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Q12965 (MYO1E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Unconventional myosin-Ie
Alternative name(s):
Myosin-Ic
Unconventional myosin 1E
Gene names
Name:MYO1E
Synonyms:MYO1C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1108 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14. Ref.5 Ref.6 Ref.8

Subunit structure

Interacts with CALM and F-actin By similarity. Interacts (via SH3 domain) with SYNJ1, DNM1 and DNM2. Interacts with ARL14EP. Ref.5 Ref.6 Ref.11

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cytoplasmic vesicle. Cytoplasmic vesicleclathrin-coated vesicle. Cell junction By similarity. Note: Colocalizes with F-actin By similarity. In cultured podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with cytoplasmic vesicles, including endocytic clathrin-coated vesicles. Colocalizes with dynamin at cytoplasmic vesicles. Ref.6 Ref.8 Ref.12

Tissue specificity

Expressed in the immune system. In the kidney, predominantly expressed in the glomerulus, including podocytes. Ref.11 Ref.12

Involvement in disease

Focal segmental glomerulosclerosis 6 (FSGS6) [MIM:614131]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. FSGS6 is a childhood-onset disorder resulting in nephrotic syndrome, which includes massive proteinuria, hypoalbuminemia, hyperlipidemia, and edema.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13

Sequence similarities

Contains 1 IQ domain.

Contains 1 myosin head-like domain.

Contains 1 SH3 domain.

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-1 (MYH1).

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSH3 domain
   LigandActin-binding
ATP-binding
Calmodulin-binding
Lipid-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.5. Source: GOC

actin filament-based movement

Traceable author statement Ref.1. Source: UniProtKB

endocytosis

Inferred from mutant phenotype Ref.6. Source: UniProtKB

glomerular basement membrane development

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular filtration

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular visceral epithelial cell development

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

platelet-derived growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

post-embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactin cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

adherens junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

clathrin-coated vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from direct assay Ref.6. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

myosin complex

Traceable author statement Ref.5. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled

Inferred from direct assay Ref.5. Source: UniProtKB

actin filament binding

Inferred from direct assay Ref.5. Source: UniProtKB

calmodulin binding

Inferred from direct assay Ref.5. Source: UniProtKB

microfilament motor activity

Traceable author statement Ref.1. Source: UniProtKB

motor activity

Traceable author statement Ref.1. Source: ProtInc

phosphatidylinositol binding

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARL14EPQ8N8R72EBI-4279548,EBI-2807994
Dnm1P215752EBI-4279548,EBI-80070From a different organism.
DNM2P505702EBI-4279548,EBI-346547
Synj1Q629102EBI-4279548,EBI-1149123From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11081108Unconventional myosin-Ie
PRO_0000123450

Regions

Domain1 – 679679Myosin head-like
Domain695 – 72430IQ
Domain1051 – 110858SH3
Nucleotide binding112 – 1198ATP Potential
Region581 – 59111Actin-binding Potential

Amino acid modifications

Modified residue9801Phosphoserine Ref.7 Ref.9
Modified residue10021Phosphoserine Ref.7

Natural variations

Natural variant1591A → P in FSGS6; the mutant shows diffuse cytosolic localization with a punctate pattern. Ref.12 Ref.13
VAR_065958
Natural variant1851D → G. Ref.12
Corresponds to variant rs141565214 [ dbSNP | Ensembl ].
VAR_065959
Natural variant2211A → V. Ref.12
VAR_065960
Natural variant7951G → R. Ref.12
Corresponds to variant rs180951130 [ dbSNP | Ensembl ].
VAR_065961
Natural variant10491P → H. Ref.12
Corresponds to variant rs147579391 [ dbSNP | Ensembl ].
VAR_065962

Experimental info

Sequence conflict889 – 8924WSAG → GVQGA in AAA62667. Ref.1
Sequence conflict9841N → I in AAA62667. Ref.1
Sequence conflict10971Q → P in AAA62667. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q12965 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 3073050B9BB4DDC6

FASTA1,108127,062
        10         20         30         40         50         60 
MGSKGVYQYH WQSHNVKHSG VDDMVLLSKI TENSIVENLK KRYMDDYIFT YIGSVLISVN 

        70         80         90        100        110        120 
PFKQMPYFGE KEIEMYQGAA QYENPPHIYA LADNMYRNMI IDRENQCVII SGESGAGKTV 

       130        140        150        160        170        180 
AAKYIMSYIS RVSGGGTKVQ HVKDIILQSN PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP 

       190        200        210        220        230        240 
GGEPDGGKIS NFLLEKSRVV MRNPGERSFH IFYQLIEGAS AEQKHSLGIT SMDYYYYLSL 

       250        260        270        280        290        300 
SGSYKVDDID DRREFQETLH AMNVIGIFAE EQTLVLQIVA GILHLGNISF KEVGNYAAVE 

       310        320        330        340        350        360 
SEEFLAFPAY LLGINQDRLK EKLTSRQMDS KWGGKSESIH VTLNVEQACY TRDALAKALH 

       370        380        390        400        410        420 
ARVFDFLVDS INKAMEKDHE EYNIGVLDIY GFEIFQKNGF EQFCINFVNE KLQQIFIELT 

       430        440        450        460        470        480 
LKAEQEEYVQ EGIRWTPIEY FNNKIVCDLI ENKVNPPGIM SILDDVCATM HAVGEGADQT 

       490        500        510        520        530        540 
LLQKLQMQIG SHEHFNSWNQ GFIIHHYAGK VSYDMDGFCE RNRDVLFMDL IELMQSSELP 

       550        560        570        580        590        600 
FIKSLFPENL QADKKGRPTT AGSKIKKQAN DLVSTLMKCT PHYIRCIKPN ETKKPRDWEE 

       610        620        630        640        650        660 
SRVKHQVEYL GLKENIRVRR AGYAYRRIFQ KFLQRYAILT KATWPSWQGE EKQGVLHLLQ 

       670        680        690        700        710        720 
SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR VIQKSWRKFV ARKKYVQMRE 

       730        740        750        760        770        780 
EASDLLLNKK ERRRNSINRN FIGDYIGMEE HPELQQFVGK REKIDFADTV TKYDRRFKGV 

       790        800        810        820        830        840 
KRDLLLTPKC LYLIGREKVK QGPDKGLVKE VLKRKIEIER ILSVSLSTMQ DDIFILHEQE 

       850        860        870        880        890        900 
YDSLLESVFK TEFLSLLAKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFH 

       910        920        930        940        950        960 
QGFGDLAVLK PSNKVLQVSI GPGLPKNSRP TRRNTTQNTG YSSGTQNANY PVRAAPPPPG 

       970        980        990       1000       1010       1020 
YHQNGVIRNQ YVPYPHAPGS QRSNQKSLYT SMARPPLPRQ QSTSSDRVSQ TPESLDFLKV 

      1030       1040       1050       1060       1070       1080 
PDQGAAGVRR QTTSRPPPAG GRPKPQPKPK PQVPQCKALY AYDAQDTDEL SFNANDIIDI 

      1090       1100 
IKEDPSGWWT GRLRGKQGLF PNNYVTKI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and mRNA expression of human unconventional myosin-IC. A homologue of amoeboid myosins-I with a single IQ motif and an SH3 domain."
Bement W.M., Wirth J.A., Mooseker M.S.
J. Mol. Biol. 243:356-363(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types."
Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.
Proc. Natl. Acad. Sci. U.S.A. 91:6549-6553(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 107-196.
[4]Erratum
Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.
Proc. Natl. Acad. Sci. U.S.A. 91:11767-11767(1994) [PubMed] [Europe PMC] [Abstract]
[5]"The kinetic mechanism of Myo1e (human myosin-IC)."
El Mezgueldi M., Tang N., Rosenfeld S.S., Ostap E.M.
J. Biol. Chem. 277:21514-21521(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ATP HYDROLYSIS, INTERACTION WITH F-ACTIN AND CALM.
[6]"Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis."
Krendel M., Osterweil E.K., Mooseker M.S.
FEBS Lett. 581:644-650(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SYNJ1; DNM1 AND DNM2.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980 AND SER-1002, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Myo1e binds anionic phospholipids with high affinity."
Feeser E.A., Ignacio C.M., Krendel M., Ostap E.M.
Biochemistry 49:9353-9360(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"A Genome-wide multidimensional RNAi screen reveals pathways controlling MHC class II antigen presentation."
Paul P., van den Hoorn T., Jongsma M.L., Bakker M.J., Hengeveld R., Janssen L., Cresswell P., Egan D.A., van Ham M., Ten Brinke A., Ovaa H., Beijersbergen R.L., Kuijl C., Neefjes J.
Cell 145:268-283(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARL14EP, TISSUE SPECIFICITY.
[12]"MYO1E mutations and childhood familial focal segmental glomerulosclerosis."
Mele C., Iatropoulos P., Donadelli R., Calabria A., Maranta R., Cassis P., Buelli S., Tomasoni S., Piras R., Krendel M., Bettoni S., Morigi M., Delledonne M., Pecoraro C., Abbate I., Capobianchi M.R., Hildebrandt F., Otto E. expand/collapse author list , Schaefer F., Macciardi F., Ozaltin F., Emre S., Ibsirlioglu T., Benigni A., Remuzzi G., Noris M.
N. Engl. J. Med. 365:295-306(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT FSGS6 PRO-159, VARIANTS GLY-185; VAL-221; ARG-795 AND HIS-1049, CHARACTERIZATION OF VARIANT FSGS6 PRO-159.
[13]"Exome sequencing identified MYO1E and NEIL1 as candidate genes for human autosomal recessive steroid-resistant nephrotic syndrome."
Sanna-Cherchi S., Burgess K.E., Nees S.N., Caridi G., Weng P.L., Dagnino M., Bodria M., Carrea A., Allegretta M.A., Kim H.R., Perry B.J., Gigante M., Clark L.N., Kisselev S., Cusi D., Gesualdo L., Allegri L., Scolari F. expand/collapse author list , D'Agati V., Shapiro L.S., Pecoraro C., Palomero T., Ghiggeri G.M., Gharavi A.G.
Kidney Int. 80:389-396(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FSGS6 PRO-159.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14391 mRNA. Translation: AAA62667.1.
AC092756 Genomic DNA. No translation available.
L29139 mRNA. Translation: AAA20902.1.
PIRS53601.
RefSeqNP_004989.2. NM_004998.3.
UniGeneHs.654506.

3D structure databases

ProteinModelPortalQ12965.
SMRQ12965. Positions 1054-1108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110727. 24 interactions.
DIPDIP-884N.
IntActQ12965. 7 interactions.
MINTMINT-3026848.
STRING9606.ENSP00000288235.

PTM databases

PhosphoSiteQ12965.

Polymorphism databases

DMDM215274106.

Proteomic databases

PaxDbQ12965.
PRIDEQ12965.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288235; ENSP00000288235; ENSG00000157483.
GeneID4643.
KEGGhsa:4643.
UCSCuc002aga.4. human.

Organism-specific databases

CTD4643.
GeneCardsGC15M059428.
H-InvDBHIX0038144.
HGNCHGNC:7599. MYO1E.
HPAHPA023886.
MIM601479. gene.
614131. phenotype.
neXtProtNX_Q12965.
Orphanet93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBPA31401.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000260265.
HOVERGENHBG100702.
InParanoidQ12965.
KOK10356.
OMAKLKKENW.
OrthoDBEOG7V49XQ.
PhylomeDBQ12965.
TreeFamTF312960.

Gene expression databases

ArrayExpressQ12965.
BgeeQ12965.
CleanExHS_MYO1C.
HS_MYO1E.
GenevestigatorQ12965.

Family and domain databases

InterProIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
PR00452. SH3DOMAIN.
SMARTSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50096. IQ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO1E. human.
GeneWikiMYO1E.
GenomeRNAi4643.
NextBio17892.
PROQ12965.
SOURCESearch...

Entry information

Entry nameMYO1E_HUMAN
AccessionPrimary (citable) accession number: Q12965
Secondary accession number(s): Q14778
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 134 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM