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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi111 – 1188ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. kinetochore organization Source: MGI
  3. meiotic chromosome condensation Source: MGI
  4. meiotic chromosome segregation Source: MGI
  5. 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

ReactomeiREACT_196580. Condensation of Prophase Chromosomes.
REACT_196632. 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
ProteomesiUP000000589: 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

  1. condensin complex Source: MGI
  2. cytoplasm Source: MGI
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12861286Structural maintenance of chromosomes protein 4PRO_0000119008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineBy similarity
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei141 – 1411PhosphoserineBy similarity
Modified residuei379 – 3791N6-acetyllysine1 Publication
Modified residuei677 – 6771N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8CG47.
PaxDbiQ8CG47.
PRIDEiQ8CG47.

PTM databases

PhosphoSiteiQ8CG47.

Expressioni

Gene expression databases

BgeeiQ8CG47.
CleanExiMM_SMC4.
ExpressionAtlasiQ8CG47. baseline and differential.
GenevestigatoriQ8CG47.

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

Protein-protein interaction databases

BioGridi213863. 1 interaction.
IntActiQ8CG47. 1 interaction.

Structurei

Secondary structure

1
1286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi596 – 60712Combined sources
Beta strandi608 – 6103Combined sources
Beta strandi613 – 6164Combined sources
Helixi617 – 6193Combined sources
Helixi625 – 6273Combined sources
Helixi628 – 6347Combined sources
Helixi636 – 6394Combined sources
Beta strandi640 – 6445Combined sources
Helixi646 – 65813Combined sources
Beta strandi666 – 6683Combined sources
Helixi669 – 6713Combined sources
Helixi673 – 6753Combined sources
Helixi685 – 6873Combined sources
Helixi691 – 6944Combined sources
Helixi700 – 71011Combined sources
Beta strandi714 – 7185Combined sources
Helixi719 – 7268Combined sources
Beta strandi735 – 7373Combined sources
Beta strandi749 – 7513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L51X-ray1.51B595-752[»]
ProteinModelPortaliQ8CG47.
SMRiQ8CG47. Positions 595-752.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CG47.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni590 – 767178Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili270 – 589320Sequence AnalysisAdd
BLAST
Coiled coili768 – 1018251Sequence AnalysisAdd
BLAST
Coiled coili1068 – 113366Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi64 – 696Poly-Pro
Compositional biasi1189 – 122436Ala/Asp-rich (DA-box)Add
BLAST

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

eggNOGiCOG1196.
GeneTreeiENSGT00580000081617.
HOGENOMiHOG000184777.
HOVERGENiHBG106696.
InParanoidiQ8CG47.
KOiK06675.
OMAiPSEEIDN.
OrthoDBiEOG7RJPQJ.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti454 – 4541E → V in BAC40608. (PubMed:15489334)Curated

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_006502108.1. XM_006502045.1.
XP_006502109.1. XM_006502046.1.
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_006502108.1. XM_006502045.1.
XP_006502109.1. XM_006502046.1.
UniGeneiMm.206841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L51X-ray1.51B595-752[»]
ProteinModelPortaliQ8CG47.
SMRiQ8CG47. Positions 595-752.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213863. 1 interaction.
IntActiQ8CG47. 1 interaction.

PTM databases

PhosphoSiteiQ8CG47.

Proteomic databases

MaxQBiQ8CG47.
PaxDbiQ8CG47.
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

eggNOGiCOG1196.
GeneTreeiENSGT00580000081617.
HOGENOMiHOG000184777.
HOVERGENiHBG106696.
InParanoidiQ8CG47.
KOiK06675.
OMAiPSEEIDN.
OrthoDBiEOG7RJPQJ.
PhylomeDBiQ8CG47.
TreeFamiTF101158.

Enzyme and pathway databases

ReactomeiREACT_196580. Condensation of Prophase Chromosomes.
REACT_196632. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

ChiTaRSiSmc4. mouse.
EvolutionaryTraceiQ8CG47.
NextBioi330998.
PROiQ8CG47.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CG47.
CleanExiMM_SMC4.
ExpressionAtlasiQ8CG47. baseline and differential.
GenevestigatoriQ8CG47.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The evolution of SMC proteins: phylogenetic analysis and structural implications."
    Cobbe N., Heck M.M.S.
    Mol. Biol. Evol. 21:332-347(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and C57BL/6J.
    Tissue: Brain and Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-602.
    Strain: NOD.
    Tissue: Thymus.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

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: February 4, 2015
This is version 114 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

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.