHC		34.3428889911
146UbiquitinationDLVRGEDKDTTEDFE
CHHCCCCCCCHHHHH		53.3123749301
169UbiquitinationIDGTFEEKERTRSGE
CCCCCCHHHCCCCCC		45.3523749301
174PhosphorylationEEKERTRSGEEEELE
CHHHCCCCCCHHHHC		50.3619795423
187PhosphorylationLENEENDSASEDTRV
HCCCCCCCCCCCCCC		45.3219795423
189PhosphorylationNEENDSASEDTRVTL
CCCCCCCCCCCCCCC		39.7019795423
192PhosphorylationNDSASEDTRVTLPHE
CCCCCCCCCCCCCHH		24.0019795423
374PhosphorylationELTRQLVSPNMMKQL
HHHHHHCCHHHHHHH		21.1025005228
524PhosphorylationYVDSNDRSELKENED
CCCCCCHHHHHHCCC		50.5828889911
545PhosphorylationDDEVEDDTNQVESAN
CHHHCCCCHHCCCCC		39.6119823750
550PhosphorylationDDTNQVESANTSIDG
CCCHHCCCCCCCCCH		28.1421551504
553PhosphorylationNQVESANTSIDGEEV
HHCCCCCCCCCHHHH		27.1219823750
554PhosphorylationQVESANTSIDGEEVI
HCCCCCCCCCHHHHH		20.6328889911
708UbiquitinationNECIEYEKGHDTRLG
CCEEEEECCCCCCCH		61.7219722269
799PhosphorylationVYDKGERTMGTVDDY
CCCCCCCCCCCHHHH		18.6928889911
831PhosphorylationDEGEGYVSFDEDEPQ
CCCCCCEECCCCCCC		20.6327017623
851PhosphorylationDSVRSKESNSSEGKR
CCCCCCCCCCCCCCC		45.8324961812
853PhosphorylationVRSKESNSSEGKRDQ
CCCCCCCCCCCCCCH		38.7621440633
854PhosphorylationRSKESNSSEGKRDQE
CCCCCCCCCCCCCHH		55.4024961812
874UbiquitinationYVNEDGTKTRLNFNP
EECCCCCEEEECCCC		36.8623749301
875PhosphorylationVNEDGTKTRLNFNPD
ECCCCCEEEECCCCC		39.9829688323
883PhosphorylationRLNFNPDSDATEQVP
EECCCCCCCCCCCCC		30.3319779198
886PhosphorylationFNPDSDATEQVPGEV
CCCCCCCCCCCCCCC		31.7629688323
898AcetylationGEVNRDHKIPLKLKR
CCCCCCCCCCCEEEE		50.7624489116
906PhosphorylationIPLKLKRSFTDACKS
CCCEEEEHHHHHHHC		30.8021440633
908PhosphorylationLKLKRSFTDACKSET
CEEEEHHHHHHHCCC		24.7521440633
912UbiquitinationRSFTDACKSETIPNN
EHHHHHHHCCCCCCC		53.7123749301
936PhosphorylationFQFSNELSDGWESSP
EECCCCCCCCCCCCC		28.0927017623
941PhosphorylationELSDGWESSPSNSIP
CCCCCCCCCCCCCCC		40.8327017623
944PhosphorylationDGWESSPSNSIPKRA
CCCCCCCCCCCCCCC		45.1927017623
960PhosphorylationPSKNGMNSPMFQHQF
CCCCCCCCHHHHHHH		14.6221551504
971PhosphorylationQHQFELHSPTDEFGG
HHHHEECCCCCCCCC		41.9621440633
973PhosphorylationQFELHSPTDEFGGHK
HHEECCCCCCCCCCH		51.6927017623
1053PhosphorylationMGVVKFNSEHYRD--
HCEEEECCHHCCC--		28.9621440633
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 SA185_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SA185_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 SA185_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRN2_YEASTRAT1physical
14759368
SA185_YEASTSAP185physical
14759368
PP11_YEASTSIT4physical
14759368
DED1_YEASTDED1physical
14759368
HRR25_YEASTHRR25physical
11805837
YM59_YEASTYMR209Cphysical
11805837
TIP41_YEASTTIP41physical
11805837
DUR1_YEASTDUR1,2physical
11805837
PP11_YEASTSIT4physical
11805837
ARP4_YEASTARP4physical
11805837
YRA1_YEASTYRA1physical
11805837
EFTU_YEASTTUF1physical
11805837
CSK22_YEASTCKA2physical
11805837
TRA1_YEASTTRA1physical
11805837
ATE1_YEASTATE1physical
11805837
EAF1_YEASTEAF1physical
11805837
TAF14_YEASTTAF14physical
11805837
ESA1_YEASTESA1physical
11805837
TAF4_YEASTTAF4physical
11805837
VDAC1_YEASTPOR1physical
11805837
EPL1_YEASTEPL1physical
11805837
IF4E_YEASTCDC33physical
11805837
SA190_YEASTSAP190genetic
8649382
SA190_YEASTSAP190genetic
15367655
SAP4_YEASTSAP4genetic
15367655
SA155_YEASTSAP155genetic
15367655
IPYR_YEASTIPP1physical
16554755
PP11_YEASTSIT4physical
16554755
UTP22_YEASTUTP22physical
16554755
RRP12_YEASTRRP12physical
16554755
BEM2_YEASTBEM2physical
16429126
CDC25_YEASTCDC25physical
16429126
HRK1_YEASTHRK1physical
16429126
MDS3_YEASTMDS3physical
16429126
RTS3_YEASTRTS3physical
16429126
PP11_YEASTSIT4physical
16429126
EF3A_YEASTYEF3physical
16429126
ZRT1_YEASTZRT1genetic
17314980
DBF4_YEASTDBF4genetic
17314980
MED3_YEASTPGD1genetic
17314980
UBP3_YEASTUBP3genetic
17314980
RXT2_YEASTRXT2genetic
17314980
RPB1_YEASTRPO21genetic
17314980
MUS81_YEASTMUS81genetic
17314980
REI1_YEASTREI1genetic
17314980
SLA1_YEASTSLA1genetic
17314980
JIP4_YEASTJIP4genetic
17314980
SRB8_YEASTSRB8genetic
17314980
PP11_YEASTSIT4physical
19749176
SA190_YEASTSAP190genetic
19749176
YOR1_YEASTYOR1genetic
20093466
EFM3_YEASTEFM3genetic
20093466
EF1G2_YEASTTEF4genetic
20093466
RL40A_YEASTRPL40Bgenetic
20093466
RL40B_YEASTRPL40Bgenetic
20093466
MLP1_YEASTMLP1genetic
20093466
YPT6_YEASTYPT6genetic
20093466
YL346_YEASTYLR346Cgenetic
20093466
MSC1_YEASTMSC1genetic
20093466
PKR1_YEASTPKR1genetic
20093466
CIK1_YEASTCIK1genetic
20093466
PMS1_YEASTPMS1genetic
20093466
MED9_YEASTCSE2genetic
20093466
ERFD_YEASTSHR5genetic
20093466
MSH2_YEASTMSH2genetic
20093466
YO029_YEASTYOL029Cgenetic
20093466
PIN2_YEASTPIN2genetic
20093466
AZF1_YEASTAZF1genetic
20093466
BEM2_YEASTBEM2physical
20489023
CSK22_YEASTCKA2physical
20489023
EAF1_YEASTEAF1physical
20489023
EPL1_YEASTEPL1physical
20489023
IDHP_YEASTIDP1physical
20489023
KOG1_YEASTKOG1physical
20489023
LST8_YEASTLST8physical
20489023
MKS1_YEASTMKS1physical
20489023
RTS3_YEASTRTS3physical
20489023
PP11_YEASTSIT4physical
20489023
SYP1_YEASTSYP1physical
20489023
TCO89_YEASTTCO89physical
20489023
TIP41_YEASTTIP41physical
20489023
TOR1_YEASTTOR1physical
20489023
TRA1_YEASTTRA1physical
20489023
AF9_YEASTYAF9physical
20489023
PHS_YEASTYHL018Wphysical
20489023
SA190_YEASTSAP190genetic
20608983
YOR1_YEASTYOR1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
EFM3_YEASTEFM3genetic
27708008
RL40A_YEASTRPL40Bgenetic
27708008
RL40B_YEASTRPL40Bgenetic
27708008
MLP1_YEASTMLP1genetic
27708008
MSC1_YEASTMSC1genetic
27708008
PKR1_YEASTPKR1genetic
27708008
YO029_YEASTYOL029Cgenetic
27708008
ERFD_YEASTSHR5genetic
27708008
PIN2_YEASTPIN2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SA185_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-135, AND MASSSPECTROMETRY.

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