ID   ASE1_YEAST              Reviewed;         885 AA.
AC   P50275; D6W2C1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Anaphase spindle elongation protein;
GN   Name=ASE1; OrderedLocusNames=YOR058C; ORFNames=YOR29-09;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7559759; DOI=10.1083/jcb.130.6.1373;
RA   Pellman D., Bagget M., Tu Y.H., Fink G.R.;
RT   "Two microtubule-associated proteins required for anaphase spindle movement
RT   in Saccharomyces cerevisiae.";
RL   J. Cell Biol. 130:1373-1385(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9133743;
RX   DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA   Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT   "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT   presence of two tRNAs and 24 new open reading frames.";
RL   Yeast 13:379-390(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
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   [5]
RP   INTERACTION WITH CDC48.
RX   PubMed=14636562; DOI=10.1016/s0092-8674(03)00815-8;
RA   Cao K., Nakajima R., Meyer H.H., Zheng Y.;
RT   "The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of
RT   mitosis.";
RL   Cell 115:355-367(2003).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP   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: Required for anaphase spindle elongation.
CC       {ECO:0000269|PubMed:7559759}.
CC   -!- SUBUNIT: Interacts with CDC48; the interaction is likely to result in
CC       CDC5 degradation. {ECO:0000269|PubMed:14636562}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:7559759}.
CC   -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {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; U20235; AAA75026.1; -; Genomic_DNA.
DR   EMBL; Z74966; CAA99251.1; -; Genomic_DNA.
DR   EMBL; Z70678; CAA94543.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10837.1; -; Genomic_DNA.
DR   PIR; S59660; S59660.
DR   RefSeq; NP_116582.1; NM_001183477.1.
DR   AlphaFoldDB; P50275; -.
DR   SMR; P50275; -.
DR   BioGRID; 34456; 282.
DR   DIP; DIP-7343N; -.
DR   IntAct; P50275; 2.
DR   MINT; P50275; -.
DR   STRING; 4932.YOR058C; -.
DR   iPTMnet; P50275; -.
DR   MaxQB; P50275; -.
DR   PaxDb; P50275; -.
DR   PRIDE; P50275; -.
DR   TopDownProteomics; P50275; -.
DR   EnsemblFungi; YOR058C_mRNA; YOR058C; YOR058C.
DR   GeneID; 854223; -.
DR   KEGG; sce:YOR058C; -.
DR   SGD; S000005584; ASE1.
DR   VEuPathDB; FungiDB:YOR058C; -.
DR   eggNOG; KOG4302; Eukaryota.
DR   GeneTree; ENSGT00390000009453; -.
DR   HOGENOM; CLU_333226_0_0_1; -.
DR   InParanoid; P50275; -.
DR   OMA; NFKMELN; -.
DR   BioCyc; YEAST:G3O-33598-MON; -.
DR   PRO; PR:P50275; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P50275; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005874; C:microtubule; HDA:SGD.
DR   GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR   GO; GO:0005880; C:nuclear microtubule; IDA:SGD.
DR   GO; GO:0005819; C:spindle; IDA:SGD.
DR   GO; GO:0051233; C:spindle midzone; IDA:SGD.
DR   GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR   GO; GO:0000073; P:initial mitotic spindle pole body separation; IGI:SGD.
DR   GO; GO:0001578; P:microtubule bundle formation; IDA:SGD.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0000022; P:mitotic spindle elongation; IMP:SGD.
DR   GO; GO:0051256; P:mitotic spindle midzone assembly; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IMP:SGD.
DR   GO; GO:0000920; P:septum digestion after cytokinesis; IMP:SGD.
DR   GO; GO:0051255; P:spindle midzone assembly; IMP:SGD.
DR   InterPro; IPR007145; MAP65_Ase1_PRC1.
DR   PANTHER; PTHR19321; PTHR19321; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome.
FT   CHAIN           1..885
FT                   /note="Anaphase spindle elongation protein"
FT                   /id="PRO_0000064694"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   885 AA;  101624 MW;  6EDE11E887E89207 CRC64;
     METATSSPLP IKSRRNSENS GSTTVIPHMN PSLATPLTVS TMVNQSNSKE FMKLTPVRIR
     DFGSPLKNVS TNYHFLDSEN GKGNTMDNMY RENFILISKD LEKLLENLNV IYQNIGYSNT
     EIITKEKIIF TTISNSIKQF FEQADEELKR LSAENGIEQD ILNNILERIN DPSGIKTIPD
     LYIRNAILLQ ESKTVPQSPK KPLSLLSKKA ALDTAKKFVL GSFLPRLRDY LKSLITLKHL
     IQSVKENLPG LTEADNEAIA EFPELSTLTA YLLQIENGKG DIGLSMKFII DNRKDILKGS
     AFKTINEESV KHMNEVIKIY EEEYERRFKS VLTKKVSISS ICEQLGTPLA TLIGEDFEQD
     LRSYGEEENS TSEIPNFHPV DRERMSKIDI TLEKLQAIHK ERADKKRLLM EQCQKLWTRL
     KISQEYIKTF MRNNSSLSTE SLGRISKEVM RLEAMKKKLI KKLISDSWDK IQELWRTLQY
     SEESRSKFII VFEELRNSAT TLQEDELLLE TCENELKRLE EKLTLYKPIL KLISDFESLQ
     EDQEFLERSS KDSSRLLSRN SHKILLTEEK MRKRITRHFP RVINDLRIKL EEADGLFDQP
     FLFKGKPLSE AIDIQQQEIE AKYPRCRVRM QRSKKGKCGA NKENKVIKNT FKATESSIRV
     PIGLNLNDAN ITYKTPSKKT IQGLTKNDLS QENSLARHMQ GTTKLSSPNR RATRLLAPTV
     ISRNSKGNIE RPTLNRNRSS DLSSSPRINH THGEHAVKPR QLFPIPLNKV DTKGSHIPQL
     TKEKALELLK RSTGTTGKEN VRSPERKSSL EDYAQKLSSP YKEPEHSIYK LSMSPEGKFQ
     LNIQQKDIES GFDDTSMMED ENDKDFITWK NEQVSKLNGF SFTDI