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CA1AA_XENLA
ID   CA1AA_XENLA             Reviewed;         896 AA.
AC   Q98TA5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Chromatin assembly factor 1 subunit A-A;
DE            Short=CAF-1 subunit A;
DE   AltName: Full=Chromatin assembly factor I p150 subunit A;
DE            Short=CAF-I 150 kDa subunit A;
DE            Short=CAF-I p150-A;
DE            Short=xp150;
GN   Name=chaf1a-a; Synonyms=caip150;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HOMODIMER, AND SUBCELLULAR LOCATION.
RX   PubMed=11296234; DOI=10.1093/emboj/20.8.2015;
RA   Quivy J.-P., Grandi P., Almouzni G.;
RT   "Dimerization of the largest subunit of chromatin assembly factor 1:
RT   importance in vitro and during Xenopus early development.";
RL   EMBO J. 20:2015-2027(2001).
CC   -!- FUNCTION: Involved in chromatin assembly in DNA replication and DNA
CC       repair. {ECO:0000250, ECO:0000269|PubMed:11296234}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q98TA5; Q7ZZH7: dbf4; NbExp=2; IntAct=EBI-8563970, EBI-8563988;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11296234}.
CC   -!- SIMILARITY: Belongs to the CHAF1A family. {ECO:0000305}.
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DR   EMBL; AF222339; AAK31811.1; -; mRNA.
DR   RefSeq; NP_001082096.1; NM_001088627.1.
DR   AlphaFoldDB; Q98TA5; -.
DR   IntAct; Q98TA5; 1.
DR   MINT; Q98TA5; -.
DR   PRIDE; Q98TA5; -.
DR   GeneID; 398222; -.
DR   KEGG; xla:398222; -.
DR   CTD; 398222; -.
DR   Xenbase; XB-GENE-17342845; chaf1a.L.
DR   OrthoDB; 1362011at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 398222; Expressed in blastula and 19 other tissues.
DR   GO; GO:0033186; C:CAF-1 complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0031497; P:chromatin assembly; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IMP:UniProtKB.
DR   InterPro; IPR029105; CAF1-p150_C2.
DR   InterPro; IPR029091; CAF1_p150_N.
DR   InterPro; IPR022043; CAF1A.
DR   Pfam; PF15539; CAF1-p150_C2; 1.
DR   Pfam; PF15557; CAF1-p150_N; 1.
DR   Pfam; PF12253; CAF1A; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Chaperone; DNA damage; DNA repair; DNA replication; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..896
FT                   /note="Chromatin assembly factor 1 subunit A-A"
FT                   /id="PRO_0000373884"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..678
FT                   /note="Necessary for homodimerization, competence for
FT                   chromatin assembly"
FT   REGION          724..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..297
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   896 AA;  101067 MW;  8A4F0FABA3CA0783 CRC64;
     MPGKEAAVNV MQSSTKSNTK KMVQARLPFK RLNPVPKDEG CLEEKKVRIT KNVSPQKMLH
     SLNSSMEDME NDCDMETETV PIPKAVNGKG PLDNYIRKAP KVSHAPSITT IDLTEESNIS
     ISNDCPLNGE SETHLANGTL ALEESTPNLP LSAKEECTVS LENKTVENTH FSELKSDQLH
     QAAATSTSAS NFSPERVVKE DCNSSADDDS ASVSSSSSPV SLSSPDAQTG SQFRNRSSPS
     TSTTPTGKVT ANKTSADKNK TKDKDKQRQA EKEERERAKK EARSAKKKKR QGLLKNLQRK
     RGKTSESSGK EYKKEKKERE DKEKAEKMKL KEEKKREKLE ALEAKQEEKR KKDEEKRQKE
     EEKRQKEEEK RLKEEEKRVK AEKAEITRFF QKPKTPQAPK TFSRSCGKFA PFEIKKGMAL
     APLCRIDFEP EASEELDRFL QEQNSKIYFF DEIKKRKPRK MGQTTVPTVN SFEVDDVQVL
     GESDPVLGSN MLEGHIKDIG VPERKKFGRM KLLQFCENHR PAYWGTCNRR SRVINSRKPW
     AQDTGMLDYE VDSDEEWEEE EPGESLSHSE GENDDDPKED DEDDDGFFVP HGYLSDDEGV
     SDEECTDPEN QKFRQKLKAK EWYELQTNGK KIRAMQPVVI GCVWWDSKAS EISLLQKFSA
     CILESPAVDE ELAQEISSAQ SLKDRQILSK LVPLLHGNVN GSKIMIQEFQ EYCRRGLFLE
     DNASDAAGNE STSPNVTPQT PSNIIVPSKA RLKRLISENS VYEKRPDHRM CWYVHSDVLK
     GLQQDNLPVP CQWTYITQVN SVAKEDNGAN GGSLQSLPLS GKRKSAGSMP ITKFMKRAKD
     LETAINTDMD GFQADNEEDD DDCMILEDQQ AKDAEDSTIE CKINLNDSAV LASCQN
 
 
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