SMC4_YEAST - dbPTM
SMC4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMC4_YEAST
UniProt AC Q12267
Protein Name Structural maintenance of chromosomes protein 4
Gene Name SMC4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1418
Subcellular Localization Nucleus. Cytoplasm. Chromosome. In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromos
Protein Description Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases..
Protein Sequence MSDSPLSKRQKRKSAQEPELSLDQGDAEEDSQVENRVNLSENTPEPDLPALEASYSKSYTPRKLVLSSGENRYAFSQPTNSTTTSLHVPNLQPPKTSSRGRDHKSYSQSPPRSPGRSPTRRLELLQLSPVKNSRVELQKIYDRHQSSSKQQSRLFINELVLENFKSYAGKQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRLSDLIHKSEAFPSLQSCSVAVHFQYVIDESSGTSRIDEEKPGLIITRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLILQGEVENIAQMKPKAEKESDDGLLEYLEDIIGTANYKPLIEERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETALEFLEKEKQLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKVLTALSRLQKSGRINGFHGRLGDLGVIDDSFDVAISTACPRLDDVVVDTVECAQHCIDYLRKNKLGYARFILLDRLRQFNLQPISTPENVPRLFDLVKPKNPKFSNAFYSVLRDTLVAQNLKQANNVAYGKKRFRVVTVDGKLIDISGTMSGGGNHVAKGLMKLGTNQSDKVDDYTPEEVDKIERELSERENNFRVASDTVHEMEEELKKLRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEMAYVKAVSDKAQLNVVMKNLERLRGEYNDLQSETKTKKEKIKGLQDEIMKIGGIKLQMQNSKVESVCQKLDILVAKLKKVKSASKKSGGDVVKFQKLLQNSERDVELSSDELKVIEEQLKHTKLALAENDTNMNETLNLKVELKEQSEQLKEQMEDMEESINEFKSIEIEMKNKLEKLNSLLTYIKSEITQQEKGLNELSIRDVTHTLGMLDDNKMDSVKEDVKNNQELDQEYRSCETQDESEIKDAETSCDNYHPMNIDETSDEVSRGIPRLSEDELRELDVELIESKINELSYYVEETNVDIGVLEEYARRLAEFKRRKLDLNNAVQKRDEVKEQLGILKKKRFDEFMAGFNIISMTLKEMYQMITMGGNAELELVDSLDPFSEGVTFSVMPPKKSWRNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAQQLVGVYKRDNRTKSTTIKNIDILNRT
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------MSDSPLSKR
------CCCCCCCHH
59.0930377154
2Acetylation------MSDSPLSKR
------CCCCCCCHH
59.0922814378
4Phosphorylation----MSDSPLSKRQK
----CCCCCCCHHHH
36.7128152593
7Phosphorylation-MSDSPLSKRQKRKS
-CCCCCCCHHHHHHH
29.2228889911
8AcetylationMSDSPLSKRQKRKSA
CCCCCCCHHHHHHHC
67.5425381059
14PhosphorylationSKRQKRKSAQEPELS
CHHHHHHHCCCCCCC
38.9428889911
21PhosphorylationSAQEPELSLDQGDAE
HCCCCCCCCCCCCHH
28.3928889911
31PhosphorylationQGDAEEDSQVENRVN
CCCHHHHHHHHHHCC
39.1328889911
40PhosphorylationVENRVNLSENTPEPD
HHHHCCCCCCCCCCC
24.4825752575
43PhosphorylationRVNLSENTPEPDLPA
HCCCCCCCCCCCCHH
25.6124961812
67PhosphorylationTPRKLVLSSGENRYA
CCCEEEECCCCCCEE
28.9021440633
68PhosphorylationPRKLVLSSGENRYAF
CCEEEECCCCCCEEE
46.0621440633
73PhosphorylationLSSGENRYAFSQPTN
ECCCCCCEEECCCCC
24.4723749301
105PhosphorylationSRGRDHKSYSQSPPR
CCCCCCCCCCCCCCC
26.9622369663
106PhosphorylationRGRDHKSYSQSPPRS
CCCCCCCCCCCCCCC
18.6122369663
107PhosphorylationGRDHKSYSQSPPRSP
CCCCCCCCCCCCCCC
31.1322369663
109PhosphorylationDHKSYSQSPPRSPGR
CCCCCCCCCCCCCCC
30.8222369663
113PhosphorylationYSQSPPRSPGRSPTR
CCCCCCCCCCCCCCH
37.1622369663
117PhosphorylationPPRSPGRSPTRRLEL
CCCCCCCCCCHHHHH
36.2222369663
119PhosphorylationRSPGRSPTRRLELLQ
CCCCCCCCHHHHHHH
29.6622369663
128PhosphorylationRLELLQLSPVKNSRV
HHHHHHCCCCCCCHH
18.0622369663
139AcetylationNSRVELQKIYDRHQS
CCHHHHHHHHHHHCC
56.7225381059
147PhosphorylationIYDRHQSSSKQQSRL
HHHHHCCCCHHHHHH
34.6828889911
148PhosphorylationYDRHQSSSKQQSRLF
HHHHCCCCHHHHHHH
39.4728889911
152PhosphorylationQSSSKQQSRLFINEL
CCCCHHHHHHHHHHH
28.5828889911
278PhosphorylationYINEKESSYTEVTKL
ECCCCCCCHHHHHHH
36.8527214570
528AcetylationDLTQLLEKERSILDD
HHHHHHHHHHHHHHH
59.4022865919
605PhosphorylationEKILAKKTHKQELQD
HHHHCHHHCHHHHHH
33.3319795423
623PhosphorylationDLKKKLNSLKDERSQ
HHHHHHHHHHHHHHH
47.4328889911
809PhosphorylationKKRFRVVTVDGKLID
CCCEEEEEECCEEEE
15.2629136822
818PhosphorylationDGKLIDISGTMSGGG
CCEEEEECCCCCCCC
25.1821551504
820PhosphorylationKLIDISGTMSGGGNH
EEEEECCCCCCCCCH
11.0229136822
822PhosphorylationIDISGTMSGGGNHVA
EEECCCCCCCCCHHH
33.8429136822
869PhosphorylationENNFRVASDTVHEME
HCCCCCCHHHHHHHH
30.8427017623
871PhosphorylationNFRVASDTVHEMEEE
CCCCCHHHHHHHHHH
22.6727017623
905PhosphorylationMEADSLASELTLAEQ
HHHHHHHHHHHHHHH
38.1327017623
1095AcetylationEMKNKLEKLNSLLTY
HHHHHHHHHHHHHHH
64.5024489116
1160PhosphorylationSCETQDESEIKDAET
HCCCCCHHHHCCCHH
53.5721440633
1167PhosphorylationSEIKDAETSCDNYHP
HHHCCCHHCCCCCCC
36.0519779198
1168PhosphorylationEIKDAETSCDNYHPM
HHCCCHHCCCCCCCC
15.8119779198

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 SMC4_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMC4_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 SMC4_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUF2_YEASTNUF2physical
11087867
NNF2_YEASTNNF2physical
11087867
SMC2_YEASTSMC2genetic
18846224
CND2_YEASTBRN1physical
21441928
LEU3_YEASTLEU2physical
21441928
RFA1_YEASTRFA1physical
21441928
RFA3_YEASTRFA3physical
21441928
SLI15_YEASTSLI15physical
21441928
SMC1_YEASTSMC1physical
21441928
SMC2_YEASTSMC2physical
21441928
SMC3_YEASTSMC3physical
21441928
CND3_YEASTYCG1physical
21441928
CND1_YEASTYCS4physical
21441928
MOD5_YEASTMOD5physical
23898186
DPOA2_YEASTPOL12genetic
27708008
RPAB1_YEASTRPB5genetic
27708008
CDK1_YEASTCDC28genetic
27708008
CDC37_YEASTCDC37genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
CDC23_YEASTCDC23genetic
27708008
SEC22_YEASTSEC22genetic
27708008
MED7_YEASTMED7genetic
27708008
MED4_YEASTMED4genetic
27708008
GPN2_YEASTGPN2genetic
27708008
RS29B_YEASTRPS29Bgenetic
27708008
KCC1_YEASTCMK1genetic
27708008
CGR1_YEASTCGR1genetic
27708008
SDS3_YEASTSDS3genetic
27708008
ILM1_YEASTILM1genetic
27708008
VPS13_YEASTVPS13genetic
27708008
CDC73_YEASTCDC73genetic
27708008
SCS7_YEASTSCS7genetic
27708008
PHO23_YEASTPHO23genetic
27708008
SIN3_YEASTSIN3genetic
27708008
CDC24_YEASTCDC24genetic
27708008
STU1_YEASTSTU1genetic
27708008
ERD2_YEASTERD2genetic
27708008
CND2_YEASTBRN1genetic
27708008
SLI15_YEASTSLI15genetic
27708008
TAF5_YEASTTAF5genetic
27708008
CDC10_YEASTCDC10genetic
27708008
SCC1_YEASTMCD1genetic
27708008
MPS1_YEASTMPS1genetic
27708008
NSE4_YEASTNSE4genetic
27708008
DBF4_YEASTDBF4genetic
27708008
UBC3_YEASTCDC34genetic
27708008
SEC7_YEASTSEC7genetic
27708008
SCC2_YEASTSCC2genetic
27708008
CND3_YEASTYCG1genetic
27708008
PANK_YEASTCAB1genetic
27708008
RSP5_YEASTRSP5genetic
27708008
PP12_YEASTGLC7genetic
27708008
TFC4_YEASTTFC4genetic
27708008
NUP57_YEASTNUP57genetic
27708008
COAD_YEASTCAB4genetic
27708008
FDFT_YEASTERG9genetic
27708008
STS1_YEASTSTS1genetic
27708008
GRP78_YEASTKAR2genetic
27708008
SMC3_YEASTSMC3genetic
27708008
KRE9_YEASTKRE9genetic
27708008
PRP21_YEASTPRP21genetic
27708008
NUP85_YEASTNUP85genetic
27708008
POB3_YEASTPOB3genetic
27708008
SEC65_YEASTSEC65genetic
27708008
ERO1_YEASTERO1genetic
27708008
TAP42_YEASTTAP42genetic
27708008
LCB1_YEASTLCB1genetic
27708008
RPC6_YEASTRPC34genetic
27708008
SEC12_YEASTSEC12genetic
27708008
NOG2_YEASTNOG2genetic
27708008
NUF2_YEASTNUF2genetic
27708008
DED1_YEASTDED1genetic
27708008
CLP1_YEASTCLP1genetic
27708008
TIM50_YEASTTIM50genetic
27708008
NSL1_YEASTNSL1genetic
27708008
ORC4_YEASTORC4genetic
27708008
RPN4_YEASTRPN4genetic
27708008
THI3_YEASTTHI3genetic
27708008
ATC1_YEASTPMR1genetic
27708008
EFM4_YEASTEFM4genetic
27708008
HPM1_YEASTHPM1genetic
27708008
VPS70_YEASTVPS70genetic
27708008
XPT1_YEASTXPT1genetic
27708008
DHOM_YEASTHOM6genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
MAOM_YEASTMAE1genetic
27708008
VPS24_YEASTVPS24genetic
27708008
NU100_YEASTNUP100genetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
APN1_YEASTAPN1genetic
27708008
MYO3_YEASTMYO3genetic
27708008
RS27A_YEASTRPS27Agenetic
27708008
SET3_YEASTSET3genetic
27708008
YK21_YEASTYKR041Wgenetic
27708008
RHO4_YEASTRHO4genetic
27708008
SRP40_YEASTSRP40genetic
27708008
RNP1_YEASTRNP1genetic
27708008
YL054_YEASTYLL054Cgenetic
27708008
YCT1_YEASTYCT1genetic
27708008
YL056_YEASTYLL056Cgenetic
27708008
SS120_YEASTSSP120genetic
27708008
YL281_YEASTYLR281Cgenetic
27708008
EXG1_YEASTEXG1genetic
27708008
DIC1_YEASTDIC1genetic
27708008
YL352_YEASTYLR352Wgenetic
27708008
RS22B_YEASTRPS22Bgenetic
27708008
PSY3_YEASTPSY3genetic
27708008
CSR1_YEASTCSR1genetic
27708008
CCW14_YEASTCCW14genetic
27708008
CST9_YEASTCST9genetic
27708008
RL31B_YEASTRPL31Bgenetic
27708008
PUN1_YEASTPUN1genetic
27708008
YMP8_YEASTYMR018Wgenetic
27708008
OCA2_YEASTOCA2genetic
27708008
TOM7_YEASTTOM7genetic
27708008
FAR11_YEASTFAR11genetic
27708008
CPT1_YEASTCPT1genetic
27708008
WDR6_YEASTRTT10genetic
27708008
CGS5_YEASTCLB5genetic
27708008
CND3_YEASTYCG1physical
25691469

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMC4_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-40; THR-43; SER-113 ANDTHR-809, AND MASS SPECTROMETRY.

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