CHM1B_HUMAN
ID CHM1B_HUMAN Reviewed; 199 AA.
AC Q7LBR1; Q96E89; Q9HD41;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Charged multivesicular body protein 1b;
DE AltName: Full=CHMP1.5;
DE AltName: Full=Chromatin-modifying protein 1b;
DE Short=CHMP1b;
DE AltName: Full=Vacuolar protein sorting-associated protein 46-2;
DE Short=Vps46-2;
DE Short=hVps46-2;
GN Name=CHMP1B; Synonyms=C18orf2;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11474171; DOI=10.1159/000056940;
RA Vuoristo J.T., Berrettini W.H., Ala-Kokko L.;
RT "C18orf2, a novel, highly conserved intronless gene within intron 5 of the
RT GNAL gene on chromosome 18p11.";
RL Cytogenet. Cell Genet. 93:19-22(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11559747; DOI=10.1242/jcs.114.13.2383;
RA Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.;
RT "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and
RT cell-cycle progression.";
RL J. Cell Sci. 114:2383-2393(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma, and Ovary;
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 [4]
RP INTERACTION WITH CHMP1A; VPS4A AND VPS4B.
RX PubMed=14505570; DOI=10.1016/s0092-8674(03)00714-1;
RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
RT "The protein network of HIV budding.";
RL Cell 114:701-713(2003).
RN [5]
RP FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH CHMP1A; CHMP2A AND VPS4A.
RX PubMed=14519844; DOI=10.1073/pnas.2133846100;
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RT "Divergent retroviral late-budding domains recruit vacuolar protein sorting
RT factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [6]
RP ERRATUM OF PUBMED:14519844.
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPAST.
RX PubMed=15537668; DOI=10.1093/hmg/ddi003;
RA Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E., Sanderson C.M.;
RT "The hereditary spastic paraplegia protein spastin interacts with the
RT ESCRT-III complex-associated endosomal protein CHMP1B.";
RL Hum. Mol. Genet. 14:19-38(2005).
RN [8]
RP INTERACTION WITH VPS4A.
RX PubMed=16174732; DOI=10.1073/pnas.0502165102;
RA Scott A., Gaspar J., Stuchell-Brereton M.D., Alam S.L., Skalicky J.J.,
RA Sundquist W.I.;
RT "Structure and ESCRT-III protein interactions of the MIT domain of human
RT VPS4A.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13813-13818(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH STAMBP.
RX PubMed=16730941; DOI=10.1016/j.ygeno.2006.04.003;
RA Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E.,
RA Sanderson C.M.;
RT "A systematic analysis of human CHMP protein interactions: additional MIT
RT domain-containing proteins bind to multiple components of the human ESCRT
RT III complex.";
RL Genomics 88:333-346(2006).
RN [10]
RP INTERACTION WITH VPS4A AND VPS4B, AND MUTAGENESIS OF LEU-192 AND LEU-195.
RX PubMed=17928862; DOI=10.1038/nature06172;
RA Stuchell-Brereton M.D., Skalicky J.J., Kieffer C., Karren M.A.,
RA Ghaffarian S., Sundquist W.I.;
RT "ESCRT-III recognition by VPS4 ATPases.";
RL Nature 449:740-744(2007).
RN [11]
RP INTERACTION WITH VTA1 AND VPS4B, AND MUTAGENESIS OF 158-ASP-GLU-159.
RX PubMed=18385515; DOI=10.1091/mbc.e07-12-1263;
RA Shim S., Merrill S.A., Hanson P.I.;
RT "Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications
RT for ESCRT-III disassembly.";
RL Mol. Biol. Cell 19:2661-2672(2008).
RN [12]
RP INTERACTION WITH IST1; VTA1; VPS4A; MITD1 AND STAMBP.
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 [13]
RP FUNCTION, AND INTERACTION WITH IST1.
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 [14]
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 [15]
RP INTERACTION WITH VPS4A.
RX PubMed=21543490; DOI=10.1128/jvi.02610-10;
RA Kuang Z., Seo E.J., Leis J.;
RT "Mechanism of inhibition of retrovirus release from cells by interferon-
RT induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
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 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 145-194 IN COMPLEX WITH SPAST,
RP SUBCELLULAR LOCATION, INTERACTION WITH VPS4A, AND MUTAGENESIS OF THR-178;
RP ALA-181; GLU-184; LEU-188 AND LEU-192.
RX PubMed=18997780; DOI=10.1038/nsmb.1512;
RA Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J., Blackstone C.,
RA Hurley J.H.;
RT "Structural basis for midbody targeting of spastin by the ESCRT-III protein
RT CHMP1B.";
RL Nat. Struct. Mol. Biol. 15:1278-1286(2008).
CC -!- FUNCTION: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III) which is
CC involved in multivesicular bodies (MVBs) formation and sorting of
CC endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome and mostly are delivered to lysosomes
CC enabling degradation of membrane proteins, such as stimulated growth
CC factor receptors, lysosomal enzymes and lipids. The MVB pathway appears
CC to require the sequential function of ESCRT-O, -I,-II and -III
CC complexes. ESCRT-III proteins mostly dissociate from the invaginating
CC membrane before the ILV is released. The ESCRT machinery also functions
CC in topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis and the budding of enveloped viruses
CC (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to
CC mediate the necessary vesicle extrusion and/or membrane fission
CC activities, possibly in conjunction with the AAA ATPase VPS4. Involved
CC in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to
CC the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent
CC virus release. {ECO:0000269|PubMed:14519844,
CC ECO:0000269|PubMed:19129479}.
CC -!- SUBUNIT: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III). ESCRT-III
CC components are thought to multimerize to form a flat lattice on the
CC perimeter membrane of the endosome. Several assembly forms of ESCRT-III
CC may exist that interact and act sequentially. Interacts with CHMP1A.
CC Interacts with VTA1; the interaction probably involves the open
CC conformation of CHMP1B. Interacts with CHMP2A. Interacts with VPS4A;
CC the interaction is direct. Interacts with VPS4B; the interaction is
CC direct. Interacts with SPAST (via MIT domain); the interaction is
CC direct. Interacts with IST1. Interacts with MITD1. Interacts with
CC STAMBP. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
CC ECO:0000269|PubMed:15537668, ECO:0000269|PubMed:16174732,
CC ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17928862,
CC ECO:0000269|PubMed:18385515, ECO:0000269|PubMed:18997780,
CC ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480,
CC ECO:0000269|PubMed:21543490}.
CC -!- INTERACTION:
CC Q7LBR1; Q7LBR1: CHMP1B; NbExp=3; IntAct=EBI-2118090, EBI-2118090;
CC Q7LBR1; P53990-4: IST1; NbExp=3; IntAct=EBI-2118090, EBI-15788863;
CC Q7LBR1; Q8WV92: MITD1; NbExp=3; IntAct=EBI-2118090, EBI-2691489;
CC Q7LBR1; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2118090, EBI-79165;
CC Q7LBR1; P62491: RAB11A; NbExp=3; IntAct=EBI-2118090, EBI-745098;
CC Q7LBR1; O75643: SNRNP200; NbExp=3; IntAct=EBI-2118090, EBI-1045395;
CC Q7LBR1; O95630: STAMBP; NbExp=21; IntAct=EBI-2118090, EBI-396676;
CC Q7LBR1; P40818: USP8; NbExp=5; IntAct=EBI-2118090, EBI-1050865;
CC Q7LBR1; Q9UN37: VPS4A; NbExp=4; IntAct=EBI-2118090, EBI-1171942;
CC Q7LBR1; Q9NP79: VTA1; NbExp=3; IntAct=EBI-2118090, EBI-740160;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome. Late endosome
CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC Note=Localizes to the midbody of dividing cells, colocalizing with
CC CEP55 and CHMP5. Localized at the periphery of the Fleming body.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in pancreas, kidney,
CC skeletal muscle, liver, lung, placenta and brain.
CC {ECO:0000269|PubMed:11474171}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG01449.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF306520; AAL48200.1; -; Genomic_DNA.
DR EMBL; AF281064; AAG01449.1; ALT_INIT; mRNA.
DR EMBL; BC065933; AAH65933.1; -; mRNA.
DR EMBL; BC012733; AAH12733.3; -; mRNA.
DR CCDS; CCDS54180.1; -.
DR RefSeq; NP_065145.2; NM_020412.4.
DR PDB; 3EAB; X-ray; 2.50 A; G/H/I/J/K/L=148-197.
DR PDB; 3JC1; EM; 4.00 A; Ab/Ad/Af/Ah/Aj/Al/An/Ap/Ar/At/Av/Ax/Az/Bb/Bd/Bf/Bh/Bj/Bl/Bn/Bp/Br/Bt/Bv/Bx/Bz/Cb/Cd/Cf/Ch=4-163.
DR PDB; 4TXQ; X-ray; 2.21 A; C/D=176-199.
DR PDB; 4TXR; X-ray; 1.00 A; B=176-199.
DR PDB; 6E8G; EM; 2.90 A; 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/T=1-199.
DR PDB; 6TZ4; EM; 3.20 A; 02/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=1-199.
DR PDB; 6TZ5; EM; 3.10 A; 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/T/UA=1-199.
DR PDB; 6TZ9; EM; 6.20 A; A/AA/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/X/Y/Z=1-199.
DR PDBsum; 3EAB; -.
DR PDBsum; 3JC1; -.
DR PDBsum; 4TXQ; -.
DR PDBsum; 4TXR; -.
DR PDBsum; 6E8G; -.
DR PDBsum; 6TZ4; -.
DR PDBsum; 6TZ5; -.
DR PDBsum; 6TZ9; -.
DR AlphaFoldDB; Q7LBR1; -.
DR SMR; Q7LBR1; -.
DR BioGRID; 121394; 43.
DR ComplexPortal; CPX-329; ESCRT-III complex.
DR CORUM; Q7LBR1; -.
DR DIP; DIP-48534N; -.
DR IntAct; Q7LBR1; 41.
DR MINT; Q7LBR1; -.
DR STRING; 9606.ENSP00000432279; -.
DR iPTMnet; Q7LBR1; -.
DR PhosphoSitePlus; Q7LBR1; -.
DR BioMuta; CHMP1B; -.
DR DMDM; 73917735; -.
DR EPD; Q7LBR1; -.
DR jPOST; Q7LBR1; -.
DR MassIVE; Q7LBR1; -.
DR MaxQB; Q7LBR1; -.
DR PaxDb; Q7LBR1; -.
DR PeptideAtlas; Q7LBR1; -.
DR PRIDE; Q7LBR1; -.
DR ProteomicsDB; 68850; -.
DR Antibodypedia; 54046; 117 antibodies from 23 providers.
DR DNASU; 57132; -.
DR Ensembl; ENST00000526991.3; ENSP00000432279.1; ENSG00000255112.3.
DR GeneID; 57132; -.
DR KEGG; hsa:57132; -.
DR MANE-Select; ENST00000526991.3; ENSP00000432279.1; NM_020412.5; NP_065145.2.
DR UCSC; uc002kqe.4; human.
DR CTD; 57132; -.
DR DisGeNET; 57132; -.
DR GeneCards; CHMP1B; -.
DR HGNC; HGNC:24287; CHMP1B.
DR HPA; ENSG00000255112; Tissue enriched (skeletal).
DR MIM; 606486; gene.
DR neXtProt; NX_Q7LBR1; -.
DR OpenTargets; ENSG00000255112; -.
DR PharmGKB; PA142672110; -.
DR VEuPathDB; HostDB:ENSG00000255112; -.
DR eggNOG; KOG3232; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_080826_0_1_1; -.
DR InParanoid; Q7LBR1; -.
DR OMA; VMDRFET; -.
DR OrthoDB; 1441797at2759; -.
DR PhylomeDB; Q7LBR1; -.
DR TreeFam; TF300076; -.
DR PathwayCommons; Q7LBR1; -.
DR SignaLink; Q7LBR1; -.
DR SIGNOR; Q7LBR1; -.
DR BioGRID-ORCS; 57132; 17 hits in 1080 CRISPR screens.
DR EvolutionaryTrace; Q7LBR1; -.
DR GeneWiki; CHMP1B; -.
DR GenomeRNAi; 57132; -.
DR Pharos; Q7LBR1; Tbio.
DR PRO; PR:Q7LBR1; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q7LBR1; protein.
DR Bgee; ENSG00000255112; Expressed in gastrocnemius and 195 other tissues.
DR Genevisible; Q7LBR1; HS.
DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IDA:AgBase.
DR GO; GO:0000815; C:ESCRT III complex; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:ComplexPortal.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; IDA:ComplexPortal.
DR GO; GO:0030117; C:membrane coat; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:HPA.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; IDA:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0090541; F:MIT domain binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
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:1902774; P:late endosome to lysosome transport; IMP:ComplexPortal.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0036258; P:multivesicular body assembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0061763; P:multivesicular body-lysosome fusion; IC:ComplexPortal.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:ComplexPortal.
DR GO; GO:0031468; P:nuclear membrane reassembly; IMP:ComplexPortal.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; IDA:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0051469; P:vesicle fusion with vacuole; IC:ComplexPortal.
DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:ComplexPortal.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm; Endosome;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..199
FT /note="Charged multivesicular body protein 1b"
FT /id="PRO_0000211454"
FT REGION 132..156
FT /note="Interaction with IST1"
FT REGION 167..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..199
FT /note="Interaction with SPAST"
FT /evidence="ECO:0000269|PubMed:15537668"
FT REGION 180..199
FT /note="Interaction with VTA1"
FT REGION 180..196
FT /note="Interaction with VPS4A, MITD1 and STAMBP"
FT /evidence="ECO:0000269|PubMed:19129480"
FT REGION 183..199
FT /note="Interaction with VPS4B"
FT COILED 26..48
FT /evidence="ECO:0000255"
FT COILED 178..199
FT /evidence="ECO:0000255"
FT MOTIF 186..196
FT /note="MIT-interacting motif"
FT COMPBIAS 168..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 158..159
FT /note="DE->AA: Diminishes interaction with VPS4B."
FT /evidence="ECO:0000269|PubMed:18385515"
FT MUTAGEN 178
FT /note="T->R: Abolishes interaction with SPAST and no effect
FT on interaction with VPS4A; when associated with R-181 and
FT R-184."
FT /evidence="ECO:0000269|PubMed:18997780"
FT MUTAGEN 181
FT /note="A->R: Abolishes interaction with SPAScT and no
FT effect on interaction with VPS4A; when associated with R-
FT 178 and R-184."
FT /evidence="ECO:0000269|PubMed:18997780"
FT MUTAGEN 184
FT /note="E->A: Decreases interaction with SPAST."
FT /evidence="ECO:0000269|PubMed:18997780"
FT MUTAGEN 184
FT /note="E->R: Abolishes interaction with SPAST and no effect
FT on interaction with VPS4A; when associated with R-178 and
FT R-181."
FT /evidence="ECO:0000269|PubMed:18997780"
FT MUTAGEN 188
FT /note="L->A: Abolishes interaction with SPAST and VPS4A;
FT when associated with A-192."
FT /evidence="ECO:0000269|PubMed:18997780"
FT MUTAGEN 192
FT /note="L->A: Abolishes interaction with SPAST and VPS4A;
FT when associated with A-188."
FT /evidence="ECO:0000269|PubMed:17928862,
FT ECO:0000269|PubMed:18997780"
FT MUTAGEN 192
FT /note="L->A: Abolishes interaction with VPS4B."
FT /evidence="ECO:0000269|PubMed:17928862,
FT ECO:0000269|PubMed:18997780"
FT MUTAGEN 195
FT /note="L->A: Abolishes interaction with VPS4B."
FT /evidence="ECO:0000269|PubMed:17928862"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:3EAB"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:4TXR"
SQ SEQUENCE 199 AA; 22109 MW; 8071E94D20D85AB5 CRC64;
MSNMEKHLFN LKFAAKELSR SAKKCDKEEK AEKAKIKKAI QKGNMEVARI HAENAIRQKN
QAVNFLRMSA RVDAVAARVQ TAVTMGKVTK SMAGVVKSMD ATLKTMNLEK ISALMDKFEH
QFETLDVQTQ QMEDTMSSTT TLTTPQNQVD MLLQEMADEA GLDLNMELPQ GQTGSVGTSV
ASAEQDELSQ RLARLRDQV
