Reviewed, UniProtKB/Swiss-Prot Q12267 (SMC4_YEAST)

Names and origin

Protein names

Recommended name:
    Structural maintenance of chromosomes protein 4

Gene names

Name:	SMC4
Ordered Locus Names:	YLR086W
ORF Names:	L9449.5

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1418 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Subunit structure	Forms an 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.
Subcellular location	Nucleus. Cytoplasm. 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.
Domain	The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC2, forming a V-shaped heterodimer By similarity.
Miscellaneous	Present with 573 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the SMC family. SMC4 subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA condensation Mitosis
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic chromosome condensation Ref.2 Inferred from mutant phenotype. Source: SGD tRNA gene clustering Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear condensin complex Ref.2 Inferred from physical interaction. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BOI1	P38041	1	EBI-17430,EBI-3719

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1418	1418	Structural maintenance of chromosomes protein 4		PRO_0000119018
Regions
	Nucleotide binding	185 – 192	8	ATP Potential
	Region	674 – 848	175	Flexible hinge
	Coiled coil	345 – 673	329	Potential
	Coiled coil	849 – 1172	324	Potential
	Coiled coil	1224 – 1263	40	Potential
	Compositional bias	1323 – 1358	36	Ala/Asp-rich (DA-box)
Amino acid modifications
	Modified residue	40	1	Phosphoserine Ref.4
	Modified residue	43	1	Phosphothreonine Ref.4
	Modified residue	113	1	Phosphoserine Ref.4
	Modified residue	809	1	Phosphothreonine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q12267-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F0E6B72FE8BFD374	FASTA	1,418	162,189
	10 20 30 40 50 60 MSDSPLSKRQ KRKSAQEPEL SLDQGDAEED SQVENRVNLS ENTPEPDLPA LEASYSKSYT 70 80 90 100 110 120 PRKLVLSSGE NRYAFSQPTN STTTSLHVPN LQPPKTSSRG RDHKSYSQSP PRSPGRSPTR 130 140 150 160 170 180 RLELLQLSPV KNSRVELQKI YDRHQSSSKQ QSRLFINELV LENFKSYAGK QVVGPFHTSF 190 200 210 220 230 240 SAVVGPNGSG KSNVIDSMLF VFGFRANKMR QDRLSDLIHK SEAFPSLQSC SVAVHFQYVI 250 260 270 280 290 300 DESSGTSRID EEKPGLIITR KAFKNNSSKY YINEKESSYT EVTKLLKNEG IDLDHKRFLI 310 320 330 340 350 360 LQGEVENIAQ MKPKAEKESD DGLLEYLEDI IGTANYKPLI EERMGQIENL NEVCLEKENR 370 380 390 400 410 420 FEIVDREKNS LESGKETALE FLEKEKQLTL LRSKLFQFKL LQSNSKLAST LEKISSSNKD 430 440 450 460 470 480 LEDEKMKFQE SLKKVDEIKA QRKEIKDRIS SCSSKEKTLV LERRELEGTR VSLEERTKNL 490 500 510 520 530 540 VSKMEKAEKT LKSTKHSISE AENMLEELRG QQTEHETEIK DLTQLLEKER SILDDIKLSL 550 560 570 580 590 600 KDKTKNISAE IIRHEKELEP WDLQLQEKES QIQLAESELS LLEETQAKLK KNVETLEEKI 610 620 630 640 650 660 LAKKTHKQEL QDLILDLKKK LNSLKDERSQ GEKNFTSAHL KLKEMQKVLN AHRQRAMEAR 670 680 690 700 710 720 SSLSKAQNKS KVLTALSRLQ KSGRINGFHG RLGDLGVIDD SFDVAISTAC PRLDDVVVDT 730 740 750 760 770 780 VECAQHCIDY LRKNKLGYAR FILLDRLRQF NLQPISTPEN VPRLFDLVKP KNPKFSNAFY 790 800 810 820 830 840 SVLRDTLVAQ NLKQANNVAY GKKRFRVVTV DGKLIDISGT MSGGGNHVAK GLMKLGTNQS 850 860 870 880 890 900 DKVDDYTPEE VDKIERELSE RENNFRVASD TVHEMEEELK KLRDHEPDLE SQISKAEMEA 910 920 930 940 950 960 DSLASELTLA EQQVKEAEMA YVKAVSDKAQ LNVVMKNLER LRGEYNDLQS ETKTKKEKIK 970 980 990 1000 1010 1020 GLQDEIMKIG GIKLQMQNSK VESVCQKLDI LVAKLKKVKS ASKKSGGDVV KFQKLLQNSE 1030 1040 1050 1060 1070 1080 RDVELSSDEL KVIEEQLKHT KLALAENDTN MNETLNLKVE LKEQSEQLKE QMEDMEESIN 1090 1100 1110 1120 1130 1140 EFKSIEIEMK NKLEKLNSLL TYIKSEITQQ EKGLNELSIR DVTHTLGMLD DNKMDSVKED 1150 1160 1170 1180 1190 1200 VKNNQELDQE YRSCETQDES EIKDAETSCD NYHPMNIDET SDEVSRGIPR LSEDELRELD 1210 1220 1230 1240 1250 1260 VELIESKINE LSYYVEETNV DIGVLEEYAR RLAEFKRRKL DLNNAVQKRD EVKEQLGILK 1270 1280 1290 1300 1310 1320 KKRFDEFMAG FNIISMTLKE MYQMITMGGN AELELVDSLD PFSEGVTFSV MPPKKSWRNI 1330 1340 1350 1360 1370 1380 TNLSGGEKTL SSLALVFALH KYKPTPLYVM DEIDAALDFR NVSIVANYIK ERTKNAQFIV 1390 1400 1410 ISLRNNMFEL AQQLVGVYKR DNRTKSTTIK NIDILNRT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"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: 10811823] [Abstract] Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; BRN1; YCS4 AND YCG1.
[3]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; THR-43; SER-113 AND THR-809, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z73258 Genomic DNA. Translation: CAA97646.1. Z73259 Genomic DNA. Translation: CAA97648.1. U53880 Genomic DNA. Translation: AAB67590.1.
PIR	S64918.
RefSeq	NP_013187.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3007N.
IntAct	Q12267. 10 interactions.
STRING	Q12267.
Proteomic databases
PRIDE	Q12267.
Genome annotation databases
Ensembl	YLR086W; YLR086W; YLR086W; Saccharomyces cerevisiae. [Genome view]
GeneID	850775.
GenomeReviews	Gene locus YLR086W in contig Y13138_GR.
KEGG	sce:YLR086W.
NMPDR	fig|4932.3.peg.4178.
Organism-specific databases
CYGD	YLR086w.
SGD	S000004076. SMC4.
Phylogenomic databases
HOGENOM	Q12267.
OMA	PSEEIDN.
Gene expression databases
ArrayExpress	Q12267.
Genevestigator	Q12267.
GermOnline	YLR086W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003395. RecF/RecN/SMC_N. IPR010935. SMC_hinge. [Graphical view]
Pfam	PF06470. SMC_hinge. 1 hit. PF02463. SMC_N. 1 hit. [Graphical view]
ProDom	PD000006. ABC_transporter. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
NextBio	966951.

Entry information

Entry name

SMC4_YEAST

Accession

Primary (citable) accession number: Q12267

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)