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Q96SB8

- SMC6_HUMAN

UniProt

Q96SB8 - SMC6_HUMAN

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Protein
Structural maintenance of chromosomes protein 6
Gene
SMC6, SMC6L1
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 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 – 838ATP Reviewed prediction

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
Complete GO annotation...

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.3 Publications

GO - Cellular componenti

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

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 6
PRO_0000270956Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei669 – 6691Phosphoserine1 Publication

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. 9 interactions.
MINTiMINT-2815361.
STRINGi9606.ENSP00000323439.

Structurei

3D structure databases

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

Family & Domainsi

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili226 – 451226 Reviewed prediction
Add
BLAST
Coiled coili660 – 914255 Reviewed prediction
Add
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.

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.

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.
VSP_022253

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti483 – 4831N → Y in BAB15236. 1 Publication
Sequence conflicti868 – 8681D → N in BAB15236. 1 Publication
Sequence conflicti1082 – 10821V → A in BAB15236. 1 Publication

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. 9 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

« 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] (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: July 9, 2014
This is version 98 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

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