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IST1 homolog (hIST1) (Putative MAPK-activating protein PM28)

 IST1_HUMAN              Reviewed;         364 AA.
P53990; A8KAH5; J3QLU7; Q3SYM4; Q9BQ81; Q9BWN2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-OCT-2018, entry version 157.
RecName: Full=IST1 homolog;
Short=hIST1;
AltName: Full=Putative MAPK-activating protein PM28;
Name=IST1; Synonyms=KIAA0174;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung fibroblast;
PubMed=12761501; DOI=10.1038/sj.onc.1206406;
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
Sugano S.;
"Large-scale identification and characterization of human genes that
activate NF-kappaB and MAPK signaling pathways.";
Oncogene 22:3307-3318(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
TISSUE=Testis, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
TISSUE=Eye, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[7]
FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH
CHMP1A; CHMP1B; VPS4A; VTA1; MITD1; STAMBP; SPAST AND USP8, AND
MUTAGENESIS OF 360-LEU-LYS-361.
PubMed=19129480; DOI=10.1091/mbc.E08-05-0474;
Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M.,
Ameer-Beg S., Bowers K., Martin-Serrano J.;
"Essential role of hIST1 in cytokinesis.";
Mol. Biol. Cell 20:1374-1387(2009).
[8]
FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH
VPS37B; VTA1; CHMP1A; CHMP1B; VPS4A AND VPS4B, INTERACTION WITH THE
ESCRT-1 COMPLEX, AND MUTAGENESIS OF LEU-323; LEU-326; LEU-353 AND
LEU-360.
PubMed=19129479; DOI=10.1091/mbc.E08-05-0475;
Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M.,
Sundquist W.I.;
"Biochemical analyses of human IST1 and its function in cytokinesis.";
Mol. Biol. Cell 20:1360-1373(2009).
[9]
INTERACTION WITH SPART, AND SUBCELLULAR LOCATION.
PubMed=20719964; DOI=10.1091/mbc.E09-10-0879;
Renvoise B., Parker R.L., Yang D., Bakowska J.C., Hurley J.H.,
Blackstone C.;
"SPG20 protein spartin is recruited to midbodies by ESCRT-III protein
Ist1 and participates in cytokinesis.";
Mol. Biol. Cell 21:3293-3303(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
INTERACTION WITH MITD1.
PubMed=23015756; DOI=10.1091/mbc.E12-04-0292;
Lee S., Chang J., Renvoise B., Tipirneni A., Yang S., Blackstone C.;
"MITD1 is recruited to midbodies by ESCRT-III and participates in
cytokinesis.";
Mol. Biol. Cell 23:4347-4361(2012).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
FUNCTION, AND INTERACTION WITH SPAST.
PubMed=23897888; DOI=10.1083/jcb.201211045;
Allison R., Lumb J.H., Fassier C., Connell J.W., Ten Martin D.,
Seaman M.N., Hazan J., Reid E.;
"An ESCRT-spastin interaction promotes fission of recycling tubules
from the endosome.";
J. Cell Biol. 202:527-543(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPAST.
PubMed=26040712; DOI=10.1038/nature14408;
Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W.,
Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.;
"Spastin and ESCRT-III coordinate mitotic spindle disassembly and
nuclear envelope sealing.";
Nature 522:231-235(2015).
-!- FUNCTION: ESCRT-III-like protein involved in specific functions of
the ESCRT machinery. Is required for efficient abscission during
cytokinesis, but not for HIV-1 budding. The involvement in the MVB
pathway is not established. Involved in recruiting VPS4A and/or
VPS4B to the midbody of dividing cells (PubMed:19129479,
PubMed:19129480). During late anaphase, involved in nuclear
envelope reassembly and mitotic spindle disassembly together with
the ESCRT-III complex: IST1 acts by mediating the recruitment of
SPAST to the nuclear membrane, leading to microtubule severing
(PubMed:26040712). Regulates early endosomal tubulation together
with the ESCRT-III complex by mediating the recruitment of SPAST
(PubMed:23897888). {ECO:0000269|PubMed:19129479,
ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:23897888,
ECO:0000269|PubMed:26040712}.
-!- SUBUNIT: Interacts with CHMP1A, CHMP1B, VPS4A and VTA1. Interacts
with SPAST, STAMBP, and USP8. May interact with VPS37B. May
associate with the ESCRT-I complex. Interacts with MITD1, in
competition with VSP4 (PubMed:23015756). Interacts with SPART (via
MIT domain); leading to the recruitment of SPART to midbodies
(PubMed:20719964). Interacts with SPAST (PubMed:23897888,
PubMed:26040712). {ECO:0000269|PubMed:19129479,
ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:20719964,
ECO:0000269|PubMed:23015756, ECO:0000269|PubMed:23897888,
ECO:0000269|PubMed:26040712}.
-!- INTERACTION:
P13798:APEH; NbExp=4; IntAct=EBI-945994, EBI-723792;
P54253:ATXN1; NbExp=2; IntAct=EBI-945994, EBI-930964;
Q7Z479:CAPN7; NbExp=3; IntAct=EBI-945994, EBI-10213454;
Q9Y6W3:CAPN7; NbExp=6; IntAct=EBI-945994, EBI-1765641;
Q7LBR1:CHMP1B; NbExp=3; IntAct=EBI-15788863, EBI-2118090;
Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-945994, EBI-741480;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
{ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:20719964}. Midbody
{ECO:0000269|PubMed:20719964}. Nucleus envelope
{ECO:0000269|PubMed:26040712}. Note=Localizes to centrosome and
midbody of dividing cells (PubMed:19129480, PubMed:19129479,
PubMed:20719964). Colocalized with SPART to the ends of Flemming
bodies during cytokinesis (PubMed:20719964). Localizes to the
nuclear envelope during late anaphase (PubMed:26040712).
{ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480,
ECO:0000269|PubMed:20719964, ECO:0000269|PubMed:26040712}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=P53990-1; Sequence=Displayed;
Name=2;
IsoId=P53990-2; Sequence=VSP_017118, VSP_017119;
Note=No experimental confirmation available.;
Name=5;
IsoId=P53990-5; Sequence=VSP_047075, VSP_047076;
Name=4;
IsoId=P53990-4; Sequence=VSP_017118;
Name=3;
IsoId=P53990-3; Sequence=VSP_017118, VSP_017120;
Note=No experimental confirmation available.;
Name=6;
IsoId=P53990-6; Sequence=VSP_055118, VSP_017118;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- SIMILARITY: Belongs to the IST1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA11491.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB097052; BAC77405.1; -; mRNA.
EMBL; D79996; BAA11491.2; ALT_INIT; mRNA.
EMBL; AK057258; BAG51894.1; -; mRNA.
EMBL; AK293022; BAF85711.1; -; mRNA.
EMBL; AK293040; BAF85729.1; -; mRNA.
EMBL; AC009127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000116; AAH00116.1; -; mRNA.
EMBL; BC000430; AAH00430.1; -; mRNA.
EMBL; BC004359; AAH04359.1; -; mRNA.
EMBL; BC103745; AAI03746.1; -; mRNA.
CCDS; CCDS10905.1; -. [P53990-3]
CCDS; CCDS59271.1; -. [P53990-5]
CCDS; CCDS59272.1; -. [P53990-4]
CCDS; CCDS59273.1; -. [P53990-2]
CCDS; CCDS59274.1; -. [P53990-6]
RefSeq; NP_001257904.1; NM_001270975.1. [P53990-4]
RefSeq; NP_001257905.1; NM_001270976.1. [P53990-5]
RefSeq; NP_001257906.1; NM_001270977.1. [P53990-2]
RefSeq; NP_001257907.1; NM_001270978.1. [P53990-6]
RefSeq; NP_055576.2; NM_014761.3. [P53990-3]
UniGene; Hs.232194; -.
PDB; 3FRR; X-ray; 1.80 A; A=1-189.
PDB; 3FRS; X-ray; 2.61 A; A=5-189.
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.
PDB; 4U7E; X-ray; 1.60 A; A=341-364.
PDB; 4U7I; X-ray; 1.79 A; B=341-364.
PDB; 4U7Y; X-ray; 2.50 A; B=341-364.
PDB; 4WZX; X-ray; 1.39 A; E=342-364.
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.
PDBsum; 3FRR; -.
PDBsum; 3FRS; -.
PDBsum; 3JC1; -.
PDBsum; 4U7E; -.
PDBsum; 4U7I; -.
PDBsum; 4U7Y; -.
PDBsum; 4WZX; -.
PDBsum; 6E8G; -.
ProteinModelPortal; P53990; -.
SMR; P53990; -.
BioGrid; 115141; 49.
DIP; DIP-42546N; -.
IntAct; P53990; 31.
MINT; P53990; -.
STRING; 9606.ENSP00000330408; -.
iPTMnet; P53990; -.
PhosphoSitePlus; P53990; -.
SwissPalm; P53990; -.
DMDM; 1723119; -.
EPD; P53990; -.
MaxQB; P53990; -.
PaxDb; P53990; -.
PeptideAtlas; P53990; -.
PRIDE; P53990; -.
ProteomicsDB; 56636; -.
ProteomicsDB; 56637; -. [P53990-2]
ProteomicsDB; 56638; -. [P53990-3]
ProteomicsDB; 56639; -. [P53990-4]
DNASU; 9798; -.
Ensembl; ENST00000329908; ENSP00000330408; ENSG00000182149. [P53990-3]
Ensembl; ENST00000378798; ENSP00000368075; ENSG00000182149. [P53990-2]
Ensembl; ENST00000378799; ENSP00000368076; ENSG00000182149. [P53990-4]
Ensembl; ENST00000535424; ENSP00000438399; ENSG00000182149. [P53990-5]
Ensembl; ENST00000538850; ENSP00000463711; ENSG00000182149. [P53990-6]
Ensembl; ENST00000541571; ENSP00000455860; ENSG00000182149. [P53990-4]
Ensembl; ENST00000544564; ENSP00000457844; ENSG00000182149. [P53990-4]
Ensembl; ENST00000606369; ENSP00000475853; ENSG00000182149. [P53990-6]
GeneID; 9798; -.
KEGG; hsa:9798; -.
UCSC; uc002fbk.3; human. [P53990-1]
CTD; 9798; -.
DisGeNET; 9798; -.
EuPathDB; HostDB:ENSG00000182149.20; -.
GeneCards; IST1; -.
HGNC; HGNC:28977; IST1.
HPA; HPA041802; -.
HPA; HPA054532; -.
MIM; 616434; gene.
neXtProt; NX_P53990; -.
OpenTargets; ENSG00000182149; -.
PharmGKB; PA142671633; -.
eggNOG; KOG2027; Eukaryota.
eggNOG; ENOG410YG52; LUCA.
GeneTree; ENSGT00390000007453; -.
HOGENOM; HOG000205346; -.
HOVERGEN; HBG052171; -.
InParanoid; P53990; -.
KO; K19476; -.
OMA; DVKKGGP; -.
OrthoDB; EOG091G0CZX; -.
PhylomeDB; P53990; -.
TreeFam; TF314258; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; IST1; human.
EvolutionaryTrace; P53990; -.
GenomeRNAi; 9798; -.
PMAP-CutDB; P53990; -.
PRO; PR:P53990; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000182149; Expressed in 235 organ(s), highest expression level in left lobe of thyroid gland.
CleanEx; HS_KIAA0174; -.
ExpressionAtlas; P53990; baseline and differential.
Genevisible; P53990; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0090541; F:MIT domain binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
GO; GO:0009838; P:abscission; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IMP:UniProtKB.
GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IMP:UniProtKB.
GO; GO:1904903; P:ESCRT III complex disassembly; NAS:ParkinsonsUK-UCL.
GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
GO; GO:0036258; P:multivesicular body assembly; NAS:ParkinsonsUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0048672; P:positive regulation of collateral sprouting; IEA:Ensembl.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB.
GO; GO:0008104; P:protein localization; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:InterPro.
GO; GO:0046745; P:viral capsid secondary envelopment; IDA:UniProtKB.
GO; GO:0019076; P:viral release from host cell; IDA:UniProtKB.
InterPro; IPR005061; Ist1.
PANTHER; PTHR12161; PTHR12161; 1.
Pfam; PF03398; Ist1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 364 IST1 homolog.
/FTId=PRO_0000050727.
REGION 1 168 Interaction with CHMP1A and CHMP1B.
REGION 64 279 Interaction with VPS37B.
{ECO:0000269|PubMed:19129479}.
REGION 190 364 Interaction with VTA1.
REGION 348 364 Interaction with VPS4A, VTA1, MITD1
STAMBP and USP8.
{ECO:0000269|PubMed:19129480}.
MOTIF 321 332 Type-2 MIT-interacting motif.
MOTIF 351 361 MIT-interacting motif.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 43 43 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
VAR_SEQ 1 148 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_055118.
VAR_SEQ 1 1 M -> MVFKLKTKEEQHSM (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047075.
VAR_SEQ 228 228 V -> VPM (in isoform 2, isoform 3,
isoform 4 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_017118.
VAR_SEQ 237 237 P -> PMP (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047076.
VAR_SEQ 252 282 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017119.
VAR_SEQ 283 364 VDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDNFVL
PELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
-> MTLMLIRISLLHRLLVLDPSQKPLQSFLPDLQITMTTL
SYQSCHLCQTHYQLHLLVPAPQHLKTLTLMIFPGGLKS
(in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017120.
MUTAGEN 323 323 L->D: Diminishes interaction with VPS4A.
Greatly diminishes interaction with
VPS4A; when associated with A-353.
{ECO:0000269|PubMed:19129479}.
MUTAGEN 326 326 L->D: Diminishes interaction with VPS4A.
Greatly diminishes interaction with VPS4A
and abolishes interaction with VTA1; when
associated with A-353. Greatly diminishes
interaction with VPS4A; when associated
with A-360.
{ECO:0000269|PubMed:19129479}.
MUTAGEN 353 353 L->A: Diminishes interaction with VPS4A.
Greatly diminishes interaction with VPS4A
and abolishes interaction with VTA1; when
associated with D-326. Greatly diminishes
interaction with VPS4A; when associated
with D-323.
{ECO:0000269|PubMed:19129479}.
MUTAGEN 360 361 LK->AA: Abolishes interaction with VTA1,
MITD1 and USP8; diminishes interaction
with VPS4A.
{ECO:0000269|PubMed:19129480}.
MUTAGEN 360 360 L->A: Diminishes interaction with VPS4A.
Greatly diminishes interaction with
VPS4A; when associated with D-326.
{ECO:0000269|PubMed:19129479}.
HELIX 8 45 {ECO:0000244|PDB:3FRR}.
HELIX 49 81 {ECO:0000244|PDB:3FRR}.
HELIX 83 87 {ECO:0000244|PDB:3FRR}.
HELIX 94 96 {ECO:0000244|PDB:3FRR}.
HELIX 97 110 {ECO:0000244|PDB:3FRR}.
TURN 111 113 {ECO:0000244|PDB:3FRR}.
HELIX 115 128 {ECO:0000244|PDB:3FRR}.
HELIX 130 137 {ECO:0000244|PDB:3FRR}.
TURN 138 141 {ECO:0000244|PDB:3FRR}.
HELIX 146 151 {ECO:0000244|PDB:3FRR}.
HELIX 159 173 {ECO:0000244|PDB:3FRR}.
HELIX 181 185 {ECO:0000244|PDB:3FRR}.
HELIX 350 360 {ECO:0000244|PDB:4WZX}.
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


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