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Protein

MIT domain-containing protein 1

Gene

MITD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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: UniProtKB
  2. protein domain specific binding Source: UniProtKB
  3. protein homodimerization activity Source: UniProtKB

GO - Biological processi

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

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: UniProtKB
  2. extrinsic component of membrane Source: UniProtKB
  3. intracellular membrane-bounded organelle Source: HPA
  4. late endosome membrane Source: UniProtKB-SubCell
  5. midbody Source: UniProtKB
Complete GO annotation...

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

BgeeiQ8WV92.
CleanExiHS_MITD1.
ExpressionAtlasiQ8WV92. baseline and differential.
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. 6 interactions.
IntActiQ8WV92. 3 interactions.
STRINGi9606.ENSP00000289359.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000010868.
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

        10         20         30         40         50
MAKSGLRQDP QSTAAATVLK RAVELDSESR YPQALVCYQE GIDLLLQVLK
60 70 80 90 100
GTKDNTKRCN LREKISKYMD RAENIKKYLD QEKEDGKYHK QIKIEENATG
110 120 130 140 150
FSYESLFREY LNETVTEVWI EDPYIRHTHQ LYNFLRFCEM LIKRPCKVKT
160 170 180 190 200
IHLLTSLDEG IEQVQQSRGL QEIEESLRSH GVLLEVQYSS SIHDREIRFN
210 220 230 240
NGWMIKIGRG LDYFKKPQSR FSLGYCDFDL RPCHETTVDI FHKKHTKNI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi126197. 6 interactions.
IntActiQ8WV92. 3 interactions.
STRINGi9606.ENSP00000289359.

PTM databases

PhosphoSiteiQ8WV92.

Polymorphism databases

DMDMi74730820.

Proteomic databases

MaxQBiQ8WV92.
PaxDbiQ8WV92.
PRIDEiQ8WV92.

Protocols and materials databases

DNASUi129531.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi129531.
GeneCardsiGC02M099777.
HGNCiHGNC:25207. MITD1.
HPAiHPA036162.
HPA036163.
neXtProtiNX_Q8WV92.
PharmGKBiPA147357601.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG295654.
GeneTreeiENSGT00390000010868.
HOGENOMiHOG000006736.
HOVERGENiHBG056049.
InParanoidiQ8WV92.
OMAiRFNNGWM.
PhylomeDBiQ8WV92.
TreeFamiTF313066.

Miscellaneous databases

GenomeRNAii129531.
NextBioi82602.
PROiQ8WV92.

Gene expression databases

BgeeiQ8WV92.
CleanExiHS_MITD1.
ExpressionAtlasiQ8WV92. baseline and differential.
GenevestigatoriQ8WV92.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.