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Protein

Spindle assembly abnormal protein 6 homolog

Gene

SASS6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. Overexpression results in excess foci-bearing centriolar markers.3 Publications

GO - Biological processi

  1. centriole replication Source: UniProtKB
  2. centrosome duplication Source: UniProtKB
Complete GO annotation...

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 Componenti: 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
Complete GO annotation...

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

BgeeiQ6UVJ0.
CleanExiHS_SASS6.
ExpressionAtlasiQ6UVJ0. baseline and differential.
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. 9 interactions.
IntActiQ6UVJ0. 8 interactions.
MINTiMINT-6776971.
STRINGi9606.ENSP00000287482.

Structurei

3D structure databases

ProteinModelPortaliQ6UVJ0.
SMRiQ6UVJ0. Positions 1-202.
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.
GeneTreeiENSGT00390000006932.
HOGENOMiHOG000124668.
HOVERGENiHBG079167.
InParanoidiQ6UVJ0.
KOiK16487.
OMAiFLASCLK.
OrthoDBiEOG764727.
PhylomeDBiQ6UVJ0.
TreeFamiTF326199.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q6UVJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVLFHQLV PLQVKCKDCE ERRVSIRMSI ELQSVSNPVH RKDLVIRLTD
60 70 80 90 100
DTDPFFLYNL VISEEDFQSL KFQQGLLVDF LAFPQKFIDL LQQCTQEHAK
110 120 130 140 150
EIPRFLLQLV SPAAILDNSP AFLNVVETNP FKHLTHLSLK LLPGNDVEIK
160 170 180 190 200
KFLAGCLKCS KEEKLSLMQS LDDATKQLDF TRKTLAEKKQ ELDKLRNEWA
210 220 230 240 250
SHTAALTNKH SQELTNEKEK ALQAQVQYQQ QHEQQKKDLE ILHQQNIHQL
260 270 280 290 300
QNRLSELEAA NKDLTERKYK GDSTIRELKA KLSGVEEELQ RTKQEVLSLR
310 320 330 340 350
RENSTLDVEC HEKEKHVNQL QTKVAVLEQE IKDKDQLVLR TKEAFDTIQE
360 370 380 390 400
QKVVLEENGE KNQVQLGKLE ATIKSLSAEL LKANEIIKKL QGDLKTLMGK
410 420 430 440 450
LKLKNTVTIQ QEKLLAEKEE KLQKEQKELQ DVGQSLRIKE QEVCKLQEQL
460 470 480 490 500
EATVKKLEES KQLLKNNEKL ITWLNKELNE NQLVRKQDVL GPSTTPPAHS
510 520 530 540 550
SSNTIRSGIS PNLNVVDGRL TYPTCGIGYP VSSAFAFQNT FPHSISAKNT
560 570 580 590 600
SHPGSGTKVQ FNLQFTKPNA SLGDVQSGAT ISMPCSTDKE NGENVGLESK
610 620 630 640 650
YLKKREDSIP LRGLSQNLFS NSDHQRDGTL GALHTSSKPT ALPSASSAYF

PGQLPNS
Length:657
Mass (Da):74,397
Last modified:July 4, 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:
EMBLi
GenBanki
DDBJi
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_194292.2.
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:
EMBLi
GenBanki
DDBJi
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_194292.2.
UniGeneiHs.591447.

3D structure databases

ProteinModelPortaliQ6UVJ0.
SMRiQ6UVJ0. Positions 1-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127880. 9 interactions.
IntActiQ6UVJ0. 8 interactions.
MINTiMINT-6776971.
STRINGi9606.ENSP00000287482.

PTM databases

PhosphoSiteiQ6UVJ0.

Polymorphism databases

DMDMi62511032.

Proteomic databases

MaxQBiQ6UVJ0.
PaxDbiQ6UVJ0.
PeptideAtlasiQ6UVJ0.
PRIDEiQ6UVJ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi163786.
GeneCardsiGC01M100549.
HGNCiHGNC:25403. SASS6.
HPAiHPA028187.
MIMi609321. gene.
neXtProtiNX_Q6UVJ0.
PharmGKBiPA142670950.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG117813.
GeneTreeiENSGT00390000006932.
HOGENOMiHOG000124668.
HOVERGENiHBG079167.
InParanoidiQ6UVJ0.
KOiK16487.
OMAiFLASCLK.
OrthoDBiEOG764727.
PhylomeDBiQ6UVJ0.
TreeFamiTF326199.

Miscellaneous databases

ChiTaRSiSASS6. human.
GeneWikiiSASS6.
GenomeRNAii163786.
NextBioi88409.
PROiQ6UVJ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6UVJ0.
CleanExiHS_SASS6.
ExpressionAtlasiQ6UVJ0. baseline and differential.
GenevestigatoriQ6UVJ0.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. Shan Y.X., Chen K., Yu L.
    Submitted (JUL-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(2005) [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(2002) [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(2003) [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(2004) [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(2004) [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(2005) [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(2007) [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(2008) [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(2009) [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(2010) [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 11, 2005
Last sequence update: July 4, 2004
Last modified: March 31, 2015
This is version 92 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

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.