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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

  • 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
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000158411-MONOMER.

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

HGNCiHGNC:25207. MITD1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extrinsic component of membrane Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • late endosome membrane Source: UniProtKB-SubCell
  • midbody Source: UniProtKB
Complete GO annotation...

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

WithEntry#Exp.IntActNotes
CHMP2AO436335EBI-2691489,EBI-2692789
CHMP5Q9NZZ33EBI-2691489,EBI-751303
revP046182EBI-2691489,EBI-6164309From a different organism.
ZFYVE19Q96K213EBI-2691489,EBI-6448240
ZFYVE19Q96K21-33EBI-2691489,EBI-10187928

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi126197. 22 interactors.
IntActiQ8WV92. 26 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

Sequence similaritiesi

Contains 1 MIT domain.Curated

Phylogenomic databases

eggNOGiKOG4509. Eukaryota.
ENOG410XQAH. LUCA.
GeneTreeiENSGT00390000010868.
HOGENOMiHOG000006736.
HOVERGENiHBG056049.
InParanoidiQ8WV92.
OMAiEAGKYHK.
OrthoDBiEOG091G0LZH.
PhylomeDBiQ8WV92.
TreeFamiTF313066.

Family and domain databases

Gene3Di1.20.58.280. 1 hit.
InterProiIPR007330. MIT.
IPR032341. MIT_C.
[Graphical view]
PfamiPF04212. MIT. 1 hit.
PF16565. MIT_C. 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)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.

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_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.

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...

Protein-protein interaction databases

BioGridi126197. 22 interactors.
IntActiQ8WV92. 26 interactors.
STRINGi9606.ENSP00000289359.

PTM databases

iPTMnetiQ8WV92.
PhosphoSitePlusiQ8WV92.

Polymorphism and mutation databases

BioMutaiMITD1.
DMDMi74730820.

Proteomic databases

EPDiQ8WV92.
MaxQBiQ8WV92.
PaxDbiQ8WV92.
PeptideAtlasiQ8WV92.
PRIDEiQ8WV92.

Protocols and materials databases

DNASUi129531.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi129531.
GeneCardsiMITD1.
HGNCiHGNC:25207. MITD1.
HPAiHPA036162.
HPA036163.
neXtProtiNX_Q8WV92.
OpenTargetsiENSG00000158411.
PharmGKBiPA147357601.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4509. Eukaryota.
ENOG410XQAH. LUCA.
GeneTreeiENSGT00390000010868.
HOGENOMiHOG000006736.
HOVERGENiHBG056049.
InParanoidiQ8WV92.
OMAiEAGKYHK.
OrthoDBiEOG091G0LZH.
PhylomeDBiQ8WV92.
TreeFamiTF313066.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000158411-MONOMER.

Miscellaneous databases

GenomeRNAii129531.
PROiQ8WV92.

Gene expression databases

BgeeiENSG00000158411.
CleanExiHS_MITD1.
ExpressionAtlasiQ8WV92. baseline and differential.
GenevisibleiQ8WV92. HS.

Family and domain databases

Gene3Di1.20.58.280. 1 hit.
InterProiIPR007330. MIT.
IPR032341. MIT_C.
[Graphical view]
PfamiPF04212. MIT. 1 hit.
PF16565. MIT_C. 1 hit.
[Graphical view]
SMARTiSM00745. MIT. 1 hit.
[Graphical view]
SUPFAMiSSF116846. SSF116846. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 119 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

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 one 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.