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Q8IY18

- SMC5_HUMAN

UniProt

Q8IY18 - SMC5_HUMAN

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Protein

Structural maintenance of chromosomes protein 5

Gene

SMC5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 SMC6.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi80 – 878ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular senescence Source: UniProtKB
  2. double-strand break repair via homologous recombination Source: UniProtKB
  3. mitotic nuclear division Source: UniProtKB-KW
  4. positive regulation of maintenance of mitotic sister chromatid cohesion Source: UniProtKB
  5. positive regulation of mitotic metaphase/anaphase transition Source: UniProtKB
  6. telomere maintenance via recombination Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 5
Short name:
SMC protein 5
Short name:
SMC-5
Short name:
hSMC5
Gene namesi
Name:SMC5
Synonyms:KIAA0594, SMC5L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:20465. SMC5.

Subcellular locationi

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

GO - Cellular componenti

  1. cell junction Source: HPA
  2. chromosome, telomeric region Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. PML body Source: UniProtKB
  5. Smc5-Smc6 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134993662.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11011101Structural maintenance of chromosomes protein 5PRO_0000270951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351Phosphoserine2 Publications

Post-translational modificationi

Sumoylated.1 Publication
Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8IY18.
PaxDbiQ8IY18.
PRIDEiQ8IY18.

PTM databases

PhosphoSiteiQ8IY18.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ8IY18.
CleanExiHS_SMC5.
GenevestigatoriQ8IY18.

Organism-specific databases

HPAiHPA054900.

Interactioni

Subunit structurei

Forms a heterodimer with SMC6. Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NDNL2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SMC6Q96SB83EBI-605405,EBI-605415

Protein-protein interaction databases

BioGridi116754. 16 interactions.
IntActiQ8IY18. 6 interactions.
STRINGi9606.ENSP00000354957.

Structurei

3D structure databases

ProteinModelPortaliQ8IY18.
SMRiQ8IY18. Positions 56-264, 903-1053.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni446 – 646201Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili207 – 445239Sequence AnalysisAdd
BLAST
Coiled coili647 – 828182Sequence AnalysisAdd
BLAST
Coiled coili888 – 92740Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi991 – 102636Ala/Asp-rich (DA-box)Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the SMC family. SMC5 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1196.
GeneTreeiENSGT00550000074963.
HOGENOMiHOG000154342.
HOVERGENiHBG093963.
InParanoidiQ8IY18.
OMAiNLNMVIG.
OrthoDBiEOG72JWFH.
PhylomeDBiQ8IY18.
TreeFamiTF105708.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR027131. SMC5.
[Graphical view]
PANTHERiPTHR19306:SF1. PTHR19306:SF1. 1 hit.
PfamiPF02463. SMC_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Q8IY18 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATPSKKTST PSPQPSKRAL PRDPSSEVPS KRKNSAPQLP LLQSSGPFVE
60 70 80 90 100
GSIVRISMEN FLTYDICEVS PGPHLNMIVG ANGTGKSSIV CAICLGLAGK
110 120 130 140 150
PAFMGRADKV GFFVKRGCSR GMVEIELFRA SGNLVITREI DVAKNQSFWF
160 170 180 190 200
INKKSTTQKI VEEKVAALNI QVGNLCQFLP QDKVGEFAKL SKIELLEATE
210 220 230 240 250
KSIGPPEMHK YHCELKNLRE KEKQLETSCK EKTEYLQKMV QRNERYKQDV
260 270 280 290 300
ERFYERKRHL DLIEMLEAKR PWVEYENVRQ EYEEVKLVRD RVKEEVRKLK
310 320 330 340 350
EGQIPVTCRI EEMENERHNL EARIKEKATD IKEASQKCKQ KQDVIERKDK
360 370 380 390 400
HIEELQQALI VKQNEELDRQ RRIGNTRKMI EDLQNELKTT ENCENLQPQI
410 420 430 440 450
DAITNDLRRI QDEKALCEGE IIDKRRERET LEKEKKSVDD HIVRFDNLMN
460 470 480 490 500
QKEDKLRQRF RDTYDAVLWL RNNRDKFKQR VCEPIMLTIN MKDNKNAKYI
510 520 530 540 550
ENHIPSNDLR AFVFESQEDM EVFLKEVRDN KKLRVNAVIA PKSSYADKAP
560 570 580 590 600
SRSLNELKQY GFFSYLRELF DAPDPVMSYL CCQYHIHEVP VGTEKTRERI
610 620 630 640 650
ERVIQETRLK QIYTAEEKYV VKTSFYSNKV ISSNTSLKVA QFLTVTVDLE
660 670 680 690 700
QRRHLEEQLK EIHRKLQAVD SGLIALRETS KHLEHKDNEL RQKKKELLER
710 720 730 740 750
KTKKRQLEQK ISSKLGSLKL MEQDTCNLEE EERKASTKIK EINVQKAKLV
760 770 780 790 800
TELTNLIKIC TSLHIQKVDL ILQNTTVISE KNKLESDYMA ASSQLRLTEQ
810 820 830 840 850
HFIELDENRQ RLLQKCKELM KRARQVCNLG AEQTLPQEYQ TQVPTIPNGH
860 870 880 890 900
NSSLPMVFQD LPNTLDEIDA LLTEERSRAS CFTGLNPTIV QEYTKREEEI
910 920 930 940 950
EQLTEELKGK KVELDQYREN ISQVKERWLN PLKELVEKIN EKFSNFFSSM
960 970 980 990 1000
QCAGEVDLHT ENEEDYDKYG IRIRVKFRSS TQLHELTPHH QSGGERSVST
1010 1020 1030 1040 1050
MLYLMALQEL NRCPFRVVDE INQGMDPINE RRVFEMVVNT ACKENTSQYF
1060 1070 1080 1090 1100
FITPKLLQNL PYSEKMTVLF VYNGPHMLEP NTWNLKAFQR RRRRITFTQP

S
Length:1,101
Mass (Da):128,806
Last modified:January 9, 2007 - v2
Checksum:i54393D50688A914A
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti306 – 3061V → I.3 Publications
Corresponds to variant rs1180116 [ dbSNP | Ensembl ].
VAR_029824
Natural varianti308 – 3081C → R.2 Publications
Corresponds to variant rs1180117 [ dbSNP | Ensembl ].
VAR_029825
Natural varianti682 – 6821H → R.
Corresponds to variant rs11142365 [ dbSNP | Ensembl ].
VAR_061869

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6632.1.
RefSeqiNP_055925.2. NM_015110.3.
UniGeneiHs.534189.
Hs.601181.

Genome annotation databases

EnsembliENST00000361138; ENSP00000354957; ENSG00000198887.
GeneIDi23137.
KEGGihsa:23137.
UCSCiuc004ahr.2. human.

Polymorphism databases

DMDMi122070387.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6632.1.
RefSeqi NP_055925.2. NM_015110.3.
UniGenei Hs.534189.
Hs.601181.

3D structure databases

ProteinModelPortali Q8IY18.
SMRi Q8IY18. Positions 56-264, 903-1053.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116754. 16 interactions.
IntActi Q8IY18. 6 interactions.
STRINGi 9606.ENSP00000354957.

PTM databases

PhosphoSitei Q8IY18.

Polymorphism databases

DMDMi 122070387.

Proteomic databases

MaxQBi Q8IY18.
PaxDbi Q8IY18.
PRIDEi Q8IY18.

Protocols and materials databases

DNASUi 23137.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361138 ; ENSP00000354957 ; ENSG00000198887 .
GeneIDi 23137.
KEGGi hsa:23137.
UCSCi uc004ahr.2. human.

Organism-specific databases

CTDi 23137.
GeneCardsi GC09P072873.
H-InvDB HIX0201342.
HGNCi HGNC:20465. SMC5.
HPAi HPA054900.
MIMi 609386. gene.
neXtProti NX_Q8IY18.
PharmGKBi PA134993662.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1196.
GeneTreei ENSGT00550000074963.
HOGENOMi HOG000154342.
HOVERGENi HBG093963.
InParanoidi Q8IY18.
OMAi NLNMVIG.
OrthoDBi EOG72JWFH.
PhylomeDBi Q8IY18.
TreeFami TF105708.

Miscellaneous databases

ChiTaRSi SMC5. human.
GeneWikii SMC5.
GenomeRNAii 23137.
NextBioi 44403.
PROi Q8IY18.
SOURCEi Search...

Gene expression databases

Bgeei Q8IY18.
CleanExi HS_SMC5.
Genevestigatori Q8IY18.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR027131. SMC5.
[Graphical view ]
PANTHERi PTHR19306:SF1. PTHR19306:SF1. 1 hit.
Pfami PF02463. SMC_N. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSMC5_HUMAN
AccessioniPrimary (citable) accession number: Q8IY18
Secondary accession number(s): A6NM81
, O60335, Q05D92, Q5VZ60, Q96SB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: October 29, 2014
This is version 95 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3