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Q96SB8

- SMC6_HUMAN

UniProt

Q96SB8 - SMC6_HUMAN

Protein

Structural maintenance of chromosomes protein 6

Gene

SMC6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    Core component of the SMC5-SMC6 complex, a complex involved in 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.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi76 – 838ATPSequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular senescence Source: UniProtKB
    2. double-strand break repair via homologous recombination Source: InterPro
    3. telomere maintenance via recombination Source: UniProtKB

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Structural maintenance of chromosomes protein 6
    Short name:
    SMC protein 6
    Short name:
    SMC-6
    Short name:
    hSMC6
    Gene namesi
    Name:SMC6
    Synonyms:SMC6L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:20466. SMC6.

    Subcellular locationi

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

    GO - Cellular componenti

    1. chromosome, telomeric region Source: UniProtKB
    2. intracellular Source: LIFEdb
    3. nucleolus Source: HPA
    4. nucleus Source: HPA
    5. PML body Source: UniProtKB
    6. Smc5-Smc6 complex Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134892702.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10911091Structural maintenance of chromosomes protein 6PRO_0000270956Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei669 – 6691Phosphoserine2 Publications

    Post-translational modificationi

    Sumoylated by NSMCE2/MMS21.2 Publications
    Ubiquitinated.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96SB8.
    PaxDbiQ96SB8.
    PRIDEiQ96SB8.

    PTM databases

    PhosphoSiteiQ96SB8.

    Expressioni

    Tissue specificityi

    Widely expressed. Overexpressed in testis.1 Publication

    Gene expression databases

    ArrayExpressiQ96SB8.
    BgeeiQ96SB8.
    CleanExiHS_SMC6.
    GenevestigatoriQ96SB8.

    Organism-specific databases

    HPAiCAB037186.
    HPA042733.

    Interactioni

    Subunit structurei

    Forms a heterodimer with SMC5. 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
    NSMCE1Q8WV227EBI-605415,EBI-2557372
    NSMCE2Q96MF72EBI-605415,EBI-2557388
    SMC5Q8IY183EBI-605415,EBI-605405

    Protein-protein interaction databases

    BioGridi122802. 12 interactions.
    DIPiDIP-34562N.
    IntActiQ96SB8. 10 interactions.
    MINTiMINT-2815361.
    STRINGi9606.ENSP00000323439.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96SB8.
    SMRiQ96SB8. Positions 59-90, 985-1036.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni452 – 659208Flexible hingeAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili226 – 451226Sequence AnalysisAdd
    BLAST
    Coiled coili660 – 914255Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi987 – 102236Ala/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 SMC5, forming a V-shaped heterodimer.By similarity

    Sequence similaritiesi

    Belongs to the SMC family. SMC6 subfamily.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1196.
    HOGENOMiHOG000286038.
    HOVERGENiHBG093964.
    InParanoidiQ96SB8.
    OMAiNPMTILT.
    OrthoDBiEOG747PJ0.
    PhylomeDBiQ96SB8.
    TreeFamiTF314520.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR027132. SMC6.
    [Graphical view]
    PANTHERiPTHR19306:SF2. PTHR19306:SF2. 1 hit.
    PfamiPF02463. SMC_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96SB8-1) [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

    MAKRKEENFS SPKNAKRPRQ EELEDFDKDG DEDECKGTTL TAAEVGIIES     50
    IHLKNFMCHS MLGPFKFGSN VNFVVGNNGS GKSAVLTALI VGLGGRAVAT 100
    NRGSSLKGFV KDGQNSADIS ITLRNRGDDA FKASVYGNSI LIQQHISIDG 150
    SRSYKLKSAT GSVVSTRKEE LIAILDHFNI QVDNPVSVLT QEMSKQFLQS 200
    KNEGDKYKFF MKATQLEQMK EDYSYIMETK ERTKEQIHQG EERLTELKRQ 250
    CVEKEERFQS IAGLSTMKTN LESLKHEMAW AVVNEIEKQL NAIRDNIKIG 300
    EDRAARLDRK MEEQQVRLNE AEQKYKDIQD KLEKISEETN ARAPECMALK 350
    ADVVAKKRAY NEAEVLYNRS LNEYKALKKD DEQLCKRIEE LKKSTDQSLE 400
    PERLERQKKI SWLKERVKAF QNQENSVNQE IEQFQQAIEK DKEEHGKIKR 450
    EELDVKHALS YNQRQLKELK DSKTDRLKRF GPNVPALLEA IDDAYRQGHF 500
    TYKPVGPLGA CIHLRDPELA LAIESCLKGL LQAYCCHNHA DERVLQALMK 550
    RFYLPGTSRP PIIVSEFRNE IYDVRHRAAY HPDFPTVLTA LEIDNAVVAN 600
    SLIDMRGIET VLLIKNNSVA RAVMQSQKPP KNCREAFTAD GDQVFAGRYY 650
    SSENTRPKFL SRDVDSEISD LENEVENKTA QILNLQQHLS ALEKDIKHNE 700
    ELLKRCQLHY KELKMKIRKN ISEIRELENI EEHQSVDIAT LEDEAQENKS 750
    KMKMVEEHME QQKENMEHLK SLKIEAENKY DAIKFKINQL SELADPLKDE 800
    LNLADSEVDN QKRGKRHYEE KQKEHLDTLN KKKRELDMKE KELEEKMSQA 850
    RQICPERIEV EKSASILDKE INRLRQKIQA EHASHGDREE IMRQYQEARE 900
    TYLDLDSKVR TLKKFIKLLG EIMEHRFKTY QQFRRCLTLR CKLYFDNLLS 950
    QRAYCGKMNF DHKNETLSIS VQPGEGNKAA FNDMRALSGG ERSFSTVCFI 1000
    LSLWSIAESP FRCLDEFDVY MDMVNRRIAM DLILKMADSQ RFRQFILLTP 1050
    QSMSSLPSSK LIRILRMSDP ERGQTTLPFR PVTQEEDDDQ R 1091
    Length:1,091
    Mass (Da):126,326
    Last modified:January 9, 2007 - v2
    Checksum:i03C6F478E34285E6
    GO
    Isoform 2 (identifier: Q96SB8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         80-80: S → SWSAVVRSRLNATSASQVQAILLFQPC

    Note: No experimental confirmation available.

    Show »
    Length:1,117
    Mass (Da):129,154
    Checksum:i3CB9F8CA48BC0ECE
    GO

    Sequence cautioni

    The sequence AAH32675.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAB15236.1 differs from that shown. Reason: Frameshift at position 718.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti483 – 4831N → Y in BAB15236. (PubMed:14702039)Curated
    Sequence conflicti868 – 8681D → N in BAB15236. (PubMed:14702039)Curated
    Sequence conflicti1082 – 10821V → A in BAB15236. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti292 – 2921A → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035875
    Natural varianti464 – 4641R → G.2 Publications
    Corresponds to variant rs35195207 [ dbSNP | Ensembl ].
    VAR_052441
    Natural varianti691 – 6911A → T.3 Publications
    Corresponds to variant rs1065381 [ dbSNP | Ensembl ].
    VAR_029826
    Natural varianti928 – 9281K → Q.
    Corresponds to variant rs35257753 [ dbSNP | Ensembl ].
    VAR_052442
    Natural varianti1046 – 10461I → M.
    Corresponds to variant rs10221907 [ dbSNP | Ensembl ].
    VAR_029827

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei80 – 801S → SWSAVVRSRLNATSASQVQA ILLFQPC in isoform 2. 1 PublicationVSP_022253

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ310551 mRNA. Translation: CAC39248.1.
    AL136544 mRNA. Translation: CAB66479.1.
    AK025769 mRNA. Translation: BAB15236.1. Frameshift.
    AK292421 mRNA. Translation: BAF85110.1.
    AL832979 mRNA. Translation: CAH56327.1.
    AC097377 Genomic DNA. Translation: AAX88851.1.
    CH471053 Genomic DNA. Translation: EAX00866.1.
    CH471053 Genomic DNA. Translation: EAX00867.1.
    CH471053 Genomic DNA. Translation: EAX00868.1.
    BC032675 mRNA. Translation: AAH32675.1. Sequence problems.
    BC039828 mRNA. Translation: AAH39828.1.
    CCDSiCCDS1690.1. [Q96SB8-1]
    RefSeqiNP_001135758.1. NM_001142286.1. [Q96SB8-1]
    NP_078900.1. NM_024624.5. [Q96SB8-1]
    UniGeneiHs.526728.

    Genome annotation databases

    EnsembliENST00000351948; ENSP00000323439; ENSG00000163029. [Q96SB8-1]
    ENST00000381272; ENSP00000370672; ENSG00000163029. [Q96SB8-2]
    ENST00000402989; ENSP00000384539; ENSG00000163029. [Q96SB8-1]
    ENST00000448223; ENSP00000404092; ENSG00000163029. [Q96SB8-1]
    GeneIDi79677.
    KEGGihsa:79677.
    UCSCiuc002rcn.3. human. [Q96SB8-1]
    uc002rcp.1. human. [Q96SB8-2]

    Polymorphism databases

    DMDMi122070455.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ310551 mRNA. Translation: CAC39248.1 .
    AL136544 mRNA. Translation: CAB66479.1 .
    AK025769 mRNA. Translation: BAB15236.1 . Frameshift.
    AK292421 mRNA. Translation: BAF85110.1 .
    AL832979 mRNA. Translation: CAH56327.1 .
    AC097377 Genomic DNA. Translation: AAX88851.1 .
    CH471053 Genomic DNA. Translation: EAX00866.1 .
    CH471053 Genomic DNA. Translation: EAX00867.1 .
    CH471053 Genomic DNA. Translation: EAX00868.1 .
    BC032675 mRNA. Translation: AAH32675.1 . Sequence problems.
    BC039828 mRNA. Translation: AAH39828.1 .
    CCDSi CCDS1690.1. [Q96SB8-1 ]
    RefSeqi NP_001135758.1. NM_001142286.1. [Q96SB8-1 ]
    NP_078900.1. NM_024624.5. [Q96SB8-1 ]
    UniGenei Hs.526728.

    3D structure databases

    ProteinModelPortali Q96SB8.
    SMRi Q96SB8. Positions 59-90, 985-1036.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122802. 12 interactions.
    DIPi DIP-34562N.
    IntActi Q96SB8. 10 interactions.
    MINTi MINT-2815361.
    STRINGi 9606.ENSP00000323439.

    PTM databases

    PhosphoSitei Q96SB8.

    Polymorphism databases

    DMDMi 122070455.

    Proteomic databases

    MaxQBi Q96SB8.
    PaxDbi Q96SB8.
    PRIDEi Q96SB8.

    Protocols and materials databases

    DNASUi 79677.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351948 ; ENSP00000323439 ; ENSG00000163029 . [Q96SB8-1 ]
    ENST00000381272 ; ENSP00000370672 ; ENSG00000163029 . [Q96SB8-2 ]
    ENST00000402989 ; ENSP00000384539 ; ENSG00000163029 . [Q96SB8-1 ]
    ENST00000448223 ; ENSP00000404092 ; ENSG00000163029 . [Q96SB8-1 ]
    GeneIDi 79677.
    KEGGi hsa:79677.
    UCSCi uc002rcn.3. human. [Q96SB8-1 ]
    uc002rcp.1. human. [Q96SB8-2 ]

    Organism-specific databases

    CTDi 79677.
    GeneCardsi GC02M017845.
    HGNCi HGNC:20466. SMC6.
    HPAi CAB037186.
    HPA042733.
    MIMi 609387. gene.
    neXtProti NX_Q96SB8.
    PharmGKBi PA134892702.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1196.
    HOGENOMi HOG000286038.
    HOVERGENi HBG093964.
    InParanoidi Q96SB8.
    OMAi NPMTILT.
    OrthoDBi EOG747PJ0.
    PhylomeDBi Q96SB8.
    TreeFami TF314520.

    Miscellaneous databases

    ChiTaRSi SMC6. human.
    GeneWikii SMC6.
    GenomeRNAii 79677.
    NextBioi 68922.
    PROi Q96SB8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96SB8.
    Bgeei Q96SB8.
    CleanExi HS_SMC6.
    Genevestigatori Q96SB8.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR027132. SMC6.
    [Graphical view ]
    PANTHERi PTHR19306:SF2. PTHR19306:SF2. 1 hit.
    Pfami PF02463. SMC_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1), INTERACTION WITH SMC5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, VARIANTS GLY-464 AND THR-691.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Amygdala.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 467-1091, VARIANT THR-691.
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Stomach.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-717 (ISOFORM 2), VARIANTS GLY-464 AND THR-691.
      Tissue: Ovary.
    8. "Coordination of DNA damage responses via the Smc5/Smc6 complex."
      Harvey S.H., Sheedy D.M., Cuddihy A.R., O'Connell M.J.
      Mol. Cell. Biol. 24:662-674(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NSMCE1.
    9. "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, SUMOYLATION.
    10. "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.
    11. "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.
    12. "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, INTERACTION WITH NSMCE1; NSMCE2; EID3; NSMCE4A AND NDNL2, IDENTIFICATION IN THE SMC5-SMC6 COMPLEX, SUMOYLATION, UBIQUITINATION.
    13. "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-669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-292.

    Entry informationi

    Entry nameiSMC6_HUMAN
    AccessioniPrimary (citable) accession number: Q96SB8
    Secondary accession number(s): A8K8Q6
    , D6W518, Q05BV4, Q9H0X3, Q9H6M0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 99 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 2
      Human chromosome 2: 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