SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8WV92

- MITD1_HUMAN

UniProt

Q8WV92 - MITD1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
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.3 Publications

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
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

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.

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841E → EGK in CAH10777. 1 Publication
Sequence conflicti130 – 1301Q → QV in CAH10777. 1 Publication

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

« 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: July 9, 2014
This is version 95 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