CHM4C_HUMAN
ID CHM4C_HUMAN Reviewed; 233 AA.
AC Q96CF2; B2RBZ1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Charged multivesicular body protein 4c;
DE AltName: Full=Chromatin-modifying protein 4c;
DE Short=CHMP4c;
DE AltName: Full=SNF7 homolog associated with Alix 3;
DE AltName: Full=SNF7-3 {ECO:0000303|PubMed:14583093};
DE Short=hSnf7-3 {ECO:0000303|PubMed:14583093};
DE AltName: Full=Vacuolar protein sorting-associated protein 32-3;
DE Short=Vps32-3;
DE Short=hVps32-3;
GN Name=CHMP4C; Synonyms=SHAX3;
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 [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP PDCD6IP.
RX PubMed=14678797; DOI=10.1016/j.abb.2003.09.038;
RA Katoh K., Shibata H., Hatta K., Maki M.;
RT "CHMP4b is a major binding partner of the ALG-2-interacting protein Alix
RT among the three CHMP4 isoforms.";
RL Arch. Biochem. Biophys. 421:159-165(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH PDCD6IP.
RX PubMed=14583093; DOI=10.1042/bj20031347;
RA Peck J.W., Bowden E.T., Burbelo P.D.;
RT "Structure and function of human Vps20 and Snf7 proteins.";
RL Biochem. J. 377:693-700(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH PDCD6IP.
RX PubMed=14505569; DOI=10.1016/s0092-8674(03)00653-6;
RA Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.;
RT "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in
RT virus budding.";
RL Cell 114:689-699(2003).
RN [7]
RP FUNCTION IN HIV-1 BUDDING, SELF-ASSOCIATION, AND INTERACTION WITH CHMPC4A;
RP CHMPC4B; VPS4A AND PDCD6IP.
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 [8]
RP FUNCTION IN HIV-1 BUDDING, SELF-ASSOCIATION, AND INTERACTION WITH CHMP2A;
RP CHMP4A; CHMP4B; CHMP6 AND PDCD6IP.
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 [9]
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 [10]
RP FUNCTION.
RX PubMed=22660413; DOI=10.1038/ncb2502;
RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA David G.;
RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL Nat. Cell Biol. 14:677-685(2012).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-210, AND MUTAGENESIS
RP OF SER-210.
RX PubMed=22422861; DOI=10.1126/science.1217180;
RA Carlton J.G., Caballe A., Agromayor M., Kloc M., Martin-Serrano J.;
RT "ESCRT-III governs the Aurora B-mediated abscission checkpoint through
RT CHMP4C.";
RL Science 336:220-225(2012).
RN [12]
RP FUNCTION.
RX PubMed=24814515; DOI=10.1038/ncb2959;
RA Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K.,
RA Andersen J.S., Raiborg C., Stenmark H.;
RT "ANCHR mediates Aurora-B-dependent abscission checkpoint control through
RT retention of VPS4.";
RL Nat. Cell Biol. 16:550-560(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 221-233 IN COMPLEX WITH PDCD6IP.
RX PubMed=18511562; DOI=10.1073/pnas.0801567105;
RA McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.;
RT "ALIX-CHMP4 interactions in the human ESCRT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008).
CC -!- FUNCTION: Probable core component of the endosomal sorting required for
CC transport complex III (ESCRT-III) which is involved in multivesicular
CC bodies (MVBs) formation and sorting of endosomal cargo proteins into
CC MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by
CC invagination and scission from the limiting membrane of the endosome
CC and mostly are delivered to lysosomes enabling degradation of membrane
CC proteins, such as stimulated growth factor receptors, lysosomal enzymes
CC and lipids. The MVB pathway appears to require the sequential function
CC of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC dissociate from the invaginating membrane before the ILV is released.
CC The ESCRT machinery also functions in topologically equivalent membrane
CC fission events, such as the terminal stages of cytokinesis and the
CC budding of enveloped viruses (HIV-1 and other lentiviruses). Key
CC component of the cytokinesis checkpoint, a process required to delay
CC abscission to prevent both premature resolution of intercellular
CC chromosome bridges and accumulation of DNA damage: upon phosphorylation
CC by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent
CC VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission
CC checkpoint signaling is terminated at late cytokinesis. Deactivation of
CC AURKB results in dephosphorylation of CHMP4C followed by its
CC dissociation from ANCHR and VPS4 and subsequent abscission
CC (PubMed:22422861, PubMed:24814515). 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 HIV-1 p6- and p9-dependent virus release. CHMP4A/B/C are required
CC for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413).
CC {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570,
CC ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:22422861,
CC ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:24814515}.
CC -!- SUBUNIT: Probable core component of the endosomal sorting required for
CC transport complex III (ESCRT-III). ESCRT-III components are thought to
CC multimerize to form a flat lattice on the perimeter membrane of the
CC endosome. Several assembly forms of ESCRT-III may exist that interact
CC and act sequentially. Self-associates. Interacts with CHMP2A. Interacts
CC with CHMP4A. Interacts with CHMP4B. Interacts with CHMP6. Interacts
CC with VPS4A. Interacts with PDCD6IP; the interaction is direct.
CC {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570,
CC ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14583093,
CC ECO:0000269|PubMed:14678797, ECO:0000269|PubMed:18511562}.
CC -!- INTERACTION:
CC Q96CF2; Q8WUM4: PDCD6IP; NbExp=3; IntAct=EBI-1221015, EBI-310624;
CC Q96CF2; P40818: USP8; NbExp=2; IntAct=EBI-1221015, EBI-1050865;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Late endosome membrane
CC {ECO:0000305|PubMed:14583093}; Peripheral membrane protein
CC {ECO:0000305}. Midbody, Midbody ring {ECO:0000269|PubMed:22422861}.
CC Note=Localizes to the midbody during late cytokinesis. During its
CC recruitment, localizes initially to the midbody arms, before being
CC directed to the central region, the midbody ring, also called Flemming
CC body. Phosphorylation at Ser-210 by AURKB triggers localization to
CC midbody ring. {ECO:0000269|PubMed:22422861}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, spleen and kidney.
CC {ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:14678797}.
CC -!- DOMAIN: The acidic C-terminus and the basic N-terminus are thought to
CC render the protein in a closed, soluble and inactive conformation
CC through an autoinhibitory intramolecular interaction. The open and
CC active conformation, which enables membrane binding and
CC oligomerization, is achieved by interaction with other cellular binding
CC partners, probably including other ESCRT components (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-210 by AURKB during cytokinesis: together
CC with ZFYVE19/ANCHR, phosphorylated CHMP4C retains abscission-competent
CC VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission
CC checkpoint signaling is terminated at late cytokinesis.
CC {ECO:0000269|PubMed:22422861}.
CC -!- MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AB120734; BAC87888.1; -; mRNA.
DR EMBL; AY329086; AAQ91195.1; -; mRNA.
DR EMBL; AK314873; BAG37388.1; -; mRNA.
DR EMBL; CH471068; EAW87107.1; -; Genomic_DNA.
DR EMBL; BC014321; AAH14321.1; -; mRNA.
DR CCDS; CCDS6233.1; -.
DR RefSeq; NP_689497.1; NM_152284.3.
DR PDB; 3C3R; X-ray; 2.02 A; B=221-233.
DR PDB; 5MK3; X-ray; 2.00 A; E/F/G/H=216-233.
DR PDB; 5V3R; X-ray; 1.91 A; B=216-233.
DR PDB; 5WA1; X-ray; 1.87 A; B=216-233.
DR PDBsum; 3C3R; -.
DR PDBsum; 5MK3; -.
DR PDBsum; 5V3R; -.
DR PDBsum; 5WA1; -.
DR AlphaFoldDB; Q96CF2; -.
DR SMR; Q96CF2; -.
DR BioGRID; 124946; 683.
DR ComplexPortal; CPX-329; ESCRT-III complex.
DR CORUM; Q96CF2; -.
DR DIP; DIP-38342N; -.
DR IntAct; Q96CF2; 13.
DR MINT; Q96CF2; -.
DR STRING; 9606.ENSP00000297265; -.
DR GlyGen; Q96CF2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96CF2; -.
DR PhosphoSitePlus; Q96CF2; -.
DR BioMuta; CHMP4C; -.
DR DMDM; 73917755; -.
DR EPD; Q96CF2; -.
DR jPOST; Q96CF2; -.
DR MassIVE; Q96CF2; -.
DR MaxQB; Q96CF2; -.
DR PaxDb; Q96CF2; -.
DR PeptideAtlas; Q96CF2; -.
DR PRIDE; Q96CF2; -.
DR ProteomicsDB; 76183; -.
DR Antibodypedia; 12567; 74 antibodies from 18 providers.
DR DNASU; 92421; -.
DR Ensembl; ENST00000297265.5; ENSP00000297265.4; ENSG00000164695.5.
DR GeneID; 92421; -.
DR KEGG; hsa:92421; -.
DR MANE-Select; ENST00000297265.5; ENSP00000297265.4; NM_152284.4; NP_689497.1.
DR UCSC; uc003ycl.4; human.
DR CTD; 92421; -.
DR DisGeNET; 92421; -.
DR GeneCards; CHMP4C; -.
DR HGNC; HGNC:30599; CHMP4C.
DR HPA; ENSG00000164695; Tissue enhanced (intestine).
DR MIM; 610899; gene.
DR neXtProt; NX_Q96CF2; -.
DR OpenTargets; ENSG00000164695; -.
DR PharmGKB; PA142672113; -.
DR VEuPathDB; HostDB:ENSG00000164695; -.
DR eggNOG; KOG1656; Eukaryota.
DR GeneTree; ENSGT00940000159257; -.
DR HOGENOM; CLU_071097_0_1_1; -.
DR InParanoid; Q96CF2; -.
DR OMA; FNELAAW; -.
DR OrthoDB; 1490465at2759; -.
DR PhylomeDB; Q96CF2; -.
DR TreeFam; TF314269; -.
DR PathwayCommons; Q96CF2; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-5620971; Pyroptosis.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-HSA-9679504; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR Reactome; R-HSA-9694676; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR SignaLink; Q96CF2; -.
DR SIGNOR; Q96CF2; -.
DR BioGRID-ORCS; 92421; 16 hits in 1078 CRISPR screens.
DR EvolutionaryTrace; Q96CF2; -.
DR GeneWiki; CHMP4C; -.
DR GenomeRNAi; 92421; -.
DR Pharos; Q96CF2; Tbio.
DR PRO; PR:Q96CF2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96CF2; protein.
DR Bgee; ENSG00000164695; Expressed in amniotic fluid and 136 other tissues.
DR Genevisible; Q96CF2; HS.
DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; IDA: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:0030496; C:midbody; IDA:FlyBase.
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:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0009838; P:abscission; IMP:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal.
DR GO; GO:1902774; P:late endosome to lysosome transport; IMP:ComplexPortal.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0036258; P:multivesicular body assembly; TAS: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:0032466; P:negative regulation of cytokinesis; IMP:UniProtKB.
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; IEA:UniProtKB-KW.
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:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
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:ComplexPortal.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..233
FT /note="Charged multivesicular body protein 4c"
FT /id="PRO_0000211495"
FT REGION 1..153
FT /note="Intramolecular interaction with C-terminus"
FT /evidence="ECO:0000250"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..233
FT /note="Intramolecular interaction with N-terminus"
FT /evidence="ECO:0000250"
FT REGION 173..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 125..183
FT /evidence="ECO:0000255"
FT COMPBIAS 183..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:22422861"
FT VARIANT 232
FT /note="A -> T (in dbSNP:rs35094336)"
FT /id="VAR_052028"
FT MUTAGEN 210
FT /note="S->A: Abolishes localization to the Flemming body
FT and ability to delay abscission."
FT /evidence="ECO:0000269|PubMed:22422861"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:5WA1"
SQ SEQUENCE 233 AA; 26411 MW; C18050F0A6C4C899 CRC64;
MSKLGKFFKG GGSSKSRAAP SPQEALVRLR ETEEMLGKKQ EYLENRIQRE IALAKKHGTQ
NKRAALQALK RKKRFEKQLT QIDGTLSTIE FQREALENSH TNTEVLRNMG FAAKAMKSVH
ENMDLNKIDD LMQEITEQQD IAQEISEAFS QRVGFGDDFD EDELMAELEE LEQEELNKKM
TNIRLPNVPS SSLPAQPNRK PGMSSTARRS RAASSQRAEE EDDDIKQLAA WAT
