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Protein

Structural maintenance of chromosomes protein 4

Gene

cut3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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 bindingi155 – 1628ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic chromosome condensation Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-2514853. Condensation of Prometaphase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 4
Alternative name(s):
Cell untimely torn protein 3
Chromosome segregation protein cut3
Gene namesi
Name:cut3
Synonyms:smc4
ORF Names:SPBC146.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC146.03c.
PomBaseiSPBC146.03c. cut3.

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: PomBase
  • cytosol Source: PomBase
  • nuclear condensin complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191T → A: Defects in chromosome condensation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13241324Structural maintenance of chromosomes protein 4PRO_0000119017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphothreonine; by CDC21 Publication

Post-translational modificationi

Phosphorylated by CDC2 on Thr-19 at metaphase.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41004.

PTM databases

iPTMnetiP41004.

Interactioni

Subunit structurei

Forms a heterodimer with cut14/smc2. Component of the condensin complex, which contains the smc2 and smc4 heterodimer, and three non smc subunits that probably regulate the complex: cnd1, cnd2 and cnd3. Interacts with C1739.07.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cnd2Q9Y7R32EBI-1149474,EBI-1149594
cut14P410035EBI-1149474,EBI-1149523
SPCC1739.07O744693EBI-1149474,EBI-1149494

Protein-protein interaction databases

BioGridi276367. 62 interactions.
DIPiDIP-35048N.
IntActiP41004. 5 interactions.
MINTiMINT-4689999.

Structurei

3D structure databases

ProteinModelPortaliP41004.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni629 – 824196Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili310 – 33728Sequence analysisAdd
BLAST
Coiled coili370 – 628259Sequence analysisAdd
BLAST
Coiled coili825 – 1077253Sequence analysisAdd
BLAST
Coiled coili1297 – 132428Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1230 – 126536Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with cut14, forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC4 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000184777.
InParanoidiP41004.
KOiK06675.
OMAiNNLRENI.
OrthoDBiEOG7M0P0T.
PhylomeDBiP41004.

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.

P41004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKGIFRTS STPSIVDVTP DRGERPRKLV RSVLESPSQK DVASIVKIEQ
60 70 80 90 100
TPSRPFFNDF LKKRITDSLN ERPNLLNKFM SAQDGTPSKS TGFNERSSQL
110 120 130 140 150
VSEFTTTEDI ENCEETTQVL PPRLVVYELR LTNFKSYAGT QIVGPFHPSF
160 170 180 190 200
SSIVGPNGSG KSNVIDALLF VFGFRASKLR QSKASALIHK SATHPSLDSC
210 220 230 240 250
DVEITFKEVN SDFTYVDGSE LTVRRTAYKN NTSKYFVNGV ESSFSAVSNL
260 270 280 290 300
LKEKGIDLNH KRFLILQGEV ESIAQMKPRA ISEGDDGLLE YLEDIIGTSK
310 320 330 340 350
YKPIIEENMQ ELSNSDDICA EKESRLKLVL SEKAKLEDSK NSVLSFLKDE
360 370 380 390 400
NELFMKQNQL YRTILYETRN KKTLVQNLLN SLEGKLQAHL EKFEQTERDI
410 420 430 440 450
SEKNEEVKSL REKAAKVKND CTSEKKTRQS YEQQTVKIEE QLKFLLNKEK
460 470 480 490 500
KLKKSIEALS FEKSEAENSL SSHDIDSQKL NSEIADLSLR LQQEELSLDD
510 520 530 540 550
IRKSLQGKTE GISNAIEEKQ KAMAPALEKI NQLTSEKQIL QVELDMLLNK
560 570 580 590 600
ENDLINDVES SQSSLDKLRN DAEENRNILS SKLKVLSDLK GEKKDVSKNI
610 620 630 640 650
ERKKETVHNT YRNLMSNRTK LEEMKASLSS SRSRGNVLES LQRLHESDNL
660 670 680 690 700
NGFFGRLGDL ATIDEAYDVA ISTACPALNH IVVDNIETGQ KCVAFLRSNN
710 720 730 740 750
LGRASFIILK ELAQKNLARI QTPENVPRLF DLLRFNDQKF APAFYNVLQN
760 770 780 790 800
TLVAKNLEQA NRIAYGKTRW RVVTLSGQLI DKSGTMTGGG TRVKKGGMSS
810 820 830 840 850
AITSDVSPAS VETCDKQVQL EDTRYRQHLS ELESLNQRFT EISERIPSAE
860 870 880 890 900
LEISKLQLDV SACDRLVAGE ERRILQLKSD LKSIRNNNER KRNLQNKISN
910 920 930 940 950
MDKEVEAINI NNEGLVTEIK TLQDKIMEIG GIRYRIQKSK VDDLHEQLKF
960 970 980 990 1000
VKDKLNKMSF KKKKNEQRSQ SFQVELSNLT SEYDTTTESI ATLKTELQSL
1010 1020 1030 1040 1050
NKYVDEHKSR LREFENALWD INSSIDELVK FIEFESKQMN SVKAERIELE
1060 1070 1080 1090 1100
NQIQEQRTAL SEVGNNENKY LKLMSNLKLH NLTEFCDQTT MDSTFPEYSE
1110 1120 1130 1140 1150
DELSSVDKSE LVSNISVLKK KTEDREVDIN VLSEYRRCNK EAEKRDSDYQ
1160 1170 1180 1190 1200
SELQKRTDLK KVVTDLQSQR LDEFMYGFGI ISMKLKEMYQ IITMGGNAEL
1210 1220 1230 1240 1250
ELVDSLDPFS EGVLFSVMPP KKSWKNISNL SGGEKTLSSL ALVFALHNYK
1260 1270 1280 1290 1300
PTPLYVMDEI DAALDFKNVS IVANYIKERT KNAQFIVISL RSNMFELSSR
1310 1320
LVGIYKTANM TKSVTINNKE ILTD
Length:1,324
Mass (Da):150,653
Last modified:April 27, 2001 - v2
Checksum:iF28CEDC322E5C622
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti382 – 3821L → V in BAA06454 (PubMed:7957061).Curated
Sequence conflicti393 – 3931F → C in BAA06454 (PubMed:7957061).Curated
Sequence conflicti1316 – 13161I → L in BAA06454 (PubMed:7957061).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30788 Genomic DNA. Translation: BAA06454.1.
CU329671 Genomic DNA. Translation: CAB46756.1.
AB027959 Genomic DNA. Translation: BAA87263.1.
PIRiS51622.
RefSeqiNP_595392.1. NM_001021299.2.

Genome annotation databases

EnsemblFungiiSPBC146.03c.1; SPBC146.03c.1:pep; SPBC146.03c.
GeneIDi2539817.
KEGGispo:SPBC146.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30788 Genomic DNA. Translation: BAA06454.1.
CU329671 Genomic DNA. Translation: CAB46756.1.
AB027959 Genomic DNA. Translation: BAA87263.1.
PIRiS51622.
RefSeqiNP_595392.1. NM_001021299.2.

3D structure databases

ProteinModelPortaliP41004.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276367. 62 interactions.
DIPiDIP-35048N.
IntActiP41004. 5 interactions.
MINTiMINT-4689999.

PTM databases

iPTMnetiP41004.

Proteomic databases

MaxQBiP41004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC146.03c.1; SPBC146.03c.1:pep; SPBC146.03c.
GeneIDi2539817.
KEGGispo:SPBC146.03c.

Organism-specific databases

EuPathDBiFungiDB:SPBC146.03c.
PomBaseiSPBC146.03c. cut3.

Phylogenomic databases

HOGENOMiHOG000184777.
InParanoidiP41004.
KOiK06675.
OMAiNNLRENI.
OrthoDBiEOG7M0P0T.
PhylomeDBiP41004.

Enzyme and pathway databases

ReactomeiR-SPO-2514853. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

NextBioi20800966.
PROiP41004.

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. "Fission yeast cut3 and cut14, members of a ubiquitous protein family, are required for chromosome condensation and segregation in mitosis."
    Saka Y., Sutani T., Yamashita Y., Saitoh S., Takeuchi M., Nakaseko Y., Yanagida M.
    EMBO J. 13:4938-4952(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 273-486, SUBCELLULAR LOCATION.
    Strain: ATCC 38364 / 968.
  4. "Fission yeast condensin complex: essential roles of non-SMC subunits for 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH CUT14; CND1; CND2 AND CND3, PHOSPHORYLATION AT THR-19, MUTAGENESIS OF THR-19.
  5. "Cti1/C1D interacts with condensin SMC hinge and supports the DNA repair function of condensin."
    Chen E.S., Sutani T., Yanagida M.
    Proc. Natl. Acad. Sci. U.S.A. 101:8078-8083(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1739.07.
  6. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSMC4_SCHPO
AccessioniPrimary (citable) accession number: P41004
Secondary accession number(s): Q9UTW4, Q9UUF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 27, 2001
Last modified: January 20, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.