ID   NIS1_YEAS7              Reviewed;         407 AA.
AC   A6ZS02;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Protein NIS1;
DE   AltName: Full=Jumonji domain interacting protein 1;
DE   AltName: Full=Neck protein interacting with septins protein 1;
GN   Name=NIS1; Synonyms=JIP1; ORFNames=SCY_4713;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: May be involved in a mitotic signaling network. Binds
CC       sumoylated proteins and may stabilize SUMO chains (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CBF2, GIS1, NAP1, PRM8, REI1, SHS1 and SMT3.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000250|UniProtKB:P53939}.
CC       Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P53939}.
CC   -!- INDUCTION: Expression is regulated by the ACE2 and SWI5 transcription
CC       factors. {ECO:0000250}.
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DR   EMBL; AAFW02000067; EDN62734.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZS02; -.
DR   EnsemblFungi; EDN62734; EDN62734; SCY_4713.
DR   HOGENOM; CLU_057191_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein.
FT   CHAIN           1..407
FT                   /note="Protein NIS1"
FT                   /id="PRO_0000320342"
FT   REGION          40..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           391..398
FT                   /note="SUMO-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        261..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         260
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53939"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53939"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53939"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53939"
SQ   SEQUENCE   407 AA;  45909 MW;  7920C0D160F15403 CRC64;
     METYETSIGT QSYPPTLFPP PLGTGGFTTS GYIHALVDST SNSNSNSNSN SNTNSNTNSN
     SDTKIPIVQI SDDSHITHDS FKPYMEYHDA SHLRNRNISK ADQVDSTEVM EQFTQWSNYK
     MRSRSPTINA KPIRHTSQRR TDFTSKNELS KFSKNHNFIF HKGFLKRQHS IRREDRQAKV
     RSRFRSKKEL TSVLNYIELE QMDIANVLAS QSVNLHAIRN LTSRDPAVTP IPFLRSQMYA
     TSSRPPYLRN RSIRRKLPKS QPGSLPTTTP ATATKTIKQN STTPTTRSVY NKNVGRSNTS
     PSVLYHPKRR GKLNTKSHAR KEQLLLELWR EYLMLVITQR TQLRLTLLCS PGSASNESSV
     CSSNASDLDM SLLSTPSSLF QMAGETKSNP IIIPDSQDDS ILSSDPF