MHP1_YEAST
ID MHP1_YEAST Reviewed; 1398 AA.
AC P43638; D6VWE2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=MAP-homologous protein 1;
GN Name=MHP1; OrderedLocusNames=YJL042W; ORFNames=J1206;
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].
RX PubMed=8947554; DOI=10.1083/jcb.135.5.1323;
RA Irminger-Finger I., Hurt E., Roebuck A., Collart M.A., Edelstein S.J.;
RT "MHP1, an essential gene in Saccharomyces cerevisiae required for
RT microtubule function.";
RL J. Cell Biol. 135:1323-1339(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222 AND THR-577, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-311, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-311; SER-354; SER-357
RP AND THR-577, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Essential for the formation and/or stabilization of
CC microtubules. Binds to microtubules in vitro.
CC -!- INTERACTION:
CC P43638; P32598: GLC7; NbExp=5; IntAct=EBI-10880, EBI-13715;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle.
CC Note=Cytoplasmic microtubules and mitotic spindles.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X84652; CAA59145.1; -; Genomic_DNA.
DR EMBL; Z49317; CAA89333.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08758.1; -; Genomic_DNA.
DR PIR; S56814; S56814.
DR RefSeq; NP_012493.1; NM_001181475.1.
DR AlphaFoldDB; P43638; -.
DR SMR; P43638; -.
DR BioGRID; 33716; 124.
DR DIP; DIP-1260N; -.
DR IntAct; P43638; 8.
DR MINT; P43638; -.
DR STRING; 4932.YJL042W; -.
DR iPTMnet; P43638; -.
DR MaxQB; P43638; -.
DR PaxDb; P43638; -.
DR PRIDE; P43638; -.
DR EnsemblFungi; YJL042W_mRNA; YJL042W; YJL042W.
DR GeneID; 853408; -.
DR KEGG; sce:YJL042W; -.
DR SGD; S000003578; MHP1.
DR VEuPathDB; FungiDB:YJL042W; -.
DR eggNOG; ENOG502QYHN; Eukaryota.
DR HOGENOM; CLU_004492_1_0_1; -.
DR InParanoid; P43638; -.
DR OMA; TNTYFND; -.
DR BioCyc; YEAST:G3O-31507-MON; -.
DR PRO; PR:P43638; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P43638; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IDA:SGD.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:SGD.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Isopeptide bond; Microtubule;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1398
FT /note="MAP-homologous protein 1"
FT /id="PRO_0000072754"
FT REGION 21..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1258
FT /note="Tau/MAP repeat-like"
FT /evidence="ECO:0000305|PubMed:8947554"
FT REGION 1313..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 577
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 108
FT /note="R -> RV (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..184
FT /note="KSVVETNLSNVEADSGHHHHHRHHHHTEDAPAPKKVGFFKSLFGHRKKDQEQ
FT QEKERERKERSPSPTHVDRGA -> QWWRLTCLTLRLTPDIITTTATTITRKMLLHLRR
FT SDSLRVCLAIGRRIRNNRRRNEKGKSAHPLRLTWTVAR (in Ref. 1;
FT CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="K -> N (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="T -> Q (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 594..595
FT /note="ID -> MH (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="G -> A (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 659..660
FT /note="KQ -> NE (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 1175..1176
FT /note="LL -> FI (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 1309..1320
FT /note="KQGNQEETAFRT -> NRETKKRPRSEP (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 1339
FT /note="T -> S (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
FT CONFLICT 1356
FT /note="A -> H (in Ref. 1; CAA59145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1398 AA; 155207 MW; E7925D75D80E0E58 CRC64;
MDSKDTQKLL KEHRIPCIDV GWLVRPSAST SKSSRPGKSE SKANSVAPDI QMDTARPPVF
ETSVDSSSSI LSSNDKGRRH SVAASLLMDN QRANAGSTSV PTNIPPPRGR SKSVVETNLS
NVEADSGHHH HHRHHHHTED APAPKKVGFF KSLFGHRKKD QEQQEKERER KERSPSPTHV
DRGAAIRRER TATISAESPP PLQYNAPPSY NDTVVPLTRS KTESEVYYEN HPQSYYHGRM
RTYHSPEEGK VDGTSPADDH NYGGSRPDPR LMDFLRYYKS KDYKLAAFKE GNFIKSSASP
TTKKNRRASF SLHNDKPQPA KSLAHQKFDA KGRPIPPHPD APKLPSAFRK KHPSNASIVD
TVDSNSDVSS SAQNNNQTPS SHKFGAFLRK VTSYGNNNNN STNASSLSAN VNNPDTSSTS
LWSSSSMEFD PSKITTVPGL ENIRPLKHVS FATNTYFNDP PQQICSKNPR KGEVEVKPNG
SVVIHRLTPQ ERKKIMESTS LGVVVGGTGQ LKLLNPEEDD ANAKSKEEMA PQKQNEVEAH
DEEDNNSQRR NIVMAAAEAA AEARAKEAPN ELKRIVTNNE EEVTVSKTAS HLTIDKPMIS
RRGASTSSLA SMVSSDTNGT NADDEGEILP PPSLKIPHDI VYTRCCHLRE ILPIPATLKQ
LKKGSTDPIP ILQLRNPRPS MVEIWSFSDF LSIAPVLCLS LDGVQLTVQM LRIILSSLVY
KQHFQKLSLR NTPLDEEGWK VLCYFVSKAK SLHSIDLTMV PSIKTNVQKP SKSSLKSKIL
RMQCNLENRS DMNWDLLTAS IALMGGLEEI VISGAKMNSA QFKNFILVAC IATERLGLAY
NGLSKSQCDD LAKWMVQSKV TGLDVGFNDL NGKLSSFTDA VLGKIQKANE KNVFKFLSLN
GTNLRVNEHD TFENNEVLKL ISVLCYLENL KFLDISNNPA IFPHCVPTLI DFLPVFVNLV
RLHIDYNNLS STSVVMLAEI LPMCSRLNYF SMLGTELDLA SSKALAEAVR KSSSLMTLDV
DYVYMPENIK EKISLYALRN IQGELKRVNS DDKDIKDSQF SSLQDQLSLL LTEKADNSEH
YNKMVENFMA KIALARIKIS KVVHDLFDLK LNGQLNLEGK EALIRLCFIE ASLERGCDLL
KQRHNNTLKS PEAVSKSRKG GNQAQPNSES CQRMLLSSSI LQNSDHIALM PFGSAIVEKS
SPDAEDAVEF REGDDSNVNH EDVPANDQQF RDEVDIKNKY SIIKRELEHE KLVGGGDLPV
DKEILNRAAQ SLDSDQIKEF LLKNDVSTIL GVIDELHSQG YHLHHIFKKQ GNQEETAFRT
KDEQQSSQSN DSSANASPTT DPISTGSNTS RTNDNAHIPP TDAPGFDKFM NNAEENAIDA
AYDDVLDKIQ DARNSSTK
