IST1_HUMAN
ID IST1_HUMAN Reviewed; 364 AA.
AC P53990; A8KAH5; J3QLU7; Q3SYM4; Q9BQ81; Q9BWN2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=IST1 homolog;
DE Short=hIST1;
DE AltName: Full=Charged multivesicular body protein 8 {ECO:0000303|PubMed:28242692};
DE Short=CHMP8 {ECO:0000303|PubMed:28242692};
DE AltName: Full=Putative MAPK-activating protein PM28;
GN Name=IST1; Synonyms=KIAA0174;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Testis, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Eye, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CHMP1A;
RP CHMP1B; VPS4A; VTA1; MITD1; STAMBP; SPAST AND USP8, AND MUTAGENESIS OF
RP 360-LEU-LYS-361.
RX PubMed=19129480; DOI=10.1091/mbc.e08-05-0474;
RA Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M.,
RA Ameer-Beg S., Bowers K., Martin-Serrano J.;
RT "Essential role of hIST1 in cytokinesis.";
RL Mol. Biol. Cell 20:1374-1387(2009).
RN [8]
RP FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH VPS37B;
RP VTA1; CHMP1A; CHMP1B; VPS4A AND VPS4B, INTERACTION WITH THE ESCRT-1
RP COMPLEX, AND MUTAGENESIS OF LEU-323; LEU-326; LEU-353 AND LEU-360.
RX PubMed=19129479; DOI=10.1091/mbc.e08-05-0475;
RA Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M.,
RA Sundquist W.I.;
RT "Biochemical analyses of human IST1 and its function in cytokinesis.";
RL Mol. Biol. Cell 20:1360-1373(2009).
RN [9]
RP INTERACTION WITH SPART, AND SUBCELLULAR LOCATION.
RX PubMed=20719964; DOI=10.1091/mbc.e09-10-0879;
RA Renvoise B., Parker R.L., Yang D., Bakowska J.C., Hurley J.H.,
RA Blackstone C.;
RT "SPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1
RT and participates in cytokinesis.";
RL Mol. Biol. Cell 21:3293-3303(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP INTERACTION WITH MITD1.
RX PubMed=23015756; DOI=10.1091/mbc.e12-04-0292;
RA Lee S., Chang J., Renvoise B., Tipirneni A., Yang S., Blackstone C.;
RT "MITD1 is recruited to midbodies by ESCRT-III and participates in
RT cytokinesis.";
RL Mol. Biol. Cell 23:4347-4361(2012).
RN [13]
RP IDENTIFICATION BY MASS 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 [14]
RP FUNCTION, AND INTERACTION WITH SPAST.
RX PubMed=23897888; DOI=10.1083/jcb.201211045;
RA Allison R., Lumb J.H., Fassier C., Connell J.W., Ten Martin D.,
RA Seaman M.N., Hazan J., Reid E.;
RT "An ESCRT-spastin interaction promotes fission of recycling tubules from
RT the endosome.";
RL J. Cell Biol. 202:527-543(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPAST.
RX PubMed=26040712; DOI=10.1038/nature14408;
RA Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W.,
RA Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.;
RT "Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear
RT envelope sealing.";
RL Nature 522:231-235(2015).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28242692; DOI=10.1073/pnas.1613916114;
RA Gu M., LaJoie D., Chen O.S., von Appen A., Ladinsky M.S., Redd M.J.,
RA Nikolova L., Bjorkman P.J., Sundquist W.I., Ullman K.S., Frost A.;
RT "LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission
RT yeast and human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E2166-E2175(2017).
CC -!- FUNCTION: ESCRT-III-like protein involved in cytokinesis, nuclear
CC envelope reassembly and endosomal tubulation (PubMed:19129479,
CC PubMed:26040712, PubMed:28242692). Is required for efficient abscission
CC during cytokinesis (PubMed:19129479). Involved in recruiting VPS4A
CC and/or VPS4B to the midbody of dividing cells (PubMed:19129480,
CC PubMed:19129479). During late anaphase, involved in nuclear envelope
CC reassembly and mitotic spindle disassembly together with the ESCRT-III
CC complex: IST1 acts by mediating the recruitment of SPAST to the nuclear
CC membrane, leading to microtubule severing (PubMed:26040712). Recruited
CC to the reforming nuclear envelope (NE) during anaphase by LEMD2
CC (PubMed:28242692). Regulates early endosomal tubulation together with
CC the ESCRT-III complex by mediating the recruitment of SPAST
CC (PubMed:23897888). {ECO:0000269|PubMed:19129479,
CC ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:23897888,
CC ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}.
CC -!- SUBUNIT: Interacts with CHMP1A, CHMP1B, VPS4A and VTA1. Interacts with
CC SPAST, STAMBP, and USP8. May interact with VPS37B. May associate with
CC the ESCRT-I complex. Interacts with MITD1, in competition with VSP4
CC (PubMed:23015756). Interacts with SPART (via MIT domain); leading to
CC the recruitment of SPART to midbodies (PubMed:20719964). Interacts with
CC SPAST (PubMed:23897888, PubMed:26040712). {ECO:0000269|PubMed:19129479,
CC ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:20719964,
CC ECO:0000269|PubMed:23015756, ECO:0000269|PubMed:23897888,
CC ECO:0000269|PubMed:26040712}.
CC -!- INTERACTION:
CC P53990; P13798: APEH; NbExp=5; IntAct=EBI-945994, EBI-723792;
CC P53990; P54253: ATXN1; NbExp=2; IntAct=EBI-945994, EBI-930964;
CC P53990; Q7Z479: CAPN7; NbExp=3; IntAct=EBI-945994, EBI-10213454;
CC P53990; Q9Y6W3: CAPN7; NbExp=6; IntAct=EBI-945994, EBI-1765641;
CC P53990; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-945994, EBI-741480;
CC P53990-2; P54253: ATXN1; NbExp=6; IntAct=EBI-4402971, EBI-930964;
CC P53990-3; P13798: APEH; NbExp=3; IntAct=EBI-12188567, EBI-723792;
CC P53990-3; P54253: ATXN1; NbExp=9; IntAct=EBI-12188567, EBI-930964;
CC P53990-3; O95429: BAG4; NbExp=3; IntAct=EBI-12188567, EBI-2949658;
CC P53990-3; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-12188567, EBI-1057156;
CC P53990-3; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12188567, EBI-741480;
CC P53990-3; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12188567, EBI-947187;
CC P53990-4; Q7LBR1: CHMP1B; NbExp=3; IntAct=EBI-15788863, EBI-2118090;
CC P53990-4; P53990-4: IST1; NbExp=2; IntAct=EBI-15788863, EBI-15788863;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:19129479,
CC ECO:0000269|PubMed:19129480}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:20719964}. Midbody
CC {ECO:0000269|PubMed:20719964}. Nucleus envelope
CC {ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}.
CC Note=Localizes to centrosome and midbody of dividing cells
CC (PubMed:19129480, PubMed:19129479, PubMed:20719964). Colocalized with
CC SPART to the ends of Flemming bodies during cytokinesis
CC (PubMed:20719964). Localizes to the reforming nuclear envelope on
CC chromatin disks during late anaphase. {ECO:0000269|PubMed:19129479,
CC ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:20719964,
CC ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P53990-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53990-2; Sequence=VSP_017118, VSP_017119;
CC Name=5;
CC IsoId=P53990-5; Sequence=VSP_047075, VSP_047076;
CC Name=4;
CC IsoId=P53990-4; Sequence=VSP_017118;
CC Name=3;
CC IsoId=P53990-3; Sequence=VSP_017118, VSP_017120;
CC Name=6;
CC IsoId=P53990-6; Sequence=VSP_055118, VSP_017118;
CC -!- SIMILARITY: Belongs to the IST1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11491.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB097052; BAC77405.1; -; mRNA.
DR EMBL; D79996; BAA11491.2; ALT_INIT; mRNA.
DR EMBL; AK057258; BAG51894.1; -; mRNA.
DR EMBL; AK293022; BAF85711.1; -; mRNA.
DR EMBL; AK293040; BAF85729.1; -; mRNA.
DR EMBL; AC009127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000116; AAH00116.1; -; mRNA.
DR EMBL; BC000430; AAH00430.1; -; mRNA.
DR EMBL; BC004359; AAH04359.1; -; mRNA.
DR EMBL; BC103745; AAI03746.1; -; mRNA.
DR CCDS; CCDS10905.1; -. [P53990-3]
DR CCDS; CCDS59271.1; -. [P53990-5]
DR CCDS; CCDS59272.1; -. [P53990-4]
DR CCDS; CCDS59273.1; -. [P53990-2]
DR CCDS; CCDS59274.1; -. [P53990-6]
DR RefSeq; NP_001257904.1; NM_001270975.1. [P53990-4]
DR RefSeq; NP_001257905.1; NM_001270976.1. [P53990-5]
DR RefSeq; NP_001257906.1; NM_001270977.1. [P53990-2]
DR RefSeq; NP_001257907.1; NM_001270978.1. [P53990-6]
DR RefSeq; NP_055576.2; NM_014761.3. [P53990-3]
DR PDB; 3FRR; X-ray; 1.80 A; A=1-189.
DR PDB; 3FRS; X-ray; 2.61 A; A=5-189.
DR PDB; 3JC1; EM; 4.00 A; Aa/Ac/Ae/Ag/Ai/Ak/Am/Ao/Aq/As/Au/Aw/Ay/Ba/Bc/Be/Bg/Bi/Bk/Bm/Bo/Bq/Bs/Bu/Bw/By/Ca/Cc/Ce/Cg=6-187.
DR PDB; 4U7E; X-ray; 1.60 A; A=341-364.
DR PDB; 4U7I; X-ray; 1.79 A; B=341-364.
DR PDB; 4U7Y; X-ray; 2.50 A; B=341-364.
DR PDB; 4WZX; X-ray; 1.39 A; E=342-364.
DR PDB; 6E8G; EM; 2.90 A; A/BA/BB/C/DA/DB/E/FA/FB/G/HA/HB/I/JA/JB/K/LA/LB/M/NA/NB/O/PA/PB/Q/RA/RB/S/TA/TB=1-364.
DR PDB; 6TZ4; EM; 3.20 A; 01/AA/AB/B/CA/CB/D/EA/EB/F/GA/GB/H/IA/IB/J/KA/KB/L/MA/MB/N/OA/OB/P/QA/QB/R/SA/SB=1-189.
DR PDB; 6TZ5; EM; 3.10 A; A/BA/BB/C/DA/DB/E/FA/FB/G/HA/HB/I/JA/JB/K/LA/LB/M/NA/NB/O/PA/PB/Q/RA/S/TA/V/VA=1-189.
DR PDB; 6TZA; EM; 7.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-189.
DR PDBsum; 3FRR; -.
DR PDBsum; 3FRS; -.
DR PDBsum; 3JC1; -.
DR PDBsum; 4U7E; -.
DR PDBsum; 4U7I; -.
DR PDBsum; 4U7Y; -.
DR PDBsum; 4WZX; -.
DR PDBsum; 6E8G; -.
DR PDBsum; 6TZ4; -.
DR PDBsum; 6TZ5; -.
DR PDBsum; 6TZA; -.
DR AlphaFoldDB; P53990; -.
DR SMR; P53990; -.
DR BioGRID; 115141; 91.
DR DIP; DIP-42546N; -.
DR IntAct; P53990; 39.
DR MINT; P53990; -.
DR STRING; 9606.ENSP00000438399; -.
DR GlyGen; P53990; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P53990; -.
DR MetOSite; P53990; -.
DR PhosphoSitePlus; P53990; -.
DR SwissPalm; P53990; -.
DR BioMuta; IST1; -.
DR DMDM; 1723119; -.
DR EPD; P53990; -.
DR jPOST; P53990; -.
DR MassIVE; P53990; -.
DR MaxQB; P53990; -.
DR PaxDb; P53990; -.
DR PeptideAtlas; P53990; -.
DR PRIDE; P53990; -.
DR ProteomicsDB; 1902; -.
DR ProteomicsDB; 56636; -. [P53990-1]
DR ProteomicsDB; 56637; -. [P53990-2]
DR ProteomicsDB; 56638; -. [P53990-3]
DR ProteomicsDB; 56639; -. [P53990-4]
DR Antibodypedia; 44614; 143 antibodies from 26 providers.
DR DNASU; 9798; -.
DR Ensembl; ENST00000329908.12; ENSP00000330408.8; ENSG00000182149.21. [P53990-3]
DR Ensembl; ENST00000378798.9; ENSP00000368075.5; ENSG00000182149.21. [P53990-2]
DR Ensembl; ENST00000378799.11; ENSP00000368076.6; ENSG00000182149.21. [P53990-4]
DR Ensembl; ENST00000535424.5; ENSP00000438399.1; ENSG00000182149.21. [P53990-5]
DR Ensembl; ENST00000538850.5; ENSP00000463711.1; ENSG00000182149.21. [P53990-6]
DR Ensembl; ENST00000541571.6; ENSP00000455860.1; ENSG00000182149.21. [P53990-4]
DR Ensembl; ENST00000544564.5; ENSP00000457844.1; ENSG00000182149.21. [P53990-4]
DR Ensembl; ENST00000606369.5; ENSP00000475853.1; ENSG00000182149.21. [P53990-6]
DR GeneID; 9798; -.
DR KEGG; hsa:9798; -.
DR MANE-Select; ENST00000378799.11; ENSP00000368076.6; NM_001270975.2; NP_001257904.1. [P53990-4]
DR UCSC; uc002fbk.3; human. [P53990-1]
DR CTD; 9798; -.
DR DisGeNET; 9798; -.
DR GeneCards; IST1; -.
DR HGNC; HGNC:28977; IST1.
DR HPA; ENSG00000182149; Low tissue specificity.
DR MIM; 616434; gene.
DR neXtProt; NX_P53990; -.
DR OpenTargets; ENSG00000182149; -.
DR PharmGKB; PA142671633; -.
DR VEuPathDB; HostDB:ENSG00000182149; -.
DR eggNOG; KOG2027; Eukaryota.
DR GeneTree; ENSGT00390000007453; -.
DR InParanoid; P53990; -.
DR OrthoDB; 1302348at2759; -.
DR PhylomeDB; P53990; -.
DR TreeFam; TF314258; -.
DR PathwayCommons; P53990; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR SignaLink; P53990; -.
DR BioGRID-ORCS; 9798; 90 hits in 1076 CRISPR screens.
DR ChiTaRS; IST1; human.
DR EvolutionaryTrace; P53990; -.
DR GenomeRNAi; 9798; -.
DR Pharos; P53990; Tbio.
DR PRO; PR:P53990; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P53990; protein.
DR Bgee; ENSG00000182149; Expressed in left ovary and 205 other tissues.
DR ExpressionAtlas; P53990; baseline and differential.
DR Genevisible; P53990; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0090541; F:MIT domain binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0009838; P:abscission; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IMP:UniProtKB.
DR GO; GO:1904903; P:ESCRT III complex disassembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0036258; P:multivesicular body assembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; IEA:Ensembl.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0046745; P:viral capsid secondary envelopment; IDA:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; IDA:UniProtKB.
DR Gene3D; 1.20.1260.60; -; 1.
DR InterPro; IPR005061; Ist1.
DR InterPro; IPR042277; IST1-like.
DR PANTHER; PTHR12161; PTHR12161; 1.
DR Pfam; PF03398; Ist1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..364
FT /note="IST1 homolog"
FT /id="PRO_0000050727"
FT REGION 1..168
FT /note="Interaction with CHMP1A and CHMP1B"
FT REGION 64..279
FT /note="Interaction with VPS37B"
FT /evidence="ECO:0000269|PubMed:19129479"
FT REGION 190..364
FT /note="Interaction with VTA1"
FT REGION 294..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..364
FT /note="Interaction with VPS4A, VTA1, MITD1 STAMBP and USP8"
FT /evidence="ECO:0000269|PubMed:19129480"
FT MOTIF 321..332
FT /note="Type-2 MIT-interacting motif"
FT MOTIF 351..361
FT /note="MIT-interacting motif"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 43
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT VAR_SEQ 1..148
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_055118"
FT VAR_SEQ 1
FT /note="M -> MVFKLKTKEEQHSM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047075"
FT VAR_SEQ 228
FT /note="V -> VPM (in isoform 2, isoform 3, isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017118"
FT VAR_SEQ 237
FT /note="P -> PMP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047076"
FT VAR_SEQ 252..282
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017119"
FT VAR_SEQ 283..364
FT /note="VDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDNFVLPELPSVPDTLP
FT TASAGASTSASEDIDFDDLSRRFEELKKKT -> MTLMLIRISLLHRLLVLDPSQKPLQ
FT SFLPDLQITMTTLSYQSCHLCQTHYQLHLLVPAPQHLKTLTLMIFPGGLKS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017120"
FT MUTAGEN 323
FT /note="L->D: Diminishes interaction with VPS4A. Greatly
FT diminishes interaction with VPS4A; when associated with A-
FT 353."
FT /evidence="ECO:0000269|PubMed:19129479"
FT MUTAGEN 326
FT /note="L->D: Diminishes interaction with VPS4A. Greatly
FT diminishes interaction with VPS4A and abolishes interaction
FT with VTA1; when associated with A-353. Greatly diminishes
FT interaction with VPS4A; when associated with A-360."
FT /evidence="ECO:0000269|PubMed:19129479"
FT MUTAGEN 353
FT /note="L->A: Diminishes interaction with VPS4A. Greatly
FT diminishes interaction with VPS4A and abolishes interaction
FT with VTA1; when associated with D-326. Greatly diminishes
FT interaction with VPS4A; when associated with D-323."
FT /evidence="ECO:0000269|PubMed:19129479"
FT MUTAGEN 360..361
FT /note="LK->AA: Abolishes interaction with VTA1, MITD1 and
FT USP8; diminishes interaction with VPS4A."
FT /evidence="ECO:0000269|PubMed:19129480"
FT MUTAGEN 360
FT /note="L->A: Diminishes interaction with VPS4A. Greatly
FT diminishes interaction with VPS4A; when associated with D-
FT 326."
FT /evidence="ECO:0000269|PubMed:19129479"
FT HELIX 8..45
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 49..81
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:3FRR"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:3FRR"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:3FRR"
FT HELIX 350..360
FT /evidence="ECO:0007829|PDB:4WZX"
SQ SEQUENCE 364 AA; 39751 MW; 0DD3C186A52A4380 CRC64;
MLGSGFKAER LRVNLRLVIN RLKLLEKKKT ELAQKARKEI ADYLAAGKDE RARIRVEHII
REDYLVEAME ILELYCDLLL ARFGLIQSMK ELDSGLAESV STLIWAAPRL QSEVAELKIV
ADQLCAKYSK EYGKLCRTNQ IGTVNDRLMH KLSVEAPPKI LVERYLIEIA KNYNVPYEPD
SVVMAEAPPG VETDLIDVGF TDDVKKGGPG RGGSGGFTAP VGGPDGTVPM PMPMPMPSAN
TPFSYPLPKG PSDFNGLPMG TYQAFPNIHP PQIPATPPSY ESVDDINADK NISSAQIVGP
GPKPEASAKL PSRPADNYDN FVLPELPSVP DTLPTASAGA STSASEDIDF DDLSRRFEEL
KKKT
