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Protein

Structural maintenance of chromosomes protein 2

Gene

SMC2

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 bindingi32 – 398ATPSequence Analysis

GO - Molecular functioni

  • AT DNA binding Source: SGD
  • ATP binding Source: SGD
  • chromatin binding Source: SGD
  • DNA secondary structure binding Source: SGD
  • double-stranded DNA binding Source: SGD

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • meiotic chromosome condensation Source: SGD
  • meiotic chromosome separation Source: SGD
  • mitotic chromosome condensation Source: SGD
  • mitotic sister chromatid segregation Source: SGD
  • negative regulation of meiotic DNA double-strand break formation 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-30479-MONOMER.
ReactomeiREACT_284037. Condensation of Prometaphase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 2
Alternative name(s):
DA-box protein SMC2
Gene namesi
Name:SMC2
Ordered Locus Names:YFR031C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VI

Organism-specific databases

CYGDiYFR031c.
EuPathDBiFungiDB:YFR031C.
SGDiS000001927. SMC2.

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
Chaini1 – 11701170Structural maintenance of chromosomes protein 2PRO_0000119013Add
BLAST

Proteomic databases

MaxQBiP38989.
PaxDbiP38989.

Expressioni

Gene expression databases

GenevestigatoriP38989.

Interactioni

Subunit structurei

Forms a heterodimer with SMC4. 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
BRN1P381702EBI-17412,EBI-4792
SMC1P329083EBI-17412,EBI-17402
YCG1Q066803EBI-17412,EBI-4799

Protein-protein interaction databases

BioGridi31186. 55 interactions.
DIPiDIP-2983N.
IntActiP38989. 12 interactions.
MINTiMINT-435495.
STRINGi4932.YFR031C.

Structurei

Secondary structure

1
1170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi455 – 46915Combined sources
Helixi473 – 49523Combined sources
Helixi498 – 5014Combined sources
Beta strandi523 – 5264Combined sources
Helixi527 – 5293Combined sources
Helixi536 – 5405Combined sources
Helixi541 – 5488Combined sources
Helixi549 – 5535Combined sources
Beta strandi555 – 5595Combined sources
Helixi560 – 5689Combined sources
Beta strandi576 – 5805Combined sources
Turni581 – 5833Combined sources
Helixi591 – 60010Combined sources
Beta strandi604 – 6074Combined sources
Helixi608 – 6114Combined sources
Helixi616 – 6183Combined sources
Helixi619 – 6268Combined sources
Beta strandi629 – 6346Combined sources
Helixi635 – 6428Combined sources
Beta strandi650 – 6534Combined sources
Turni654 – 6563Combined sources
Beta strandi657 – 6604Combined sources
Turni661 – 6633Combined sources
Beta strandi664 – 6685Combined sources
Helixi676 – 70530Combined sources
Turni706 – 7116Combined sources
Helixi714 – 7218Combined sources
Turni722 – 7265Combined sources
Helixi727 – 7348Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RSIX-ray2.90A396-792[»]
ProteinModelPortaliP38989.
SMRiP38989. Positions 1-369, 453-735, 879-1169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni470 – 677208Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili172 – 469298Sequence AnalysisAdd
BLAST
Coiled coili678 – 1027350Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1084 – 111936Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC4, forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC2 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1196.
GeneTreeiENSGT00550000074857.
HOGENOMiHOG000163792.
InParanoidiP38989.
KOiK06674.
OMAiCQNGKIP.
OrthoDBiEOG7M0P0T.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF9. PTHR18937:SF9. 1 hit.
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. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

P38989-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVEELIIDG FKSYATRTVI TDWDPQFNAI TGLNGSGKSN ILDAICFVLG
60 70 80 90 100
IASMSTVRAS SLQDLIYKRG QAGVTKASVT IVFDNTDKSN SPIGFTNSPQ
110 120 130 140 150
ISVTRQVVLG GTSKYLINGH RAPQQSVLQL FQSVQLNINN PNFLIMQGKI
160 170 180 190 200
TKVLNMKPSE ILSLIEEAAG TKMFEDRREK AERTMSKKET KLQENRTLLT
210 220 230 240 250
EEIEPKLEKL RNEKRMFLEF QSTQTDLEKT ERIVVSYEYY NIKHKHTSIR
260 270 280 290 300
ETLENGETRM KMLNEFVKKT SEEIDSLNED VEEIKLQKEK ELHKEGTISK
310 320 330 340 350
LENKENGLLN EISRLKTSLS IKVENLNDTT EKSKALESEI ASSSAKLIEK
360 370 380 390 400
KSAYANTEKD YKMVQEQLSK QRDLYKRKEE LVSTLTTGIS STGAADGGYN
410 420 430 440 450
AQLAKAKTEL NEVSLAIKKS SMKMELLKKE LLTIEPKLKE ATKDNELNVK
460 470 480 490 500
HVKQCQETCD KLRARLVEYG FDPSRIKDLK QREDKLKSHY YQTCKNSEYL
510 520 530 540 550
KRRVTNLEFN YTKPYPNFEA SFVHGVVGQL FQIDNDNIRY ATALQTCAGG
560 570 580 590 600
RLFNVVVQDS QTATQLLERG RLRKRVTIIP LDKIYTRPIS SQVLDLAKKI
610 620 630 640 650
APGKVELAIN LIRFDESITK AMEFIFGNSL ICEDPETAKK ITFHPKIRAR
660 670 680 690 700
SITLQGDVYD PEGTLSGGSR NTSESLLVDI QKYNQIQKQI ETIQADLNHV
710 720 730 740 750
TEELQTQYAT SQKTKTIQSD LNLSLHKLDL AKRNLDANPS SQIIARNEEI
760 770 780 790 800
LRDIGECENE IKTKQMSLKK CQEEVSTIEK DMKEYDSDKG SKLNELKKEL
810 820 830 840 850
KLLAKELEEQ ESESERKYDL FQNLELETEQ LSSELDSNKT LLHNHLKSIE
860 870 880 890 900
SLKLENSDLE GKIRGVEDDL VTVQTELNEE KKRLMDIDDE LNELETLIKK
910 920 930 940 950
KQDEKKSSEL ELQKLVHDLN KYKSNTNNME KIIEDLRQKH EFLEDFDLVR
960 970 980 990 1000
NIVKQNEGID LDTYRERSKQ LNEKFQELRK KVNPNIMNMI ENVEKKEAAL
1010 1020 1030 1040 1050
KTMIKTIEKD KMKIQETISK LNEYKRETLV KTWEKVTLDF GNIFADLLPN
1060 1070 1080 1090 1100
SFAKLVPCEG KDVTQGLEVK VKLGNIWKES LIELSGGQRS LIALSLIMAL
1110 1120 1130 1140 1150
LQFRPAPMYI LDEVDAALDL SHTQNIGHLI KTRFKGSQFI VVSLKEGMFA
1160 1170
NANRVFRTRF QDGTSVVSIM
Length:1,170
Mass (Da):133,928
Last modified:February 1, 1995 - v1
Checksum:i142B41AAE109621F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05820 Genomic DNA. Translation: AAA17416.1.
D50617 Genomic DNA. Translation: BAA09270.1.
BK006940 Genomic DNA. Translation: DAA12471.1.
PIRiA56157.
RefSeqiNP_116687.1. NM_001179996.2.

Genome annotation databases

EnsemblFungiiYFR031C; YFR031C; YFR031C.
GeneIDi850589.
KEGGisce:YFR031C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05820 Genomic DNA. Translation: AAA17416.1.
D50617 Genomic DNA. Translation: BAA09270.1.
BK006940 Genomic DNA. Translation: DAA12471.1.
PIRiA56157.
RefSeqiNP_116687.1. NM_001179996.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RSIX-ray2.90A396-792[»]
ProteinModelPortaliP38989.
SMRiP38989. Positions 1-369, 453-735, 879-1169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31186. 55 interactions.
DIPiDIP-2983N.
IntActiP38989. 12 interactions.
MINTiMINT-435495.
STRINGi4932.YFR031C.

Proteomic databases

MaxQBiP38989.
PaxDbiP38989.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYFR031C; YFR031C; YFR031C.
GeneIDi850589.
KEGGisce:YFR031C.

Organism-specific databases

CYGDiYFR031c.
EuPathDBiFungiDB:YFR031C.
SGDiS000001927. SMC2.

Phylogenomic databases

eggNOGiCOG1196.
GeneTreeiENSGT00550000074857.
HOGENOMiHOG000163792.
InParanoidiP38989.
KOiK06674.
OMAiCQNGKIP.
OrthoDBiEOG7M0P0T.

Enzyme and pathway databases

BioCyciYEAST:G3O-30479-MONOMER.
ReactomeiREACT_284037. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

NextBioi966434.
PROiP38989.

Gene expression databases

GenevestigatoriP38989.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF9. PTHR18937:SF9. 1 hit.
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. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SMC2, a Saccharomyces cerevisiae gene essential for chromosome segregation and condensation, defines a subgroup within the SMC family."
    Strunnikov A.V., Hogan E., Koshland D.
    Genes Dev. 9:587-599(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Fifteen open reading frames in a 30.8 kb region of the right arm of chromosome VI from Saccharomyces cerevisiae."
    Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H., Hanaoka F., Murakami Y.
    Yeast 12:177-190(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  5. "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 SMC4; BRN1; YCS4 AND YCG1.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSMC2_YEAST
AccessioniPrimary (citable) accession number: P38989
Secondary accession number(s): D6VTR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 27, 2015
This is version 143 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 3290 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 VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

External Data

Dasty 3

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 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.