Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q12965

- MYO1E_HUMAN

UniProt

Q12965 - MYO1E_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Unconventional myosin-Ie

Gene

MYO1E

Organism
Homo sapiens (Human)
Status
Reviewed - 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. ATP catabolic process Source: GOC
  3. endocytosis Source: UniProtKB
  4. glomerular basement membrane development Source: UniProtKB
  5. glomerular filtration Source: UniProtKB
  6. glomerular visceral epithelial cell development Source: UniProtKB
  7. in utero embryonic development 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: 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. cytoplasm Source: UniProtKB
  5. cytoplasmic vesicle Source: UniProtKB-KW
  6. cytoskeleton Source: UniProtKB
  7. extracellular vesicular exosome Source: UniProt
  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) [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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
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. 28 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.
OMAiKLKKENW.
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 25, 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U14391 mRNA. Translation: AAA62667.1 .
AC092756 Genomic DNA. No translation available.
L29139 mRNA. Translation: AAA20902.1 .
CCDSi CCDS32254.1.
PIRi S53601.
RefSeqi NP_004989.2. NM_004998.3.
UniGenei Hs.654506.

3D structure databases

ProteinModelPortali Q12965.
SMRi Q12965. Positions 1054-1108.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110727. 28 interactions.
DIPi DIP-884N.
IntActi Q12965. 7 interactions.
MINTi MINT-3026848.
STRINGi 9606.ENSP00000288235.

PTM databases

PhosphoSitei Q12965.

Polymorphism databases

DMDMi 215274106.

Proteomic databases

MaxQBi Q12965.
PaxDbi Q12965.
PRIDEi Q12965.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000288235 ; ENSP00000288235 ; ENSG00000157483 .
GeneIDi 4643.
KEGGi hsa:4643.
UCSCi uc002aga.4. human.

Organism-specific databases

CTDi 4643.
GeneCardsi GC15M059428.
H-InvDB HIX0038144.
HGNCi HGNC:7599. MYO1E.
HPAi HPA023886.
MIMi 601479. gene.
614131. phenotype.
neXtProti NX_Q12965.
Orphaneti 93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBi PA31401.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5022.
HOGENOMi HOG000260265.
HOVERGENi HBG100702.
InParanoidi Q12965.
KOi K10356.
OMAi KLKKENW.
OrthoDBi EOG7V49XQ.
PhylomeDBi Q12965.
TreeFami TF312960.

Miscellaneous databases

ChiTaRSi MYO1E. human.
GeneWikii MYO1E.
GenomeRNAii 4643.
NextBioi 17892.
PROi Q12965.
SOURCEi Search...

Gene expression databases

Bgeei Q12965.
CleanExi HS_MYO1C.
HS_MYO1E.
ExpressionAtlasi Q12965. baseline and differential.
Genevestigatori Q12965.

Family and domain databases

InterProi IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00193. MYOSINHEAVY.
PR00452. SH3DOMAIN.
SMARTi SM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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. 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(2007) [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(2010) [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(2010) [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(2011) [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 10, 2002
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 139 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