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O00159

- MYO1C_HUMAN

UniProt

O00159 - MYO1C_HUMAN

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Protein
Unconventional myosin-Ic
Gene
MYO1C
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 are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.1 Publication
Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation By similarity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881ATP
Binding sitei96 – 961ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi139 – 14810ATP
Nucleotide bindingi192 – 1965ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. motor activity Source: InterPro
  3. protein binding Source: UniProtKB
  4. receptor binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  2. innate immune response Source: Reactome
  3. mRNA transport Source: UniProtKB-KW
  4. membrane organization Source: Reactome
  5. positive regulation of cell migration Source: UniProtKB
  6. positive regulation of cell migration by vascular endothelial growth factor signaling pathway Source: UniProtKB
  7. positive regulation of protein targeting to membrane Source: UniProtKB
  8. positive regulation of vascular endothelial growth factor signaling pathway Source: UniProtKB
  9. protein targeting Source: UniProtKB
  10. protein targeting to membrane Source: UniProtKB
  11. regulation of tight junction assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-Ic
Alternative name(s):
Myosin I beta
Short name:
MMI-beta
Short name:
MMIb
Gene namesi
Name:MYO1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:7597. MYO1C.

Subcellular locationi

Isoform 1 : Cytoplasm. Nucleus
Note: Colocalizes with RNA polymerase II. Absent from nucleoli and does not colocalize with RNA polymerase I. Translocates to nuclear speckles upon exposure to inhibitors of RNA polymerase II transcription.3 Publications
Isoform 2 : Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projectionstereocilium membrane By similarity. Cell projectionruffle By similarity. Cytoplasmic vesicle By similarity
Note: Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on the cell membrane. Colocalizes in adipocytes with GLUT4 at actin-based membranes. Colocalizes with GLUT4 at insulin-induced ruffles at the cell membrane. Localizes transiently at cell membrane to region known to be enriched in PIP2. Activation of phospholipase C results in its redistribution to the cytoplasm By similarity.3 Publications
Isoform 3 : Nucleusnucleoplasm. Nucleusnucleolus. Nucleusnuclear pore complex
Note: Colocalizes with RNA polymerase II in the nucleus. Colocalizes with RNA polymerase I in nucleoli By similarity. In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC). Accumulates strongly in DFC and GC during activation of transcription. Colocalizes with transcription sites. Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6. Colocalizes in nucleoplasm with RPS6 and actin that are in contact with RNP particles. Colocalizes with RPS6 at the nuclear pore level.3 Publications

GO - Cellular componenti

  1. basal plasma membrane Source: UniProtKB
  2. brush border Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProtKB
  7. filamentous actin Source: UniProtKB
  8. lateral plasma membrane Source: UniProtKB
  9. membrane Source: UniProtKB
  10. membrane raft Source: UniProtKB
  11. microvillus Source: UniProtKB
  12. mitochondrion Source: HPA
  13. myosin I complex Source: Ensembl
  14. nuclear pore Source: UniProtKB-SubCell
  15. nucleoplasm Source: UniProtKB-SubCell
  16. nucleus Source: HPA
  17. plasma membrane Source: UniProtKB
  18. ruffle Source: UniProtKB-SubCell
  19. stereocilium membrane Source: UniProtKB-SubCell
  20. unconventional myosin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi736 – 7361S → A: Abolishes interaction with YWHAB. 1 Publication
Mutagenesisi736 – 7361S → E: Increases affinity for YWHAB. 1 Publication

Organism-specific databases

PharmGKBiPA31399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10631063Unconventional myosin-Ic
PRO_0000123445Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei383 – 3831N6-methyllysine1 Publication
Modified residuei408 – 4081Phosphoserine2 Publications
Modified residuei486 – 4861N6-acetyllysine By similarity

Post-translational modificationi

Isoform 2 contains a N-acetylmethionine at position 1.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiO00159.
PaxDbiO00159.
PeptideAtlasiO00159.
PRIDEiO00159.

PTM databases

PhosphoSiteiO00159.

Expressioni

Gene expression databases

ArrayExpressiO00159.
BgeeiO00159.
CleanExiHS_MYO1C.
GenevestigatoriO00159.

Organism-specific databases

HPAiCAB037023.
HPA001768.

Interactioni

Subunit structurei

Interacts with GLUT4 By similarity. Interacts (via its IQ motifs) with CABP1 and CIB1; the interaction with CABP1 and CIB1 is calcium-dependent. Interacts (via tail domain) with PLEKHB1 (via PH domain); the interaction is not affected by the presence or absence of calcium and CALM. Interacts with POLR1A and POLR2A. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts (via its IQ motifs) with CALM; this precludes interaction with YWHAB. Interacts with YWHAB; this precludes interaction with CALM. Interacts with RPS6 and actin.3 Publications

Protein-protein interaction databases

BioGridi110725. 38 interactions.
DIPiDIP-33109N.
IntActiO00159. 16 interactions.
MINTiMINT-1149702.
STRINGi9606.ENSP00000352834.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi51 – 533
Helixi60 – 7213
Beta strandi77 – 804
Beta strandi83 – 875
Helixi98 – 1047
Helixi109 – 1113
Helixi116 – 12914
Beta strandi134 – 1396
Helixi146 – 16015
Helixi170 – 18516
Beta strandi193 – 1964
Beta strandi198 – 2069
Beta strandi212 – 2209
Helixi225 – 2273
Helixi238 – 2469
Helixi249 – 2546
Helixi261 – 2633
Turni265 – 2673
Beta strandi269 – 2713
Helixi280 – 29314
Helixi298 – 31619
Helixi333 – 34210
Helixi346 – 3549
Beta strandi355 – 3573
Beta strandi366 – 3683
Helixi371 – 40131
Beta strandi408 – 4136
Beta strandi415 – 4217
Beta strandi429 – 4313
Helixi433 – 45321
Helixi455 – 46410
Helixi477 – 4848
Turni486 – 4883
Helixi490 – 4967
Beta strandi499 – 5035
Helixi506 – 51611
Beta strandi528 – 5303
Beta strandi535 – 5373
Beta strandi539 – 5468
Beta strandi549 – 5546
Helixi558 – 5625
Helixi568 – 5758
Helixi580 – 5856
Helixi600 – 61617
Beta strandi618 – 6269
Helixi639 – 64911
Helixi651 – 66010
Beta strandi663 – 6675
Helixi668 – 6758
Helixi676 – 6783
Beta strandi682 – 6843
Helixi690 – 70112
Beta strandi707 – 7104
Beta strandi712 – 7187
Helixi720 – 75334

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BYFX-ray2.74A/C36-760[»]
ProteinModelPortaliO00159.
SMRiO00159. Positions 44-755, 771-801.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 731685Myosin motor
Add
BLAST
Domaini734 – 75724IQ 1
Add
BLAST
Domaini758 – 78629IQ 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni927 – 93812PIP2-binding motif By similarity
Add
BLAST

Domaini

Binds directly to large unilamellar vesicles (LUVs) containing phosphatidylinositol 4,5-bisphosphate (PIP2) or inositol 1,4,5-trisphosphate (InsP3). The PIP2-binding site corresponds to a putative PH domain present in its tail domain By similarity.

Sequence similaritiesi

Contains 2 IQ domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5022.
HOGENOMiHOG000260264.
InParanoidiO00159.
KOiK10356.
OMAiYAETCPA.
OrthoDBiEOG7V49XQ.
PhylomeDBiO00159.
TreeFamiTF312960.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00612. IQ. 2 hits.
PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 2 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O00159-1) [UniParc]FASTAAdd to Basket

Also known as: A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MALQVELVPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD     50
FVLLENFTSE AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH 100
MERYRGVSFY EVPPHLFAVA DTVYRALRTE RRDQAVMISG ESGAGKTEAT 150
KRLLQFYAET CPAPERGGAV RDRLLQSNPV LEAFGNAKTL RNDNSSRFGK 200
YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHIF YQLLEGGEEE 250
TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVVRKA LTVIDFTEDE 300
VEDLLSIVAS VLHLGNIHFA ANEESNAQVT TENQLKYLTR LLSVEGSTLR 350
EALTHRKIIA KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVGKINRS 400
LASKDVESPS WRSTTVLGLL DIYGFEVFQH NSFEQFCINY CNEKLQQLFI 450
ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC DLVEEKFKGI ISILDEECLR 500
PGEATDLTFL EKLEDTVKHH PHFLTHKLAD QRTRKSLGRG EFRLLHYAGE 550
VTYSVTGFLD KNNDLLFRNL KETMCSSKNP IMSQCFDRSE LSDKKRPETV 600
ATQFKMSLLQ LVEILQSKEP AYVRCIKPND AKQPGRFDEV LIRHQVKYLG 650
LLENLRVRRA GFAYRRKYEA FLQRYKSLCP ETWPTWAGRP QDGVAVLVRH 700
LGYKPEEYKM GRTKIFIRFP KTLFATEDAL EVRRQSLATK IQAAWRGFHW 750
RQKFLRVKRS AICIQSWWRG TLGRRKAAKR KWAAQTIRRL IRGFVLRHAP 800
RCPENAFFLD HVRTSFLLNL RRQLPQNVLD TSWPTPPPAL REASELLREL 850
CIKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR 900
LGTDEISPRV LQALGSEPIQ YAVPVVKYDR KGYKPRSRQL LLTPNAVVIV 950
EDAKVKQRID YANLTGISVS SLSDSLFVLH VQRADNKQKG DVVLQSDHVI 1000
ETLTKTALSA NRVNSININQ GSITFAGGPG RDGTIDFTPG SELLITKAKN 1050
GHLAVVAPRL NSR 1063
Length:1,063
Mass (Da):121,682
Last modified:January 11, 2011 - v4
Checksum:iB105197BA07317B8
GO
Isoform 2 (identifier: O00159-2) [UniParc]FASTAAdd to Basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Note: Contains a N-acetylmethionine at position 1.

Show »
Length:1,028
Mass (Da):117,907
Checksum:i06D3340F7D2A199F
GO
Isoform 3 (identifier: O00159-3) [UniParc]FASTAAdd to Basket

Also known as: B, Nuclear myosin 1, NM1, NMI

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MALQVELVPTGEIIRVVHPHRPCKL → MRYRAS

Show »
Length:1,044
Mass (Da):119,628
Checksum:iE78D68A46592DC89
GO

Sequence cautioni

The sequence AAH68013.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAE06097.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAF85599.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti795 – 7951V → I.4 Publications
Corresponds to variant rs8081370 [ dbSNP | Ensembl ].
VAR_054855
Natural varianti826 – 8261Q → R.4 Publications
Corresponds to variant rs9905106 [ dbSNP | Ensembl ].
VAR_054856

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3535Missing in isoform 2.
VSP_036861Add
BLAST
Alternative sequencei1 – 2525MALQV…RPCKL → MRYRAS in isoform 3.
VSP_036862Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371E → D in CAA67131. 1 Publication
Sequence conflicti152 – 1521R → K in CAA67131. 1 Publication
Sequence conflicti165 – 1651E → Q in CAA67131. 1 Publication
Sequence conflicti200 – 2001K → E in BU855623. 1 Publication
Sequence conflicti324 – 3241E → D in CAA67131. 1 Publication
Sequence conflicti379 – 3791D → N in CAA67131. 1 Publication
Sequence conflicti453 – 4531T → P in CAA67131. 1 Publication
Sequence conflicti832 – 8321S → Y in CAA67131. 1 Publication
Sequence conflicti986 – 9861N → I in CAA67131. 1 Publication
Sequence conflicti1062 – 10621S → Y in CAA67131. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98507 mRNA. Translation: CAA67131.1.
AK292910 mRNA. Translation: BAF85599.1. Different initiation.
AB210015 mRNA. Translation: BAE06097.1. Different initiation.
AC100748 Genomic DNA. No translation available.
BC044891 mRNA. Translation: AAH44891.2.
BC068013 mRNA. Translation: AAH68013.1. Different initiation.
BU855623 mRNA. No translation available.
CCDSiCCDS11003.1. [O00159-2]
CCDS42226.1. [O00159-1]
CCDS45562.1. [O00159-3]
PIRiA59253.
RefSeqiNP_001074248.1. NM_001080779.1. [O00159-1]
NP_001074419.1. NM_001080950.1. [O00159-3]
NP_203693.3. NM_033375.4. [O00159-2]
UniGeneiHs.286226.

Genome annotation databases

EnsembliENST00000359786; ENSP00000352834; ENSG00000197879. [O00159-1]
ENST00000361007; ENSP00000354283; ENSG00000197879. [O00159-2]
ENST00000438665; ENSP00000412197; ENSG00000197879. [O00159-3]
ENST00000575158; ENSP00000459174; ENSG00000197879. [O00159-2]
GeneIDi4641.
KEGGihsa:4641.
UCSCiuc002fsn.3. human. [O00159-3]
uc002fso.3. human. [O00159-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98507 mRNA. Translation: CAA67131.1 .
AK292910 mRNA. Translation: BAF85599.1 . Different initiation.
AB210015 mRNA. Translation: BAE06097.1 . Different initiation.
AC100748 Genomic DNA. No translation available.
BC044891 mRNA. Translation: AAH44891.2 .
BC068013 mRNA. Translation: AAH68013.1 . Different initiation.
BU855623 mRNA. No translation available.
CCDSi CCDS11003.1. [O00159-2 ]
CCDS42226.1. [O00159-1 ]
CCDS45562.1. [O00159-3 ]
PIRi A59253.
RefSeqi NP_001074248.1. NM_001080779.1. [O00159-1 ]
NP_001074419.1. NM_001080950.1. [O00159-3 ]
NP_203693.3. NM_033375.4. [O00159-2 ]
UniGenei Hs.286226.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BYF X-ray 2.74 A/C 36-760 [» ]
ProteinModelPortali O00159.
SMRi O00159. Positions 44-755, 771-801.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110725. 38 interactions.
DIPi DIP-33109N.
IntActi O00159. 16 interactions.
MINTi MINT-1149702.
STRINGi 9606.ENSP00000352834.

PTM databases

PhosphoSitei O00159.

Proteomic databases

MaxQBi O00159.
PaxDbi O00159.
PeptideAtlasi O00159.
PRIDEi O00159.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359786 ; ENSP00000352834 ; ENSG00000197879 . [O00159-1 ]
ENST00000361007 ; ENSP00000354283 ; ENSG00000197879 . [O00159-2 ]
ENST00000438665 ; ENSP00000412197 ; ENSG00000197879 . [O00159-3 ]
ENST00000575158 ; ENSP00000459174 ; ENSG00000197879 . [O00159-2 ]
GeneIDi 4641.
KEGGi hsa:4641.
UCSCi uc002fsn.3. human. [O00159-3 ]
uc002fso.3. human. [O00159-1 ]

Organism-specific databases

CTDi 4641.
GeneCardsi GC17M001367.
H-InvDB HIX0202539.
HGNCi HGNC:7597. MYO1C.
HPAi CAB037023.
HPA001768.
MIMi 606538. gene.
neXtProti NX_O00159.
PharmGKBi PA31399.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5022.
HOGENOMi HOG000260264.
InParanoidi O00159.
KOi K10356.
OMAi YAETCPA.
OrthoDBi EOG7V49XQ.
PhylomeDBi O00159.
TreeFami TF312960.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

ChiTaRSi MYO1C. human.
GeneWikii MYO1C.
GenomeRNAii 4641.
NextBioi 17880.
PROi O00159.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00159.
Bgeei O00159.
CleanExi HS_MYO1C.
Genevestigatori O00159.

Family and domain databases

InterProi IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00612. IQ. 2 hits.
PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
[Graphical view ]
PRINTSi PR00193. MYOSINHEAVY.
SMARTi SM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS50096. IQ. 2 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the genes encoding two murine and human cochlear unconventional type I myosins."
    Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P., Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D., Pujol R., Petit C.
    Genomics 40:332-341(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS ILE-795 AND ARG-826.
    Tissue: Kidney.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-795 AND ARG-826.
    Tissue: Trachea.
  3. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
    Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-795 AND ARG-826.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2), VARIANTS ILE-795 AND ARG-826.
    Tissue: Eye and Liver.
  6. Strausberg R.L.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-206 (ISOFORM 3).
    Tissue: Teratocarcinoma.
  7. Bienvenut W.V., Calvo F.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 36-43; 92-98; 104-125; 133-146; 172-188; 198-209; 255-269; 341-350; 357-396; 400-412; 562-568; 606-624; 633-643; 648-656; 666-674; 715-734; 814-822; 827-841; 875-884; 886-894; 901-930; 937-956 AND 988-1047, ACETYLATION AT MET-1 (ISOFORM 2), METHYLATION AT LYS-383, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  8. "Nuclear distribution of actin and myosin I depends on transcriptional activity of the cell."
    Kysela K., Philimonenko A.A., Philimonenko V.V., Janacek J., Kahle M., Hozak P.
    Histochem. Cell Biol. 124:347-358(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Small ribosomal subunits associate with nuclear myosin and actin in transit to the nuclear pores."
    Cisterna B., Necchi D., Prosperi E., Biggiogera M.
    FASEB J. 20:1901-1903(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS6 AND ACTIN, SUBCELLULAR LOCATION.
  10. "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
    Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
    J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Identification and characterization of a novel myosin Ic isoform that localizes to the nucleus."
    Ihnatovych I., Migocka-Patrzalek M., Dukh M., Hofmann W.A.
    Cytoskeleton 69:555-565(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1).
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Crystal structure of human myosin 1c - the motor in GLUT4 exocytosis: implications for Ca(2+)-regulation and 14-3-3 binding."
    Stefan Munnich M.H., Manstein D.J.
    J. Mol. Biol. 426:2070-2081(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 36-760 (ISOFORM 2) IN COMPLEX WITH ADP ORTHOVANADATE AND CALM, INTERACTION WITH CALM AND YWHAB, FUNCTION, ACTIN-BINDING, FUNCTION IN ACTIN-DEPENDENT ATP HYDROLYSIS, MUTAGENESIS OF SER-736.

Entry informationi

Entry nameiMYO1C_HUMAN
AccessioniPrimary (citable) accession number: O00159
Secondary accession number(s): Q4LE56, Q6NVJ7, Q86Y95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 144 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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