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Q8WV92

- MITD1_HUMAN

UniProt

Q8WV92 - MITD1_HUMAN

Protein

MIT domain-containing protein 1

Gene

MITD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Required for efficient abscission at the end of cytokinesis, together with components of the ESCRT-III complex.2 Publications

    GO - Molecular functioni

    1. phosphatidylinositol binding Source: UniProt
    2. protein binding Source: IntAct
    3. protein domain specific binding Source: UniProt
    4. protein homodimerization activity Source: UniProt

    GO - Biological processi

    1. cytokinetic cell separation Source: UniProtKB
    2. mitotic cytokinesis Source: UniProtKB
    3. mitotic cytokinetic cell separation Source: UniProt
    4. negative regulation of protein binding Source: UniProt
    5. transport Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MIT domain-containing protein 1
    Gene namesi
    Name:MITD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:25207. MITD1.

    Subcellular locationi

    Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Midbody. Membrane; Peripheral membrane protein; Cytoplasmic side
    Note: During cytokinesis, recruited to the midbody via interaction with CHMP1A. Interacts with membranes enriched in phosphoinositides.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. extrinsic component of membrane Source: UniProtKB
    3. intracellular membrane-bounded organelle Source: HPA
    4. late endosome membrane Source: UniProtKB-SubCell
    5. midbody Source: UniProt

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi69 – 691M → D: Abolishes interaction with CHMP1A, CHMP1B and CHMP2A. 1 Publication
    Mutagenesisi73 – 731E → A: Abolishes interaction with CHMP1A, CHMP1B and CHMP2A. Abolishes location at the midbody. 1 Publication
    Mutagenesisi132 – 1321Y → A: Abolishes homodimerization; when associated with A-221 and A-225. 1 Publication
    Mutagenesisi168 – 1681R → E: Strongly reduces binding to membranes; when associated with E-221 and E-231. 1 Publication
    Mutagenesisi220 – 2201R → E: Strongly reduces binding to membranes; when associated with E-168 and E-231. 1 Publication
    Mutagenesisi221 – 2211F → A: Abolishes homodimerization; when associated with A-132 and A-225. 1 Publication
    Mutagenesisi225 – 2251Y → A: Abolishes homodimerization; when associated with A-132 and A-221. 1 Publication
    Mutagenesisi231 – 2311R → E: Strongly reduces binding to membranes; when associated with E-221 and E-220. 1 Publication

    Organism-specific databases

    PharmGKBiPA147357601.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 249249MIT domain-containing protein 1PRO_0000260495Add
    BLAST

    Proteomic databases

    MaxQBiQ8WV92.
    PaxDbiQ8WV92.
    PRIDEiQ8WV92.

    PTM databases

    PhosphoSiteiQ8WV92.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8WV92.
    BgeeiQ8WV92.
    CleanExiHS_MITD1.
    GenevestigatoriQ8WV92.

    Organism-specific databases

    HPAiHPA036162.
    HPA036163.

    Interactioni

    Subunit structurei

    Homodimer. Interacts (via MIT domain) with CHMP1A, CHMP1B, CHMP2A and IST1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    revP046182EBI-2691489,EBI-6164309From a different organism.

    Protein-protein interaction databases

    BioGridi126197. 4 interactions.
    IntActiQ8WV92. 3 interactions.
    STRINGi9606.ENSP00000289359.

    Structurei

    Secondary structure

    1
    249
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2717
    Helixi31 – 5020
    Helixi55 – 8127
    Beta strandi90 – 945
    Helixi103 – 1075
    Helixi108 – 1103
    Beta strandi117 – 1215
    Helixi128 – 14215
    Beta strandi150 – 1556
    Helixi163 – 17917
    Beta strandi183 – 1886
    Beta strandi196 – 1994
    Beta strandi202 – 2076
    Turni208 – 2114
    Helixi228 – 2303
    Beta strandi236 – 2427

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YMBX-ray3.40A/B/C/D1-249[»]
    4A5XX-ray1.91A/B9-85[»]
    4A5ZX-ray2.30A/B/C/D90-243[»]
    ProteinModelPortaliQ8WV92.
    SMRiQ8WV92. Positions 9-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 8679MITAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni168 – 23164Important for association with membranesAdd
    BLAST

    Domaini

    The C-terminal domain interacts with lipid membranes containing acidic phosphoinositides and is required for location at the midbody.1 Publication
    The MIT domain interacts with the MIT-interacting motifs of several components of the ESCRT-III complex.1 Publication

    Sequence similaritiesi

    Contains 1 MIT domain.Curated

    Phylogenomic databases

    eggNOGiNOG295654.
    HOGENOMiHOG000006736.
    HOVERGENiHBG056049.
    InParanoidiQ8WV92.
    OMAiRFNNGWM.
    PhylomeDBiQ8WV92.
    TreeFamiTF313066.

    Family and domain databases

    Gene3Di1.20.58.280. 1 hit.
    InterProiIPR007330. MIT.
    [Graphical view]
    PfamiPF04212. MIT. 1 hit.
    [Graphical view]
    SMARTiSM00745. MIT. 1 hit.
    [Graphical view]
    SUPFAMiSSF116846. SSF116846. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8WV92-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKSGLRQDP QSTAAATVLK RAVELDSESR YPQALVCYQE GIDLLLQVLK    50
    GTKDNTKRCN LREKISKYMD RAENIKKYLD QEKEDGKYHK QIKIEENATG 100
    FSYESLFREY LNETVTEVWI EDPYIRHTHQ LYNFLRFCEM LIKRPCKVKT 150
    IHLLTSLDEG IEQVQQSRGL QEIEESLRSH GVLLEVQYSS SIHDREIRFN 200
    NGWMIKIGRG LDYFKKPQSR FSLGYCDFDL RPCHETTVDI FHKKHTKNI 249
    Length:249
    Mass (Da):29,314
    Last modified:March 1, 2002 - v1
    Checksum:i82D56C7F6DE3ED0B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841E → EGK in CAH10777. (PubMed:17974005)Curated
    Sequence conflicti130 – 1301Q → QV in CAH10777. (PubMed:17974005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC092587 Genomic DNA. Translation: AAX88928.1.
    BC018453 mRNA. Translation: AAH18453.1.
    AL161992 mRNA. Translation: CAH10777.1.
    CCDSiCCDS2040.1.
    RefSeqiNP_620153.1. NM_138798.1.
    UniGeneiHs.14222.

    Genome annotation databases

    EnsembliENST00000289359; ENSP00000289359; ENSG00000158411.
    GeneIDi129531.
    KEGGihsa:129531.
    UCSCiuc002szs.1. human.

    Polymorphism databases

    DMDMi74730820.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC092587 Genomic DNA. Translation: AAX88928.1 .
    BC018453 mRNA. Translation: AAH18453.1 .
    AL161992 mRNA. Translation: CAH10777.1 .
    CCDSi CCDS2040.1.
    RefSeqi NP_620153.1. NM_138798.1.
    UniGenei Hs.14222.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YMB X-ray 3.40 A/B/C/D 1-249 [» ]
    4A5X X-ray 1.91 A/B 9-85 [» ]
    4A5Z X-ray 2.30 A/B/C/D 90-243 [» ]
    ProteinModelPortali Q8WV92.
    SMRi Q8WV92. Positions 9-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126197. 4 interactions.
    IntActi Q8WV92. 3 interactions.
    STRINGi 9606.ENSP00000289359.

    PTM databases

    PhosphoSitei Q8WV92.

    Polymorphism databases

    DMDMi 74730820.

    Proteomic databases

    MaxQBi Q8WV92.
    PaxDbi Q8WV92.
    PRIDEi Q8WV92.

    Protocols and materials databases

    DNASUi 129531.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000289359 ; ENSP00000289359 ; ENSG00000158411 .
    GeneIDi 129531.
    KEGGi hsa:129531.
    UCSCi uc002szs.1. human.

    Organism-specific databases

    CTDi 129531.
    GeneCardsi GC02M099777.
    HGNCi HGNC:25207. MITD1.
    HPAi HPA036162.
    HPA036163.
    neXtProti NX_Q8WV92.
    PharmGKBi PA147357601.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295654.
    HOGENOMi HOG000006736.
    HOVERGENi HBG056049.
    InParanoidi Q8WV92.
    OMAi RFNNGWM.
    PhylomeDBi Q8WV92.
    TreeFami TF313066.

    Miscellaneous databases

    GenomeRNAii 129531.
    NextBioi 82602.
    PROi Q8WV92.

    Gene expression databases

    ArrayExpressi Q8WV92.
    Bgeei Q8WV92.
    CleanExi HS_MITD1.
    Genevestigatori Q8WV92.

    Family and domain databases

    Gene3Di 1.20.58.280. 1 hit.
    InterProi IPR007330. MIT.
    [Graphical view ]
    Pfami PF04212. MIT. 1 hit.
    [Graphical view ]
    SMARTi SM00745. MIT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF116846. SSF116846. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-249.
      Tissue: Amygdala.
    4. "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex."
      Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E., Sanderson C.M.
      Genomics 88:333-346(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHMP2A.
    5. Cited for: INTERACTION WITH CHMP1B.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "MITD1 is recruited to midbodies by ESCRT-III and participates in cytokinesis."
      Lee S., Chang J., Renvoise B., Tipirneni A., Yang S., Blackstone C.
      Mol. Biol. Cell 23:4347-4361(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHMP1A AND IST1, SUBCELLULAR LOCATION, SUBUNIT.
    8. "ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes."
      Hadders M.A., Agromayor M., Obita T., Perisic O., Caballe A., Kloc M., Lamers M.H., Williams R.L., Martin-Serrano J.
      Proc. Natl. Acad. Sci. U.S.A. 109:17424-17429(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH CHMP1A, FUNCTION, SUBUNIT, DOMAIN, INTERACTION WITH CHMP1A; CHMP1B; CHMP2A AND IST1, MUTAGENESIS OF MET-69; GLU-73; TYR-132; ARG-168; ARG-220; PHE-221; TYR-225 AND ARG-231, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiMITD1_HUMAN
    AccessioniPrimary (citable) accession number: Q8WV92
    Secondary accession number(s): Q69YV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3