UDS1_SCHPO
ID UDS1_SCHPO Reviewed; 1052 AA.
AC Q9P6S3; P78939; P78940; P78941; P78942;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Up-regulated during septation protein 1;
GN Name=uds1; ORFNames=SPBC27.04;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-1052.
RC STRAIN=972 / ATCC 24843;
RA Kohnosu A., Niwa O., Yano M., Saitoh S., Katayama T., Nagao K.,
RA Yanagida M.;
RT "S.pombe chromosome II cosmid 1228 sequence.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-52; SER-53; SER-57;
RP SER-59 AND THR-60, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20460254; DOI=10.1074/mcp.m110.000208;
RA Bicho C.C., de Lima Alves F., Chen Z.A., Rappsilber J., Sawin K.E.;
RT "A genetic engineering solution to the 'arginine conversion problem' in
RT stable isotope labeling by amino acids in cell culture (SILAC).";
RL Mol. Cell. Proteomics 9:1567-1577(2010).
CC -!- FUNCTION: Involved in septation. {ECO:0000269|PubMed:20460254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Cell tip
CC {ECO:0000269|PubMed:16823372}. Cell septum
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:20460254}.
CC -!- INDUCTION: Expression is increased between late G2 and G1/S.
CC {ECO:0000269|PubMed:20460254}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA12189.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA12190.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA12191.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA12192.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB89004.1; -; Genomic_DNA.
DR EMBL; D83992; BAA12189.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D83992; BAA12190.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D83992; BAA12191.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D83992; BAA12192.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_595659.1; NM_001021553.1.
DR AlphaFoldDB; Q9P6S3; -.
DR SMR; Q9P6S3; -.
DR BioGRID; 277025; 8.
DR STRING; 4896.SPBC27.04.1; -.
DR iPTMnet; Q9P6S3; -.
DR MaxQB; Q9P6S3; -.
DR PaxDb; Q9P6S3; -.
DR PRIDE; Q9P6S3; -.
DR EnsemblFungi; SPBC27.04.1; SPBC27.04.1:pep; SPBC27.04.
DR GeneID; 2540497; -.
DR KEGG; spo:SPBC27.04; -.
DR PomBase; SPBC27.04; uds1.
DR VEuPathDB; FungiDB:SPBC27.04; -.
DR HOGENOM; CLU_290729_0_0_1; -.
DR InParanoid; Q9P6S3; -.
DR OMA; NACEGIN; -.
DR PhylomeDB; Q9P6S3; -.
DR PRO; PR:Q9P6S3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0140278; P:mitotic division septum assembly; IEP:PomBase.
DR InterPro; IPR029191; Uds1.
DR Pfam; PF15456; Uds1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1052
FT /note="Up-regulated during septation protein 1"
FT /id="PRO_0000116855"
FT REGION 616..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 201..206
FT /note="ESATGF -> MAYLDH (in Ref. 2; BAA12192)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="F -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="N -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="L -> V (in Ref. 2; BAA12191)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="F -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="N -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="F -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="K -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1052 AA; 118263 MW; 837B3DEE12C993D0 CRC64;
MGFHGCLSTD EYEPELIEKY GNPEPPSSSI LINTRPVNPF LSTFVYVGKA SSSEDVSIST
GEEEMRTLLV ASAVKDAKGW VYLSGKDVEE IKQKIKNLQG LLGVSIKKLA VEAKIREAAK
NLMVAQAKEK KGKHKQSTIE HYEQCSRRVR ELSSKIWLIE RKLAEFYMHL LKHMVAVCIA
ELKPGSCSKV SSPVSAITAD ESATGFRDEE IMNNEEIEQL VERMSRILEI AQSMGNSIRE
PSVLDAVQMN AGERLLEQVR HLELILKQIY EKKLEEDADA KDIAPRAIVN FWRLLTELFR
GDNDTPEKSN ALPDDELDKH LKSDFDIESF CFLLHHLLSL YQTQKKELAS SNELLASVRD
ENTKKLKELQ DIIEEQSKHM ARLHREGFSE AAENNDKPKE TMPCTYDSSL ADDHSDTSNL
SKDKANTLCA QCSVYLSEKY QQQQSLLQLE SNIQQLENEK KAAKLIEKDL LSQISHVKLQ
FEQQIKAHHY AKDQVRNLND EMVALRAELE VVKAMNSQPD DPDSDYAIKQ NNALQNRLEA
LTRENELLQS RVTTLEMEKE VQEKNSATVS NLTLKQLQME NIFASLNLEN SFDFGMPLMG
PYTQQNLQLE DEISEISSPS YSSDDDRKTI SETQPAPKQN INEEFENSTS TDGSETNKNE
QGNSLSTPDN EPRLRKESLS SDVLLDGSEK PAQAELTINS ENFPVDCSLP VQTGADVVVP
DTTDEEVITS EPVKLEQPIN ENSNVEEAEK DYQPSEKDDK SLIGGILSTV EMTQSTDVND
EIENTLTIPV EVEHSDNIDK GSEENDLGKE AVDEANNNQN DVLESVVVEQ STTTDDCENK
VYEGQMNDKN SSLDMVNACE GINQTAIGFV EKPDKVTELI DEAEENIDIS QDISMTETNA
VDDEVQAENS ILQDEVEETR QDDIEKDELE DIKEVKEDEN LTTLEETIEI PANDIEVQDP
EQCSCMNSTE NDNITTENSS EIVQVIHTED DSLHFDDNVS TDSVSLGNKS RISMDSMRND
CEAFLPKKEK FGSLRTLHSF ESSMRRVSTS AA
