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Protein

Unconventional myosin-Ie

Gene

MYO1E

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 ARL14.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi112 – 1198ATPSequence Analysis

GO - Molecular functioni

  1. actin filament binding Source: UniProtKB
  2. ATPase activity, coupled Source: UniProtKB
  3. ATP binding Source: UniProtKB-KW
  4. calmodulin binding Source: UniProtKB
  5. microfilament motor activity Source: UniProtKB
  6. motor activity Source: ProtInc
  7. phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

  1. actin filament-based movement Source: UniProtKB
  2. endocytosis Source: UniProtKB
  3. glomerular basement membrane development Source: UniProtKB
  4. glomerular filtration Source: UniProtKB
  5. glomerular visceral epithelial cell development Source: UniProtKB
  6. in utero embryonic development Source: Ensembl
  7. nitrogen compound metabolic process Source: Ensembl
  8. platelet-derived growth factor receptor signaling pathway Source: Ensembl
  9. post-embryonic hemopoiesis Source: Ensembl
  10. vasculogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Lipid-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-Ie
Alternative name(s):
Myosin-Ic
Unconventional myosin 1E
Gene namesi
Name:MYO1E
Synonyms:MYO1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:7599. MYO1E.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: ProtInc
  2. adherens junction Source: UniProtKB
  3. cell-cell junction Source: UniProtKB
  4. clathrin-coated vesicle Source: UniProtKB-SubCell
  5. cytoplasm Source: UniProtKB
  6. cytoskeleton Source: UniProtKB
  7. extracellular vesicular exosome Source: UniProtKB
  8. myosin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Focal segmental glomerulosclerosis 6 (FSGS6)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:614131
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti159 – 1591A → P in FSGS6; the mutant shows diffuse cytosolic localization with a punctate pattern. 2 Publications
VAR_065958

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614131. phenotype.
Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA31401.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11081108Unconventional myosin-IePRO_0000123450Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei980 – 9801Phosphoserine2 Publications
Modified residuei1002 – 10021Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12965.
PaxDbiQ12965.
PRIDEiQ12965.

PTM databases

PhosphoSiteiQ12965.

Expressioni

Tissue specificityi

Expressed in the immune system. In the kidney, predominantly expressed in the glomerulus, including podocytes.2 Publications

Gene expression databases

BgeeiQ12965.
CleanExiHS_MYO1C.
HS_MYO1E.
ExpressionAtlasiQ12965. baseline and differential.
GenevestigatoriQ12965.

Organism-specific databases

HPAiHPA023886.

Interactioni

Subunit structurei

Interacts with CALM and F-actin (By similarity). Interacts (via SH3 domain) with SYNJ1, DNM1 and DNM2. Interacts with ARL14EP.By similarity3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi110727. 31 interactions.
DIPiDIP-884N.
IntActiQ12965. 7 interactions.
MINTiMINT-3026848.
STRINGi9606.ENSP00000288235.

Structurei

3D structure databases

ProteinModelPortaliQ12965.
SMRiQ12965. Positions 1054-1108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 692674Myosin motorAdd
BLAST
Domaini695 – 72430IQPROSITE-ProRule annotationAdd
BLAST
Domaini718 – 923206Myosin tailSequence AnalysisAdd
BLAST
Domaini1051 – 110858SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni581 – 59111Actin-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 IQ domain.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated
Contains 1 myosin tail domain.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiCOG5022.
HOGENOMiHOG000260265.
HOVERGENiHBG100702.
InParanoidiQ12965.
KOiK10356.
OMAiNANYPMR.
OrthoDBiEOG7V49XQ.
PhylomeDBiQ12965.
TreeFamiTF312960.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
PR00452. SH3DOMAIN.
SMARTiSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKGVYQYH WQSHNVKHSG VDDMVLLSKI TENSIVENLK KRYMDDYIFT
60 70 80 90 100
YIGSVLISVN PFKQMPYFGE KEIEMYQGAA QYENPPHIYA LADNMYRNMI
110 120 130 140 150
IDRENQCVII SGESGAGKTV AAKYIMSYIS RVSGGGTKVQ HVKDIILQSN
160 170 180 190 200
PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP GGEPDGGKIS NFLLEKSRVV
210 220 230 240 250
MRNPGERSFH IFYQLIEGAS AEQKHSLGIT SMDYYYYLSL SGSYKVDDID
260 270 280 290 300
DRREFQETLH AMNVIGIFAE EQTLVLQIVA GILHLGNISF KEVGNYAAVE
310 320 330 340 350
SEEFLAFPAY LLGINQDRLK EKLTSRQMDS KWGGKSESIH VTLNVEQACY
360 370 380 390 400
TRDALAKALH ARVFDFLVDS INKAMEKDHE EYNIGVLDIY GFEIFQKNGF
410 420 430 440 450
EQFCINFVNE KLQQIFIELT LKAEQEEYVQ EGIRWTPIEY FNNKIVCDLI
460 470 480 490 500
ENKVNPPGIM SILDDVCATM HAVGEGADQT LLQKLQMQIG SHEHFNSWNQ
510 520 530 540 550
GFIIHHYAGK VSYDMDGFCE RNRDVLFMDL IELMQSSELP FIKSLFPENL
560 570 580 590 600
QADKKGRPTT AGSKIKKQAN DLVSTLMKCT PHYIRCIKPN ETKKPRDWEE
610 620 630 640 650
SRVKHQVEYL GLKENIRVRR AGYAYRRIFQ KFLQRYAILT KATWPSWQGE
660 670 680 690 700
EKQGVLHLLQ SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR
710 720 730 740 750
VIQKSWRKFV ARKKYVQMRE EASDLLLNKK ERRRNSINRN FIGDYIGMEE
760 770 780 790 800
HPELQQFVGK REKIDFADTV TKYDRRFKGV KRDLLLTPKC LYLIGREKVK
810 820 830 840 850
QGPDKGLVKE VLKRKIEIER ILSVSLSTMQ DDIFILHEQE YDSLLESVFK
860 870 880 890 900
TEFLSLLAKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFH
910 920 930 940 950
QGFGDLAVLK PSNKVLQVSI GPGLPKNSRP TRRNTTQNTG YSSGTQNANY
960 970 980 990 1000
PVRAAPPPPG YHQNGVIRNQ YVPYPHAPGS QRSNQKSLYT SMARPPLPRQ
1010 1020 1030 1040 1050
QSTSSDRVSQ TPESLDFLKV PDQGAAGVRR QTTSRPPPAG GRPKPQPKPK
1060 1070 1080 1090 1100
PQVPQCKALY AYDAQDTDEL SFNANDIIDI IKEDPSGWWT GRLRGKQGLF

PNNYVTKI
Length:1,108
Mass (Da):127,062
Last modified:November 24, 2008 - v2
Checksum:i3073050B9BB4DDC6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti889 – 8924WSAG → GVQGA in AAA62667 (PubMed:7932763).Curated
Sequence conflicti984 – 9841N → I in AAA62667 (PubMed:7932763).Curated
Sequence conflicti1097 – 10971Q → P in AAA62667 (PubMed:7932763).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti159 – 1591A → P in FSGS6; the mutant shows diffuse cytosolic localization with a punctate pattern. 2 Publications
VAR_065958
Natural varianti185 – 1851D → G.1 Publication
Corresponds to variant rs141565214 [ dbSNP | Ensembl ].
VAR_065959
Natural varianti221 – 2211A → V.1 Publication
VAR_065960
Natural varianti795 – 7951G → R.1 Publication
Corresponds to variant rs180951130 [ dbSNP | Ensembl ].
VAR_065961
Natural varianti1049 – 10491P → H.1 Publication
Corresponds to variant rs147579391 [ dbSNP | Ensembl ].
VAR_065962

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14391 mRNA. Translation: AAA62667.1.
AC092756 Genomic DNA. No translation available.
L29139 mRNA. Translation: AAA20902.1.
CCDSiCCDS32254.1.
PIRiS53601.
RefSeqiNP_004989.2. NM_004998.3.
UniGeneiHs.654506.

Genome annotation databases

EnsembliENST00000288235; ENSP00000288235; ENSG00000157483.
GeneIDi4643.
KEGGihsa:4643.
UCSCiuc002aga.4. human.

Polymorphism databases

DMDMi215274106.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14391 mRNA. Translation: AAA62667.1.
AC092756 Genomic DNA. No translation available.
L29139 mRNA. Translation: AAA20902.1.
CCDSiCCDS32254.1.
PIRiS53601.
RefSeqiNP_004989.2. NM_004998.3.
UniGeneiHs.654506.

3D structure databases

ProteinModelPortaliQ12965.
SMRiQ12965. Positions 1054-1108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110727. 31 interactions.
DIPiDIP-884N.
IntActiQ12965. 7 interactions.
MINTiMINT-3026848.
STRINGi9606.ENSP00000288235.

PTM databases

PhosphoSiteiQ12965.

Polymorphism databases

DMDMi215274106.

Proteomic databases

MaxQBiQ12965.
PaxDbiQ12965.
PRIDEiQ12965.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288235; ENSP00000288235; ENSG00000157483.
GeneIDi4643.
KEGGihsa:4643.
UCSCiuc002aga.4. human.

Organism-specific databases

CTDi4643.
GeneCardsiGC15M059428.
H-InvDBHIX0038144.
HGNCiHGNC:7599. MYO1E.
HPAiHPA023886.
MIMi601479. gene.
614131. phenotype.
neXtProtiNX_Q12965.
Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA31401.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5022.
HOGENOMiHOG000260265.
HOVERGENiHBG100702.
InParanoidiQ12965.
KOiK10356.
OMAiNANYPMR.
OrthoDBiEOG7V49XQ.
PhylomeDBiQ12965.
TreeFamiTF312960.

Miscellaneous databases

ChiTaRSiMYO1E. human.
GeneWikiiMYO1E.
GenomeRNAii4643.
NextBioi17892.
PROiQ12965.
SOURCEiSearch...

Gene expression databases

BgeeiQ12965.
CleanExiHS_MYO1C.
HS_MYO1E.
ExpressionAtlasiQ12965. baseline and differential.
GenevestigatoriQ12965.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
PR00452. SH3DOMAIN.
SMARTiSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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.
    , 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(2005) [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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 107-196.
  4. Cited for: FUNCTION IN ATP HYDROLYSIS, INTERACTION WITH F-ACTIN AND CALM.
  5. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SYNJ1; DNM1 AND DNM2.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980 AND SER-1002, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Myo1e binds anionic phospholipids with high affinity."
    Feeser E.A., Ignacio C.M., Krendel M., Ostap E.M.
    Biochemistry 49:9353-9360(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARL14EP, TISSUE SPECIFICITY.
  11. 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.
  12. Cited for: VARIANT FSGS6 PRO-159.

Entry informationi

Entry nameiMYO1E_HUMAN
AccessioniPrimary (citable) accession number: Q12965
Secondary accession number(s): Q14778
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 9, 2002
Last sequence update: November 24, 2008
Last modified: March 3, 2015
This is version 141 of the entry and version 2 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

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.