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Q8WV92 (MITD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MIT domain-containing protein 1
Gene names
Name:MITD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for efficient abscission at the end of cytokinesis, together with components of the ESCRT-III complex. Ref.7 Ref.8

Subunit structure

Homodimer. Interacts (via MIT domain) with CHMP1A, CHMP1B, CHMP2A and IST1. Ref.4 Ref.5 Ref.7 Ref.8

Subcellular location

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. Ref.4 Ref.7 Ref.8

Domain

The C-terminal domain interacts with lipid membranes containing acidic phosphoinositides and is required for location at the midbody. Ref.8

The MIT domain interacts with the MIT-interacting motifs of several components of the ESCRT-III complex. Ref.8

Sequence similarities

Contains 1 MIT domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

revP046182EBI-2691489,EBI-6164309From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249MIT domain-containing protein 1
PRO_0000260495

Regions

Domain8 – 8679MIT
Region168 – 23164Important for association with membranes

Experimental info

Mutagenesis691M → D: Abolishes interaction with CHMP1A, CHMP1B and CHMP2A. Ref.8
Mutagenesis731E → A: Abolishes interaction with CHMP1A, CHMP1B and CHMP2A. Abolishes location at the midbody. Ref.8
Mutagenesis1321Y → A: Abolishes homodimerization; when associated with A-221 and A-225. Ref.8
Mutagenesis1681R → E: Strongly reduces binding to membranes; when associated with E-221 and E-231. Ref.8
Mutagenesis2201R → E: Strongly reduces binding to membranes; when associated with E-168 and E-231. Ref.8
Mutagenesis2211F → A: Abolishes homodimerization; when associated with A-132 and A-225. Ref.8
Mutagenesis2251Y → A: Abolishes homodimerization; when associated with A-132 and A-221. Ref.8
Mutagenesis2311R → E: Strongly reduces binding to membranes; when associated with E-221 and E-220. Ref.8
Sequence conflict841E → EGK in CAH10777. Ref.3
Sequence conflict1301Q → QV in CAH10777. Ref.3

Secondary structure

............................... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WV92 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 82D56C7F6DE3ED0B

FASTA24929,314
        10         20         30         40         50         60 
MAKSGLRQDP QSTAAATVLK RAVELDSESR YPQALVCYQE GIDLLLQVLK GTKDNTKRCN 

        70         80         90        100        110        120 
LREKISKYMD RAENIKKYLD QEKEDGKYHK QIKIEENATG FSYESLFREY LNETVTEVWI 

       130        140        150        160        170        180 
EDPYIRHTHQ LYNFLRFCEM LIKRPCKVKT IHLLTSLDEG IEQVQQSRGL QEIEESLRSH 

       190        200        210        220        230        240 
GVLLEVQYSS SIHDREIRFN NGWMIKIGRG LDYFKKPQSR FSLGYCDFDL RPCHETTVDI 


FHKKHTKNI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Essential role of hIST1 in cytokinesis."
Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M., Ameer-Beg S., Bowers K., Martin-Serrano J.
Mol. Biol. Cell 20:1374-1387(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHMP1B.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC092587 Genomic DNA. Translation: AAX88928.1.
BC018453 mRNA. Translation: AAH18453.1.
AL161992 mRNA. Translation: CAH10777.1.
RefSeqNP_620153.1. NM_138798.1.
UniGeneHs.14222.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YMBX-ray3.40A/B/C/D1-249[»]
4A5XX-ray1.91A/B9-85[»]
4A5ZX-ray2.30A/B/C/D91-242[»]
ProteinModelPortalQ8WV92.
SMRQ8WV92. Positions 9-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126197. 4 interactions.
IntActQ8WV92. 3 interactions.
STRING9606.ENSP00000289359.

PTM databases

PhosphoSiteQ8WV92.

Polymorphism databases

DMDM74730820.

Proteomic databases

PaxDbQ8WV92.
PRIDEQ8WV92.

Protocols and materials databases

DNASU129531.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000289359; ENSP00000289359; ENSG00000158411.
GeneID129531.
KEGGhsa:129531.
UCSCuc002szs.1. human.

Organism-specific databases

CTD129531.
GeneCardsGC02M099777.
HGNCHGNC:25207. MITD1.
HPAHPA036162.
HPA036163.
neXtProtNX_Q8WV92.
PharmGKBPA147357601.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295654.
HOGENOMHOG000006736.
HOVERGENHBG056049.
InParanoidQ8WV92.
OMARFNNGWM.
PhylomeDBQ8WV92.
TreeFamTF313066.

Gene expression databases

ArrayExpressQ8WV92.
BgeeQ8WV92.
CleanExHS_MITD1.
GenevestigatorQ8WV92.

Family and domain databases

Gene3D1.20.58.280. 1 hit.
InterProIPR007330. MIT.
[Graphical view]
PfamPF04212. MIT. 1 hit.
[Graphical view]
SMARTSM00745. MIT. 1 hit.
[Graphical view]
SUPFAMSSF116846. SSF116846. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi129531.
NextBio82602.
PROQ8WV92.

Entry information

Entry nameMITD1_HUMAN
AccessionPrimary (citable) accession number: Q8WV92
Secondary accession number(s): Q69YV0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM