Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8IY18 (SMC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural maintenance of chromosomes protein 5

Short name=SMC protein 5
Short name=SMC-5
Short name=hSMC5
Gene names
Name:SMC5
Synonyms:KIAA0594, SMC5L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1101 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. Ref.7 Ref.8 Ref.11

Subunit structure

Forms a heterodimer with SMC6. Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NDNL2. Ref.9

Subcellular location

Nucleus. Chromosome. Chromosometelomere. Note: Associates with chromatin. Localizes to PML nuclear bodies in ALT cell lines. Ref.1 Ref.8 Ref.9

Tissue specificity

Widely expressed. Ref.1

Domain

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC6, forming a V-shaped heterodimer By similarity.

Post-translational modification

Sumoylated. Ref.9

Ubiquitinated. Ref.9

Sequence similarities

Belongs to the SMC family. SMC5 subfamily.

Sequence caution

The sequence AAH17666.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA recombination
DNA repair
Mitosis
   Cellular componentChromosome
Nucleus
Telomere
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular senescence

Inferred from mutant phenotype Ref.8. Source: UniProtKB

double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.7. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of maintenance of mitotic sister chromatid cohesion

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of mitotic metaphase/anaphase transition

Inferred from mutant phenotype Ref.11. Source: UniProtKB

telomere maintenance via recombination

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentPML body

Inferred from direct assay Ref.8. Source: UniProtKB

Smc5-Smc6 complex

Inferred from direct assay Ref.9. Source: UniProtKB

cell junction

Inferred from direct assay. Source: HPA

chromosome, telomeric region

Inferred from direct assay Ref.8. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 15601840Ref.9. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SMC6Q96SB83EBI-605405,EBI-605415

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11011101Structural maintenance of chromosomes protein 5
PRO_0000270951

Regions

Nucleotide binding80 – 878ATP Potential
Region446 – 646201Flexible hinge
Coiled coil207 – 445239 Potential
Coiled coil647 – 828182 Potential
Coiled coil888 – 92740 Potential
Compositional bias991 – 102636Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue351Phosphoserine Ref.10 Ref.12

Natural variations

Natural variant3061V → I. Ref.1 Ref.2 Ref.5
Corresponds to variant rs1180116 [ dbSNP | Ensembl ].
VAR_029824
Natural variant3081C → R. Ref.1 Ref.5
Corresponds to variant rs1180117 [ dbSNP | Ensembl ].
VAR_029825
Natural variant6821H → R.
Corresponds to variant rs11142365 [ dbSNP | Ensembl ].
VAR_061869

Sequences

Sequence LengthMass (Da)Tools
Q8IY18 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: 54393D50688A914A

FASTA1,101128,806
        10         20         30         40         50         60 
MATPSKKTST PSPQPSKRAL PRDPSSEVPS KRKNSAPQLP LLQSSGPFVE GSIVRISMEN 

        70         80         90        100        110        120 
FLTYDICEVS PGPHLNMIVG ANGTGKSSIV CAICLGLAGK PAFMGRADKV GFFVKRGCSR 

       130        140        150        160        170        180 
GMVEIELFRA SGNLVITREI DVAKNQSFWF INKKSTTQKI VEEKVAALNI QVGNLCQFLP 

       190        200        210        220        230        240 
QDKVGEFAKL SKIELLEATE KSIGPPEMHK YHCELKNLRE KEKQLETSCK EKTEYLQKMV 

       250        260        270        280        290        300 
QRNERYKQDV ERFYERKRHL DLIEMLEAKR PWVEYENVRQ EYEEVKLVRD RVKEEVRKLK 

       310        320        330        340        350        360 
EGQIPVTCRI EEMENERHNL EARIKEKATD IKEASQKCKQ KQDVIERKDK HIEELQQALI 

       370        380        390        400        410        420 
VKQNEELDRQ RRIGNTRKMI EDLQNELKTT ENCENLQPQI DAITNDLRRI QDEKALCEGE 

       430        440        450        460        470        480 
IIDKRRERET LEKEKKSVDD HIVRFDNLMN QKEDKLRQRF RDTYDAVLWL RNNRDKFKQR 

       490        500        510        520        530        540 
VCEPIMLTIN MKDNKNAKYI ENHIPSNDLR AFVFESQEDM EVFLKEVRDN KKLRVNAVIA 

       550        560        570        580        590        600 
PKSSYADKAP SRSLNELKQY GFFSYLRELF DAPDPVMSYL CCQYHIHEVP VGTEKTRERI 

       610        620        630        640        650        660 
ERVIQETRLK QIYTAEEKYV VKTSFYSNKV ISSNTSLKVA QFLTVTVDLE QRRHLEEQLK 

       670        680        690        700        710        720 
EIHRKLQAVD SGLIALRETS KHLEHKDNEL RQKKKELLER KTKKRQLEQK ISSKLGSLKL 

       730        740        750        760        770        780 
MEQDTCNLEE EERKASTKIK EINVQKAKLV TELTNLIKIC TSLHIQKVDL ILQNTTVISE 

       790        800        810        820        830        840 
KNKLESDYMA ASSQLRLTEQ HFIELDENRQ RLLQKCKELM KRARQVCNLG AEQTLPQEYQ 

       850        860        870        880        890        900 
TQVPTIPNGH NSSLPMVFQD LPNTLDEIDA LLTEERSRAS CFTGLNPTIV QEYTKREEEI 

       910        920        930        940        950        960 
EQLTEELKGK KVELDQYREN ISQVKERWLN PLKELVEKIN EKFSNFFSSM QCAGEVDLHT 

       970        980        990       1000       1010       1020 
ENEEDYDKYG IRIRVKFRSS TQLHELTPHH QSGGERSVST MLYLMALQEL NRCPFRVVDE 

      1030       1040       1050       1060       1070       1080 
INQGMDPINE RRVFEMVVNT ACKENTSQYF FITPKLLQNL PYSEKMTVLF VYNGPHMLEP 

      1090       1100 
NTWNLKAFQR RRRRITFTQP S 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a novel human SMC heterodimer homologous to the Schizosaccharomyces pombe Rad18/Spr18 complex."
Taylor E.M., Moghraby J.S., Lees J.H., Smit B., Moens P.B., Lehmann A.R.
Mol. Biol. Cell 12:1583-1594(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SMC6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS ILE-306 AND ARG-308.
[2]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-306.
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANTS ILE-306 AND ARG-308.
Tissue: Mammary gland and Uterus.
[6]"Human MMS21/NSE2 is a SUMO ligase required for DNA repair."
Potts P.R., Yu H.
Mol. Cell. Biol. 25:7021-7032(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NSMCE2.
[7]"Human SMC5/6 complex promotes sister chromatid homologous recombination by recruiting the SMC1/3 cohesin complex to double-strand breaks."
Potts P.R., Porteus M.H., Yu H.
EMBO J. 25:3377-3388(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins."
Potts P.R., Yu H.
Nat. Struct. Mol. Biol. 14:581-590(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Identification of the proteins, including MAGEG1, that make up the human SMC5-6 protein complex."
Taylor E.M., Copsey A.C., Hudson J.J., Vidot S., Lehmann A.R.
Mol. Cell. Biol. 28:1197-1206(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUMOYLATION, UBIQUITINATION, IDENTIFICATION IN THE SMC5-SMC6 COMPLEX.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"SMC5 and MMS21 are required for chromosome cohesion and mitotic progression."
Behlke-Steinert S., Touat-Todeschini L., Skoufias D.A., Margolis R.L.
Cell Cycle 8:2211-2218(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ310550 mRNA. Translation: CAC39247.1.
AB011166 mRNA. Translation: BAA25520.2.
AL162390 Genomic DNA. Translation: CAH73243.1.
BC017666 mRNA. Translation: AAH17666.1. Sequence problems.
BC038225 mRNA. Translation: AAH38225.1.
CCDSCCDS6632.1.
RefSeqNP_055925.2. NM_015110.3.
UniGeneHs.534189.
Hs.601181.

3D structure databases

ProteinModelPortalQ8IY18.
SMRQ8IY18. Positions 56-264, 903-1053.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116754. 12 interactions.
IntActQ8IY18. 6 interactions.
STRING9606.ENSP00000354957.

PTM databases

PhosphoSiteQ8IY18.

Polymorphism databases

DMDM122070387.

Proteomic databases

MaxQBQ8IY18.
PaxDbQ8IY18.
PRIDEQ8IY18.

Protocols and materials databases

DNASU23137.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361138; ENSP00000354957; ENSG00000198887.
GeneID23137.
KEGGhsa:23137.
UCSCuc004ahr.2. human.

Organism-specific databases

CTD23137.
GeneCardsGC09P072873.
H-InvDBHIX0201342.
HGNCHGNC:20465. SMC5.
HPAHPA054900.
MIM609386. gene.
neXtProtNX_Q8IY18.
PharmGKBPA134993662.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1196.
HOGENOMHOG000154342.
HOVERGENHBG093963.
InParanoidQ8IY18.
OMANLNMVIG.
OrthoDBEOG72JWFH.
PhylomeDBQ8IY18.
TreeFamTF105708.

Gene expression databases

BgeeQ8IY18.
CleanExHS_SMC5.
GenevestigatorQ8IY18.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR027131. SMC5.
[Graphical view]
PANTHERPTHR19306:SF1. PTHR19306:SF1. 1 hit.
PfamPF02463. SMC_N. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSSMC5. human.
GeneWikiSMC5.
GenomeRNAi23137.
NextBio44403.
PROQ8IY18.
SOURCESearch...

Entry information

Entry nameSMC5_HUMAN
AccessionPrimary (citable) accession number: Q8IY18
Secondary accession number(s): A6NM81 expand/collapse secondary AC list , O60335, Q05D92, Q5VZ60, Q96SB9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM