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PCNA1_ARATH
ID   PCNA1_ARATH             Reviewed;         263 AA.
AC   Q9M7Q7; A7UIK5; Q9LNV6;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Proliferating cellular nuclear antigen 1;
DE            Short=PCNA 1;
GN   Name=PCNA; Synonyms=PCNA1; OrderedLocusNames=At1g07370; ORFNames=F22G5.29;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Park S.C., Park E.H., Cho J.W.;
RT   "Cloning and characterization of Arabidopsis proliferating cellular nuclear
RT   antigen (PCNA).";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Di Rubbo A., Vonarx E.J., Kunz B.A.;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   INTERACTION WITH ATXR5 AND ATXR6.
RX   PubMed=16771839; DOI=10.1111/j.1365-313x.2006.02799.x;
RA   Raynaud C., Sozzani R., Glab N., Domenichini S., Perennes C., Cella R.,
RA   Kondorosi E., Bergounioux C.;
RT   "Two cell-cycle regulated SET-domain proteins interact with proliferating
RT   cell nuclear antigen (PCNA) in Arabidopsis.";
RL   Plant J. 47:395-407(2006).
RN   [8]
RP   INTERACTION WITH POLH.
RX   PubMed=18494853; DOI=10.1111/j.1365-313x.2008.03562.x;
RA   Anderson H.J., Vonarx E.J., Pastushok L., Nakagawa M., Katafuchi A.,
RA   Gruz P., Di Rubbo A., Grice D.M., Osmond M.J., Sakamoto A.N., Nohmi T.,
RA   Xiao W., Kunz B.A.;
RT   "Arabidopsis thaliana Y-family DNA polymerase eta catalyses translesion
RT   synthesis and interacts functionally with PCNA2.";
RL   Plant J. 55:895-908(2008).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-256 IN COMPLEX WITH HUMAN P21
RP   PEPTIDE, AND SUBUNIT.
RX   PubMed=19388052; DOI=10.1002/pro.117;
RA   Strzalka W., Oyama T., Tori K., Morikawa K.;
RT   "Crystal structures of the Arabidopsis thaliana proliferating cell nuclear
RT   antigen 1 and 2 proteins complexed with the human p21 C-terminal segment.";
RL   Protein Sci. 18:1072-1080(2009).
CC   -!- FUNCTION: This protein is an auxiliary protein of DNA polymerase delta
CC       and is involved in the control of eukaryotic DNA replication by
CC       increasing the polymerase's processibility during elongation of the
CC       leading strand. {ECO:0000250}.
CC   -!- SUBUNIT: Homo- and heterotrimer. Interacts with POLH, ATXR5 and ATXR6.
CC       {ECO:0000269|PubMed:16771839, ECO:0000269|PubMed:18494853,
CC       ECO:0000269|PubMed:19388052}.
CC   -!- INTERACTION:
CC       Q9M7Q7; Q8H2D5: POLH; NbExp=2; IntAct=EBI-1810458, EBI-1810451;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
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DR   EMBL; AF083220; AAF40018.1; -; mRNA.
DR   EMBL; EU072917; ABU25233.1; -; mRNA.
DR   EMBL; AC022464; AAF79566.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28115.1; -; Genomic_DNA.
DR   EMBL; AF462821; AAL58911.1; -; mRNA.
DR   EMBL; AY098969; AAM19979.1; -; mRNA.
DR   EMBL; AY086852; AAM63900.1; -; mRNA.
DR   RefSeq; NP_172217.1; NM_100611.4.
DR   PDB; 2ZVV; X-ray; 2.00 A; A/B=1-256.
DR   PDB; 6O09; X-ray; 2.06 A; A/C/D/F/H/K=1-263.
DR   PDBsum; 2ZVV; -.
DR   PDBsum; 6O09; -.
DR   AlphaFoldDB; Q9M7Q7; -.
DR   SMR; Q9M7Q7; -.
DR   BioGRID; 22490; 46.
DR   IntAct; Q9M7Q7; 7.
DR   STRING; 3702.AT1G07370.1; -.
DR   iPTMnet; Q9M7Q7; -.
DR   PaxDb; Q9M7Q7; -.
DR   PRIDE; Q9M7Q7; -.
DR   ProteomicsDB; 236846; -.
DR   EnsemblPlants; AT1G07370.1; AT1G07370.1; AT1G07370.
DR   GeneID; 837249; -.
DR   Gramene; AT1G07370.1; AT1G07370.1; AT1G07370.
DR   KEGG; ath:AT1G07370; -.
DR   Araport; AT1G07370; -.
DR   TAIR; locus:2025062; AT1G07370.
DR   eggNOG; KOG1636; Eukaryota.
DR   HOGENOM; CLU_043978_3_0_1; -.
DR   InParanoid; Q9M7Q7; -.
DR   OMA; EMKLINM; -.
DR   OrthoDB; 1012066at2759; -.
DR   PhylomeDB; Q9M7Q7; -.
DR   EvolutionaryTrace; Q9M7Q7; -.
DR   PRO; PR:Q9M7Q7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9M7Q7; baseline and differential.
DR   Genevisible; Q9M7Q7; AT.
DR   GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0043626; C:PCNA complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central.
DR   GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:TAIR.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR   GO; GO:0019985; P:translesion synthesis; IBA:GO_Central.
DR   HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR   IDEAL; IID50102; -.
DR   InterPro; IPR000730; Pr_cel_nuc_antig.
DR   InterPro; IPR022649; Pr_cel_nuc_antig_C.
DR   InterPro; IPR022659; Pr_cel_nuc_antig_CS.
DR   InterPro; IPR022648; Pr_cel_nuc_antig_N.
DR   Pfam; PF02747; PCNA_C; 1.
DR   Pfam; PF00705; PCNA_N; 1.
DR   PRINTS; PR00339; PCNACYCLIN.
DR   TIGRFAMs; TIGR00590; pcna; 1.
DR   PROSITE; PS01251; PCNA_1; 1.
DR   PROSITE; PS00293; PCNA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..263
FT                   /note="Proliferating cellular nuclear antigen 1"
FT                   /id="PRO_0000149177"
FT   DNA_BIND        61..80
FT                   /evidence="ECO:0000255"
FT   CONFLICT        48
FT                   /note="V -> A (in Ref. 1; AAF40018 and 2; ABU25233)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   HELIX           10..19
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          24..31
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          34..40
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          44..53
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   HELIX           72..80
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          97..104
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          111..117
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          134..140
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   HELIX           141..152
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          156..163
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          166..173
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          176..182
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          196..201
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          203..208
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   HELIX           209..215
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   HELIX           216..221
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          223..229
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          235..241
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   TURN            242..244
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          245..251
FT                   /evidence="ECO:0007829|PDB:2ZVV"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:6O09"
SQ   SEQUENCE   263 AA;  29122 MW;  DA63C0F637CDB5D7 CRC64;
     MLELRLVQGS LLKKVLESIK DLVNDANFDC SSTGFSLQAM DSSHVALVSL LLRSEGFEHY
     RCDRNLSMGM NLGNMSKMLK CAGNDDIITI KADDGGDTVT FMFESPTQDK IADFEMKLMD
     IDSEHLGIPD AEYHSIVRMP SNEFSRICKD LSSIGDTVVI SVTKEGVKFS TAGDIGTANI
     VLRQNTTVDK PEDAIVIEMK EPVSLSFALR YMNSFTKATP LSDTVTISLS SELPVVVEYK
     VAEMGYIRYY LAPKIEEEED TNP
 
 
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