CTF4_YEAST
ID CTF4_YEAST Reviewed; 927 AA.
AC Q01454; D6W4D2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=DNA polymerase alpha-binding protein;
DE AltName: Full=Chromosome replication protein CHL15;
DE AltName: Full=Chromosome transmission fidelity protein 4;
DE AltName: Full=Protein POB1;
GN Name=CTF4; Synonyms=CHL15, POB1; OrderedLocusNames=YPR135W;
GN ORFNames=P9659.7;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC STRAIN=7208-12;
RX PubMed=1448101; DOI=10.1128/mcb.12.12.5724-5735.1992;
RA Miles J., Formosa T.;
RT "Evidence that POB1, a Saccharomyces cerevisiae protein that binds to DNA
RT polymerase alpha, acts in DNA metabolism in vivo.";
RL Mol. Cell. Biol. 12:5724-5735(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1341195; DOI=10.1128/mcb.12.12.5736-5747.1992;
RA Kouprina N.Y., Kroll E.S., Bannikov V.M., Bliskovsky V.V., Gizatullin R.Z.,
RA Kirillov A.V., Shestopalov B.V., Zakharyev V.M., Hieter P., Spencer F.,
RA Larionov V.;
RT "CTF4 (CHL15) mutants exhibit defective DNA metabolism in the yeast
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:5736-5747(1992).
RN [3]
RP ERRATUM OF PUBMED:1341195.
RA Kouprina N.Y., Kroll E.S., Bannikov V.M., Bliskovsky V.V., Gizatullin R.Z.,
RA Kirillov A.V., Shestopalov B.V., Zakharyev V.M., Hieter P., Spencer F.,
RA Larionov V.;
RL Mol. Cell. Biol. 13:7202-7202(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8316240;
RA Kouprina N.Y., Kroll E.S., Koryabin M.Y., Shestopalov B.V.,
RA Bliskovsky V.V., Bannikov V.M., Gizatullin R.Z., Kirillov A.V.,
RA Kravtsov V.Y., Zakharyev V.M.;
RT "CHL15 -- a new gene controlling the replication of chromosomes in
RT Saccharomycetes yeast: cloning, physical mapping, sequencing, and sequence
RT analysis.";
RL Mol. Biol. (Mosk.) 27:569-588(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-379, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-379; THR-401;
RP THR-411 AND SER-463, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-379 AND SER-398, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Accessory factor for DNA replication. It plays a role in
CC accurately duplicating the genome in vivo.
CC -!- INTERACTION:
CC Q01454; Q01454: CTF4; NbExp=6; IntAct=EBI-5209, EBI-5209;
CC Q01454; Q08496: DIA2; NbExp=5; IntAct=EBI-5209, EBI-31943;
CC Q01454; Q06164: MMS22; NbExp=4; IntAct=EBI-5209, EBI-31156;
CC Q01454; P13382: POL1; NbExp=14; IntAct=EBI-5209, EBI-6128;
CC Q01454; Q12488: PSF1; NbExp=7; IntAct=EBI-5209, EBI-22066;
CC Q01454; Q03406: SLD5; NbExp=14; IntAct=EBI-5209, EBI-37437;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 3280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M94769; AAA34887.1; -; Genomic_DNA.
DR EMBL; S63246; AAB27308.1; -; Genomic_DNA.
DR EMBL; U40829; AAB68276.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11548.1; -; Genomic_DNA.
DR PIR; A45039; A45039.
DR RefSeq; NP_015461.1; NM_001184232.1.
DR PDB; 4C8H; X-ray; 2.69 A; A/B/C=471-927.
DR PDB; 4C8S; X-ray; 3.00 A; A/B/C=471-927.
DR PDB; 4C93; X-ray; 2.69 A; A/B/C=471-927.
DR PDB; 4C95; X-ray; 2.69 A; A/B/C=471-927.
DR PDB; 5HOG; X-ray; 3.09 A; A/B/C=471-927.
DR PDB; 5HOI; X-ray; 3.30 A; A/B/C=472-927.
DR PDB; 5NXQ; X-ray; 2.41 A; A/B/C=471-927.
DR PDB; 6PTJ; EM; 3.80 A; E/F/G=1-927.
DR PDB; 6PTN; EM; 5.80 A; E/F/G=1-927.
DR PDB; 6PTO; EM; 7.00 A; X/Y/Z=1-927.
DR PDB; 6SKL; EM; 3.70 A; F/G/H=1-927.
DR PDB; 7PMN; EM; 3.20 A; F/G/H=1-927.
DR PDBsum; 4C8H; -.
DR PDBsum; 4C8S; -.
DR PDBsum; 4C93; -.
DR PDBsum; 4C95; -.
DR PDBsum; 5HOG; -.
DR PDBsum; 5HOI; -.
DR PDBsum; 5NXQ; -.
DR PDBsum; 6PTJ; -.
DR PDBsum; 6PTN; -.
DR PDBsum; 6PTO; -.
DR PDBsum; 6SKL; -.
DR PDBsum; 7PMN; -.
DR AlphaFoldDB; Q01454; -.
DR SMR; Q01454; -.
DR BioGRID; 36302; 609.
DR ComplexPortal; CPX-1165; CUL8-MMS1-MMS22-CTF4 E3 ubiquitin ligase complex.
DR DIP; DIP-4640N; -.
DR IntAct; Q01454; 27.
DR MINT; Q01454; -.
DR STRING; 4932.YPR135W; -.
DR iPTMnet; Q01454; -.
DR MaxQB; Q01454; -.
DR PaxDb; Q01454; -.
DR PRIDE; Q01454; -.
DR EnsemblFungi; YPR135W_mRNA; YPR135W; YPR135W.
DR GeneID; 856254; -.
DR KEGG; sce:YPR135W; -.
DR SGD; S000006339; CTF4.
DR VEuPathDB; FungiDB:YPR135W; -.
DR eggNOG; KOG1274; Eukaryota.
DR GeneTree; ENSGT00390000002030; -.
DR HOGENOM; CLU_004219_2_0_1; -.
DR InParanoid; Q01454; -.
DR OMA; NAWFPIC; -.
DR BioCyc; YEAST:G3O-34271-MON; -.
DR PRO; PR:Q01454; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q01454; protein.
DR GO; GO:0035361; C:Cul8-RING ubiquitin ligase complex; IC:ComplexPortal.
DR GO; GO:0000228; C:nuclear chromosome; IDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IMP:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR022100; Mcl1_mid.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12341; Mcl1_mid; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA replication; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1448101"
FT CHAIN 2..927
FT /note="DNA polymerase alpha-binding protein"
FT /id="PRO_0000050948"
FT REPEAT 10..49
FT /note="WD 1"
FT REPEAT 134..173
FT /note="WD 2"
FT REPEAT 227..266
FT /note="WD 3"
FT REPEAT 273..313
FT /note="WD 4"
FT REPEAT 699..739
FT /note="WD 5"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 112
FT /note="G -> E (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="V -> F (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="V -> F (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="N -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="E -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 489..496
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 498..507
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 510..519
FT /evidence="ECO:0007829|PDB:5NXQ"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:5NXQ"
FT TURN 549..551
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 553..560
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 588..592
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 596..600
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 606..611
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 615..621
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 624..631
FT /evidence="ECO:0007829|PDB:5NXQ"
FT TURN 632..634
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 635..643
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 648..656
FT /evidence="ECO:0007829|PDB:5NXQ"
FT HELIX 667..670
FT /evidence="ECO:0007829|PDB:5NXQ"
FT HELIX 674..679
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 686..689
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 703..709
FT /evidence="ECO:0007829|PDB:5NXQ"
FT TURN 713..715
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 717..723
FT /evidence="ECO:0007829|PDB:5NXQ"
FT HELIX 724..731
FT /evidence="ECO:0007829|PDB:5NXQ"
FT TURN 732..734
FT /evidence="ECO:0007829|PDB:5HOG"
FT STRAND 738..748
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 751..763
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 772..775
FT /evidence="ECO:0007829|PDB:5NXQ"
FT HELIX 783..788
FT /evidence="ECO:0007829|PDB:5NXQ"
FT HELIX 792..795
FT /evidence="ECO:0007829|PDB:4C8S"
FT HELIX 819..843
FT /evidence="ECO:0007829|PDB:5NXQ"
FT STRAND 847..849
FT /evidence="ECO:0007829|PDB:5NXQ"
FT HELIX 851..875
FT /evidence="ECO:0007829|PDB:5NXQ"
FT HELIX 879..887
FT /evidence="ECO:0007829|PDB:5NXQ"
FT HELIX 892..904
FT /evidence="ECO:0007829|PDB:5NXQ"
FT HELIX 908..925
FT /evidence="ECO:0007829|PDB:5NXQ"
SQ SEQUENCE 927 AA; 104425 MW; E2ABBB244B5F8B4D CRC64;
MVSVIDKLVF DFGGKTLVSL APDNNTLCVA NKNGLTKILK TNNPEEEPET LDSSKLVSSI
KCYSNSHFLM TTMQGDALRY NIDSSQEELL ARFALPLRDC CVIHSGKMAV FGGDDLELIL
LELDDETHKK HAIKIDEQVS QISYNSQMNI LAVSMINGKV QIFSLTSTIP NKVHELNDYI
VANSYDDTHR DKILSNMMDD IDKDNDNDLS ETADPDENNV ADPEFCAANR ICTRVAWHPK
GLHFALPCAD DTVKIFSIKG YSLQKTLSTN LSSTKAHFID LQFDPLRGTY IAAVDLNNKL
TVWNWETSEI HYTREFKRKI TNIAWKIQAD SKTLDLVLGT WSGSIAIVQN LAESVVSNIP
DQSVAESSTK HGLFVDSESD LENLEGNDDI NKSDKLFSDI TQEANAEDVF TQTHDGPSGL
SEKRKYNFED EEDFIDDDDG AGYISGKKPH NEHSYSRVHK THSFPISLAN TGKFRYMPFS
PAGTPFGFTD RRYLTMNEVG YVSTVKNSEQ YSITVSFFDV GRFREYHFED LFGYDLCFLN
EKGTLFGQSK TGQIQYRPHD SIHSNWTKII PLQAGERITS VAATPVRVIV GTSLGYFRSF
NQFGVPFAVE KTSPIVALTA QNYRVFSVHY SQFHGLSYSL SELGTSSKRY YKRECPLPMS
LPNINSDMKK DANLDYYNFN PMGIKSLFFS SYGDPCIFGS DNTLLLLSKW RSPEESKWLP
ILDSNMEIWK MSGGKETTDI HVWPLALAYD TLNCILVKGK HIWPEFPLPL PSEMEIRMPV
FVKSKLLEEN KAILNKKNEI GADTEAEEGE EDKEIQIPVS MAAEEEYLRS KVLSELLTDT
LENDGEMYGN ENEVLAALNG AYDKALLRLF ASACSDQNVE KALSLAHELK QDRALTAAVK
ISERAELPSL VKKINNIREA RYEQQLK
