Q8WV92 (MITD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
MIT domain-containing protein 1

Gene names

Name:

MITD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Transport
Cellular component	Endosome Membrane
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokinesis after mitosis Inferred from mutant phenotype Ref.8. Source: UniProtKB cytokinetic cell separation involved in cell cycle cytokinesis Inferred from mutant phenotype Ref.8. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extrinsic to membrane Inferred from direct assay Ref.8. Source: UniProtKB intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rev	P04618	2	EBI-2691489,EBI-6164309	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 249

249

MIT domain-containing protein 1

PRO_0000260495

Regions

Domain

8 – 86

79

MIT

Region

168 – 231

64

Important for association with membranes

Experimental info

Mutagenesis

69

1

M → D: Abolishes interaction with CHMP1A, CHMP1B and CHMP2A. Ref.8

Mutagenesis

73

1

E → A: Abolishes interaction with CHMP1A, CHMP1B and CHMP2A. Abolishes location at the midbody. Ref.8

Mutagenesis

132

1

Y → A: Abolishes homodimerization; when associated with A-221 and A-225. Ref.8

Mutagenesis

168

1

R → E: Strongly reduces binding to membranes; when associated with E-221 and E-231. Ref.8

Mutagenesis

220

1

R → E: Strongly reduces binding to membranes; when associated with E-168 and E-231. Ref.8

Mutagenesis

221

1

F → A: Abolishes homodimerization; when associated with A-132 and A-225. Ref.8

Mutagenesis

225

1

Y → A: Abolishes homodimerization; when associated with A-132 and A-221. Ref.8

Mutagenesis

231

1

R → E: Strongly reduces binding to membranes; when associated with E-221 and E-220. Ref.8

Sequence conflict

84

1

E → EGK in CAH10777. Ref.3

Sequence conflict

130

1

Q → QV in CAH10777. Ref.3

Secondary structure

1

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249

Helix Strand Turn

Details...

Helix

11 – 27

17

Helix

31 – 50

20

Helix

55 – 81

27

Beta strand

91 – 94

4

Helix

103 – 107

5

Helix

108 – 110

3

Beta strand

117 – 121

5

Helix

128 – 142

15

Beta strand

150 – 155

6

Helix

163 – 179

17

Beta strand

183 – 188

6

Beta strand

196 – 199

4

Beta strand

202 – 207

6

Turn

208 – 211

4

Helix

228 – 230

3

Beta strand

236 – 242

7

Sequences

	Sequence		Length	Mass (Da)
	Q8WV92 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 82D56C7F6DE3ED0B	FASTA	249	29,314
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00103065.

RefSeq

NP_620153.1. NM_138798.1.

UniGene

Hs.14222.

3D structure databases

PDBe
RCSB PDB
PDBj

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	91-242	[»]

ProteinModelPortal

Q8WV92.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8WV92. 3 interactions.

STRING

9606.ENSP00000289359.

PTM databases

PhosphoSite

Q8WV92.

Polymorphism databases

DMDM

74730820.

Proteomic databases

PaxDb

Q8WV92.

PRIDE

Q8WV92.

Protocols and materials databases

DNASU

129531.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000289359; ENSP00000289359; ENSG00000158411.

GeneID

129531.

KEGG

hsa:129531.

UCSC

uc002szs.1. human.

Organism-specific databases

CTD

129531.

GeneCards

GC02M099777.

HGNC

HGNC:25207. MITD1.

HPA

HPA036162.

neXtProt

NX_Q8WV92.

PharmGKB

PA147357601.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG295654.

HOGENOM

HOG000006736.

HOVERGEN

HBG056049.

InParanoid

Q8WV92.

OMA

RFNNGWM.

PhylomeDB

Q8WV92.

Gene expression databases

ArrayExpress

Q8WV92.

Bgee

Q8WV92.

CleanEx

HS_MITD1.

Genevestigator

Q8WV92.

GermOnline

ENSG00000158411. Homo sapiens.

Family and domain databases

InterPro

IPR007330. MIT.
[Graphical view]

Pfam

PF04212. MIT. 1 hit.
[Graphical view]

SMART

SM00745. MIT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

129531.

NextBio

82602.

Entry information

Entry name

MITD1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.