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Q80UK7 (SAS6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spindle assembly abnormal protein 6 homolog
Gene names
Name:Sass6
Synonyms:Sas6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. Ref.4

Subunit structure

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

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity. Note: Component of the centrosome. Associated only transiently with nascent procentrioles during centriole biogenesis By similarity. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Ref.4

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 By similarity.

Sequence similarities

Contains 1 PISA domain.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentriole

Inferred from direct assay PubMed 24075808. Source: UniProtKB

deuterosome

Inferred from direct assay PubMed 24075808. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80UK7-1)

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.
Isoform 2 (identifier: Q80UK7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     558-560: HFN → AKC
     561-654: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 654654Spindle assembly abnormal protein 6 homolog
PRO_0000189973

Regions

Domain39 – 9153PISA
Coiled coil175 – 471297 Potential

Amino acid modifications

Modified residue5091Phosphoserine By similarity
Modified residue6541Phosphoserine By similarity

Natural variations

Alternative sequence558 – 5603HFN → AKC in isoform 2.
VSP_013318
Alternative sequence561 – 65494Missing in isoform 2.
VSP_013319

Experimental info

Sequence conflict191C → R in BAB28799. Ref.1
Sequence conflict3951K → N in BAB28799. Ref.1
Sequence conflict5791N → D in AAH50110. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: BB83293FBC00DD42

FASTA65474,054
        10         20         30         40         50         60 
MSQVLFQQLV PLLVKCKDCE ERRGSVRVSI ELQSLSNPVH RKDLVIRLTD DTDPFFLYNL 

        70         80         90        100        110        120 
VISEEDFQSL KLQQGLLVDF LAFPQKFIDL LQQCMQEHAK ETPRFLLQLL SSATLLENSP 

       130        140        150        160        170        180 
VLLNVVETNP FKHLIHLSLK LLPGNDVEIK KFLAGCLKCS KEEKLSLTRS LDDVTRQLHI 

       190        200        210        220        230        240 
TQETLSEKMQ ELDKLRSEWA SHTASLTNKH SQELTAEKEK ALQTQVQCQQ QHEQQKKELE 

       250        260        270        280        290        300 
TLHQRNIHQL QSRLSELEAA NKELTERKYK GDSTVRELKA KLAGVEEELQ RAKQEVLSLR 

       310        320        330        340        350        360 
RENCTLDTEC HEKEKHINQL QTKVAVLEQE IKDKDQLVLR TKEAFDTIQE QKVALEENGE 

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

       430        440        450        460        470        480 
MLQKERKESQ DAGQFLRAKE QEVCRLQEQL ETTVQKLEES KQLLKNNEKL ITWLNKELNE 

       490        500        510        520        530        540 
NQLVRKQDTL GTSATPHSTS NSTIRSGLSP NLNVVDRLNY PSCGIGYPVS SALTFQNAFP 

       550        560        570        580        590        600 
HVVAAKNTSH PISGPKVHFN LQLTKPSASI DGQPGAAVNR PCSNDKENGE TLGLESKYLK 

       610        620        630        640        650 
RREASIPLRG LSQNLLSDSD HQKDGMLGAF QLSSKPTVLP SSSSAYFPGQ LPSS 

« Hide

Isoform 2 [UniParc].

Checksum: F0B854FE0FC5B79C
Show »

FASTA56064,002

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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).
Strain: ICR.
Tissue: Trophoblast stem cell.
[4]"The Cep63 paralogue Deup1 enables massive de novo centriole biogenesis for vertebrate multiciliogenesis."
Zhao H., Zhu L., Zhu Y., Cao J., Li S., Huang Q., Xu T., Huang X., Yan X., Zhu X.
Nat. Cell Biol. 15:1434-1444(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK013338 mRNA. Translation: BAB28799.1.
AC131038 Genomic DNA. No translation available.
BC050110 mRNA. Translation: AAH50110.1.
RefSeqNP_082625.2. NM_028349.3.
UniGeneMm.440836.

3D structure databases

ProteinModelPortalQ80UK7.
SMRQ80UK7. Positions 1-206, 322-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215561. 13 interactions.
IntActQ80UK7. 14 interactions.

PTM databases

PhosphoSiteQ80UK7.

Proteomic databases

PRIDEQ80UK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029571; ENSMUSP00000029571; ENSMUSG00000027959. [Q80UK7-1]
GeneID72776.
KEGGmmu:72776.
UCSCuc008rcm.1. mouse. [Q80UK7-2]
uc008rcn.2. mouse. [Q80UK7-1]

Organism-specific databases

CTD163786.
MGIMGI:1920026. Sass6.

Phylogenomic databases

eggNOGNOG117813.
GeneTreeENSGT00390000006932.
HOGENOMHOG000124668.
HOVERGENHBG079167.
InParanoidQ80UK7.
KOK16487.
OMAFLASCLK.
OrthoDBEOG764727.
TreeFamTF326199.

Gene expression databases

BgeeQ80UK7.
CleanExMM_SASS6.
GenevestigatorQ80UK7.

Family and domain databases

ProtoNetSearch...

Other

NextBio336909.
PROQ80UK7.
SOURCESearch...

Entry information

Entry nameSAS6_MOUSE
AccessionPrimary (citable) accession number: Q80UK7
Secondary accession number(s): Q9CYT4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot