JNM1_YEAST
ID JNM1_YEAST Reviewed; 373 AA.
AC P36224; D6W0C1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Nuclear migration protein JNM1;
GN Name=JNM1; Synonyms=INS1; OrderedLocusNames=YMR294W;
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=8138567; DOI=10.1083/jcb.125.1.143;
RA McMillan J.N., Tatchell K.;
RT "The JNM1 gene in the yeast Saccharomyces cerevisiae is required for
RT nuclear migration and spindle orientation during the mitotic cell cycle.";
RL J. Cell Biol. 125:143-158(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 IDENTIFICATION IN THE DYNACTIN COMPLEX, AND FUNCTION OF THE DYNACTIN
RP COMPLEX.
RX PubMed=9658168; DOI=10.1091/mbc.9.7.1741;
RA Kahana J.A., Schlenstedt G., Evanchuk D.M., Geiser J.R., Hoyt M.A.,
RA Silver P.A.;
RT "The yeast dynactin complex is involved in partitioning the mitotic spindle
RT between mother and daughter cells during anaphase B.";
RL Mol. Biol. Cell 9:1741-1756(1998).
RN [5]
RP FUNCTION OF THE DYNACTIN COMPLEX.
RX PubMed=15311283; DOI=10.1038/ncb1162;
RA Suzuki M., Igarashi R., Sekiya M., Utsugi T., Morishita S., Yukawa M.,
RA Ohya Y.;
RT "Dynactin is involved in a checkpoint to monitor cell wall synthesis in
RT Saccharomyces cerevisiae.";
RL Nat. Cell Biol. 6:861-871(2004).
RN [6]
RP INTERACTION WITH ARP1.
RX PubMed=15975903; DOI=10.1091/mbc.e05-02-0093;
RA Clark S.W., Rose M.D.;
RT "Alanine scanning of Arp1 delineates a putative binding site for
RT Jnm1/dynamitin and Nip100/p150Glued.";
RL Mol. Biol. Cell 16:3999-4012(2005).
RN [7]
RP SELF-ASSOCIATION, AND INTERACTION WITH ARP1 AND ARP10.
RX PubMed=16291862; DOI=10.1091/mbc.e05-05-0449;
RA Clark S.W., Rose M.D.;
RT "Arp10p is a pointed-end-associated component of yeast dynactin.";
RL Mol. Biol. Cell 17:738-748(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, 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).
CC -!- FUNCTION: Component of the dynactin complex which assists cytoplasmic
CC dynein by increasing its processivity and by regulation of its cargo
CC binding (By similarity). The dynactin complex is required for the
CC spindle translocation late in anaphase and is involved in a cell wall
CC synthesis checkpoint. JNM1 is associated with the rod and links it to
CC the projecting sidearm. Required for proper nuclear migration during
CC the mitotic cell cycle and for astral microtubule development.
CC {ECO:0000250, ECO:0000269|PubMed:15311283, ECO:0000269|PubMed:9658168}.
CC -!- SUBUNIT: Component of the dynactin complex composed of at least ARP1,
CC JNM1, NIP100 and ARP10. Dynactin comprises a short rod of ARP1 polymers
CC attached to ARP10 at its pointed-end and probably associated with the
CC capping protein at its barbed-end. The rod structure is implicated in
CC dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1
CC filament and is implicated in motor binding (By similarity). Interacts
CC with ARP1. {ECO:0000250, ECO:0000269|PubMed:15975903,
CC ECO:0000269|PubMed:16291862, ECO:0000269|PubMed:9658168}.
CC -!- INTERACTION:
CC P36224; P38696: ARP1; NbExp=7; IntAct=EBI-9415, EBI-2920;
CC P36224; Q04549: ARP10; NbExp=3; IntAct=EBI-9415, EBI-2977;
CC P36224; P33420: NIP100; NbExp=2; IntAct=EBI-9415, EBI-12049;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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DR EMBL; Z25750; CAA81023.1; -; Genomic_DNA.
DR EMBL; X80836; CAA56803.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10195.1; -; Genomic_DNA.
DR PIR; S47455; S47455.
DR RefSeq; NP_014022.1; NM_001182802.1.
DR AlphaFoldDB; P36224; -.
DR SMR; P36224; -.
DR BioGRID; 35474; 432.
DR ComplexPortal; CPX-1805; Dynactin.
DR DIP; DIP-2387N; -.
DR IntAct; P36224; 7.
DR STRING; 4932.YMR294W; -.
DR iPTMnet; P36224; -.
DR MaxQB; P36224; -.
DR PaxDb; P36224; -.
DR PRIDE; P36224; -.
DR EnsemblFungi; YMR294W_mRNA; YMR294W; YMR294W.
DR GeneID; 855339; -.
DR KEGG; sce:YMR294W; -.
DR SGD; S000004908; JNM1.
DR VEuPathDB; FungiDB:YMR294W; -.
DR eggNOG; ENOG502S656; Eukaryota.
DR HOGENOM; CLU_063117_0_0_1; -.
DR InParanoid; P36224; -.
DR OMA; FKHIESD; -.
DR BioCyc; YEAST:G3O-32964-MON; -.
DR PRO; PR:P36224; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P36224; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005869; C:dynactin complex; IDA:SGD.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:SGD.
DR GO; GO:0030048; P:actin filament-based movement; IC:ComplexPortal.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IMP:SGD.
DR InterPro; IPR028133; Dynamitin.
DR PANTHER; PTHR15346; PTHR15346; 2.
DR Pfam; PF04912; Dynamitin; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..373
FT /note="Nuclear migration protein JNM1"
FT /id="PRO_0000084289"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 114..139
FT /evidence="ECO:0000255"
FT COILED 200..245
FT /evidence="ECO:0000255"
FT COILED 331..367
FT /evidence="ECO:0000255"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 92
FT /note="N -> S (in Ref. 1; CAA81023)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="K -> R (in Ref. 1; CAA81023)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="P -> A (in Ref. 1; CAA81023)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="D -> E (in Ref. 1; CAA81023)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="S -> N (in Ref. 1; CAA81023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 43607 MW; 80646B78B484AE56 CRC64;
MNVIDLSDPA INVDYDSLIG IDNEESQEIF ENEVKEDGQQ EEQEEASSRK DGLIVEPGRD
VESLRRAIRD QLLFKIHRQN QSDCADARKL SNDEEDESRQ QKLERIREEL EELKIENLTS
EMQTEIKELC EIQSKLATES SSRLTNLRKK LLETYEGQDT VILPNIILDT SNIKRLQKLD
QKISLMERFV GIPEALEAEE DRKSVHSKVN ELYRSIQLLQ GDDKAEGKLQ KFRDRLVELN
EEFENSLLGK KIQQDLRLKD DTVSKLVMPE NKVKEINSMY SMFKQYQDSL PLLAERMKSL
NKMNNRVIEV YETTKGLDSQ ITSIQEQGKV WLKALNELDK KFDEQEVKIR ENMEQIRRKI
DTLEDEALQR NSK
