SMC4_SCHPO - dbPTM
SMC4_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMC4_SCHPO
UniProt AC P41004
Protein Name Structural maintenance of chromosomes protein 4
Gene Name cut3
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1324
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 MSDKGIFRTSSTPSIVDVTPDRGERPRKLVRSVLESPSQKDVASIVKIEQTPSRPFFNDFLKKRITDSLNERPNLLNKFMSAQDGTPSKSTGFNERSSQLVSEFTTTEDIENCEETTQVLPPRLVVYELRLTNFKSYAGTQIVGPFHPSFSSIVGPNGSGKSNVIDALLFVFGFRASKLRQSKASALIHKSATHPSLDSCDVEITFKEVNSDFTYVDGSELTVRRTAYKNNTSKYFVNGVESSFSAVSNLLKEKGIDLNHKRFLILQGEVESIAQMKPRAISEGDDGLLEYLEDIIGTSKYKPIIEENMQELSNSDDICAEKESRLKLVLSEKAKLEDSKNSVLSFLKDENELFMKQNQLYRTILYETRNKKTLVQNLLNSLEGKLQAHLEKFEQTERDISEKNEEVKSLREKAAKVKNDCTSEKKTRQSYEQQTVKIEEQLKFLLNKEKKLKKSIEALSFEKSEAENSLSSHDIDSQKLNSEIADLSLRLQQEELSLDDIRKSLQGKTEGISNAIEEKQKAMAPALEKINQLTSEKQILQVELDMLLNKENDLINDVESSQSSLDKLRNDAEENRNILSSKLKVLSDLKGEKKDVSKNIERKKETVHNTYRNLMSNRTKLEEMKASLSSSRSRGNVLESLQRLHESDNLNGFFGRLGDLATIDEAYDVAISTACPALNHIVVDNIETGQKCVAFLRSNNLGRASFIILKELAQKNLARIQTPENVPRLFDLLRFNDQKFAPAFYNVLQNTLVAKNLEQANRIAYGKTRWRVVTLSGQLIDKSGTMTGGGTRVKKGGMSSAITSDVSPASVETCDKQVQLEDTRYRQHLSELESLNQRFTEISERIPSAELEISKLQLDVSACDRLVAGEERRILQLKSDLKSIRNNNERKRNLQNKISNMDKEVEAININNEGLVTEIKTLQDKIMEIGGIRYRIQKSKVDDLHEQLKFVKDKLNKMSFKKKKNEQRSQSFQVELSNLTSEYDTTTESIATLKTELQSLNKYVDEHKSRLREFENALWDINSSIDELVKFIEFESKQMNSVKAERIELENQIQEQRTALSEVGNNENKYLKLMSNLKLHNLTEFCDQTTMDSTFPEYSEDELSSVDKSELVSNISVLKKKTEDREVDINVLSEYRRCNKEAEKRDSDYQSELQKRTDLKKVVTDLQSQRLDEFMYGFGIISMKLKEMYQIITMGGNAELELVDSLDPFSEGVLFSVMPPKKSWKNISNLSGGEKTLSSLALVFALHNYKPTPLYVMDEIDAALDFKNVSIVANYIKERTKNAQFIVISLRSNMFELSSRLVGIYKTANMTKSVTINNKEILTD
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
9PhosphorylationSDKGIFRTSSTPSIV
CCCCCCCCCCCCCEE		19.1125720772
10PhosphorylationDKGIFRTSSTPSIVD
CCCCCCCCCCCCEEE		28.1428889911
11PhosphorylationKGIFRTSSTPSIVDV
CCCCCCCCCCCEEEC		43.6629996109
12PhosphorylationGIFRTSSTPSIVDVT
CCCCCCCCCCEEECC		22.3325720772
14PhosphorylationFRTSSTPSIVDVTPD
CCCCCCCCEEECCCC		35.0225720772
19PhosphorylationTPSIVDVTPDRGERP
CCCEEECCCCCCCCC		18.2728889911
32PhosphorylationRPRKLVRSVLESPSQ
CCHHHHHHHHHCCCC		24.4721712547
36PhosphorylationLVRSVLESPSQKDVA
HHHHHHHCCCCCCHH		26.2021712547
38PhosphorylationRSVLESPSQKDVASI
HHHHHCCCCCCHHHH		60.1724763107
51PhosphorylationSIVKIEQTPSRPFFN
HHEEEECCCCCCCHH		15.5021712547
53PhosphorylationVKIEQTPSRPFFNDF
EEEECCCCCCCHHHH		56.8424763107
66PhosphorylationDFLKKRITDSLNERP
HHHHHHHHHHHHHCC		24.4629996109
68PhosphorylationLKKRITDSLNERPNL
HHHHHHHHHHHCCCH		25.1721712547
86PhosphorylationFMSAQDGTPSKSTGF
HHHCCCCCCCCCCCC		32.4529996109
88PhosphorylationSAQDGTPSKSTGFNE
HCCCCCCCCCCCCCH		38.7929996109
899PhosphorylationRNLQNKISNMDKEVE
HHHHHHHHCCHHHHH		27.9321712547
917PhosphorylationINNEGLVTEIKTLQD
CCCCCHHHHHHHHHH		36.7221712547
1323PhosphorylationINNKEILTD------
ECCEEECCC------		45.3725720772
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
19TPhosphorylationKinaseCDK1P04551
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMC4_SCHPO !!
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_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMC2_SCHPOcut14physical
10485849
CND1_SCHPOcnd1physical
10485849
CND2_SCHPOcnd2physical
10485849
CND3_SCHPOcnd3physical
10485849
SFC3_SCHPOsfc3genetic
19910488
PCS1_SCHPOcsm1genetic
21633354
SFC3_SCHPOsfc3genetic
21633354
KU80_SCHPOpku80physical
23084836
YOI5_SCHPOSPBC1778.05cgenetic
22681890
YL33_SCHPOsil1genetic
22681890
6PGL_SCHPOSPCC16C4.10genetic
22681890
YNTB_SCHPOSPBC9B6.11cgenetic
22681890
RAF2_SCHPOraf2genetic
22681890
ARP6_SCHPOarp6genetic
22681890
RT109_SCHPOrtt109genetic
22681890
YAC5_SCHPOcph1genetic
22681890
CCQ1_SCHPOccq1genetic
22681890
CLR4_SCHPOclr4genetic
22681890
SEY1_SCHPOSPAC222.14cgenetic
22681890
ULP2_SCHPOulp2genetic
22681890
SNF5_SCHPOsnf5genetic
22681890
GCN5_SCHPOgcn5genetic
22681890
PAB2_SCHPOpab2genetic
22681890
YG64_SCHPOSPBC15C4.04cgenetic
22681890
ARP42_SCHPOarp42genetic
22681890
NIC1_SCHPOnic1genetic
22681890
NU124_SCHPOnup124genetic
22681890
APQ12_SCHPOapq12genetic
22681890
TLS1_SCHPOtls1genetic
22681890
YFM8_SCHPOSPAC222.08cgenetic
22681890
HASP_SCHPOhrk1genetic
22681890
LIZ1_SCHPOliz1genetic
22681890
FKBP4_SCHPOfkbp39genetic
22681890
YLP3_SCHPOred1genetic
22681890
RAF1_SCHPOraf1genetic
22681890
SAT1_SCHPOsat1genetic
22681890
YNH1_SCHPOSPBC32H8.01cgenetic
22681890
RF1M_SCHPOmrf1genetic
22681890
ASE1_SCHPOase1genetic
22681890
SGF29_SCHPOsgf29genetic
22681890
TOP2_SCHPOtop2genetic
24362309
ARP9_SCHPOarp9genetic
24362309
YA27_SCHPOcph2genetic
24362309
ULP2_SCHPOulp2genetic
24362309
MED10_SCHPOnut2genetic
24362309
SMC2_SCHPOcut14genetic
24362309
CND1_SCHPOcnd1genetic
24362309
CND3_SCHPOcnd3genetic
24362309
ARK1_SCHPOark1genetic
24362309
SNF21_SCHPOsnf21genetic
24362309
YIQ4_SCHPOSPAC824.04genetic
24945319
CPSFX_SCHPOppn1genetic
24945319
SSU72_SCHPOssu72genetic
24945319
CID14_SCHPOcid14genetic
24945319
PTPA1_SCHPOypa1genetic
24945319
PIN1_SCHPOpin1genetic
24945319
MMS19_SCHPOmms19genetic
24945319
SEN1_SCHPOsen1genetic
24945319
TOP1_SCHPOtop1genetic
24945319
TFS2_SCHPOtfs1genetic
24945319
PP11_SCHPOdis2genetic
24945319
SMC2_SCHPOcut14physical
25520186
MED6_SCHPOmed6genetic
26204128
SFC3_SCHPOsfc3genetic
26704981
GCN5_SCHPOgcn5genetic
27266525
CND2_SCHPOcnd2physical
27266525
ADA2_SCHPOada2genetic
27266525
NGG1_SCHPOngg1genetic
27266525
MST2_SCHPOmst2genetic
27266525
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMC4_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Fission yeast condensin complex: essential roles of non-SMC subunitsfor condensation and Cdc2 phosphorylation of Cut3/SMC4.";
Sutani T., Yuasa T., Tomonaga T., Dohmae N., Takio K., Yanagida M.;
Genes Dev. 13:2271-2283(1999).
Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH CUT14; CND1; CND2 AND CND3,PHOSPHORYLATION AT THR-19, AND MUTAGENESIS OF THR-19.

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