PDC6I_MOUSE
ID PDC6I_MOUSE Reviewed; 869 AA.
AC Q9WU78; O88695; O89014; Q3TED2; Q8BSL8; Q8R0H5; Q99LR3; Q9QZN8;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Programmed cell death 6-interacting protein;
DE AltName: Full=ALG-2-interacting protein 1;
DE AltName: Full=ALG-2-interacting protein X;
DE AltName: Full=E2F1-inducible protein;
DE AltName: Full=Eig2;
GN Name=Pdcd6ip; Synonyms=Aip1, Alix;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH PDCD6.
RC TISSUE=Brain;
RX PubMed=10200558; DOI=10.1038/sj.cdd.4400456;
RA Missotten M., Nichols A., Rieger K., Sadoul R.;
RT "Alix, a novel mouse protein undergoing calcium-dependent interaction with
RT the apoptosis-linked-gene 2 (ALG-2) protein.";
RL Cell Death Differ. 6:124-129(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9880530; DOI=10.1074/jbc.274.3.1533;
RA Vito P., Pellegrini L., Guiet C., D'Adamio L.;
RT "Cloning of AIP1, a novel protein that associates with the apoptosis-linked
RT gene ALG-2 in a Ca2+-dependent reaction.";
RL J. Biol. Chem. 274:1533-1540(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Forelimb, Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 671-869.
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
RX PubMed=10556317; DOI=10.1093/nar/27.23.4609;
RA Wang A.J., Pierce A., Judson-Kremer K., Gaddis S., Aldaz C.M.,
RA Johnson D.G., MacLeod M.C.;
RT "Rapid analysis of gene expression (RAGE) facilitates universal expression
RT profiling.";
RL Nucleic Acids Res. 27:4609-4618(1999).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH SDCBP.
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 [10]
RP SUBCELLULAR LOCATION.
RX PubMed=23523921; DOI=10.1016/j.febslet.2013.03.012;
RA Romancino D.P., Paterniti G., Campos Y., De Luca A., Di Felice V.,
RA d'Azzo A., Bongiovanni A.;
RT "Identification and characterization of the nano-sized vesicles released by
RT muscle cells.";
RL FEBS Lett. 587:1379-1384(2013).
RN [11]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH F-ACTIN; TJP1 AND PARD3.
RX PubMed=27336173; DOI=10.1038/ncomms11876;
RA Campos Y., Qiu X., Gomero E., Wakefield R., Horner L., Brutkowski W.,
RA Han Y.G., Solecki D., Frase S., Bongiovanni A., d'Azzo A.;
RT "Alix-mediated assembly of the actomyosin-tight junction polarity complex
RT preserves epithelial polarity and epithelial barrier.";
RL Nat. Commun. 7:11876-11876(2016).
CC -!- FUNCTION: Multifunctional protein involved in endocytosis,
CC multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis
CC and maintenance of tight junction integrity. Class E VPS protein
CC involved in concentration and sorting of cargo proteins of the
CC multivesicular body (MVB) for incorporation into intralumenal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome. Binds to the phospholipid
CC lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal
CC membranes. The MVB pathway requires the sequential function of ESCRT-O,
CC -I,-II and -III complexes. The ESCRT machinery also functions in
CC topologically equivalent membrane fission events, such as the terminal
CC stages of cytokinesis. Adapter for a subset of ESCRT-III proteins, such
CC as CHMP4, to function at distinct membranes. Required for completion of
CC cytokinesis. May play a role in the regulation of both apoptosis and
CC cell proliferation. Regulates exosome biogenesis in concert with SDC1/4
CC and SDCBP (By similarity). By interacting with F-actin, PARD3 and TJP1
CC secures the proper assembly and positioning of actomyosin-tight
CC junction complex at the apical sides of adjacent epithelial cells that
CC defines a spatial membrane domain essential for the maintenance of
CC epithelial cell polarity and barrier (PubMed:27336173).
CC {ECO:0000250|UniProtKB:Q8WUM4, ECO:0000269|PubMed:27336173}.
CC -!- SUBUNIT: Self-associates (By similarity). Interacts with SH3KBP1 (By
CC similarity). Interacts with PDCD6 in a calcium-dependent manner (By
CC similarity). Interacts with TSG101 in a calcium-dependent manner;
CC PDCD6IP homooligomerization may be required for TSG101-binding (By
CC similarity). Interacts with SGSM3 (By similarity). Directly interacts
CC with CHMP4A, CHMP4B and CHMP4C (By similarity). Directly interacts with
CC CEP55 in a 1:2 stoechiometry; this interaction is required for PDCD6IP
CC targeting to the midbody (By similarity). May interact with PDGFRB (By
CC similarity). Interacts with SH3GL1 and SH3GL2/endophilin-1 (By
CC similarity). Forms a complex with SDCBP and SDC2 (PubMed:22660413).
CC Found in a complex with F-actin, TJP1/ZO-1 and PARD3 (PubMed:27336173).
CC Interacts with CD2AP (By similarity). Interacts with ARRDC1 (By
CC similarity). {ECO:0000250|UniProtKB:Q8WUM4,
CC ECO:0000250|UniProtKB:Q9QZA2, ECO:0000269|PubMed:22660413,
CC ECO:0000269|PubMed:27336173}.
CC -!- INTERACTION:
CC Q9WU78; Q8CIH5: Plcg2; NbExp=7; IntAct=EBI-641897, EBI-617954;
CC Q9WU78; O08992: Sdcbp; NbExp=3; IntAct=EBI-641897, EBI-538265;
CC Q9WU78-1; Q9CQY1: Atg12; NbExp=3; IntAct=EBI-15788421, EBI-2911788;
CC Q9WU78-1; Q9WU78-1: Pdcd6ip; NbExp=6; IntAct=EBI-15788421, EBI-15788421;
CC Q9WU78-1; Q9H444: CHMP4B; Xeno; NbExp=2; IntAct=EBI-15788421, EBI-749627;
CC Q9WU78-1; P17931: LGALS3; Xeno; NbExp=2; IntAct=EBI-15788421, EBI-1170392;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9QZA2}. Melanosome
CC {ECO:0000250|UniProtKB:Q8WUM4}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q8WUM4}. Secreted,
CC extracellular exosome {ECO:0000269|PubMed:23523921}. Cell junction,
CC tight junction {ECO:0000269|PubMed:27336173}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q8WUM4}. Note=Colocalized with CEP55 in the
CC midbody during cytokinesis and at centrosomes in non-dividing cells (By
CC similarity). Component of the actomyosin-tight junction complex
CC (PubMed:27336173). {ECO:0000250|UniProtKB:Q8WUM4,
CC ECO:0000269|PubMed:27336173}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9WU78-1; Sequence=Displayed;
CC Name=2; Synonyms=Alix-SF, Short;
CC IsoId=Q9WU78-2; Sequence=VSP_007502;
CC Name=3;
CC IsoId=Q9WU78-3; Sequence=VSP_007501;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:27336173). High
CC expression in choroid plexus and low expression in cerebral cortex (at
CC protein level) (PubMed:27336173). {ECO:0000269|PubMed:27336173}.
CC -!- PTM: May be phosphorylated on tyrosine residues by activated PDGFRB.
CC {ECO:0000250|UniProtKB:Q8WUM4}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are viable and have a normal
CC lifespan, although they are smaller in size. Mutant mice develop
CC progressive and severe bilateral hydrocephalus (PubMed:27336173).
CC {ECO:0000269|PubMed:27336173}.
CC -!- MISCELLANEOUS: [Isoform 2]: Does not interact with ALG-2.
CC {ECO:0000305}.
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DR EMBL; AJ005073; CAA06329.1; -; mRNA.
DR EMBL; AJ005074; CAA06330.1; -; mRNA.
DR EMBL; AF119955; AAD26813.1; -; mRNA.
DR EMBL; AK031256; BAC27323.1; -; mRNA.
DR EMBL; AK167574; BAE39637.1; -; mRNA.
DR EMBL; AK169704; BAE41316.1; -; mRNA.
DR EMBL; AC162177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466621; EDL08950.1; -; Genomic_DNA.
DR EMBL; BC002261; AAH02261.1; -; mRNA.
DR EMBL; BC026823; AAH26823.1; -; mRNA.
DR EMBL; AF176514; AAD53115.1; -; mRNA.
DR CCDS; CCDS23588.1; -. [Q9WU78-1]
DR CCDS; CCDS52947.1; -. [Q9WU78-3]
DR RefSeq; NP_001158149.1; NM_001164677.1. [Q9WU78-3]
DR RefSeq; NP_001158150.1; NM_001164678.1.
DR RefSeq; NP_035182.2; NM_011052.2. [Q9WU78-1]
DR AlphaFoldDB; Q9WU78; -.
DR SMR; Q9WU78; -.
DR BioGRID; 202072; 10.
DR ComplexPortal; CPX-3283; Syndecan-1-syntenin-1-ALIX complex.
DR DIP; DIP-41418N; -.
DR ELM; Q9WU78; -.
DR IntAct; Q9WU78; 15.
DR MINT; Q9WU78; -.
DR STRING; 10090.ENSMUSP00000107492; -.
DR iPTMnet; Q9WU78; -.
DR PhosphoSitePlus; Q9WU78; -.
DR SwissPalm; Q9WU78; -.
DR REPRODUCTION-2DPAGE; Q9WU78; -.
DR UCD-2DPAGE; Q9WU78; -.
DR EPD; Q9WU78; -.
DR jPOST; Q9WU78; -.
DR MaxQB; Q9WU78; -.
DR PaxDb; Q9WU78; -.
DR PeptideAtlas; Q9WU78; -.
DR PRIDE; Q9WU78; -.
DR ProteomicsDB; 301775; -. [Q9WU78-1]
DR ProteomicsDB; 301776; -. [Q9WU78-2]
DR ProteomicsDB; 301777; -. [Q9WU78-3]
DR DNASU; 18571; -.
DR Ensembl; ENSMUST00000035086; ENSMUSP00000035086; ENSMUSG00000032504. [Q9WU78-1]
DR Ensembl; ENSMUST00000111861; ENSMUSP00000107492; ENSMUSG00000032504. [Q9WU78-3]
DR GeneID; 18571; -.
DR KEGG; mmu:18571; -.
DR UCSC; uc009rwn.2; mouse. [Q9WU78-1]
DR UCSC; uc009rwo.2; mouse. [Q9WU78-3]
DR CTD; 10015; -.
DR MGI; MGI:1333753; Pdcd6ip.
DR VEuPathDB; HostDB:ENSMUSG00000032504; -.
DR eggNOG; KOG2220; Eukaryota.
DR GeneTree; ENSGT01040000240872; -.
DR HOGENOM; CLU_007181_2_0_1; -.
DR InParanoid; Q9WU78; -.
DR OMA; SEWIHHM; -.
DR OrthoDB; 550620at2759; -.
DR TreeFam; TF323502; -.
DR Reactome; R-MMU-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-MMU-5675482; Regulation of necroptotic cell death.
DR BioGRID-ORCS; 18571; 23 hits in 72 CRISPR screens.
DR ChiTaRS; Pdcd6ip; mouse.
DR PRO; PR:Q9WU78; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9WU78; protein.
DR Bgee; ENSMUSG00000032504; Expressed in embryonic post-anal tail and 262 other tissues.
DR Genevisible; Q9WU78; MM.
DR GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; ISS:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0031871; F:proteinase activated receptor binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0061952; P:midbody abscission; ISO:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:InterPro.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:MGI.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISO:MGI.
DR GO; GO:1903551; P:regulation of extracellular exosome assembly; ISO:MGI.
DR GO; GO:0090559; P:regulation of membrane permeability; IMP:UniProtKB.
DR GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0046755; P:viral budding; ISO:MGI.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:MGI.
DR Gene3D; 1.25.40.280; -; 1.
DR InterPro; IPR025304; ALIX_V_dom.
DR InterPro; IPR045251; BRO1-like.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR PANTHER; PTHR23030; PTHR23030; 1.
DR Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR Pfam; PF03097; BRO1; 1.
DR SMART; SM01041; BRO1; 1.
DR PROSITE; PS51180; BRO1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Cell cycle; Cell division;
KW Cell junction; Cytoplasm; Cytoskeleton; Methylation; Phosphoprotein;
KW Protein transport; Reference proteome; Secreted; Tight junction; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT CHAIN 2..869
FT /note="Programmed cell death 6-interacting protein"
FT /id="PRO_0000218892"
FT DOMAIN 3..392
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 176..503
FT /note="Interaction with CHMP4A, CHMP4B and CHMP4C"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT REGION 383..869
FT /note="Interaction with SDCBP"
FT /evidence="ECO:0000269|PubMed:22660413"
FT REGION 503..869
FT /note="Self-association"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT REGION 715..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..720
FT /note="Interaction with TSG101"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT REGION 798..807
FT /note="Interaction with CEP55"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT REGION 838..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..767
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..869
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 741
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT MOD_RES 745
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUM4"
FT VAR_SEQ 159..805
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10200558"
FT /id="VSP_007502"
FT VAR_SEQ 239
FT /note="K -> KYFYFQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007501"
FT CONFLICT 329..333
FT /note="LDPIG -> SGSYR (in Ref. 2; AAD26813)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="L -> V (in Ref. 1; CAA06329)"
FT /evidence="ECO:0000305"
FT CONFLICT 547..548
FT /note="EV -> DL (in Ref. 2; AAD26813)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="N -> T (in Ref. 6; AAH26823)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="L -> V (in Ref. 2; AAD26813)"
FT /evidence="ECO:0000305"
FT CONFLICT 640..641
FT /note="KQ -> NE (in Ref. 2; AAD26813)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="G -> R (in Ref. 2; AAD26813)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="P -> L (in Ref. 1; CAA06330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 869 AA; 96024 MW; BFDC87ACA183C5D4 CRC64;
MASFIWVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR RSALGRPLDK
HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD KGSLFGGSVK LALASLGYEK
SCVLFNCAAL ASQIAAEQNL DNDEGLKTAA KQYQFASGAF LHIKDTVLSA LSREPTVDIS
PDTVGTLSLI MLAQAQEVFF LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDTLPKE
VFPTLAAKQC IMQANAEYHQ SILAKQQKKF GEEIARLQHA AELIKNVASR YDEYVNVKDF
SDKINRALTA AKKDNDFIYH DRVPDLKDLD PIGKATLVKP TPVNVPVSQK FTDLFEKMVP
VSVQQSLAVF SQRKADLVNR SIAQMREATT LANGVLASLN LPAAIEDVSG DTVPQSILTK
STSVVEQGGI QTVDQLIKEL PELLQRNREI LEESLRLLDE EEATDNDLRA KFKDRWQRTP
SNDLYKPLRA EGAKFRAVLD KAVQADGQVK ERYQSHRDTI ALLCKPEPEL NAAIPSANPA
KTMQGSEVVS VLKSLLSNLD EIKKERESLE NDLKSVNFDM TSKFLTALAQ DGVINEEALS
VTELDRIYGG LTSKVQESLK KQEGLLKNIQ VSHQEFSKMK QSNNEANLRE EVLKNLATAY
DNFVELVANL KEGTKFYNEL TEILVRFQNK CSDIVFARKT ERDELLKDLQ QSIAREPSAP
SIPPPAYQSS PAAGHAAAPP TPAPRTMPPA KPQPPARPPP PVLPANRVPP ASAAAAPAGV
GTASAAPPQT PGSAPPPQAQ GPPYPTYPGY PGYCQMPMPM GYNPYAYGQY NMPYPPVYHQ
SPGQAPYPGP QQPTYPFPQP PQQSYYPQQ
