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Protein

Structural maintenance of chromosomes protein 4

Gene

SMC4

Organism
Homo sapiens (Human)
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.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi113 – 120ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • kinetochore organization Source: Ensembl
  • meiotic chromosome condensation Source: Ensembl
  • meiotic chromosome segregation Source: Ensembl
  • mitotic chromosome condensation Source: UniProtKB
  • mitotic sister chromatid segregation 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-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-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
Short name:
hCAP-C
XCAP-C homolog
Gene namesi
Name:SMC4
Synonyms:CAPC, SMC4L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:14013. SMC4.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Chromosome 1 Publication

  • 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.

GO - Cellular componenti

  • condensin complex Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi10051.
OpenTargetsiENSG00000113810.
PharmGKBiPA37834.

Polymorphism and mutation databases

BioMutaiSMC4.
DMDMi30173386.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001190061 – 1288Structural maintenance of chromosomes protein 4Add BLAST1288

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22PhosphoserineCombined sources1
Modified residuei28PhosphoserineCombined sources1
Modified residuei39PhosphothreonineCombined sources1
Modified residuei41PhosphoserineCombined sources1
Modified residuei50PhosphoserineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Modified residuei381N6-acetyllysineBy similarity1
Modified residuei679N6-acetyllysineCombined sources1
Modified residuei982PhosphoserineCombined sources1
Modified residuei1056PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NTJ3.
MaxQBiQ9NTJ3.
PaxDbiQ9NTJ3.
PeptideAtlasiQ9NTJ3.
PRIDEiQ9NTJ3.

PTM databases

iPTMnetiQ9NTJ3.
PhosphoSitePlusiQ9NTJ3.

Expressioni

Tissue specificityi

Widely expressed. Higher expression in testis, colon, thymus.1 Publication

Gene expression databases

BgeeiENSG00000113810.
CleanExiHS_SMC4.
ExpressionAtlasiQ9NTJ3. baseline and differential.
GenevisibleiQ9NTJ3. HS.

Organism-specific databases

HPAiCAB055509.
HPA029449.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCAPHQ150032EBI-356173,EBI-1046410
SMC2O953473EBI-356173,EBI-355822

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115362. 56 interactors.
DIPiDIP-32946N.
IntActiQ9NTJ3. 34 interactors.
MINTiMINT-5005675.
STRINGi9606.ENSP00000341382.

Structurei

Secondary structure

11288
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi573 – 608Combined sources36
Beta strandi614 – 618Combined sources5
Helixi619 – 622Combined sources4
Helixi627 – 629Combined sources3
Helixi630 – 636Combined sources7
Helixi638 – 641Combined sources4
Beta strandi642 – 646Combined sources5
Helixi648 – 660Combined sources13
Beta strandi665 – 670Combined sources6
Helixi671 – 677Combined sources7
Helixi687 – 689Combined sources3
Helixi693 – 696Combined sources4
Helixi702 – 712Combined sources11
Beta strandi716 – 720Combined sources5
Helixi721 – 729Combined sources9
Beta strandi730 – 733Combined sources4
Beta strandi737 – 739Combined sources3
Beta strandi751 – 753Combined sources3
Beta strandi763 – 765Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4U4PX-ray1.89B566-809[»]
ProteinModelPortaliQ9NTJ3.
SMRiQ9NTJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni589 – 766Flexible hingeAdd BLAST178

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili272 – 588Sequence analysisAdd BLAST317
Coiled coili767 – 1020Sequence analysisAdd BLAST254
Coiled coili1109 – 1129Sequence analysisAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi18 – 23Poly-Pro6
Compositional biasi66 – 71Poly-Pro6
Compositional biasi1191 – 1226Ala/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.
InParanoidiQ9NTJ3.
KOiK06675.
OMAiENNMKSC.
OrthoDBiEOG091G01SY.
PhylomeDBiQ9NTJ3.
TreeFamiTF101158.

Family and domain databases

Gene3Di3.40.50.300. 4 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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NTJ3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPRKGTQPST ARRREEGPPP PSPDGASSDA EPEPPSGRTE SPATAAETAS
60 70 80 90 100
EELDNRSLEE ILNSIPPPPP PAMTNEAGAP RLMITHIVNQ NFKSYAGEKI
110 120 130 140 150
LGPFHKRFSC IIGPNGSGKS NVIDSMLFVF GYRAQKIRSK KLSVLIHNSD
160 170 180 190 200
EHKDIQSCTV EVHFQKIIDK EGDDYEVIPN SNFYVSRTAC RDNTSVYHIS
210 220 230 240 250
GKKKTFKDVG NLLRSHGIDL DHNRFLILQG EVEQIAMMKP KGQTEHDEGM
260 270 280 290 300
LEYLEDIIGC GRLNEPIKVL CRRVEILNEH RGEKLNRVKM VEKEKDALEG
310 320 330 340 350
EKNIAIEFLT LENEIFRKKN HVCQYYIYEL QKRIAEMETQ KEKIHEDTKE
360 370 380 390 400
INEKSNILSN EMKAKNKDVK DTEKKLNKIT KFIEENKEKF TQLDLEDVQV
410 420 430 440 450
REKLKHATSK AKKLEKQLQK DKEKVEEFKS IPAKSNNIIN ETTTRNNALE
460 470 480 490 500
KEKEKEEKKL KEVMDSLKQE TQGLQKEKES REKELMGFSK SVNEARSKMD
510 520 530 540 550
VAQSELDIYL SRHNTAVSQL TKAKEALIAA SETLKERKAA IRDIEGKLPQ
560 570 580 590 600
TEQELKEKEK ELQKLTQEET NFKSLVHDLF QKVEEAKSSL AMNRSRGKVL
610 620 630 640 650
DAIIQEKKSG RIPGIYGRLG DLGAIDEKYD VAISSCCHAL DYIVVDSIDI
660 670 680 690 700
AQECVNFLKR QNIGVATFIG LDKMAVWAKK MTEIQTPENT PRLFDLVKVK
710 720 730 740 750
DEKIRQAFYF ALRDTLVADN LDQATRVAYQ KDRRWRVVTL QGQIIEQSGT
760 770 780 790 800
MTGGGSKVMK GRMGSSLVIE ISEEEVNKME SQLQNDSKKA MQIQEQKVQL
810 820 830 840 850
EERVVKLRHS EREMRNTLEK FTASIQRLIE QEEYLNVQVK ELEANVLATA
860 870 880 890 900
PDKKKQKLLE ENVSAFKTEY DAVAEKAGKV EAEVKRLHNT IVEINNHKLK
910 920 930 940 950
AQQDKLDKIN KQLDECASAI TKAQVAIKTA DRNLQKAQDS VLRTEKEIKD
960 970 980 990 1000
TEKEVDDLTA ELKSLEDKAA EVVKNTNAAE ESLPEIQKEH RNLLQELKVI
1010 1020 1030 1040 1050
QENEHALQKD ALSIKLKLEQ IDGHIAEHNS KIKYWHKEIS KISLHPIEDN
1060 1070 1080 1090 1100
PIEEISVLSP EDLEAIKNPD SITNQIALLE ARCHEMKPNL GAIAEYKKKE
1110 1120 1130 1140 1150
ELYLQRVAEL DKITYERDSF RQAYEDLRKQ RLNEFMAGFY IITNKLKENY
1160 1170 1180 1190 1200
QMLTLGGDAE LELVDSLDPF SEGIMFSVRP PKKSWKKIFN LSGGEKTLSS
1210 1220 1230 1240 1250
LALVFALHHY KPTPLYFMDE IDAALDFKNV SIVAFYIYEQ TKNAQFIIIS
1260 1270 1280
LRNNMFEISD RLIGIYKTYN ITKSVAVNPK EIASKGLC
Length:1,288
Mass (Da):147,182
Last modified:April 23, 2003 - v2
Checksum:i9D164D6EB0602464
GO
Isoform 2 (identifier: Q9NTJ3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     980-1037: Missing.

Note: No experimental confirmation available.
Show »
Length:1,230
Mass (Da):140,278
Checksum:iDBFFD68DB1C10454
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti272R → Q in AAC72361 (PubMed:9789013).Curated1
Sequence conflicti283E → D in CAB66811 (PubMed:11230166).Curated1
Sequence conflicti392 – 393QL → HV in AAC72361 (PubMed:9789013).Curated2
Sequence conflicti594R → S in AAC72361 (PubMed:9789013).Curated1
Sequence conflicti645V → G in CAD38803 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052439181S → R.Corresponds to variant rs35214835dbSNPEnsembl.1
Natural variantiVAR_052440356N → S.Corresponds to variant rs33999879dbSNPEnsembl.1
Natural variantiVAR_059843415E → D.Corresponds to variant rs2164675dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_007245980 – 1037Missing in isoform 2. 1 PublicationAdd BLAST58

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019987 mRNA. Translation: BAA73535.1.
AL136877 mRNA. Translation: CAB66811.1.
AL833949 mRNA. Translation: CAD38803.1.
AC024221 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78639.1.
CH471052 Genomic DNA. Translation: EAW78640.1.
AF092564 mRNA. Translation: AAC72361.1.
CCDSiCCDS3189.1. [Q9NTJ3-1]
PIRiT46486.
RefSeqiNP_001002800.1. NM_001002800.2. [Q9NTJ3-1]
NP_001275682.1. NM_001288753.1.
NP_005487.3. NM_005496.3. [Q9NTJ3-1]
XP_011510613.1. XM_011512311.2. [Q9NTJ3-1]
UniGeneiHs.58992.

Genome annotation databases

EnsembliENST00000344722; ENSP00000341382; ENSG00000113810. [Q9NTJ3-1]
ENST00000357388; ENSP00000349961; ENSG00000113810. [Q9NTJ3-1]
ENST00000462787; ENSP00000420734; ENSG00000113810. [Q9NTJ3-2]
GeneIDi10051.
KEGGihsa:10051.
UCSCiuc003fdh.5. human. [Q9NTJ3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019987 mRNA. Translation: BAA73535.1.
AL136877 mRNA. Translation: CAB66811.1.
AL833949 mRNA. Translation: CAD38803.1.
AC024221 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78639.1.
CH471052 Genomic DNA. Translation: EAW78640.1.
AF092564 mRNA. Translation: AAC72361.1.
CCDSiCCDS3189.1. [Q9NTJ3-1]
PIRiT46486.
RefSeqiNP_001002800.1. NM_001002800.2. [Q9NTJ3-1]
NP_001275682.1. NM_001288753.1.
NP_005487.3. NM_005496.3. [Q9NTJ3-1]
XP_011510613.1. XM_011512311.2. [Q9NTJ3-1]
UniGeneiHs.58992.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4U4PX-ray1.89B566-809[»]
ProteinModelPortaliQ9NTJ3.
SMRiQ9NTJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115362. 56 interactors.
DIPiDIP-32946N.
IntActiQ9NTJ3. 34 interactors.
MINTiMINT-5005675.
STRINGi9606.ENSP00000341382.

PTM databases

iPTMnetiQ9NTJ3.
PhosphoSitePlusiQ9NTJ3.

Polymorphism and mutation databases

BioMutaiSMC4.
DMDMi30173386.

Proteomic databases

EPDiQ9NTJ3.
MaxQBiQ9NTJ3.
PaxDbiQ9NTJ3.
PeptideAtlasiQ9NTJ3.
PRIDEiQ9NTJ3.

Protocols and materials databases

DNASUi10051.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344722; ENSP00000341382; ENSG00000113810. [Q9NTJ3-1]
ENST00000357388; ENSP00000349961; ENSG00000113810. [Q9NTJ3-1]
ENST00000462787; ENSP00000420734; ENSG00000113810. [Q9NTJ3-2]
GeneIDi10051.
KEGGihsa:10051.
UCSCiuc003fdh.5. human. [Q9NTJ3-1]

Organism-specific databases

CTDi10051.
DisGeNETi10051.
GeneCardsiSMC4.
HGNCiHGNC:14013. SMC4.
HPAiCAB055509.
HPA029449.
MIMi605575. gene.
neXtProtiNX_Q9NTJ3.
OpenTargetsiENSG00000113810.
PharmGKBiPA37834.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0996. Eukaryota.
COG1196. LUCA.
GeneTreeiENSGT00580000081617.
HOGENOMiHOG000184777.
HOVERGENiHBG106696.
InParanoidiQ9NTJ3.
KOiK06675.
OMAiENNMKSC.
OrthoDBiEOG091G01SY.
PhylomeDBiQ9NTJ3.
TreeFamiTF101158.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikiiSMC4.
GenomeRNAii10051.
PROiQ9NTJ3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113810.
CleanExiHS_SMC4.
ExpressionAtlasiQ9NTJ3. baseline and differential.
GenevisibleiQ9NTJ3. HS.

Family and domain databases

Gene3Di3.40.50.300. 4 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_HUMAN
AccessioniPrimary (citable) accession number: Q9NTJ3
Secondary accession number(s): A6NLT9
, D3DNL8, O95752, Q8NDL4, Q9UNT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: November 30, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.