Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NASP-related protein sim3

Gene

sim3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Histone H3 and H3-like CENP-A-specific chaperone. Promotes delivery and incorporation of CENP-A in centromeric chromatin, probably by escorting nascent CENP-A to CENP-A chromatin assembly factors. Required for central core silencing and normal chromosome segregation.1 Publication

GO - Biological processi

  • CENP-A containing nucleosome assembly Source: PomBase
  • chromatin maintenance Source: PomBase
  • histone exchange Source: PomBase
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
NASP-related protein sim3
Alternative name(s):
CENP-A escort protein sim3
Silencing in the middle of the centromere protein 3
Gene namesi
Name:sim3
ORF Names:SPBC577.15c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC577.15c.
PomBaseiSPBC577.15c. sim3.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: PomBase
  • nucleoplasm Source: PomBase
  • nucleus Source: PomBase
  • protein complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811G → E in sim3-143; Reduces interaction with CENP-A and causes abnormal mitotic phenotypes, including hypercondensed chromatin, lagging chromosomes in anaphase, and unequal segregation of chromosomes. 1 Publication
Mutagenesisi207 – 2071E → K in sim3-205; Reduces interaction with CENP-A and causes abnormal mitotic phenotypes, including hypercondensed chromatin, lagging chromosomes in anaphase, and unequal segregation of chromosomes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396NASP-related protein sim3PRO_0000363381Add
BLAST

Proteomic databases

MaxQBiQ9USQ4.

Interactioni

Subunit structurei

Interacts with cnp1, hht1, hht2 and hht3; has a preference for CENP-A (cnp1) over histone H3 (hht1/2/3).1 Publication

Protein-protein interaction databases

BioGridi277411. 13 interactions.
MINTiMINT-4708488.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati32 – 6534TPR 1Add
BLAST
Repeati89 – 12234TPR 2Add
BLAST
Repeati199 – 23234TPR 3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili267 – 32963Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi390 – 3956Poly-Lys

Sequence similaritiesi

Belongs to the NASP family.Curated
Contains 3 TPR repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

InParanoidiQ9USQ4.
KOiK11372.
OMAiVEPDDRN.
OrthoDBiEOG7G1VH8.
PhylomeDBiQ9USQ4.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR019544. Tetratricopeptide_SHNi-TPR_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF10516. SHNi-TPR. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 2 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9USQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDTKTLEN SKGNSATDAD TKNPSSSDSR AIEQLVTQGN MAYAQKNYEE
60 70 80 90 100
AVDKYGQALM QSESIHGSES LENRNVLWLY GKSLFQIAIE NSQVLGNALG
110 120 130 140 150
AKESVSQATE SFEEPEAIGS FTFSGQKIEN KYTVNEENSS IAHPEKESEE
160 170 180 190 200
KETNEASPAS EEDEDDFNVA WEVLDLTRVM QSKAVDAYPD SKDEKIRLAD
210 220 230 240 250
IYDLLGELSL EIENFSQASQ DLKTALEWKE KVYNVSNNTL LSEAHYKLAL
260 270 280 290 300
ALEFTNPEDP SNKSRACEHV EKAAEILKNV LNERENEVTD KKGKGKQKAE
310 320 330 340 350
ESTLTSDLEN LREMLSELEQ KTLDLKHGAP SLEEAVMSKM HESSLLSKDS
360 370 380 390
SSLAQAVAEA VKNANDLGGL VKRKRTKQEV TSSSQKEGPK DKKKKD
Length:396
Mass (Da):43,903
Last modified:May 1, 2000 - v1
Checksum:i2077DFC3449FC270
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB54823.1.
PIRiT40559.
RefSeqiNP_595313.1. NM_001021220.2.

Genome annotation databases

EnsemblFungiiSPBC577.15c.1; SPBC577.15c.1:pep; SPBC577.15c.
GeneIDi2540895.
KEGGispo:SPBC577.15c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB54823.1.
PIRiT40559.
RefSeqiNP_595313.1. NM_001021220.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277411. 13 interactions.
MINTiMINT-4708488.

Proteomic databases

MaxQBiQ9USQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC577.15c.1; SPBC577.15c.1:pep; SPBC577.15c.
GeneIDi2540895.
KEGGispo:SPBC577.15c.

Organism-specific databases

EuPathDBiFungiDB:SPBC577.15c.
PomBaseiSPBC577.15c. sim3.

Phylogenomic databases

InParanoidiQ9USQ4.
KOiK11372.
OMAiVEPDDRN.
OrthoDBiEOG7G1VH8.
PhylomeDBiQ9USQ4.

Miscellaneous databases

PROiQ9USQ4.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR019544. Tetratricopeptide_SHNi-TPR_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF10516. SHNi-TPR. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 2 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "A NASP (N1/N2)-related protein, Sim3, binds CENP-A and is required for its deposition at fission yeast centromeres."
    Dunleavy E.M., Pidoux A.L., Monet M., Bonilla C., Richardson W., Hamilton G.L., Ekwall K., McLaughlin P.J., Allshire R.C.
    Mol. Cell 28:1029-1044(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CNP1 AND HHT1; HHT2 AND HHT3, MUTAGENESIS OF GLY-81 AND GLU-207.

Entry informationi

Entry nameiSIM3_SCHPO
AccessioniPrimary (citable) accession number: Q9USQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.