Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Structural maintenance of chromosomes protein 4

Gene

Smc4

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi111 – 118ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • kinetochore organization Source: MGI
  • meiotic chromosome condensation Source: MGI
  • meiotic chromosome segregation Source: MGI
  • mitotic chromosome condensation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2299718. Condensation of Prophase Chromosomes.
R-MMU-2514853. Condensation of Prometaphase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 4
Short name:
SMC protein 4
Short name:
SMC-4
Alternative name(s):
Chromosome-associated polypeptide C
XCAP-C homolog
Gene namesi
Name:Smc4
Synonyms:Capc, Smc4l1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1917349. Smc4.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Chromosome By similarity

  • 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, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001190081 – 1286Structural maintenance of chromosomes protein 4Add BLAST1286

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21PhosphoserineBy similarity1
Modified residuei27PhosphoserineBy similarity1
Modified residuei40PhosphoserineBy similarity1
Modified residuei141PhosphoserineBy similarity1
Modified residuei379N6-acetyllysineCombined sources1
Modified residuei677N6-acetyllysineBy similarity1
Modified residuei980PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CG47.
MaxQBiQ8CG47.
PaxDbiQ8CG47.
PeptideAtlasiQ8CG47.
PRIDEiQ8CG47.

PTM databases

iPTMnetiQ8CG47.
PhosphoSitePlusiQ8CG47.
SwissPalmiQ8CG47.

Expressioni

Gene expression databases

BgeeiENSMUSG00000034349.
CleanExiMM_SMC4.
ExpressionAtlasiQ8CG47. baseline and differential.
GenevisibleiQ8CG47. MM.

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: BRRN1/CAPH, CNAP1/CAPD2 and CAPG (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Yy1Q008992EBI-6921575,EBI-6921536

GO - Molecular functioni

Protein-protein interaction databases

BioGridi213863. 8 interactors.
IntActiQ8CG47. 9 interactors.
STRINGi10090.ENSMUSP00000047872.

Structurei

Secondary structure

11286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi596 – 607Combined sources12
Beta strandi608 – 610Combined sources3
Beta strandi613 – 616Combined sources4
Helixi617 – 619Combined sources3
Helixi625 – 627Combined sources3
Helixi628 – 634Combined sources7
Helixi636 – 639Combined sources4
Beta strandi640 – 644Combined sources5
Helixi646 – 658Combined sources13
Beta strandi666 – 668Combined sources3
Helixi669 – 671Combined sources3
Helixi673 – 675Combined sources3
Helixi685 – 687Combined sources3
Helixi691 – 694Combined sources4
Helixi700 – 710Combined sources11
Beta strandi714 – 718Combined sources5
Helixi719 – 726Combined sources8
Beta strandi735 – 737Combined sources3
Beta strandi749 – 751Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L51X-ray1.51B595-752[»]
ProteinModelPortaliQ8CG47.
SMRiQ8CG47.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CG47.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni590 – 767Flexible hingeAdd BLAST178

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili270 – 589Sequence analysisAdd BLAST320
Coiled coili768 – 1018Sequence analysisAdd BLAST251
Coiled coili1068 – 1133Sequence analysisAdd BLAST66

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi64 – 69Poly-Pro6
Compositional biasi1189 – 1224Ala/Asp-rich (DA-box)Add BLAST36

Domaini

The 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

eggNOGiKOG0996. Eukaryota.
COG1196. LUCA.
GeneTreeiENSGT00580000081617.
HOGENOMiHOG000184777.
HOVERGENiHBG106696.
InParanoidiQ8CG47.
KOiK06675.
OMAiPPVPPYC.
OrthoDBiEOG091G01SY.
PhylomeDBiQ8CG47.
TreeFamiTF101158.

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. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8CG47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRKGTKPST ACHQEEGPPP SQDGAHSDEE MEQPAGEAES AAPAKPPGEE
60 70 80 90 100
LDNRSLEEIL NSIPPPPPPA MASEAGAPRL MITHIVNQNF KSYAGEKVLG
110 120 130 140 150
PFHKRFSCII GPNGSGKSNV IDSMLFVFGY RAQKIRSKKL SVLIHNSDEH
160 170 180 190 200
KDIQSCTVEV HFQKIIDKEG DDYEVLPNSN FYVSRTAYRD STSVYHISGK
210 220 230 240 250
KKTFKDVGNL LRSHGIDLDH NRFLILQGEV EQIAMMKPKG QTEHDEGMLE
260 270 280 290 300
YLEDIIGCGR LNEPIKVLCR RVEILNEHRG EKLNRVKMVE KEKDALEGEK
310 320 330 340 350
NIAIEFLTLE NEMFKKKNHI CQYYIYDLQN RIAEITTQKE KIHEDTKEIT
360 370 380 390 400
EKSNVLSNEM KAKNSAVKDV EKKLNKVTKF IEQNKEKFTQ LDLEDVQVRE
410 420 430 440 450
KLKHATSKAK KLEKQLQKDK EKVEELKSVP AKSKTVINET TTRNNSLEKE
460 470 480 490 500
REKEEKKLKE VMDSLKQETQ GLQKEKEIQE KELMGFNKSV NEARSKMEVA
510 520 530 540 550
QSELDIYLSR HNTAVSQLSK AKEALITASE TLKERKAAIK DINTKLPQTQ
560 570 580 590 600
QELKEKEKEL QKLTQEEINL KSLVHDLFQK VEEAKSSLAM NRSRGKVLDA
610 620 630 640 650
IIQEKKSGRI PGIYGRLGDL GAIDEKYDIA ISSCCHALDY IVVDSIDTAQ
660 670 680 690 700
ECVNFLKKHN IGIATFIGLD KMTVWAKKMS KIQTPENTPR LFDLVKVKNE
710 720 730 740 750
EIRQAFYFAL RDTLVANNLD QATRVAYQRD RRWRVVTLQG QIIEQSGTMS
760 770 780 790 800
GGGSKVMRGR MGSSVIDEIS VEEVNKMESQ LERHSKQAMQ IQEQKVQHEE
810 820 830 840 850
AVVKLRHSER DMRNTLEKFA ASIQGLSEQE EYLCVQIKEL EANVLTTAPD
860 870 880 890 900
RKQQKLLEEN VSVFKKEYDA VAEKAGKVEA EIKRLHNTII DINNRKLKAQ
910 920 930 940 950
QNKLDTINKQ LDECASAITK AQVAIKTADR NLKKAQDSVC RTEKEIKDTE
960 970 980 990 1000
KEINDLKTEL KNIEDKAEEV INNTKTAETS LPEIQKEHRN LLQELKVIQE
1010 1020 1030 1040 1050
NEHALQKDAL SIKLKLEQID GHISEHNSKI KYWQKEISKI KLHPVEDNPV
1060 1070 1080 1090 1100
ETVAVLSQEE LEAIKNPESI TNEIALLEAQ CREMKPNLGA IAEYKKKEDL
1110 1120 1130 1140 1150
YLQRVAELDK ITSERDNFRQ AYEDLRKQRL NEFMAGFYVI TNKLKENYQM
1160 1170 1180 1190 1200
LTLGGDAELE LVDSLDPFSE GIMFSVRPPK KSWKKIFNLS GGEKTLSSLA
1210 1220 1230 1240 1250
LVFALHHYKP TPLYFMDEID AALDFKNVSI VAFYIYEQTK NAQFIIISLR
1260 1270 1280
NNMFEISDRL IGIYKTYNST KSVAVNPKQI ASKGLC
Length:1,286
Mass (Da):146,895
Last modified:March 1, 2003 - v1
Checksum:iCFEAD84199C3CEB5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti454E → V in BAC40608 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ534940 mRNA. Translation: CAD59183.1.
BC005507 mRNA. Translation: AAH05507.1.
BC062939 mRNA. Translation: AAH62939.1.
AK088350 mRNA. Translation: BAC40297.1.
AK088846 mRNA. Translation: BAC40608.2.
CCDSiCCDS17401.1.
RefSeqiNP_598547.1. NM_133786.3.
XP_006502109.1. XM_006502046.2.
UniGeneiMm.206841.

Genome annotation databases

EnsembliENSMUST00000042901; ENSMUSP00000047872; ENSMUSG00000034349.
GeneIDi70099.
KEGGimmu:70099.
UCSCiuc008pma.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ534940 mRNA. Translation: CAD59183.1.
BC005507 mRNA. Translation: AAH05507.1.
BC062939 mRNA. Translation: AAH62939.1.
AK088350 mRNA. Translation: BAC40297.1.
AK088846 mRNA. Translation: BAC40608.2.
CCDSiCCDS17401.1.
RefSeqiNP_598547.1. NM_133786.3.
XP_006502109.1. XM_006502046.2.
UniGeneiMm.206841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L51X-ray1.51B595-752[»]
ProteinModelPortaliQ8CG47.
SMRiQ8CG47.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213863. 8 interactors.
IntActiQ8CG47. 9 interactors.
STRINGi10090.ENSMUSP00000047872.

PTM databases

iPTMnetiQ8CG47.
PhosphoSitePlusiQ8CG47.
SwissPalmiQ8CG47.

Proteomic databases

EPDiQ8CG47.
MaxQBiQ8CG47.
PaxDbiQ8CG47.
PeptideAtlasiQ8CG47.
PRIDEiQ8CG47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042901; ENSMUSP00000047872; ENSMUSG00000034349.
GeneIDi70099.
KEGGimmu:70099.
UCSCiuc008pma.1. mouse.

Organism-specific databases

CTDi10051.
MGIiMGI:1917349. Smc4.

Phylogenomic databases

eggNOGiKOG0996. Eukaryota.
COG1196. LUCA.
GeneTreeiENSGT00580000081617.
HOGENOMiHOG000184777.
HOVERGENiHBG106696.
InParanoidiQ8CG47.
KOiK06675.
OMAiPPVPPYC.
OrthoDBiEOG091G01SY.
PhylomeDBiQ8CG47.
TreeFamiTF101158.

Enzyme and pathway databases

ReactomeiR-MMU-2299718. Condensation of Prophase Chromosomes.
R-MMU-2514853. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

ChiTaRSiSmc4. mouse.
EvolutionaryTraceiQ8CG47.
PROiQ8CG47.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034349.
CleanExiMM_SMC4.
ExpressionAtlasiQ8CG47. baseline and differential.
GenevisibleiQ8CG47. MM.

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. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSMC4_MOUSE
AccessioniPrimary (citable) accession number: Q8CG47
Secondary accession number(s): Q8BTS7, Q8BTY9, Q99K21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.