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Q6UVJ0

- SAS6_HUMAN

UniProt

Q6UVJ0 - SAS6_HUMAN

Protein

Spindle assembly abnormal protein 6 homolog

Gene

SASS6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication: required both for mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. Overexpression results in excess foci-bearing centriolar markers.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. centriole replication Source: UniProtKB
    2. centrosome duplication Source: UniProtKB

    Keywords - Biological processi

    Cell cycle

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spindle assembly abnormal protein 6 homolog
    Short name:
    HsSAS-6
    Gene namesi
    Name:SASS6
    Synonyms:SAS6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25403. SASS6.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole
    Note: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles By similarity. Component of the centrosome. Associated only transiently with nascent procentrioles during centriole biogenesis.By similarity

    GO - Cellular componenti

    1. centriole Source: UniProtKB
    2. centrosome Source: UniProtKB
    3. deuterosome Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1311F → D: Fails to multimerize via N-terminus. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670950.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 657657Spindle assembly abnormal protein 6 homologPRO_0000189972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei510 – 5101Phosphoserine1 Publication
    Modified residuei657 – 6571Phosphoserine2 Publications

    Post-translational modificationi

    Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase complex during S phase, leading to its degradation and preventing centriole reduplication.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ6UVJ0.
    PaxDbiQ6UVJ0.
    PeptideAtlasiQ6UVJ0.
    PRIDEiQ6UVJ0.

    PTM databases

    PhosphoSiteiQ6UVJ0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6UVJ0.
    BgeeiQ6UVJ0.
    CleanExiHS_SASS6.
    GenevestigatoriQ6UVJ0.

    Organism-specific databases

    HPAiHPA028187.

    Interactioni

    Subunit structurei

    Nine homodimers form a cartwheel structure with an internal diameter of 23 nM and radial spokes connecting to the microtubule triplets By similarity. Part of a ternary complex composed of SASS6, CENPJ and CEP350. Interacts with FBXW5.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CEP135Q66GS98EBI-1570153,EBI-1046993
    STILQ154683EBI-1570153,EBI-7488405

    Protein-protein interaction databases

    BioGridi127880. 5 interactions.
    IntActiQ6UVJ0. 8 interactions.
    MINTiMINT-6776971.
    STRINGi9606.ENSP00000287482.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6UVJ0.
    SMRiQ6UVJ0. Positions 1-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 9153PISAAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili166 – 471306Sequence AnalysisAdd
    BLAST

    Domaini

    The 35 nM long coiled-coil domain mediates homodimerization while the globular N-terminus links the dimers at an angle of 40 degrees to form the inner ring.By similarity

    Sequence similaritiesi

    Contains 1 PISA domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG117813.
    HOGENOMiHOG000124668.
    HOVERGENiHBG079167.
    InParanoidiQ6UVJ0.
    KOiK16487.
    OMAiFLASCLK.
    OrthoDBiEOG764727.
    PhylomeDBiQ6UVJ0.
    TreeFamiTF326199.

    Sequencei

    Sequence statusi: Complete.

    Q6UVJ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQVLFHQLV PLQVKCKDCE ERRVSIRMSI ELQSVSNPVH RKDLVIRLTD    50
    DTDPFFLYNL VISEEDFQSL KFQQGLLVDF LAFPQKFIDL LQQCTQEHAK 100
    EIPRFLLQLV SPAAILDNSP AFLNVVETNP FKHLTHLSLK LLPGNDVEIK 150
    KFLAGCLKCS KEEKLSLMQS LDDATKQLDF TRKTLAEKKQ ELDKLRNEWA 200
    SHTAALTNKH SQELTNEKEK ALQAQVQYQQ QHEQQKKDLE ILHQQNIHQL 250
    QNRLSELEAA NKDLTERKYK GDSTIRELKA KLSGVEEELQ RTKQEVLSLR 300
    RENSTLDVEC HEKEKHVNQL QTKVAVLEQE IKDKDQLVLR TKEAFDTIQE 350
    QKVVLEENGE KNQVQLGKLE ATIKSLSAEL LKANEIIKKL QGDLKTLMGK 400
    LKLKNTVTIQ QEKLLAEKEE KLQKEQKELQ DVGQSLRIKE QEVCKLQEQL 450
    EATVKKLEES KQLLKNNEKL ITWLNKELNE NQLVRKQDVL GPSTTPPAHS 500
    SSNTIRSGIS PNLNVVDGRL TYPTCGIGYP VSSAFAFQNT FPHSISAKNT 550
    SHPGSGTKVQ FNLQFTKPNA SLGDVQSGAT ISMPCSTDKE NGENVGLESK 600
    YLKKREDSIP LRGLSQNLFS NSDHQRDGTL GALHTSSKPT ALPSASSAYF 650
    PGQLPNS 657
    Length:657
    Mass (Da):74,397
    Last modified:July 5, 2004 - v1
    Checksum:i6D19696BC748849F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti259 – 2591A → V.
    Corresponds to variant rs13375867 [ dbSNP | Ensembl ].
    VAR_021590

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY359522 mRNA. Translation: AAQ57128.1.
    AL445928, AC093019 Genomic DNA. Translation: CAH72248.1.
    CH471097 Genomic DNA. Translation: EAW72974.1.
    CH471097 Genomic DNA. Translation: EAW72975.1.
    AL834265 mRNA. Translation: CAD38940.1.
    CCDSiCCDS764.1.
    RefSeqiNP_919268.1. NM_194292.1.
    UniGeneiHs.591447.

    Genome annotation databases

    EnsembliENST00000287482; ENSP00000287482; ENSG00000156876.
    GeneIDi163786.
    KEGGihsa:163786.
    UCSCiuc001dsu.3. human.

    Polymorphism databases

    DMDMi62511032.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY359522 mRNA. Translation: AAQ57128.1 .
    AL445928 , AC093019 Genomic DNA. Translation: CAH72248.1 .
    CH471097 Genomic DNA. Translation: EAW72974.1 .
    CH471097 Genomic DNA. Translation: EAW72975.1 .
    AL834265 mRNA. Translation: CAD38940.1 .
    CCDSi CCDS764.1.
    RefSeqi NP_919268.1. NM_194292.1.
    UniGenei Hs.591447.

    3D structure databases

    ProteinModelPortali Q6UVJ0.
    SMRi Q6UVJ0. Positions 1-171.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127880. 5 interactions.
    IntActi Q6UVJ0. 8 interactions.
    MINTi MINT-6776971.
    STRINGi 9606.ENSP00000287482.

    PTM databases

    PhosphoSitei Q6UVJ0.

    Polymorphism databases

    DMDMi 62511032.

    Proteomic databases

    MaxQBi Q6UVJ0.
    PaxDbi Q6UVJ0.
    PeptideAtlasi Q6UVJ0.
    PRIDEi Q6UVJ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000287482 ; ENSP00000287482 ; ENSG00000156876 .
    GeneIDi 163786.
    KEGGi hsa:163786.
    UCSCi uc001dsu.3. human.

    Organism-specific databases

    CTDi 163786.
    GeneCardsi GC01M100549.
    HGNCi HGNC:25403. SASS6.
    HPAi HPA028187.
    MIMi 609321. gene.
    neXtProti NX_Q6UVJ0.
    PharmGKBi PA142670950.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG117813.
    HOGENOMi HOG000124668.
    HOVERGENi HBG079167.
    InParanoidi Q6UVJ0.
    KOi K16487.
    OMAi FLASCLK.
    OrthoDBi EOG764727.
    PhylomeDBi Q6UVJ0.
    TreeFami TF326199.

    Miscellaneous databases

    GeneWikii SASS6.
    GenomeRNAii 163786.
    NextBioi 88409.
    PROi Q6UVJ0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6UVJ0.
    Bgeei Q6UVJ0.
    CleanExi HS_SASS6.
    Genevestigatori Q6UVJ0.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. Shan Y.X., Chen K., Yu L.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-657.
      Tissue: Amygdala.
    5. "Proteomic characterization of the human centrosome by protein correlation profiling."
      Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.
      Nature 426:570-574(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Lymphoblast.
    6. "Centriole assembly requires both centriolar and pericentriolar material proteins."
      Dammermann A., Mueller-Reichert T., Pelletier L., Habermann B., Desai A., Oegema K.
      Dev. Cell 7:815-829(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "SAS-6 defines a protein family required for centrosome duplication in C. elegans and in human cells."
      Leidel S., Delattre M., Cerutti L., Baumer K., Goenczy P.
      Nat. Cell Biol. 7:115-125(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "The Polo kinase Plk4 functions in centriole duplication."
      Habedanck R., Stierhof Y.-D., Wilkinson C.J., Nigg E.A.
      Nat. Cell Biol. 7:1140-1146(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Role of CAP350 in centriolar tubule stability and centriole assembly."
      Le Clech M.
      PLoS ONE 3:E3855-E3855(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CENPJ AND CEP350.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510 AND SER-657, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6 to control centrosome duplication."
      Puklowski A., Homsi Y., Keller D., May M., Chauhan S., Kossatz U., Grunwald V., Kubicka S., Pich A., Manns M.P., Hoffmann I., Gonczy P., Malek N.P.
      Nat. Cell Biol. 13:1004-1009(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH FBXW5.
    17. Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-131.

    Entry informationi

    Entry nameiSAS6_HUMAN
    AccessioniPrimary (citable) accession number: Q6UVJ0
    Secondary accession number(s): D3DT55, Q8N3K0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 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 1
      Human chromosome 1: 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