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Q8CG47

- SMC4_MOUSE

UniProt

Q8CG47 - SMC4_MOUSE

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Protein

Structural maintenance of chromosomes protein 4

Gene
Smc4, Capc, Smc4l1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi111 – 1188ATP Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

  1. kinetochore organization Source: MGI
  2. meiotic chromosome condensation Source: MGI
  3. meiotic chromosome segregation Source: MGI
  4. 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.

GO - Cellular componenti

  1. condensin complex Source: Ensembl
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
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 – 211Phosphoserine By similarity
Modified residuei27 – 271Phosphoserine By similarity
Modified residuei40 – 401Phosphoserine By similarity
Modified residuei141 – 1411Phosphoserine By similarity
Modified residuei379 – 3791N6-acetyllysine1 Publication
Modified residuei677 – 6771N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8CG47.
PaxDbiQ8CG47.
PRIDEiQ8CG47.

PTM databases

PhosphoSiteiQ8CG47.

Expressioni

Gene expression databases

ArrayExpressiQ8CG47.
BgeeiQ8CG47.
CleanExiMM_SMC4.
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.

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 – 60712
Beta strandi608 – 6103
Beta strandi613 – 6164
Helixi617 – 6193
Helixi625 – 6273
Helixi628 – 6347
Helixi636 – 6394
Beta strandi640 – 6445
Helixi646 – 65813
Beta strandi666 – 6683
Helixi669 – 6713
Helixi673 – 6753
Helixi685 – 6873
Helixi691 – 6944
Helixi700 – 71011
Beta strandi714 – 7185
Helixi719 – 7268
Beta strandi735 – 7373
Beta strandi749 – 7513

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L51X-ray1.51B595-752[»]
ProteinModelPortaliQ8CG47.
SMRiQ8CG47. Positions 595-752.

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 – 589320 Reviewed predictionAdd
BLAST
Coiled coili768 – 1018251 Reviewed predictionAdd
BLAST
Coiled coili1068 – 113366 Reviewed predictionAdd
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.

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

MRRKGTKPST ACHQEEGPPP SQDGAHSDEE MEQPAGEAES AAPAKPPGEE     50
LDNRSLEEIL NSIPPPPPPA MASEAGAPRL MITHIVNQNF KSYAGEKVLG 100
PFHKRFSCII GPNGSGKSNV IDSMLFVFGY RAQKIRSKKL SVLIHNSDEH 150
KDIQSCTVEV HFQKIIDKEG DDYEVLPNSN FYVSRTAYRD STSVYHISGK 200
KKTFKDVGNL LRSHGIDLDH NRFLILQGEV EQIAMMKPKG QTEHDEGMLE 250
YLEDIIGCGR LNEPIKVLCR RVEILNEHRG EKLNRVKMVE KEKDALEGEK 300
NIAIEFLTLE NEMFKKKNHI CQYYIYDLQN RIAEITTQKE KIHEDTKEIT 350
EKSNVLSNEM KAKNSAVKDV EKKLNKVTKF IEQNKEKFTQ LDLEDVQVRE 400
KLKHATSKAK KLEKQLQKDK EKVEELKSVP AKSKTVINET TTRNNSLEKE 450
REKEEKKLKE VMDSLKQETQ GLQKEKEIQE KELMGFNKSV NEARSKMEVA 500
QSELDIYLSR HNTAVSQLSK AKEALITASE TLKERKAAIK DINTKLPQTQ 550
QELKEKEKEL QKLTQEEINL KSLVHDLFQK VEEAKSSLAM NRSRGKVLDA 600
IIQEKKSGRI PGIYGRLGDL GAIDEKYDIA ISSCCHALDY IVVDSIDTAQ 650
ECVNFLKKHN IGIATFIGLD KMTVWAKKMS KIQTPENTPR LFDLVKVKNE 700
EIRQAFYFAL RDTLVANNLD QATRVAYQRD RRWRVVTLQG QIIEQSGTMS 750
GGGSKVMRGR MGSSVIDEIS VEEVNKMESQ LERHSKQAMQ IQEQKVQHEE 800
AVVKLRHSER DMRNTLEKFA ASIQGLSEQE EYLCVQIKEL EANVLTTAPD 850
RKQQKLLEEN VSVFKKEYDA VAEKAGKVEA EIKRLHNTII DINNRKLKAQ 900
QNKLDTINKQ LDECASAITK AQVAIKTADR NLKKAQDSVC RTEKEIKDTE 950
KEINDLKTEL KNIEDKAEEV INNTKTAETS LPEIQKEHRN LLQELKVIQE 1000
NEHALQKDAL SIKLKLEQID GHISEHNSKI KYWQKEISKI KLHPVEDNPV 1050
ETVAVLSQEE LEAIKNPESI TNEIALLEAQ CREMKPNLGA IAEYKKKEDL 1100
YLQRVAELDK ITSERDNFRQ AYEDLRKQRL NEFMAGFYVI TNKLKENYQM 1150
LTLGGDAELE LVDSLDPFSE GIMFSVRPPK KSWKKIFNLS GGEKTLSSLA 1200
LVFALHHYKP TPLYFMDEID AALDFKNVSI VAFYIYEQTK NAQFIIISLR 1250
NNMFEISDRL IGIYKTYNST KSVAVNPKQI ASKGLC 1286
Length:1,286
Mass (Da):146,895
Last modified:March 1, 2003 - v1
Checksum:iCFEAD84199C3CEB5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti454 – 4541E → V in BAC40608. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS17401.1.
RefSeqi NP_598547.1. NM_133786.3.
XP_006502108.1. XM_006502045.1.
XP_006502109.1. XM_006502046.1.
UniGenei Mm.206841.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L51 X-ray 1.51 B 595-752 [» ]
ProteinModelPortali Q8CG47.
SMRi Q8CG47. Positions 595-752.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 213863. 1 interaction.
IntActi Q8CG47. 1 interaction.

PTM databases

PhosphoSitei Q8CG47.

Proteomic databases

MaxQBi Q8CG47.
PaxDbi Q8CG47.
PRIDEi Q8CG47.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000042901 ; ENSMUSP00000047872 ; ENSMUSG00000034349 .
GeneIDi 70099.
KEGGi mmu:70099.
UCSCi uc008pma.1. mouse.

Organism-specific databases

CTDi 10051.
MGIi MGI:1917349. Smc4.

Phylogenomic databases

eggNOGi COG1196.
GeneTreei ENSGT00580000081617.
HOGENOMi HOG000184777.
HOVERGENi HBG106696.
InParanoidi Q8CG47.
KOi K06675.
OMAi PSEEIDN.
OrthoDBi EOG7RJPQJ.
PhylomeDBi Q8CG47.
TreeFami TF101158.

Enzyme and pathway databases

Reactomei REACT_196580. Condensation of Prophase Chromosomes.
REACT_196632. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

ChiTaRSi SMC4. mouse.
EvolutionaryTracei Q8CG47.
NextBioi 330998.
PROi Q8CG47.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8CG47.
Bgeei Q8CG47.
CleanExi MM_SMC4.
Genevestigatori Q8CG47.

Family and domain databases

Gene3Di 3.40.50.300. 3 hits.
InterProi IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view ]
Pfami PF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF005719. SMC. 1 hit.
SMARTi SM00968. SMC_hinge. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 109 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

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