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RFA2_PONAB
ID   RFA2_PONAB              Reviewed;         270 AA.
AC   Q5RC43;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Replication protein A 32 kDa subunit;
DE            Short=RP-A p32;
DE   AltName: Full=Replication factor A protein 2;
DE            Short=RF-A protein 2;
GN   Name=RPA2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: As part of the heterotrimeric replication protein A complex
CC       (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates,
CC       that form during DNA replication or upon DNA stress. It prevents their
CC       reannealing and in parallel, recruits and activates different proteins
CC       and complexes involved in DNA metabolism. Thereby, it plays an
CC       essential role both in DNA replication and the cellular response to DNA
CC       damage. In the cellular response to DNA damage, the RPA complex
CC       controls DNA repair and DNA damage checkpoint activation. Through
CC       recruitment of ATRIP activates the ATR kinase a master regulator of the
CC       DNA damage response. It is required for the recruitment of the DNA
CC       double-strand break repair factors RAD51 and RAD52 to chromatin in
CC       response to DNA damage. Also recruits to sites of DNA damage proteins
CC       like XPA and XPG that are involved in nucleotide excision repair and is
CC       required for this mechanism of DNA repair. Also plays a role in base
CC       excision repair (BER) probably through interaction with UNG. Also
CC       recruits SMARCAL1/HARP, which is involved in replication fork restart,
CC       to sites of DNA damage. May also play a role in telomere maintenance.
CC       {ECO:0000250|UniProtKB:P15927}.
CC   -!- SUBUNIT: Component of the replication protein A complex (RPA/RP-A), a
CC       heterotrimeric complex composed of RPA1, RPA2 and RPA3. Interacts with
CC       PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair
CC       where it ubiquitinates the replication protein A complex (RPA).
CC       Interacts with SERTAD3. Interacts with TIPIN. Interacts with TIMELESS.
CC       Interacts with PPP4R2; the interaction is direct, DNA damage-dependent
CC       and mediates the recruitment of the PP4 catalytic subunit PPP4C.
CC       Interacts (hyperphosphorylated) with RAD51. Interacts with SMARCAL1;
CC       the interaction is direct and mediates the recruitment to the RPA
CC       complex of SMARCAL1. Interacts with RAD52 and XPA; those interactions
CC       are direct and associate RAD52 and XPA to the RPA complex. Interacts
CC       with FBH1. Interacts with ETAA1; the interaction is direct and promotes
CC       ETAA1 recruitment at stalled replication forks. Interacts with DDI2 (By
CC       similarity). {ECO:0000250|UniProtKB:P15927}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15927}. Nucleus,
CC       PML body {ECO:0000250|UniProtKB:P15927}. Note=Redistributes to discrete
CC       nuclear foci upon DNA damage in an ATR-dependent manner.
CC       {ECO:0000250|UniProtKB:P15927}.
CC   -!- PTM: Differentially phosphorylated throughout the cell cycle, becoming
CC       phosphorylated at the G1-S transition and dephosphorylated in late
CC       mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2
CC       and cyclin B-CDK1, respectively during DNA replication and mitosis.
CC       Dephosphorylation may require the serine/threonine-protein phosphatase
CC       4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further
CC       phosphorylation. Becomes hyperphosphorylated on additional residues
CC       including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage.
CC       Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily
CC       recruited to DNA repair nuclear foci as a hypophosphorylated form it
CC       undergoes subsequent hyperphosphorylation, catalyzed by ATR.
CC       Hyperphosphorylation is required for RAD51 recruitment to chromatin and
CC       efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3
CC       presence. {ECO:0000250|UniProtKB:P15927}.
CC   -!- PTM: DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19
CC       mediates ATRIP recruitment to the RPA complex at sites of DNA damage
CC       and activation of ATR. Ubiquitinated by RFWD3 at stalled replication
CC       forks in response to DNA damage: ubiquitination by RFWD3 does not lead
CC       to degradation by the proteasome and promotes removal of the RPA
CC       complex from stalled replication forks, promoting homologous
CC       recombination. {ECO:0000250|UniProtKB:P15927}.
CC   -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC       {ECO:0000305}.
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DR   EMBL; CR858438; CAH90667.1; -; mRNA.
DR   RefSeq; NP_001125362.2; NM_001131890.2.
DR   AlphaFoldDB; Q5RC43; -.
DR   BMRB; Q5RC43; -.
DR   SMR; Q5RC43; -.
DR   STRING; 9601.ENSPPYP00000001907; -.
DR   GeneID; 100172265; -.
DR   KEGG; pon:100172265; -.
DR   CTD; 6118; -.
DR   eggNOG; KOG3108; Eukaryota.
DR   InParanoid; Q5RC43; -.
DR   OrthoDB; 924826at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0006298; P:mismatch repair; ISS:UniProtKB.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR   GO; GO:0034502; P:protein localization to chromosome; ISS:UniProtKB.
DR   GO; GO:2000001; P:regulation of DNA damage checkpoint; ISS:UniProtKB.
DR   GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR040260; RFA2-like.
DR   InterPro; IPR014646; Rfa2/RPA32.
DR   InterPro; IPR014892; RPA_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13989; PTHR13989; 1.
DR   Pfam; PF08784; RPA_C; 1.
DR   PIRSF; PIRSF036949; RPA32; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA damage; DNA recombination; DNA repair; DNA replication;
KW   DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..270
FT                   /note="Replication protein A 32 kDa subunit"
FT                   /id="PRO_0000097272"
FT   DNA_BIND        74..148
FT                   /note="OB"
FT   REGION          21..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..270
FT                   /note="Interaction with RAD52, TIPIN, UNG and XPA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P15927"
FT   MOD_RES         4
FT                   /note="Phosphoserine; by PRKDC"
FT                   /evidence="ECO:0000250|UniProtKB:P15927"
FT   MOD_RES         8
FT                   /note="Phosphoserine; by PRKDC"
FT                   /evidence="ECO:0000250|UniProtKB:P15927"
FT   MOD_RES         21
FT                   /note="Phosphothreonine; by PRKDC"
FT                   /evidence="ECO:0000250|UniProtKB:P15927"
FT   MOD_RES         23
FT                   /note="Phosphoserine; by CDK2"
FT                   /evidence="ECO:0000250|UniProtKB:P15927"
FT   MOD_RES         29
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:P15927"
FT   MOD_RES         33
FT                   /note="Phosphoserine; by PRKDC"
FT                   /evidence="ECO:0000250|UniProtKB:P15927"
FT   CROSSLNK        37
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P15927"
FT   CROSSLNK        38
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P15927"
SQ   SEQUENCE   270 AA;  29235 MW;  4CCFB8F7D317D13B CRC64;
     MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT ISQLLSATLV
     DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA PMDVRQWVDT DDASSENTVV
     PPETYVKVAG HLRSFQNKKS LVAFKIMPLE DMNEFTTHIL EVINAHMVLS KANSQPSAGR
     APISNPGMSE AGNFGGNSFM PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS
     SVKQAMDFLS NEGHIYSTVD DDHFKSTDAE
 
 
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