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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).By similarity

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. receptor binding Source: UniProtKB

GO - Biological processi

  1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  2. innate immune response Source: Reactome
  3. membrane organization Source: Reactome
  4. mRNA transport Source: UniProtKB-KW
  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 1 Publication. Nucleus 1 Publication
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.
Isoform 2 : Cytoplasm. Cell membrane By similarity; Peripheral membrane protein By similarity; 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).By similarity
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.By similarity

GO - Cellular componenti

  1. basal plasma membrane Source: UniProtKB
  2. brush border Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. cytoplasmic vesicle Source: UniProtKB-KW
  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-KW
  15. nucleus Source: HPA
  16. plasma membrane Source: UniProtKB
  17. stereocilium Source: Ensembl
  18. 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

Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKBiPA31399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10631063Unconventional myosin-IcPRO_0000123445Add
BLAST

Amino acid modifications

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

BgeeiO00159.
CleanExiHS_MYO1C.
ExpressionAtlasiO00159. baseline and differential.
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.By similarity3 Publications

Protein-protein interaction databases

BioGridi110725. 39 interactions.
DIPiDIP-33109N.
IntActiO00159. 16 interactions.
MINTiMINT-1149702.
STRINGi9606.ENSP00000352834.

Structurei

Secondary structure

1
1063
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi51 – 533Combined sources
Helixi60 – 7213Combined sources
Beta strandi77 – 804Combined sources
Beta strandi83 – 875Combined sources
Helixi98 – 1047Combined sources
Helixi109 – 1113Combined sources
Helixi116 – 12914Combined sources
Beta strandi134 – 1396Combined sources
Helixi146 – 16015Combined sources
Helixi170 – 18516Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi198 – 2069Combined sources
Beta strandi212 – 2209Combined sources
Helixi225 – 2273Combined sources
Helixi238 – 2469Combined sources
Helixi249 – 2546Combined sources
Helixi261 – 2633Combined sources
Turni265 – 2673Combined sources
Beta strandi269 – 2713Combined sources
Helixi280 – 29314Combined sources
Helixi298 – 31619Combined sources
Helixi333 – 34210Combined sources
Helixi346 – 3549Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi366 – 3683Combined sources
Helixi371 – 40131Combined sources
Beta strandi408 – 4136Combined sources
Beta strandi415 – 4217Combined sources
Beta strandi429 – 4313Combined sources
Helixi433 – 45321Combined sources
Helixi455 – 46410Combined sources
Helixi477 – 4848Combined sources
Turni486 – 4883Combined sources
Helixi490 – 4967Combined sources
Beta strandi499 – 5035Combined sources
Helixi506 – 51611Combined sources
Beta strandi528 – 5303Combined sources
Beta strandi535 – 5373Combined sources
Beta strandi539 – 5468Combined sources
Beta strandi549 – 5546Combined sources
Helixi558 – 5625Combined sources
Helixi568 – 5758Combined sources
Helixi580 – 5856Combined sources
Helixi600 – 61617Combined sources
Beta strandi618 – 6269Combined sources
Helixi639 – 64911Combined sources
Helixi651 – 66010Combined sources
Beta strandi663 – 6675Combined sources
Helixi668 – 6758Combined sources
Helixi676 – 6783Combined sources
Beta strandi682 – 6843Combined sources
Helixi690 – 70112Combined sources
Beta strandi707 – 7104Combined sources
Beta strandi712 – 7187Combined sources
Helixi720 – 75334Combined sources

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, 768-802.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 731685Myosin motorAdd
BLAST
Domaini734 – 75724IQ 1PROSITE-ProRule annotationAdd
BLAST
Domaini758 – 78629IQ 2PROSITE-ProRule annotationAdd
BLAST
Domaini873 – 1058186Myosin tailSequence AnalysisAdd
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 the myosin tail domain (PH-like) present in its tail domain (By similarity).By similarity

Sequence similaritiesi

Contains 2 IQ domains.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated
Contains 1 myosin tail domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00760000118956.
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) [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

        10         20         30         40         50
MALQVELVPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD
60 70 80 90 100
FVLLENFTSE AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH
110 120 130 140 150
MERYRGVSFY EVPPHLFAVA DTVYRALRTE RRDQAVMISG ESGAGKTEAT
160 170 180 190 200
KRLLQFYAET CPAPERGGAV RDRLLQSNPV LEAFGNAKTL RNDNSSRFGK
210 220 230 240 250
YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHIF YQLLEGGEEE
260 270 280 290 300
TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVVRKA LTVIDFTEDE
310 320 330 340 350
VEDLLSIVAS VLHLGNIHFA ANEESNAQVT TENQLKYLTR LLSVEGSTLR
360 370 380 390 400
EALTHRKIIA KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVGKINRS
410 420 430 440 450
LASKDVESPS WRSTTVLGLL DIYGFEVFQH NSFEQFCINY CNEKLQQLFI
460 470 480 490 500
ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC DLVEEKFKGI ISILDEECLR
510 520 530 540 550
PGEATDLTFL EKLEDTVKHH PHFLTHKLAD QRTRKSLGRG EFRLLHYAGE
560 570 580 590 600
VTYSVTGFLD KNNDLLFRNL KETMCSSKNP IMSQCFDRSE LSDKKRPETV
610 620 630 640 650
ATQFKMSLLQ LVEILQSKEP AYVRCIKPND AKQPGRFDEV LIRHQVKYLG
660 670 680 690 700
LLENLRVRRA GFAYRRKYEA FLQRYKSLCP ETWPTWAGRP QDGVAVLVRH
710 720 730 740 750
LGYKPEEYKM GRTKIFIRFP KTLFATEDAL EVRRQSLATK IQAAWRGFHW
760 770 780 790 800
RQKFLRVKRS AICIQSWWRG TLGRRKAAKR KWAAQTIRRL IRGFVLRHAP
810 820 830 840 850
RCPENAFFLD HVRTSFLLNL RRQLPQNVLD TSWPTPPPAL REASELLREL
860 870 880 890 900
CIKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR
910 920 930 940 950
LGTDEISPRV LQALGSEPIQ YAVPVVKYDR KGYKPRSRQL LLTPNAVVIV
960 970 980 990 1000
EDAKVKQRID YANLTGISVS SLSDSLFVLH VQRADNKQKG DVVLQSDHVI
1010 1020 1030 1040 1050
ETLTKTALSA NRVNSININQ GSITFAGGPG RDGTIDFTPG SELLITKAKN
1060
GHLAVVAPRL NSR
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371E → D in CAA67131. (PubMed:9119401)Curated
Sequence conflicti152 – 1521R → K in CAA67131. (PubMed:9119401)Curated
Sequence conflicti165 – 1651E → Q in CAA67131. (PubMed:9119401)Curated
Sequence conflicti200 – 2001K → E in BU855623. 1 PublicationCurated
Sequence conflicti324 – 3241E → D in CAA67131. (PubMed:9119401)Curated
Sequence conflicti379 – 3791D → N in CAA67131. (PubMed:9119401)Curated
Sequence conflicti453 – 4531T → P in CAA67131. (PubMed:9119401)Curated
Sequence conflicti832 – 8321S → Y in CAA67131. (PubMed:9119401)Curated
Sequence conflicti986 – 9861N → I in CAA67131. (PubMed:9119401)Curated
Sequence conflicti1062 – 10621S → Y in CAA67131. (PubMed:9119401)Curated

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. 2 PublicationsVSP_036861Add
BLAST
Alternative sequencei1 – 2525MALQV…RPCKL → MRYRAS in isoform 3. 1 PublicationVSP_036862Add
BLAST

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, 768-802.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110725. 39 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.
Orphaneti 90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKBi PA31399.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5022.
GeneTreei ENSGT00760000118956.
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

Bgeei O00159.
CleanExi HS_MYO1C.
ExpressionAtlasi O00159. baseline and differential.
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: October 29, 2014
This is version 146 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