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Protein

MIT domain-containing protein 1

Gene

MITD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • phosphatidylinositol binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • cell separation after cytokinesis Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • negative regulation of protein binding Source: UniProtKB

Keywordsi

Biological processCell 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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000158411.10
HGNCiHGNC:25207 MITD1
neXtProtiNX_Q8WV92

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi69M → D: Abolishes interaction with CHMP1A, CHMP1B and CHMP2A. 1 Publication1
Mutagenesisi73E → A: Abolishes interaction with CHMP1A, CHMP1B and CHMP2A. Abolishes location at the midbody. 1 Publication1
Mutagenesisi132Y → A: Abolishes homodimerization; when associated with A-221 and A-225. 1 Publication1
Mutagenesisi168R → E: Strongly reduces binding to membranes; when associated with E-221 and E-231. 1 Publication1
Mutagenesisi220R → E: Strongly reduces binding to membranes; when associated with E-168 and E-231. 1 Publication1
Mutagenesisi221F → A: Abolishes homodimerization; when associated with A-132 and A-225. 1 Publication1
Mutagenesisi225Y → A: Abolishes homodimerization; when associated with A-132 and A-221. 1 Publication1
Mutagenesisi231R → E: Strongly reduces binding to membranes; when associated with E-221 and E-220. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000158411
PharmGKBiPA147357601

Polymorphism and mutation databases

BioMutaiMITD1
DMDMi74730820

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002604951 – 249MIT domain-containing protein 1Add BLAST249

Proteomic databases

EPDiQ8WV92
MaxQBiQ8WV92
PaxDbiQ8WV92
PeptideAtlasiQ8WV92
PRIDEiQ8WV92

PTM databases

iPTMnetiQ8WV92
PhosphoSitePlusiQ8WV92

Expressioni

Gene expression databases

BgeeiENSG00000158411
CleanExiHS_MITD1
ExpressionAtlasiQ8WV92 baseline and differential
GenevisibleiQ8WV92 HS

Organism-specific databases

HPAiHPA036162
HPA036163

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi126197, 24 interactors
IntActiQ8WV92, 28 interactors
STRINGi9606.ENSP00000289359

Structurei

Secondary structure

1249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 27Combined sources17
Helixi31 – 50Combined sources20
Helixi55 – 81Combined sources27
Beta strandi90 – 94Combined sources5
Helixi103 – 107Combined sources5
Helixi108 – 110Combined sources3
Beta strandi117 – 121Combined sources5
Helixi128 – 142Combined sources15
Beta strandi150 – 155Combined sources6
Helixi163 – 179Combined sources17
Beta strandi183 – 188Combined sources6
Beta strandi196 – 199Combined sources4
Beta strandi202 – 207Combined sources6
Turni208 – 211Combined sources4
Helixi228 – 230Combined sources3
Beta strandi236 – 242Combined sources7

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 86MITAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni168 – 231Important for association with membranesAdd BLAST64

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

Phylogenomic databases

eggNOGiKOG4509 Eukaryota
ENOG410XQAH LUCA
GeneTreeiENSGT00390000010868
HOGENOMiHOG000006736
HOVERGENiHBG056049
InParanoidiQ8WV92
OMAiGHIMEAI
OrthoDBiEOG091G0LZH
PhylomeDBiQ8WV92
TreeFamiTF313066

Family and domain databases

Gene3Di3.30.870.30, 1 hit
InterProiView protein in InterPro
IPR007330 MIT
IPR032341 MIT_C
IPR038113 MIT_C_sf
IPR036181 MIT_dom_sf
PfamiView protein in Pfam
PF04212 MIT, 1 hit
PF16565 MIT_C, 1 hit
SMARTiView protein in SMART
SM00745 MIT, 1 hit
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)DescriptionActionsGraphical viewLength
Sequence conflicti84E → EGK in CAH10777 (PubMed:17974005).Curated1
Sequence conflicti130Q → QV in CAH10777 (PubMed:17974005).Curated1

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_001307346.1, NM_001320417.1
NP_001307347.1, NM_001320418.1
NP_001307348.1, NM_001320419.1
NP_620153.1, NM_138798.2
UniGeneiHs.14222

Genome annotation databases

EnsembliENST00000289359; ENSP00000289359; ENSG00000158411
GeneIDi129531
KEGGihsa:129531
UCSCiuc002szs.2 human

Similar proteinsi

Entry informationi

Entry nameiMITD1_HUMAN
AccessioniPrimary (citable) accession number: Q8WV92
Secondary accession number(s): Q69YV0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2002
Last modified: May 23, 2018
This is version 131 of the entry and version 1 of the sequence. See 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

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