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Protein

Spindle assembly abnormal protein 6 homolog

Gene

sass6

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

GO - Biological processi

  • centriole replication Source: InterPro
  • centrosome duplication Source: ZFIN
  • embryonic cleavage Source: ZFIN
  • mitotic spindle organization Source: ZFIN
  • nuclear division Source: ZFIN
  • spermatogenesis Source: ZFIN
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
ORF Names:zgc:55668
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-040426-2784. sass6.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 627627Spindle assembly abnormal protein 6 homologPRO_0000189975Add
BLAST

Proteomic databases

PaxDbiQ7ZVT3.

Interactioni

Subunit structurei

Nine homodimers form a cartwheel structure with an internal diameter of 23 nM and radial spokes connecting to the microtubule triplets.1 Publication

Protein-protein interaction databases

STRINGi7955.ENSDARP00000075634.

Structurei

Secondary structure

1
627
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1514Combined sources
Beta strandi17 – 193Combined sources
Beta strandi22 – 3312Combined sources
Beta strandi36 – 405Combined sources
Beta strandi43 – 508Combined sources
Beta strandi53 – 6210Combined sources
Helixi64 – 7411Combined sources
Helixi80 – 823Combined sources
Helixi83 – 9715Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi121 – 1277Combined sources
Beta strandi134 – 14310Combined sources
Helixi146 – 1538Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y3VX-ray1.92A/B/C/D1-156[»]
2Y3WX-ray1.98A/B/C1-179[»]
ProteinModelPortaliQ7ZVT3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7ZVT3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 9153PISAAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili153 – 473321Sequence 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.

Sequence similaritiesi

Contains 1 PISA domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IF03. Eukaryota.
ENOG410XQWJ. LUCA.
HOGENOMiHOG000124668.
HOVERGENiHBG079167.
InParanoidiQ7ZVT3.
KOiK16487.
PhylomeDBiQ7ZVT3.

Family and domain databases

InterProiIPR029678. SAS-6.
IPR032396. SAS-6_N.
[Graphical view]
PANTHERiPTHR18937:SF279. PTHR18937:SF279. 2 hits.
PfamiPF16531. SAS-6_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7ZVT3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTELLFNKRL QVLVKSKDTD ERRSVIRVSI ELQLPSSPVH RKDLVVRLTD
60 70 80 90 100
DTDLYFLYNL IISEEDFQSL KVQQGLLIDF TSFPQKFIDL LEQCICEQDK
110 120 130 140 150
ESPRFLLQLS SSSSAFDHSP SNLNIVETNA FKHLTHLSLK LLPGSDTDIK
160 170 180 190 200
KYLASCLSSV KEEKQQLQQK LRKTEEDLTR QLNYAQQTLS EKSRELDKLR
210 220 230 240 250
SEWTSQTTSL SSRHMQDLTA EREKALETQS RLQQQNEQLR QELESSHHRS
260 270 280 290 300
TQQLQTKVSE LETANRELID KKYKSDSTIR DLKAKLTSLE EECQRSKQQV
310 320 330 340 350
LSLRRENSAL DSECHEKERL LNQLQTRVAV LEQEIKDKDQ LVLRTKEVLE
360 370 380 390 400
ATQQQKNSVE GNAESKQLQI SKLESTVKSL SEELIKANGI IKKLQADLKA
410 420 430 440 450
LLGKIKVKNS VTVPQEKILQ ETSDKLQRQQ RELQDTQQRL SLKEEEAAKL
460 470 480 490 500
KEQLEATVQK LDESREVLKT NENVITWLNK QLNENQLSRK QETVAMFETP
510 520 530 540 550
AAALRSAAVP HNMAFPITST INSKYPLALS CVSSGSRSVL TSSNGPKVQF
560 570 580 590 600
NPMSVKPSAA EVSPAAFSQP ANKENSEPVG LDSKYFERRD DSIPLRGLLP
610 620
SMHLNREVPK PLNTAAAKAT PSAFFPG
Length:627
Mass (Da):71,315
Last modified:June 1, 2003 - v1
Checksum:i068636706A28E4E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC045420 mRNA. Translation: AAH45420.1.
RefSeqiNP_998603.1. NM_213438.1.
UniGeneiDr.77479.

Genome annotation databases

GeneIDi406747.
KEGGidre:406747.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC045420 mRNA. Translation: AAH45420.1.
RefSeqiNP_998603.1. NM_213438.1.
UniGeneiDr.77479.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y3VX-ray1.92A/B/C/D1-156[»]
2Y3WX-ray1.98A/B/C1-179[»]
ProteinModelPortaliQ7ZVT3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000075634.

Proteomic databases

PaxDbiQ7ZVT3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi406747.
KEGGidre:406747.

Organism-specific databases

CTDi163786.
ZFINiZDB-GENE-040426-2784. sass6.

Phylogenomic databases

eggNOGiENOG410IF03. Eukaryota.
ENOG410XQWJ. LUCA.
HOGENOMiHOG000124668.
HOVERGENiHBG079167.
InParanoidiQ7ZVT3.
KOiK16487.
PhylomeDBiQ7ZVT3.

Miscellaneous databases

EvolutionaryTraceiQ7ZVT3.
NextBioi20818266.
PROiQ7ZVT3.

Family and domain databases

InterProiIPR029678. SAS-6.
IPR032396. SAS-6_N.
[Graphical view]
PANTHERiPTHR18937:SF279. PTHR18937:SF279. 2 hits.
PfamiPF16531. SAS-6_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: AB.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1-179, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.

Entry informationi

Entry nameiSAS6_DANRE
AccessioniPrimary (citable) accession number: Q7ZVT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2003
Last modified: January 20, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.