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Q6UVJ0 (SAS6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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:
Spindle assembly abnormal protein 6 homolog

Short name=HsSAS-6
Gene names
Name:SASS6
Synonyms:SAS6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.10

Subunit structure

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. Ref.11 Ref.16

Subcellular location

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. Ref.5 Ref.6 Ref.7 Ref.10 Ref.17

Domain

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.

Post-translational modification

Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase complex during S phase, leading to its degradation and preventing centriole reduplication. Ref.16

Sequence similarities

Contains 1 PISA domain.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcentriole replication

Inferred from mutant phenotype Ref.8Ref.10. Source: UniProtKB

centrosome duplication

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentcentriole

Inferred from direct assay Ref.10. Source: UniProtKB

centrosome

Inferred from direct assay Ref.7PubMed 21399614. Source: UniProtKB

deuterosome

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657Spindle assembly abnormal protein 6 homolog
PRO_0000189972

Regions

Domain39 – 9153PISA
Coiled coil166 – 471306 Potential

Amino acid modifications

Modified residue5101Phosphoserine Ref.12
Modified residue6571Phosphoserine Ref.12 Ref.14

Natural variations

Natural variant2591A → V.
Corresponds to variant rs13375867 [ dbSNP | Ensembl ].
VAR_021590

Experimental info

Mutagenesis1311F → D: Fails to multimerize via N-terminus. Ref.17

Sequences

Sequence LengthMass (Da)Tools
Q6UVJ0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6D19696BC748849F

FASTA65774,397
        10         20         30         40         50         60 
MSQVLFHQLV PLQVKCKDCE ERRVSIRMSI ELQSVSNPVH RKDLVIRLTD DTDPFFLYNL 

        70         80         90        100        110        120 
VISEEDFQSL KFQQGLLVDF LAFPQKFIDL LQQCTQEHAK EIPRFLLQLV SPAAILDNSP 

       130        140        150        160        170        180 
AFLNVVETNP FKHLTHLSLK LLPGNDVEIK KFLAGCLKCS KEEKLSLMQS LDDATKQLDF 

       190        200        210        220        230        240 
TRKTLAEKKQ ELDKLRNEWA SHTAALTNKH SQELTNEKEK ALQAQVQYQQ QHEQQKKDLE 

       250        260        270        280        290        300 
ILHQQNIHQL QNRLSELEAA NKDLTERKYK GDSTIRELKA KLSGVEEELQ RTKQEVLSLR 

       310        320        330        340        350        360 
RENSTLDVEC HEKEKHVNQL QTKVAVLEQE IKDKDQLVLR TKEAFDTIQE QKVVLEENGE 

       370        380        390        400        410        420 
KNQVQLGKLE ATIKSLSAEL LKANEIIKKL QGDLKTLMGK LKLKNTVTIQ QEKLLAEKEE 

       430        440        450        460        470        480 
KLQKEQKELQ DVGQSLRIKE QEVCKLQEQL EATVKKLEES KQLLKNNEKL ITWLNKELNE 

       490        500        510        520        530        540 
NQLVRKQDVL GPSTTPPAHS SSNTIRSGIS PNLNVVDGRL TYPTCGIGYP VSSAFAFQNT 

       550        560        570        580        590        600 
FPHSISAKNT SHPGSGTKVQ FNLQFTKPNA SLGDVQSGAT ISMPCSTDKE NGENVGLESK 

       610        620        630        640        650 
YLKKREDSIP LRGLSQNLFS NSDHQRDGTL GALHTSSKPT ALPSASSAYF PGQLPNS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Plk4-induced centriole biogenesis in human cells."
Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D., Nigg E.A.
Dev. Cell 13:190-202(2007) [PubMed] [Europe PMC] [Abstract]
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]"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-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]"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].
[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]"Structures of SAS-6 suggest its organization in centrioles."
van Breugel M., Hirono M., Andreeva A., Yanagisawa H.A., Yamaguchi S., Nakazawa Y., Morgner N., Petrovich M., Ebong I.O., Robinson C.V., Johnson C.M., Veprintsev D., Zuber B.
Science 331:1196-1199(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-131.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_919268.1. NM_194292.1.
UniGeneHs.591447.

3D structure databases

ProteinModelPortalQ6UVJ0.
SMRQ6UVJ0. Positions 1-202, 366-481.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127880. 5 interactions.
IntActQ6UVJ0. 8 interactions.
MINTMINT-6776971.
STRING9606.ENSP00000287482.

PTM databases

PhosphoSiteQ6UVJ0.

Polymorphism databases

DMDM62511032.

Proteomic databases

PaxDbQ6UVJ0.
PeptideAtlasQ6UVJ0.
PRIDEQ6UVJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287482; ENSP00000287482; ENSG00000156876.
GeneID163786.
KEGGhsa:163786.
UCSCuc001dsu.3. human.

Organism-specific databases

CTD163786.
GeneCardsGC01M100549.
HGNCHGNC:25403. SASS6.
HPAHPA028187.
MIM609321. gene.
neXtProtNX_Q6UVJ0.
PharmGKBPA142670950.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG117813.
HOGENOMHOG000124668.
HOVERGENHBG079167.
InParanoidQ6UVJ0.
KOK16487.
OMAFLASCLK.
OrthoDBEOG764727.
PhylomeDBQ6UVJ0.
TreeFamTF326199.

Gene expression databases

ArrayExpressQ6UVJ0.
BgeeQ6UVJ0.
CleanExHS_SASS6.
GenevestigatorQ6UVJ0.

Family and domain databases

ProtoNetSearch...

Other

GeneWikiSASS6.
GenomeRNAi163786.
NextBio88409.
PROQ6UVJ0.
SOURCESearch...

Entry information

Entry nameSAS6_HUMAN
AccessionPrimary (citable) accession number: Q6UVJ0
Secondary accession number(s): D3DT55, Q8N3K0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 83 of the entry and version 1 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 1

Human chromosome 1: entries, gene names and cross-references to MIM