SAS6_MOUSE
ID SAS6_MOUSE Reviewed; 654 AA.
AC Q80UK7; Q9CYT4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Spindle assembly abnormal protein 6 homolog {ECO:0000305};
GN Name=Sass6 {ECO:0000312|MGI:MGI:1920026}; Synonyms=Sas6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Trophoblast stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24240477; DOI=10.1038/ncb2880;
RA Zhao H., Zhu L., Zhu Y., Cao J., Li S., Huang Q., Xu T., Huang X., Yan X.,
RA Zhu X.;
RT "The Cep63 paralogue Deup1 enables massive de novo centriole biogenesis for
RT vertebrate multiciliogenesis.";
RL Nat. Cell Biol. 15:1434-1444(2013).
CC -!- FUNCTION: Central scaffolding component of the centrioles ensuring
CC their 9-fold symmetry. Required for centrosome biogenesis and
CC duplication: required both for mother-centriole-dependent centriole
CC duplication and deuterosome-dependent centriole amplification in
CC multiciliated cells (PubMed:24240477). Required for the recruitment of
CC STIL to the procentriole and for STIL-mediated centriole amplification
CC (By similarity). {ECO:0000250|UniProtKB:Q6UVJ0,
CC ECO:0000269|PubMed:24240477}.
CC -!- SUBUNIT: Nine homodimers form a cartwheel structure with an internal
CC diameter of 23 nM and radial spokes connecting to the microtubule
CC triplets. Interacts with FBXW5. Forms a complex with CENPJ and STIL.
CC Interacts with NUP62 and TUBG1 at the centrosome. Interacts with
CC CENATAC; the interaction increases with CENATAC acetylation. Interacts
CC with FZR1; the interaction is regulated by CENATAC and leads to SASS6
CC proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q6UVJ0,
CC ECO:0000250|UniProtKB:Q7ZVT3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q6UVJ0}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:24240477}. Note=Component of the centrosome.
CC Associated only transiently with nascent procentrioles during centriole
CC biogenesis (By similarity). Component of the deuterosome, a structure
CC that promotes de novo centriole amplification in multiciliated cells
CC that can generate more than 100 centrioles (PubMed:24240477).
CC {ECO:0000250|UniProtKB:Q6UVJ0, ECO:0000269|PubMed:24240477}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80UK7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80UK7-2; Sequence=VSP_013318, VSP_013319;
CC -!- DOMAIN: The 35 nM long coiled-coil domain mediates homodimerization
CC while the globular N-terminus links the dimers at an angle of 40
CC degrees to form the inner ring. {ECO:0000250|UniProtKB:Q7ZVT3}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase
CC complex during S phase, leading to its degradation and preventing
CC centriole reduplication. Ubiquitinated by the anaphase promoting
CC complex/cyclosome (APC/C) E3 ubiquitin-protein ligase complex, leading
CC to its degradation and preventing centriole reduplication.
CC {ECO:0000250|UniProtKB:Q6UVJ0}.
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DR EMBL; AK013338; BAB28799.1; -; mRNA.
DR EMBL; AC131038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050110; AAH50110.1; -; mRNA.
DR CCDS; CCDS17789.1; -. [Q80UK7-1]
DR RefSeq; NP_001276497.1; NM_001289568.1.
DR RefSeq; NP_001276500.1; NM_001289571.1.
DR RefSeq; NP_082625.2; NM_028349.3. [Q80UK7-1]
DR AlphaFoldDB; Q80UK7; -.
DR SMR; Q80UK7; -.
DR BioGRID; 215561; 20.
DR ComplexPortal; CPX-1297; CPAP-STIL complex.
DR IntAct; Q80UK7; 21.
DR STRING; 10090.ENSMUSP00000029571; -.
DR iPTMnet; Q80UK7; -.
DR PhosphoSitePlus; Q80UK7; -.
DR EPD; Q80UK7; -.
DR jPOST; Q80UK7; -.
DR MaxQB; Q80UK7; -.
DR PaxDb; Q80UK7; -.
DR PeptideAtlas; Q80UK7; -.
DR PRIDE; Q80UK7; -.
DR ProteomicsDB; 256920; -. [Q80UK7-1]
DR ProteomicsDB; 256921; -. [Q80UK7-2]
DR Antibodypedia; 33691; 138 antibodies from 20 providers.
DR DNASU; 72776; -.
DR Ensembl; ENSMUST00000198311; ENSMUSP00000143233; ENSMUSG00000027959. [Q80UK7-1]
DR Ensembl; ENSMUST00000198386; ENSMUSP00000143175; ENSMUSG00000027959. [Q80UK7-2]
DR GeneID; 72776; -.
DR KEGG; mmu:72776; -.
DR UCSC; uc008rcm.2; mouse. [Q80UK7-2]
DR UCSC; uc008rcn.3; mouse. [Q80UK7-1]
DR CTD; 163786; -.
DR MGI; MGI:1920026; Sass6.
DR VEuPathDB; HostDB:ENSMUSG00000027959; -.
DR eggNOG; ENOG502QQ4W; Eukaryota.
DR GeneTree; ENSGT00390000006932; -.
DR HOGENOM; CLU_2830555_0_0_1; -.
DR InParanoid; Q80UK7; -.
DR OMA; YHLQFVE; -.
DR OrthoDB; 345225at2759; -.
DR PhylomeDB; Q80UK7; -.
DR TreeFam; TF326199; -.
DR BioGRID-ORCS; 72776; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Sass6; mouse.
DR PRO; PR:Q80UK7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80UK7; protein.
DR Bgee; ENSMUSG00000027959; Expressed in spermatid and 196 other tissues.
DR ExpressionAtlas; Q80UK7; baseline and differential.
DR Genevisible; Q80UK7; MM.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098536; C:deuterosome; IDA:UniProtKB.
DR GO; GO:0120099; C:procentriole replication complex; ISO:MGI.
DR GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR GO; GO:0051298; P:centrosome duplication; ISO:MGI.
DR GO; GO:0046601; P:positive regulation of centriole replication; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IC:ComplexPortal.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IC:ComplexPortal.
DR Gene3D; 2.170.210.20; -; 1.
DR InterPro; IPR032396; SAS-6_N.
DR InterPro; IPR038558; SAS-6_N_sf.
DR InterPro; IPR041513; SAS6_CC.
DR Pfam; PF16531; SAS-6_N; 1.
DR Pfam; PF18594; Sas6_CC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..654
FT /note="Spindle assembly abnormal protein 6 homolog"
FT /id="PRO_0000189973"
FT DOMAIN 39..91
FT /note="PISA"
FT REGION 568..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 175..471
FT /evidence="ECO:0000255"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UVJ0"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UVJ0"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UVJ0"
FT VAR_SEQ 558..560
FT /note="HFN -> AKC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013318"
FT VAR_SEQ 561..654
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013319"
FT CONFLICT 19
FT /note="C -> R (in Ref. 1; BAB28799)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="K -> N (in Ref. 1; BAB28799)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="N -> D (in Ref. 3; AAH50110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 654 AA; 74054 MW; BB83293FBC00DD42 CRC64;
MSQVLFQQLV PLLVKCKDCE ERRGSVRVSI ELQSLSNPVH RKDLVIRLTD DTDPFFLYNL
VISEEDFQSL KLQQGLLVDF LAFPQKFIDL LQQCMQEHAK ETPRFLLQLL SSATLLENSP
VLLNVVETNP FKHLIHLSLK LLPGNDVEIK KFLAGCLKCS KEEKLSLTRS LDDVTRQLHI
TQETLSEKMQ ELDKLRSEWA SHTASLTNKH SQELTAEKEK ALQTQVQCQQ QHEQQKKELE
TLHQRNIHQL QSRLSELEAA NKELTERKYK GDSTVRELKA KLAGVEEELQ RAKQEVLSLR
RENCTLDTEC HEKEKHINQL QTKVAVLEQE IKDKDQLVLR TKEAFDTIQE QKVALEENGE
KNQIQLGKLE ATIKSLSAEL LKANEIIKKL QGDLKTLMGK LKLKNTVTIQ QEKLLAEKEE
MLQKERKESQ DAGQFLRAKE QEVCRLQEQL ETTVQKLEES KQLLKNNEKL ITWLNKELNE
NQLVRKQDTL GTSATPHSTS NSTIRSGLSP NLNVVDRLNY PSCGIGYPVS SALTFQNAFP
HVVAAKNTSH PISGPKVHFN LQLTKPSASI DGQPGAAVNR PCSNDKENGE TLGLESKYLK
RREASIPLRG LSQNLLSDSD HQKDGMLGAF QLSSKPTVLP SSSSAYFPGQ LPSS
