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Protein

Spindle assembly abnormal protein 6 homolog

Gene

Sass6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Spindle assembly abnormal protein 6 homolog
Gene namesi
Name:Sass6
Synonyms:Sas6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1920026. Sass6.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB
  • centrosome Source: MGI
  • deuterosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Spindle assembly abnormal protein 6 homologPRO_0000189973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei509 – 5091PhosphoserineBy similarity
Modified residuei654 – 6541PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ80UK7.
PRIDEiQ80UK7.

PTM databases

PhosphoSiteiQ80UK7.

Expressioni

Gene expression databases

BgeeiQ80UK7.
CleanExiMM_SASS6.
GenevestigatoriQ80UK7.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi215561. 13 interactions.
IntActiQ80UK7. 14 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ80UK7.
SMRiQ80UK7. 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 coili175 – 471297Sequence 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.
GeneTreeiENSGT00390000006932.
HOGENOMiHOG000124668.
HOVERGENiHBG079167.
InParanoidiQ80UK7.
KOiK16487.
OMAiFLASCLK.
OrthoDBiEOG764727.
TreeFamiTF326199.

Family and domain databases

InterProiIPR029678. SAS-6.
[Graphical view]
PANTHERiPTHR18937:SF193. PTHR18937:SF193. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80UK7-1) [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

        10         20         30         40         50
MSQVLFQQLV PLLVKCKDCE ERRGSVRVSI ELQSLSNPVH RKDLVIRLTD
60 70 80 90 100
DTDPFFLYNL VISEEDFQSL KLQQGLLVDF LAFPQKFIDL LQQCMQEHAK
110 120 130 140 150
ETPRFLLQLL SSATLLENSP VLLNVVETNP FKHLIHLSLK LLPGNDVEIK
160 170 180 190 200
KFLAGCLKCS KEEKLSLTRS LDDVTRQLHI TQETLSEKMQ ELDKLRSEWA
210 220 230 240 250
SHTASLTNKH SQELTAEKEK ALQTQVQCQQ QHEQQKKELE TLHQRNIHQL
260 270 280 290 300
QSRLSELEAA NKELTERKYK GDSTVRELKA KLAGVEEELQ RAKQEVLSLR
310 320 330 340 350
RENCTLDTEC HEKEKHINQL QTKVAVLEQE IKDKDQLVLR TKEAFDTIQE
360 370 380 390 400
QKVALEENGE KNQIQLGKLE ATIKSLSAEL LKANEIIKKL QGDLKTLMGK
410 420 430 440 450
LKLKNTVTIQ QEKLLAEKEE MLQKERKESQ DAGQFLRAKE QEVCRLQEQL
460 470 480 490 500
ETTVQKLEES KQLLKNNEKL ITWLNKELNE NQLVRKQDTL GTSATPHSTS
510 520 530 540 550
NSTIRSGLSP NLNVVDRLNY PSCGIGYPVS SALTFQNAFP HVVAAKNTSH
560 570 580 590 600
PISGPKVHFN LQLTKPSASI DGQPGAAVNR PCSNDKENGE TLGLESKYLK
610 620 630 640 650
RREASIPLRG LSQNLLSDSD HQKDGMLGAF QLSSKPTVLP SSSSAYFPGQ

LPSS
Length:654
Mass (Da):74,054
Last modified:July 27, 2011 - v2
Checksum:iBB83293FBC00DD42
GO
Isoform 2 (identifier: Q80UK7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     558-560: HFN → AKC
     561-654: Missing.

Note: No experimental confirmation available.

Show »
Length:560
Mass (Da):64,002
Checksum:iF0B854FE0FC5B79C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191C → R in BAB28799 (PubMed:16141072).Curated
Sequence conflicti395 – 3951K → N in BAB28799 (PubMed:16141072).Curated
Sequence conflicti579 – 5791N → D in AAH50110 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei558 – 5603HFN → AKC in isoform 2. 1 PublicationVSP_013318
Alternative sequencei561 – 65494Missing in isoform 2. 1 PublicationVSP_013319Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013338 mRNA. Translation: BAB28799.1.
AC131038 Genomic DNA. No translation available.
BC050110 mRNA. Translation: AAH50110.1.
CCDSiCCDS17789.1. [Q80UK7-1]
RefSeqiNP_001276497.1. NM_001289568.1.
NP_001276500.1. NM_001289571.1.
NP_082625.2. NM_028349.3. [Q80UK7-1]
UniGeneiMm.440836.

Genome annotation databases

EnsembliENSMUST00000029571; ENSMUSP00000029571; ENSMUSG00000027959. [Q80UK7-1]
GeneIDi72776.
KEGGimmu:72776.
UCSCiuc008rcm.1. mouse. [Q80UK7-2]
uc008rcn.2. mouse. [Q80UK7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013338 mRNA. Translation: BAB28799.1.
AC131038 Genomic DNA. No translation available.
BC050110 mRNA. Translation: AAH50110.1.
CCDSiCCDS17789.1. [Q80UK7-1]
RefSeqiNP_001276497.1. NM_001289568.1.
NP_001276500.1. NM_001289571.1.
NP_082625.2. NM_028349.3. [Q80UK7-1]
UniGeneiMm.440836.

3D structure databases

ProteinModelPortaliQ80UK7.
SMRiQ80UK7. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215561. 13 interactions.
IntActiQ80UK7. 14 interactions.

PTM databases

PhosphoSiteiQ80UK7.

Proteomic databases

MaxQBiQ80UK7.
PRIDEiQ80UK7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029571; ENSMUSP00000029571; ENSMUSG00000027959. [Q80UK7-1]
GeneIDi72776.
KEGGimmu:72776.
UCSCiuc008rcm.1. mouse. [Q80UK7-2]
uc008rcn.2. mouse. [Q80UK7-1]

Organism-specific databases

CTDi163786.
MGIiMGI:1920026. Sass6.

Phylogenomic databases

eggNOGiNOG117813.
GeneTreeiENSGT00390000006932.
HOGENOMiHOG000124668.
HOVERGENiHBG079167.
InParanoidiQ80UK7.
KOiK16487.
OMAiFLASCLK.
OrthoDBiEOG764727.
TreeFamiTF326199.

Miscellaneous databases

NextBioi336909.
PROiQ80UK7.
SOURCEiSearch...

Gene expression databases

BgeeiQ80UK7.
CleanExiMM_SASS6.
GenevestigatoriQ80UK7.

Family and domain databases

InterProiIPR029678. SAS-6.
[Graphical view]
PANTHERiPTHR18937:SF193. PTHR18937:SF193. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSAS6_MOUSE
AccessioniPrimary (citable) accession number: Q80UK7
Secondary accession number(s): Q9CYT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 27, 2011
Last modified: March 4, 2015
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.