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Protein

Structural maintenance of chromosomes protein 4

Gene

SMC4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1928ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: SGD

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • DNA unwinding involved in DNA replication Source: SGD
  • meiotic chromosome condensation Source: SGD
  • meiotic chromosome separation Source: SGD
  • mitotic chromosome condensation Source: SGD
  • mitotic sister chromatid segregation Source: SGD
  • rDNA condensation Source: SGD
  • synaptonemal complex assembly Source: SGD
  • tRNA gene clustering Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32237-MONOMER.
ReactomeiR-SCE-2514853. Condensation of Prometaphase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 4
Gene namesi
Name:SMC4
Ordered Locus Names:YLR086W
ORF Names:L9449.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR086W.
SGDiS000004076. SMC4.

Subcellular locationi

  • Nucleus
  • Cytoplasm
  • Chromosome

  • Note: 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 chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nuclear condensin complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 14181417Structural maintenance of chromosomes protein 4PRO_0000119018Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei43 – 431PhosphothreonineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ12267.

PTM databases

iPTMnetiQ12267.

Interactioni

Subunit structurei

Forms a heterodimer with SMC2. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRN1, YCS4 and YCG1/YCS5.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
YCG1Q066802EBI-17430,EBI-4799

Protein-protein interaction databases

BioGridi31359. 34 interactions.
DIPiDIP-3007N.
IntActiQ12267. 12 interactions.
MINTiMINT-436885.

Structurei

Secondary structure

1
1418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi562 – 681120Combined sources
Beta strandi688 – 6914Combined sources
Helixi692 – 6943Combined sources
Beta strandi695 – 6984Combined sources
Helixi700 – 7023Combined sources
Helixi703 – 7097Combined sources
Helixi711 – 7144Combined sources
Beta strandi715 – 7195Combined sources
Helixi721 – 73414Combined sources
Beta strandi738 – 7447Combined sources
Helixi758 – 7603Combined sources
Turni764 – 7674Combined sources
Beta strandi768 – 7725Combined sources
Helixi773 – 7753Combined sources
Helixi778 – 7825Combined sources
Beta strandi784 – 7874Combined sources
Helixi794 – 7974Combined sources
Beta strandi800 – 8034Combined sources
Beta strandi806 – 8083Combined sources
Beta strandi821 – 8233Combined sources
Beta strandi832 – 8343Combined sources
Helixi850 – 88334Combined sources
Helixi886 – 91025Combined sources
Turni911 – 9133Combined sources
Helixi914 – 92512Combined sources
Helixi929 – 94719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RSIX-ray2.90B555-951[»]
ProteinModelPortaliQ12267.
SMRiQ12267. Positions 155-503, 557-948, 1215-1397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni674 – 848175Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili345 – 673329Sequence analysisAdd
BLAST
Coiled coili849 – 1172324Sequence analysisAdd
BLAST
Coiled coili1224 – 126340Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1323 – 135836Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC2, forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC4 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00580000081617.
HOGENOMiHOG000184777.
InParanoidiQ12267.
KOiK06675.
OMAiNNLRENI.
OrthoDBiEOG7M0P0T.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12267-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSPLSKRQ KRKSAQEPEL SLDQGDAEED SQVENRVNLS ENTPEPDLPA
60 70 80 90 100
LEASYSKSYT PRKLVLSSGE NRYAFSQPTN STTTSLHVPN LQPPKTSSRG
110 120 130 140 150
RDHKSYSQSP PRSPGRSPTR RLELLQLSPV KNSRVELQKI YDRHQSSSKQ
160 170 180 190 200
QSRLFINELV LENFKSYAGK QVVGPFHTSF SAVVGPNGSG KSNVIDSMLF
210 220 230 240 250
VFGFRANKMR QDRLSDLIHK SEAFPSLQSC SVAVHFQYVI DESSGTSRID
260 270 280 290 300
EEKPGLIITR KAFKNNSSKY YINEKESSYT EVTKLLKNEG IDLDHKRFLI
310 320 330 340 350
LQGEVENIAQ MKPKAEKESD DGLLEYLEDI IGTANYKPLI EERMGQIENL
360 370 380 390 400
NEVCLEKENR FEIVDREKNS LESGKETALE FLEKEKQLTL LRSKLFQFKL
410 420 430 440 450
LQSNSKLAST LEKISSSNKD LEDEKMKFQE SLKKVDEIKA QRKEIKDRIS
460 470 480 490 500
SCSSKEKTLV LERRELEGTR VSLEERTKNL VSKMEKAEKT LKSTKHSISE
510 520 530 540 550
AENMLEELRG QQTEHETEIK DLTQLLEKER SILDDIKLSL KDKTKNISAE
560 570 580 590 600
IIRHEKELEP WDLQLQEKES QIQLAESELS LLEETQAKLK KNVETLEEKI
610 620 630 640 650
LAKKTHKQEL QDLILDLKKK LNSLKDERSQ GEKNFTSAHL KLKEMQKVLN
660 670 680 690 700
AHRQRAMEAR SSLSKAQNKS KVLTALSRLQ KSGRINGFHG RLGDLGVIDD
710 720 730 740 750
SFDVAISTAC PRLDDVVVDT VECAQHCIDY LRKNKLGYAR FILLDRLRQF
760 770 780 790 800
NLQPISTPEN VPRLFDLVKP KNPKFSNAFY SVLRDTLVAQ NLKQANNVAY
810 820 830 840 850
GKKRFRVVTV DGKLIDISGT MSGGGNHVAK GLMKLGTNQS DKVDDYTPEE
860 870 880 890 900
VDKIERELSE RENNFRVASD TVHEMEEELK KLRDHEPDLE SQISKAEMEA
910 920 930 940 950
DSLASELTLA EQQVKEAEMA YVKAVSDKAQ LNVVMKNLER LRGEYNDLQS
960 970 980 990 1000
ETKTKKEKIK GLQDEIMKIG GIKLQMQNSK VESVCQKLDI LVAKLKKVKS
1010 1020 1030 1040 1050
ASKKSGGDVV KFQKLLQNSE RDVELSSDEL KVIEEQLKHT KLALAENDTN
1060 1070 1080 1090 1100
MNETLNLKVE LKEQSEQLKE QMEDMEESIN EFKSIEIEMK NKLEKLNSLL
1110 1120 1130 1140 1150
TYIKSEITQQ EKGLNELSIR DVTHTLGMLD DNKMDSVKED VKNNQELDQE
1160 1170 1180 1190 1200
YRSCETQDES EIKDAETSCD NYHPMNIDET SDEVSRGIPR LSEDELRELD
1210 1220 1230 1240 1250
VELIESKINE LSYYVEETNV DIGVLEEYAR RLAEFKRRKL DLNNAVQKRD
1260 1270 1280 1290 1300
EVKEQLGILK KKRFDEFMAG FNIISMTLKE MYQMITMGGN AELELVDSLD
1310 1320 1330 1340 1350
PFSEGVTFSV MPPKKSWRNI TNLSGGEKTL SSLALVFALH KYKPTPLYVM
1360 1370 1380 1390 1400
DEIDAALDFR NVSIVANYIK ERTKNAQFIV ISLRNNMFEL AQQLVGVYKR
1410
DNRTKSTTIK NIDILNRT
Length:1,418
Mass (Da):162,189
Last modified:November 1, 1996 - v1
Checksum:iF0E6B72FE8BFD374
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73258 Genomic DNA. Translation: CAA97646.1.
Z73259 Genomic DNA. Translation: CAA97648.1.
U53880 Genomic DNA. Translation: AAB67590.1.
BK006945 Genomic DNA. Translation: DAA09402.1.
PIRiS64918.
RefSeqiNP_013187.1. NM_001181973.1.

Genome annotation databases

EnsemblFungiiYLR086W; YLR086W; YLR086W.
GeneIDi850775.
KEGGisce:YLR086W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73258 Genomic DNA. Translation: CAA97646.1.
Z73259 Genomic DNA. Translation: CAA97648.1.
U53880 Genomic DNA. Translation: AAB67590.1.
BK006945 Genomic DNA. Translation: DAA09402.1.
PIRiS64918.
RefSeqiNP_013187.1. NM_001181973.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RSIX-ray2.90B555-951[»]
ProteinModelPortaliQ12267.
SMRiQ12267. Positions 155-503, 557-948, 1215-1397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31359. 34 interactions.
DIPiDIP-3007N.
IntActiQ12267. 12 interactions.
MINTiMINT-436885.

PTM databases

iPTMnetiQ12267.

Proteomic databases

MaxQBiQ12267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR086W; YLR086W; YLR086W.
GeneIDi850775.
KEGGisce:YLR086W.

Organism-specific databases

EuPathDBiFungiDB:YLR086W.
SGDiS000004076. SMC4.

Phylogenomic databases

GeneTreeiENSGT00580000081617.
HOGENOMiHOG000184777.
InParanoidiQ12267.
KOiK06675.
OMAiNNLRENI.
OrthoDBiEOG7M0P0T.

Enzyme and pathway databases

BioCyciYEAST:G3O-32237-MONOMER.
ReactomeiR-SCE-2514853. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

PROiQ12267.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The condensin complex governs chromosome condensation and mitotic transmission of rDNA."
    Freeman L., Aragon-Alcaide L., Strunnikov A.V.
    J. Cell Biol. 149:811-824(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; BRN1; YCS4 AND YCG1.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43 AND SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSMC4_YEAST
AccessioniPrimary (citable) accession number: Q12267
Secondary accession number(s): D6VY86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 573 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.