Full text data of IST1
IST1
(KIAA0174)
[Confidence: low (only semi-automatic identification from reviews)]
IST1 homolog; hIST1 (Putative MAPK-activating protein PM28)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
IST1 homolog; hIST1 (Putative MAPK-activating protein PM28)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P53990
ID IST1_HUMAN Reviewed; 364 AA.
AC P53990; A8KAH5; Q3SYM4; Q9BQ81; Q9BWN2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=IST1 homolog;
DE Short=hIST1;
DE AltName: Full=Putative MAPK-activating protein PM28;
GN Name=IST1; Synonyms=KIAA0174;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
RT analysis of 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.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA 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.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH
RP CHMP1A; CHMP1B; VPS4A; VTA1; MITD1; STAMBP; SPAST AND USP8, AND
RP MUTAGENESIS OF 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 [7]
RP FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH
RP VPS37B; VTA1; CHMP1A; CHMP1B; VPS4A AND VPS4B, INTERACTION WITH THE
RP ESCRT-1 COMPLEX, AND MUTAGENESIS OF LEU-323; LEU-326; LEU-353 AND
RP 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 [8]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
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).
CC -!- FUNCTION: Proposed to be involved in specific functions of the
CC ESCRT machinery. Is required for efficient abscission during
CC cytokinesis, but not for HIV-1 budding. The involvement in the MVB
CC pathway is not established. Involved in recruiting VPS4A and/or
CC VPS4B to the midbody of dividing cells.
CC -!- SUBUNIT: Interacts with CHMP1A, CHMP1B, VPS4A and VTA1. Interacts
CC with SPAST, STAMBP, and USP8. May interact with VPS37B. May
CC associate with the ESCRT-I complex. Interacts with MITD1, in
CC competition with VSP4.
CC -!- INTERACTION:
CC P54253:ATXN1; NbExp=2; IntAct=EBI-945994, EBI-930964;
CC Q9Y6W3:CAPN7; NbExp=5; IntAct=EBI-945994, EBI-1765641;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Localizes to the
CC midbody of dividing cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P53990-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53990-2; Sequence=VSP_017118, VSP_017119;
CC Note=No experimental confirmation available;
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the IST1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11491.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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; BC000116; AAH00116.1; -; mRNA.
DR EMBL; BC000430; AAH00430.1; -; mRNA.
DR EMBL; BC004359; AAH04359.1; -; mRNA.
DR EMBL; BC103745; AAI03746.1; -; mRNA.
DR RefSeq; NP_001257904.1; NM_001270975.1.
DR RefSeq; NP_001257905.1; NM_001270976.1.
DR RefSeq; NP_001257906.1; NM_001270977.1.
DR RefSeq; NP_055576.2; NM_014761.3.
DR UniGene; Hs.232194; -.
DR PDB; 3FRR; X-ray; 1.80 A; A=1-189.
DR PDB; 3FRS; X-ray; 2.61 A; A=5-189.
DR PDBsum; 3FRR; -.
DR PDBsum; 3FRS; -.
DR ProteinModelPortal; P53990; -.
DR SMR; P53990; 2-187.
DR DIP; DIP-42546N; -.
DR IntAct; P53990; 6.
DR MINT; MINT-1461091; -.
DR STRING; 9606.ENSP00000330408; -.
DR PhosphoSite; P53990; -.
DR DMDM; 1723119; -.
DR PaxDb; P53990; -.
DR PRIDE; P53990; -.
DR DNASU; 9798; -.
DR Ensembl; ENST00000329908; ENSP00000330408; ENSG00000182149.
DR Ensembl; ENST00000378798; ENSP00000368075; ENSG00000182149.
DR Ensembl; ENST00000378799; ENSP00000368076; ENSG00000182149.
DR Ensembl; ENST00000535424; ENSP00000438399; ENSG00000182149.
DR Ensembl; ENST00000541571; ENSP00000455860; ENSG00000182149.
DR Ensembl; ENST00000544564; ENSP00000457844; ENSG00000182149.
DR GeneID; 9798; -.
DR KEGG; hsa:9798; -.
DR UCSC; uc010cgh.2; human.
DR CTD; 9798; -.
DR GeneCards; GC16P071930; -.
DR HGNC; HGNC:28977; IST1.
DR HPA; HPA041802; -.
DR neXtProt; NX_P53990; -.
DR PharmGKB; PA142671633; -.
DR eggNOG; NOG273475; -.
DR HOGENOM; HOG000205346; -.
DR InParanoid; P53990; -.
DR OMA; PTYESID; -.
DR ChiTaRS; IST1; human.
DR EvolutionaryTrace; P53990; -.
DR GenomeRNAi; 9798; -.
DR NextBio; 35464749; -.
DR PMAP-CutDB; P53990; -.
DR PRO; PR:P53990; -.
DR ArrayExpress; P53990; -.
DR Bgee; P53990; -.
DR CleanEx; HS_KIAA0174; -.
DR Genevestigator; P53990; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
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 vesicular exosome; IDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
DR GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
DR GO; GO:0009838; P:abscission; IDA:UniProtKB.
DR GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0046745; P:viral capsid secondary envelopment; IDA:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; IDA:UniProtKB.
DR InterPro; IPR005061; DUF292_euk.
DR Pfam; PF03398; Ist1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Complete proteome; Cytoplasmic vesicle; Reference proteome.
FT CHAIN 1 364 IST1 homolog.
FT /FTId=PRO_0000050727.
FT REGION 1 168 Interaction with CHMP1A and CHMP1B.
FT REGION 64 279 Interaction with VPS37B.
FT REGION 190 364 Interaction with VTA1.
FT REGION 348 364 Interaction with VPS4A, VTA1, MITD1
FT STAMBP and USP8.
FT MOTIF 321 332 Type-2 MIT-interacting motif.
FT MOTIF 351 361 MIT-interacting motif.
FT VAR_SEQ 1 1 M -> MVFKLKTKEEQHSM (in isoform 5).
FT /FTId=VSP_047075.
FT VAR_SEQ 228 228 V -> VPM (in isoform 2, isoform 3 and
FT isoform 4).
FT /FTId=VSP_017118.
FT VAR_SEQ 237 237 P -> PMP (in isoform 5).
FT /FTId=VSP_047076.
FT VAR_SEQ 252 282 Missing (in isoform 2).
FT /FTId=VSP_017119.
FT VAR_SEQ 283 364 VDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDNFVL
FT PELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
FT -> MTLMLIRISLLHRLLVLDPSQKPLQSFLPDLQITMTTL
FT SYQSCHLCQTHYQLHLLVPAPQHLKTLTLMIFPGGLKS
FT (in isoform 3).
FT /FTId=VSP_017120.
FT MUTAGEN 323 323 L->D: Diminishes interaction with VPS4A.
FT MUTAGEN 323 323 L->D: Greatly diminishes interaction with
FT VPS4A; when associated with A-353.
FT MUTAGEN 326 326 L->D: Diminishes interaction with VPS4A.
FT MUTAGEN 326 326 L->D: Greatly diminishes interaction with
FT VPS4A and abolishes interaction with
FT VTA1; when associated with A-353.
FT MUTAGEN 326 326 L->D: Greatly diminishes interaction with
FT VPS4A; when associated with A-360.
FT MUTAGEN 353 353 L->A: Diminishes interaction with VPS4A.
FT MUTAGEN 353 353 L->A: Greatly diminishes interaction with
FT VPS4A and abolishes interaction with
FT VTA1; when associated with D-326.
FT MUTAGEN 353 353 L->A: Greatly diminishes interaction with
FT VPS4A; when associated with D-323.
FT MUTAGEN 360 361 LK->AA: Abolishes interaction with VTA1,
FT MITD1 and USP8; diminishes interaction
FT with VPS4A.
FT MUTAGEN 360 360 L->A: Diminishes interaction with VPS4A.
FT MUTAGEN 360 360 L->A: Greatly diminishes interaction with
FT VPS4A; when associated with D-326.
FT HELIX 8 45
FT HELIX 49 81
FT HELIX 83 87
FT HELIX 94 96
FT HELIX 97 110
FT TURN 111 113
FT HELIX 115 128
FT HELIX 130 137
FT TURN 138 141
FT HELIX 146 151
FT HELIX 159 173
FT HELIX 181 185
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
//
ID IST1_HUMAN Reviewed; 364 AA.
AC P53990; A8KAH5; Q3SYM4; Q9BQ81; Q9BWN2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=IST1 homolog;
DE Short=hIST1;
DE AltName: Full=Putative MAPK-activating protein PM28;
GN Name=IST1; Synonyms=KIAA0174;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
RT analysis of 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.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA 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.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH
RP CHMP1A; CHMP1B; VPS4A; VTA1; MITD1; STAMBP; SPAST AND USP8, AND
RP MUTAGENESIS OF 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 [7]
RP FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH
RP VPS37B; VTA1; CHMP1A; CHMP1B; VPS4A AND VPS4B, INTERACTION WITH THE
RP ESCRT-1 COMPLEX, AND MUTAGENESIS OF LEU-323; LEU-326; LEU-353 AND
RP 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 [8]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
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).
CC -!- FUNCTION: Proposed to be involved in specific functions of the
CC ESCRT machinery. Is required for efficient abscission during
CC cytokinesis, but not for HIV-1 budding. The involvement in the MVB
CC pathway is not established. Involved in recruiting VPS4A and/or
CC VPS4B to the midbody of dividing cells.
CC -!- SUBUNIT: Interacts with CHMP1A, CHMP1B, VPS4A and VTA1. Interacts
CC with SPAST, STAMBP, and USP8. May interact with VPS37B. May
CC associate with the ESCRT-I complex. Interacts with MITD1, in
CC competition with VSP4.
CC -!- INTERACTION:
CC P54253:ATXN1; NbExp=2; IntAct=EBI-945994, EBI-930964;
CC Q9Y6W3:CAPN7; NbExp=5; IntAct=EBI-945994, EBI-1765641;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Localizes to the
CC midbody of dividing cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P53990-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53990-2; Sequence=VSP_017118, VSP_017119;
CC Note=No experimental confirmation available;
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the IST1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11491.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
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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; BC000116; AAH00116.1; -; mRNA.
DR EMBL; BC000430; AAH00430.1; -; mRNA.
DR EMBL; BC004359; AAH04359.1; -; mRNA.
DR EMBL; BC103745; AAI03746.1; -; mRNA.
DR RefSeq; NP_001257904.1; NM_001270975.1.
DR RefSeq; NP_001257905.1; NM_001270976.1.
DR RefSeq; NP_001257906.1; NM_001270977.1.
DR RefSeq; NP_055576.2; NM_014761.3.
DR UniGene; Hs.232194; -.
DR PDB; 3FRR; X-ray; 1.80 A; A=1-189.
DR PDB; 3FRS; X-ray; 2.61 A; A=5-189.
DR PDBsum; 3FRR; -.
DR PDBsum; 3FRS; -.
DR ProteinModelPortal; P53990; -.
DR SMR; P53990; 2-187.
DR DIP; DIP-42546N; -.
DR IntAct; P53990; 6.
DR MINT; MINT-1461091; -.
DR STRING; 9606.ENSP00000330408; -.
DR PhosphoSite; P53990; -.
DR DMDM; 1723119; -.
DR PaxDb; P53990; -.
DR PRIDE; P53990; -.
DR DNASU; 9798; -.
DR Ensembl; ENST00000329908; ENSP00000330408; ENSG00000182149.
DR Ensembl; ENST00000378798; ENSP00000368075; ENSG00000182149.
DR Ensembl; ENST00000378799; ENSP00000368076; ENSG00000182149.
DR Ensembl; ENST00000535424; ENSP00000438399; ENSG00000182149.
DR Ensembl; ENST00000541571; ENSP00000455860; ENSG00000182149.
DR Ensembl; ENST00000544564; ENSP00000457844; ENSG00000182149.
DR GeneID; 9798; -.
DR KEGG; hsa:9798; -.
DR UCSC; uc010cgh.2; human.
DR CTD; 9798; -.
DR GeneCards; GC16P071930; -.
DR HGNC; HGNC:28977; IST1.
DR HPA; HPA041802; -.
DR neXtProt; NX_P53990; -.
DR PharmGKB; PA142671633; -.
DR eggNOG; NOG273475; -.
DR HOGENOM; HOG000205346; -.
DR InParanoid; P53990; -.
DR OMA; PTYESID; -.
DR ChiTaRS; IST1; human.
DR EvolutionaryTrace; P53990; -.
DR GenomeRNAi; 9798; -.
DR NextBio; 35464749; -.
DR PMAP-CutDB; P53990; -.
DR PRO; PR:P53990; -.
DR ArrayExpress; P53990; -.
DR Bgee; P53990; -.
DR CleanEx; HS_KIAA0174; -.
DR Genevestigator; P53990; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
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 vesicular exosome; IDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
DR GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
DR GO; GO:0009838; P:abscission; IDA:UniProtKB.
DR GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0046745; P:viral capsid secondary envelopment; IDA:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; IDA:UniProtKB.
DR InterPro; IPR005061; DUF292_euk.
DR Pfam; PF03398; Ist1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Complete proteome; Cytoplasmic vesicle; Reference proteome.
FT CHAIN 1 364 IST1 homolog.
FT /FTId=PRO_0000050727.
FT REGION 1 168 Interaction with CHMP1A and CHMP1B.
FT REGION 64 279 Interaction with VPS37B.
FT REGION 190 364 Interaction with VTA1.
FT REGION 348 364 Interaction with VPS4A, VTA1, MITD1
FT STAMBP and USP8.
FT MOTIF 321 332 Type-2 MIT-interacting motif.
FT MOTIF 351 361 MIT-interacting motif.
FT VAR_SEQ 1 1 M -> MVFKLKTKEEQHSM (in isoform 5).
FT /FTId=VSP_047075.
FT VAR_SEQ 228 228 V -> VPM (in isoform 2, isoform 3 and
FT isoform 4).
FT /FTId=VSP_017118.
FT VAR_SEQ 237 237 P -> PMP (in isoform 5).
FT /FTId=VSP_047076.
FT VAR_SEQ 252 282 Missing (in isoform 2).
FT /FTId=VSP_017119.
FT VAR_SEQ 283 364 VDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDNFVL
FT PELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
FT -> MTLMLIRISLLHRLLVLDPSQKPLQSFLPDLQITMTTL
FT SYQSCHLCQTHYQLHLLVPAPQHLKTLTLMIFPGGLKS
FT (in isoform 3).
FT /FTId=VSP_017120.
FT MUTAGEN 323 323 L->D: Diminishes interaction with VPS4A.
FT MUTAGEN 323 323 L->D: Greatly diminishes interaction with
FT VPS4A; when associated with A-353.
FT MUTAGEN 326 326 L->D: Diminishes interaction with VPS4A.
FT MUTAGEN 326 326 L->D: Greatly diminishes interaction with
FT VPS4A and abolishes interaction with
FT VTA1; when associated with A-353.
FT MUTAGEN 326 326 L->D: Greatly diminishes interaction with
FT VPS4A; when associated with A-360.
FT MUTAGEN 353 353 L->A: Diminishes interaction with VPS4A.
FT MUTAGEN 353 353 L->A: Greatly diminishes interaction with
FT VPS4A and abolishes interaction with
FT VTA1; when associated with D-326.
FT MUTAGEN 353 353 L->A: Greatly diminishes interaction with
FT VPS4A; when associated with D-323.
FT MUTAGEN 360 361 LK->AA: Abolishes interaction with VTA1,
FT MITD1 and USP8; diminishes interaction
FT with VPS4A.
FT MUTAGEN 360 360 L->A: Diminishes interaction with VPS4A.
FT MUTAGEN 360 360 L->A: Greatly diminishes interaction with
FT VPS4A; when associated with D-326.
FT HELIX 8 45
FT HELIX 49 81
FT HELIX 83 87
FT HELIX 94 96
FT HELIX 97 110
FT TURN 111 113
FT HELIX 115 128
FT HELIX 130 137
FT TURN 138 141
FT HELIX 146 151
FT HELIX 159 173
FT HELIX 181 185
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
//