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Protein

Structural maintenance of chromosomes protein 2

Gene

cut14

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 bindingi32 – 398ATPSequence 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 2
Alternative name(s):
Cell untimely torn protein 14
Chromosome segregation protein cut14
Gene namesi
Name:cut14
Synonyms:smc2
ORF Names:SPBP4H10.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBP4H10.06c.
PomBaseiSPBP4H10.06c. cut14.

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

  • chromosome, centromeric core domain Source: PomBase
  • condensed nuclear chromosome kinetochore Source: PomBase
  • cytoplasm Source: PomBase
  • nuclear chromatin Source: PomBase
  • nuclear condensin complex Source: PomBase
  • nucleolus Source: PomBase
  • nucleus Source: PomBase
  • transcriptionally active chromatin Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11721172Structural maintenance of chromosomes protein 2PRO_0000119012Add
BLAST

Proteomic databases

MaxQBiP41003.

Interactioni

Subunit structurei

Forms a heterodimer with cut3/smc4. Component of the condensin complex, which contains the cut3 and cut14 heterodimer, and three non smc subunits that probably regulate the complex: cnd1, cnd2 and cnd3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
cut3P410045EBI-1149523,EBI-1149474

Protein-protein interaction databases

BioGridi277831. 51 interactions.
IntActiP41003. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP41003.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni508 – 675168Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili172 – 20433Sequence analysisAdd
BLAST
Coiled coili258 – 507250Sequence analysisAdd
BLAST
Coiled coili676 – 941266Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1086 – 112136Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with cut3, forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC2 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000163792.
InParanoidiP41003.
KOiK06674.
OMAiECEREHQ.
OrthoDBiEOG092C0XGI.
PhylomeDBiP41003.

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.

P41003-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIEELIIDG FKSYAVRTVI SNWDDQFNAI TGLNGSGKSN ILDAICFVLG
60 70 80 90 100
ITNMSTVRAQ NLQDLIYKRG QAGITRASVT IVFNNRDPAS SPIGFENHPQ
110 120 130 140 150
VSVTRQIIMG GTSKYLINGH RALQQNVQNL FQSVQLNINN PNFLIMQGRI
160 170 180 190 200
TKVLNMKATE ILSMIEEASG TRMFEERKEK AFRTMQRKEA KVEEINTLLR
210 220 230 240 250
EEIEPRLTKL RTEKKTFLEY QHIYNDLERL SHLCTAYDYY KLSLKVEELT
260 270 280 290 300
VQASQKHSHI AEMESSLQTS KQEVLILKEK IKKIEDERMR QMSVSSDRTL
310 320 330 340 350
DSQLQTVNEN ITRISTSIEL KNTALEEEHG DLQQIRGKAK ELETLLRGKR
360 370 380 390 400
KRLDEVLSVY EKRKDEHQSI SKDFKSQEEL ISSLTTGLST TEGHETGYSR
410 420 430 440 450
KLHEARDTLN DFKAEKETNR LKLEGLNKQI SLTKPKKAEA TKRCDQLNRE
460 470 480 490 500
IDILQNHVEK LKMSLKNTNS DITGEDVLQQ KLKQLAKDRG NLLNELDALK
510 520 530 540 550
SKLAYMEFTY TDPTPNFDRS KVKGLVAQLL TLNEENYDKQ TALEITAGGR
560 570 580 590 600
LYNLIVETEK IGAQLLQKGN LKRRVTIIPL NKITSFVASA ERVGAAKKIS
610 620 630 640 650
NNKAQLALEL IGYDDELLPA MQYVFGSTLV CDTPESAKKV TFHPSVKLKS
660 670 680 690 700
VTLDGDVYDP SGTLTGGSVN KSAGPLLQIQ KLNSLQLKLQ VVTSEYEKLE
710 720 730 740 750
TQLKDLKTQN ANFHRLEQEI QLKQHELTLL IEQRETDSSF RLLSDYQQYK
760 770 780 790 800
DDVKDLKQRL PELDRLILQS DQAIKKIERD MQEWKHNKGS KMAELEKEFN
810 820 830 840 850
QYKHKLDEFT PILEKSENDY NGVKLECEQL EGELQNHQQS LVQGESTTSL
860 870 880 890 900
IKTEIAELEL SLVNEEHNRK KLTELIEIES AKFSGLNKEI DSLSTSMKTF
910 920 930 940 950
ESEINNGELT IQKLNHEFDR LEREKSVAIT AINHLEKEND WIDGQKQHFG
960 970 980 990 1000
KQGTIFDFHS QNMRQCREQL HNLKPRFASM RKAINPKVMD MIDGVEKKEA
1010 1020 1030 1040 1050
KLRSMIKTIH RDKKKIQDTV KSIDRFKRSA LEKTWREVNS SFGEIFDELL
1060 1070 1080 1090 1100
PGNSAELQPP ENKEFTDGLE IHVKIGSIWK DSLAELSGGQ RSLVALALIM
1110 1120 1130 1140 1150
SLLKYKPAPM YILDEIDAAL DLSHTQNIGR LIKTKFKGSQ FIIVSLKEGM
1160 1170
FTNANRLFHV RFMDGSSVVQ AR
Length:1,172
Mass (Da):134,137
Last modified:February 21, 2001 - v2
Checksum:i0B785C0F2CA3025C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti455 – 4551Q → P in BAA06453 (PubMed:7957061).Curated
Sequence conflicti468 – 4692TN → PY in BAA06453 (PubMed:7957061).Curated
Sequence conflicti475 – 4773EDV → GDA in BAA06453 (PubMed:7957061).Curated
Sequence conflicti482 – 4821L → M in BAA06453 (PubMed:7957061).Curated
Sequence conflicti485 – 4851L → A in BAA06453 (PubMed:7957061).Curated
Sequence conflicti522 – 5232VK → GE in BAA06453 (PubMed:7957061).Curated
Sequence conflicti673 – 6731A → T in BAA06453 (PubMed:7957061).Curated
Sequence conflicti718 – 7181Q → R in BAA06453 (PubMed:7957061).Curated
Sequence conflicti733 – 7331Q → R in BAA06453 (PubMed:7957061).Curated
Sequence conflicti1046 – 10461F → C in BAA06453 (PubMed:7957061).Curated
Sequence conflicti1146 – 11461L → H in BAA06453 (PubMed:7957061).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30787 Genomic DNA. Translation: BAA06453.2.
CU329671 Genomic DNA. Translation: CAB83164.1.
PIRiS51623.
RefSeqiNP_596180.1. NM_001022099.2.

Genome annotation databases

EnsemblFungiiSPBP4H10.06c.1; SPBP4H10.06c.1:pep; SPBP4H10.06c.
GeneIDi2541319.
KEGGispo:SPBP4H10.06c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30787 Genomic DNA. Translation: BAA06453.2.
CU329671 Genomic DNA. Translation: CAB83164.1.
PIRiS51623.
RefSeqiNP_596180.1. NM_001022099.2.

3D structure databases

ProteinModelPortaliP41003.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277831. 51 interactions.
IntActiP41003. 2 interactions.

Proteomic databases

MaxQBiP41003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBP4H10.06c.1; SPBP4H10.06c.1:pep; SPBP4H10.06c.
GeneIDi2541319.
KEGGispo:SPBP4H10.06c.

Organism-specific databases

EuPathDBiFungiDB:SPBP4H10.06c.
PomBaseiSPBP4H10.06c. cut14.

Phylogenomic databases

HOGENOMiHOG000163792.
InParanoidiP41003.
KOiK06674.
OMAiECEREHQ.
OrthoDBiEOG092C0XGI.
PhylomeDBiP41003.

Enzyme and pathway databases

ReactomeiR-SPO-2514853. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

PROiP41003.

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...

Entry informationi

Entry nameiSMC2_SCHPO
AccessioniPrimary (citable) accession number: P41003
Secondary accession number(s): Q9P7E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 21, 2001
Last modified: September 7, 2016
This is version 128 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.