Gene

KWMTBOMO04369

Pre Gene Modal

BGIBMGA005251

Annotation

PREDICTED:_centromere_protein_S-like_[Papilio_xuthus]

Location

Bomo_Chr8(-):4785663-4788032      View in EpiBrowser

Full name

Centromere protein S      

Alternative Name

Apoptosis-inducing TAF9-like domain-containing protein 1
FANCM-associated histone fold protein 1
FANCM-interacting histone fold protein 1
Fanconi anemia-associated polypeptide of 16 kDa

Location in the cell

Nuclear   Reliability : 2.341

CDS

ATGTCTGCTTTTGAAGATTTATCTGCTTCGCAAAGGCTACGTGCAGCGTTAAAGCGGGACGTAACAGCCATCTGTTTGGAATCAACTGTCGGATTGGAAATCACCAAACCAGCAATGGACTTAATACTAGAACTGATTTATAAGAAGCTGTCTGTCTACGCCTCTGATTTAGAAGTCTTCGCAAGGCATGCTAGACGCTGCAAAATCCAAGGGGAAGATGTCAAGCTACTGGTGAGACGAAACAAATCTTTACGATCTCAACTTGAATCGAGGTCCCCAACAGCGGCTCTCAAGCGCAAGTCATCGCTCGCCGAAGATATATTCGAAGACGCATCCTCCAACTTTGACGAGCCCGCAATGAAAGACAAAATGCGCAAGGAAGAGCCGCCAATGGAAGACGCAATTGACATGACCGTTGAAAATGTCGTCGATTTGACCGCCGATTAA

Protein

MSAFEDLSASQRLRAALKRDVTAICLESTVGLEITKPAMDLILELIYKKLSVYASDLEVFARHARRCKIQGEDVKLLVRRNKSLRSQLESRSPTAALKRKSSLAEDIFEDASSNFDEPAMKDKMRKEEPPMEDAIDMTVENVVDLTAD

Description

DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:20347428, PubMed:20347429). In complex with CENPX (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM (PubMed:20347428, PubMed:20347429). In complex with CENPX and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks (PubMed:20347428). In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression (PubMed:19620631). As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure (PubMed:20347428, PubMed:22304917). DNA-binding function is fulfilled in the presence of CENPX, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (PubMed:20347428, PubMed:20347429).

Subunit

Heterodimer with CENPX, sometimes called MHF; this interaction stabilizes both partners (PubMed:19620631, PubMed:20347428, PubMed:20347429, PubMed:24522885). MHF heterodimers can assemble to form tetrameric structures (PubMed:22304917). MHF also coassemble with CENPT-CENPW heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex (PubMed:22304917, PubMed:24522885). Forms a discrete complex with FANCM and CENPX, called FANCM-MHF; this interaction, probably mediated by direct binding between CENPS and FANCM, leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling (PubMed:20347428, PubMed:20347429). Recruited by FANCM to the Fanconi anemia (FA) core complex, which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates with Bloom syndrome (BLM) complex, which consists of at least BLM, DNA topoisomerase 3-alpha (TOP3A), RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32. The super complex between FA and BLM is called BRAFT (PubMed:20347428, PubMed:20347429). Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex, composed of at least CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (PubMed:16622419).

Similarity

Belongs to the TAF9 family. CENP-S/MHF1 subfamily.

Keywords

3D-structure   Acetylation   Alternative splicing   Cell cycle   Cell division   Centromere   Chromosome   Complete proteome   DNA damage   DNA repair   DNA-binding   Kinetochore   Mitosis   Nucleus   Reference proteome  

Feature

chain  Centromere protein S
splice variant  In isoform 3.

Uniprot

H9J6V9   A0A2A4J4M9   A0A194Q148   A0A1E1WK96   A0A2H1W697   A0A3S2M5X2   + More
A0A2K6N705   H0X487   H9FU73   G3RAC8   G1RE55   H2N958   Q8N2Z9   A0A2K5MMV6   A0A096N6R5   A0A0D9S8N8   A0A1U7UB85   A0A2K5V9J7   I0FRJ7   G7NU59   G7MGU0   Q8N2Z9-2   A0A2K6GYI2   A0A2Y9F6T6   A0A341BRX7   A0A2Y9Q5W8   A0A340XV37   A0A0P6J9Z2   G1NSQ4   A0A2U3V8J9   A0A383Z4Q1   D2HXB9   G5C529   A0A3Q2GCY8  

Pubmed

19121390    24286570    26354079    25362486    25319552    16710414    + More
15489334    15328517    16622419    19620631    20347428    20347429    22304917    22814378    24522885    22002653    21993624    20010809    21993625   

EMBL

BABH01028412    AB766232    BAN29073.1    NWSH01003279    PCG66628.1    KQ459580    + More
KPI99307.1    GDQN01003763    JAT87291.1    ODYU01006620    SOQ48625.1    RSAL01000030    RVE51705.1    AAQR03101467    AAQR03101468    AAQR03101469    AAQR03101470    AAQR03101471    JU334429    AFE78182.1    CABD030000727    CABD030000728    ADFV01080659    ADFV01080660    ADFV01080661    ADFV01080662    ABGA01043965    ABGA01043966    ABGA01043967    ABGA01043968    NDHI03003447    PNJ48190.1    AF516753    AF521016    AL139424    AL354956    BC029430    AHZZ02015242    AHZZ02020767    AQIB01136407    AQIA01005920    JU471812    JV047002    AFH28616.1    AFI37073.1    CM001276    EHH49532.1    CM001253    EHH14312.1    GEBF01004246    JAN99386.1    AAPE02050832    GL193605    EFB21548.1    JH173407    EHB16640.1   

Proteomes

UP000005204    UP000218220    UP000053268    UP000283053    UP000233200    UP000005225    + More
UP000001519    UP000001073    UP000001595    UP000005640    UP000233060    UP000028761    UP000029965    UP000189704    UP000233100    UP000009130    UP000233160    UP000248484    UP000252040    UP000248483    UP000265300    UP000001074    UP000245320    UP000261681    UP000006813    UP000265020   

PRIDE

H9J6V9    Q8N2Z9   

Pfam

PF15630   CENP-S        + More
PF03002   Somatostatin

Interpro

IPR029003   CENP-S/Mhf1        + More
IPR009072   Histone-fold       
IPR033554   CENPS       
IPR018142   Somatostatin/Cortistatin_C       

SUPFAM

SSF47113   SSF47113       

Gene 3D

1.10.20.10    

ProteinModelPortal

H9J6V9   A0A2A4J4M9   A0A194Q148   A0A1E1WK96   A0A2H1W697   A0A3S2M5X2   + More
A0A2K6N705   H0X487   H9FU73   G3RAC8   G1RE55   H2N958   Q8N2Z9   A0A2K5MMV6   A0A096N6R5   A0A0D9S8N8   A0A1U7UB85   A0A2K5V9J7   I0FRJ7   G7NU59   G7MGU0   Q8N2Z9-2   A0A2K6GYI2   A0A2Y9F6T6   A0A341BRX7   A0A2Y9Q5W8   A0A340XV37   A0A0P6J9Z2   G1NSQ4   A0A2U3V8J9   A0A383Z4Q1   D2HXB9   G5C529   A0A3Q2GCY8  

PDB

4DRA     E-value=7.41256e-09,     Score=138

KEGG

101747068    K11511 centromere protein S | (RefSeq) MHF1; centromere protein S-like

PATHWAY

03460    Fanconi anemia pathway - Bombyx mori (domestic silkworm)

GO

GO:0046982   GO:0071821   GO:0006281   GO:0051382   GO:0000776   GO:0003682   GO:0003690   GO:0031297   GO:0043240   GO:0000712   GO:0005829   GO:0006974   GO:0036297   GO:0003677   GO:0000777   GO:0005654   GO:0034080   GO:0051301   GO:0031398   GO:0005576   GO:0005179   GO:0006508   GO:0015074   GO:0016311   GO:0016791   GO:0006470   GO:0004674   GO:0009058   GO:0016742   GO:0003824  

PANTHER

PTHR22980:SF4  

Subcellular location

Nucleus   Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPS is more stably bound at the kinetochore than CENPX (PubMed:19620631, PubMed:24522885). During S phase, rapidly recruited to DNA interstrand cross-links that block replication (PubMed:20347428). Recruited to DNA damage sites about 20 minutes following UV irradiation, reaching a plateau after approximately 40 minutes (PubMed:24522885).   With evidence from 7 publications.
Chromosome   Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPS is more stably bound at the kinetochore than CENPX (PubMed:19620631, PubMed:24522885). During S phase, rapidly recruited to DNA interstrand cross-links that block replication (PubMed:20347428). Recruited to DNA damage sites about 20 minutes following UV irradiation, reaching a plateau after approximately 40 minutes (PubMed:24522885).   With evidence from 7 publications.
Centromere   Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPS is more stably bound at the kinetochore than CENPX (PubMed:19620631, PubMed:24522885). During S phase, rapidly recruited to DNA interstrand cross-links that block replication (PubMed:20347428). Recruited to DNA damage sites about 20 minutes following UV irradiation, reaching a plateau after approximately 40 minutes (PubMed:24522885).   With evidence from 7 publications.
Kinetochore   Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPS is more stably bound at the kinetochore than CENPX (PubMed:19620631, PubMed:24522885). During S phase, rapidly recruited to DNA interstrand cross-links that block replication (PubMed:20347428). Recruited to DNA damage sites about 20 minutes following UV irradiation, reaching a plateau after approximately 40 minutes (PubMed:24522885).   With evidence from 7 publications.

Length:

148

Number of predicted TMHs:

0

Exp number of AAs in TMHs:

0.02082

Exp number, first 60 AAs:

0.02077

Total prob of N-in:

0.04817

outside

1  -  148

 

 

Pi

26.456861

Theta

21.777184

Tajima's D

0.906317

CLR

0.688066

CSRT

0.636318184090795

Interpretation

Uncertain