SPD1_SCHPO
ID SPD1_SCHPO Reviewed; 124 AA.
AC Q10585;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=S-phase delaying protein 1;
DE AltName: Full=Protein p14;
GN Name=spd1; ORFNames=SPAC29B12.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH CDC22.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8887552; DOI=10.1002/j.1460-2075.1996.tb00838.x;
RA Woollard A., Basi G., Nurse P.;
RT "A novel S phase inhibitor in fission yeast.";
RL EMBO J. 15:4603-4612(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11069778; DOI=10.1242/jcs.113.23.4341;
RA Borgne A., Nurse P.;
RT "The Spd1p S phase inhibitor can activate the DNA replication checkpoint
RT pathway in fission yeast.";
RL J. Cell Sci. 113:4341-4350(2000).
RN [4]
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=12695334; DOI=10.1101/gad.1090803;
RA Liu C., Powell K.A., Mundt K., Wu L., Carr A.M., Caspari T.;
RT "Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by
RT both checkpoint-dependent and -independent mechanisms.";
RL Genes Dev. 17:1130-1140(2003).
RN [5]
RP UBIQUITINATION.
RX PubMed=14701809; DOI=10.1074/jbc.m312570200;
RA Bondar T., Ponomarev A., Raychaudhuri P.;
RT "Ddb1 is required for the proteolysis of the Schizosaccharomyces pombe
RT replication inhibitor Spd1 during S phase and after DNA damage.";
RL J. Biol. Chem. 279:9937-9943(2004).
RN [6]
RP UBIQUITINATION.
RX PubMed=16252005; DOI=10.1038/sj.emboj.7600854;
RA Liu C., Poitelea M., Watson A., Yoshida S.H., Shimoda C., Holmberg C.,
RA Nielsen O., Carr A.M.;
RT "Transactivation of Schizosaccharomyces pombe cdt2+ stimulates a Pcu4-Ddb1-
RT CSN ubiquitin ligase.";
RL EMBO J. 24:3940-3951(2005).
RN [7]
RP FUNCTION, AND INTERACTION WITH CDC22.
RX PubMed=16317005; DOI=10.1074/jbc.m511716200;
RA Hakansson P., Dahl L., Chilkova O., Domkin V., Thelander L.;
RT "The Schizosaccharomyces pombe replication inhibitor Spd1 regulates
RT ribonucleotide reductase activity and dNTPs by binding to the large Cdc22
RT subunit.";
RL J. Biol. Chem. 281:1778-1783(2006).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Regulates the ribonucleotide reductase activity through its
CC mediation of the nuclear localization of suc22, the small subunit of
CC the ribonucleotide reductase. Delays the progression of the G1-S phase
CC transition, thereby ensuring the G1 phase is complete. Interacts with
CC both p34 and the p34-p56 complex, although no direct inhibitory effect
CC on the bound proteins has been demonstrated. The action of p14 may
CC happen coincidentally with the cdc10 function or may happen downstream
CC of this. {ECO:0000269|PubMed:11069778, ECO:0000269|PubMed:12695334,
CC ECO:0000269|PubMed:16317005, ECO:0000269|PubMed:8887552}.
CC -!- SUBUNIT: Interacts with cdc22. {ECO:0000269|PubMed:16317005,
CC ECO:0000269|PubMed:8887552}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DEVELOPMENTAL STAGE: The levels peak in the G1 phase of the cell cycle,
CC then mostly disappear during S phase and reappear in the G2 phase.
CC -!- PTM: Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2)
CC complex, leading to its degradation. {ECO:0000269|PubMed:12695334,
CC ECO:0000269|PubMed:14701809, ECO:0000269|PubMed:16252005}.
CC -!- SIMILARITY: Belongs to the DIF1/spd1 family. {ECO:0000305}.
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DR EMBL; X98361; CAA67006.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16248.1; -; Genomic_DNA.
DR PIR; S71888; S71888.
DR RefSeq; NP_594981.1; NM_001020412.2.
DR PDB; 6QH1; X-ray; 2.90 A; D=29-38.
DR PDBsum; 6QH1; -.
DR AlphaFoldDB; Q10585; -.
DR SMR; Q10585; -.
DR BioGRID; 279149; 51.
DR IntAct; Q10585; 1.
DR STRING; 4896.SPAC29B12.03.1; -.
DR MaxQB; Q10585; -.
DR PaxDb; Q10585; -.
DR PRIDE; Q10585; -.
DR EnsemblFungi; SPAC29B12.03.1; SPAC29B12.03.1:pep; SPAC29B12.03.
DR GeneID; 2542696; -.
DR KEGG; spo:SPAC29B12.03; -.
DR PomBase; SPAC29B12.03; spd1.
DR VEuPathDB; FungiDB:SPAC29B12.03; -.
DR HOGENOM; CLU_2005232_0_0_1; -.
DR OMA; MEGTNER; -.
DR PRO; PR:Q10585; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:PomBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IGI:PomBase.
DR GO; GO:1990846; F:ribonucleoside-diphosphate reductase inhibitor activity; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1903529; P:negative regulation of dCDP biosynthetic process; IDA:PomBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:1905117; P:regulation of ribonucleoside-diphosphate reductase activity; IBA:GO_Central.
DR InterPro; IPR013900; RNR_inhibitor.
DR PANTHER; PTHR28081; PTHR28081; 1.
DR Pfam; PF08591; RNR_inhib; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..124
FT /note="S-phase delaying protein 1"
FT /id="PRO_0000072110"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:6QH1"
SQ SEQUENCE 124 AA; 14225 MW; F43A6C9D86F55F51 CRC64;
MHSSKRVMTT KTHVEQPESS MRPQLPESIQ GSLMDVGMRV RKSISTGYKS KQTTFPAYNP
PLYNTVSENI ALKNTAFSYE PNGTKRPFEQ AIPNYNWANP PQDFEEPEWL KPFDVVMEGT
NERL
