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O00159 (MYO1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-Ic
Alternative name(s):
Myosin I beta
Short name=MMI-beta
Short name=MMIb
Gene names
Name:MYO1C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1063 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails 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. Ref.16

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. Ref.16

Subunit structure

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. Ref.9 Ref.10 Ref.16

Subcellular location

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. Ref.8 Ref.9 Ref.14

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. Ref.8 Ref.9 Ref.14

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. Ref.8 Ref.9 Ref.14

Domain

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.

Post-translational modification

Isoform 2 contains a N-acetylmethionine at position 1.

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Contains 2 IQ domains.

Contains 1 myosin motor domain.

Caution

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

Sequence caution

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.

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Membrane
Nuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

membrane organization

Traceable author statement. Source: Reactome

positive regulation of cell migration

Inferred from mutant phenotype PubMed 21402783. Source: UniProtKB

positive regulation of cell migration by vascular endothelial growth factor signaling pathway

Inferred from mutant phenotype PubMed 23262137. Source: UniProtKB

positive regulation of protein targeting to membrane

Inferred from mutant phenotype PubMed 23262137. Source: UniProtKB

positive regulation of vascular endothelial growth factor signaling pathway

Inferred from mutant phenotype PubMed 23262137. Source: UniProtKB

protein targeting

Inferred from direct assay PubMed 21402783. Source: UniProtKB

protein targeting to membrane

Inferred from direct assay PubMed 21402783. Source: UniProtKB

regulation of tight junction assembly

Inferred from mutant phenotype PubMed 21402783. Source: UniProtKB

   Cellular_componentbasal plasma membrane

Inferred from direct assay PubMed 9858156. Source: UniProtKB

brush border

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 21402783PubMed 9858156. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

filamentous actin

Inferred from direct assay PubMed 9858156. Source: UniProtKB

lateral plasma membrane

Inferred from direct assay PubMed 9858156. Source: UniProtKB

membrane

Inferred from direct assay PubMed 21402783. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 23262137. Source: UniProtKB

microvillus

Inferred from direct assay PubMed 9858156. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

myosin I complex

Inferred from electronic annotation. Source: Ensembl

nuclear pore

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay PubMed 23262137. Source: UniProtKB

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

stereocilium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

unconventional myosin complex

Traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

motor activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 21402783. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 21402783. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00159-1)

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.
Isoform 2 (identifier: O00159-2)

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.
Isoform 3 (identifier: O00159-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10631063Unconventional myosin-Ic
PRO_0000123445

Regions

Domain47 – 731685Myosin motor
Domain734 – 75724IQ 1
Domain758 – 78629IQ 2
Nucleotide binding139 – 14810ATP
Nucleotide binding192 – 1965ATP
Region927 – 93812PIP2-binding motif By similarity

Sites

Binding site881ATP
Binding site961ATP

Amino acid modifications

Modified residue3831N6-methyllysine Ref.7
Modified residue4081Phosphoserine Ref.11 Ref.12
Modified residue4861N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 3535Missing in isoform 2.
VSP_036861
Alternative sequence1 – 2525MALQV…RPCKL → MRYRAS in isoform 3.
VSP_036862
Natural variant7951V → I. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs8081370 [ dbSNP | Ensembl ].
VAR_054855
Natural variant8261Q → R. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs9905106 [ dbSNP | Ensembl ].
VAR_054856

Experimental info

Mutagenesis7361S → A: Abolishes interaction with YWHAB. Ref.16
Mutagenesis7361S → E: Increases affinity for YWHAB. Ref.16
Sequence conflict371E → D in CAA67131. Ref.1
Sequence conflict1521R → K in CAA67131. Ref.1
Sequence conflict1651E → Q in CAA67131. Ref.1
Sequence conflict2001K → E in BU855623. Ref.6
Sequence conflict3241E → D in CAA67131. Ref.1
Sequence conflict3791D → N in CAA67131. Ref.1
Sequence conflict4531T → P in CAA67131. Ref.1
Sequence conflict8321S → Y in CAA67131. Ref.1
Sequence conflict9861N → I in CAA67131. Ref.1
Sequence conflict10621S → Y in CAA67131. Ref.1

Secondary structure

............................................................................................................ 1063
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: B105197BA07317B8

FASTA1,063121,682
        10         20         30         40         50         60 
MALQVELVPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD FVLLENFTSE 

        70         80         90        100        110        120 
AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH MERYRGVSFY EVPPHLFAVA 

       130        140        150        160        170        180 
DTVYRALRTE RRDQAVMISG ESGAGKTEAT KRLLQFYAET CPAPERGGAV RDRLLQSNPV 

       190        200        210        220        230        240 
LEAFGNAKTL RNDNSSRFGK YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHIF 

       250        260        270        280        290        300 
YQLLEGGEEE TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVVRKA LTVIDFTEDE 

       310        320        330        340        350        360 
VEDLLSIVAS VLHLGNIHFA ANEESNAQVT TENQLKYLTR LLSVEGSTLR EALTHRKIIA 

       370        380        390        400        410        420 
KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVGKINRS LASKDVESPS WRSTTVLGLL 

       430        440        450        460        470        480 
DIYGFEVFQH NSFEQFCINY CNEKLQQLFI ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC 

       490        500        510        520        530        540 
DLVEEKFKGI ISILDEECLR PGEATDLTFL EKLEDTVKHH PHFLTHKLAD QRTRKSLGRG 

       550        560        570        580        590        600 
EFRLLHYAGE VTYSVTGFLD KNNDLLFRNL KETMCSSKNP IMSQCFDRSE LSDKKRPETV 

       610        620        630        640        650        660 
ATQFKMSLLQ LVEILQSKEP AYVRCIKPND AKQPGRFDEV LIRHQVKYLG LLENLRVRRA 

       670        680        690        700        710        720 
GFAYRRKYEA FLQRYKSLCP ETWPTWAGRP QDGVAVLVRH LGYKPEEYKM GRTKIFIRFP 

       730        740        750        760        770        780 
KTLFATEDAL EVRRQSLATK IQAAWRGFHW RQKFLRVKRS AICIQSWWRG TLGRRKAAKR 

       790        800        810        820        830        840 
KWAAQTIRRL IRGFVLRHAP RCPENAFFLD HVRTSFLLNL RRQLPQNVLD TSWPTPPPAL 

       850        860        870        880        890        900 
REASELLREL CIKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR 

       910        920        930        940        950        960 
LGTDEISPRV LQALGSEPIQ YAVPVVKYDR KGYKPRSRQL LLTPNAVVIV EDAKVKQRID 

       970        980        990       1000       1010       1020 
YANLTGISVS SLSDSLFVLH VQRADNKQKG DVVLQSDHVI ETLTKTALSA NRVNSININQ 

      1030       1040       1050       1060 
GSITFAGGPG RDGTIDFTPG SELLITKAKN GHLAVVAPRL NSR 

« Hide

Isoform 2 (C) [UniParc].

Checksum: 06D3340F7D2A199F
Show »

FASTA1,028117,907
Isoform 3 (B) (Nuclear myosin 1) (NM1) (NMI) [UniParc].

Checksum: E78D68A46592DC89
Show »

FASTA1,044119,628

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11003.1. [O00159-2]
CCDS42226.1. [O00159-1]
CCDS45562.1. [O00159-3]
PIRA59253.
RefSeqNP_001074248.1. NM_001080779.1. [O00159-1]
NP_001074419.1. NM_001080950.1. [O00159-3]
NP_203693.3. NM_033375.4. [O00159-2]
UniGeneHs.286226.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BYFX-ray2.74A/C36-760[»]
ProteinModelPortalO00159.
SMRO00159. Positions 44-755, 771-801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110725. 38 interactions.
DIPDIP-33109N.
IntActO00159. 15 interactions.
MINTMINT-1149702.
STRING9606.ENSP00000352834.

PTM databases

PhosphoSiteO00159.

Proteomic databases

MaxQBO00159.
PaxDbO00159.
PeptideAtlasO00159.
PRIDEO00159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359786; ENSP00000352834; ENSG00000197879. [O00159-1]
ENST00000361007; ENSP00000354283; ENSG00000197879. [O00159-2]
ENST00000438665; ENSP00000412197; ENSG00000197879. [O00159-3]
ENST00000575158; ENSP00000459174; ENSG00000197879. [O00159-2]
GeneID4641.
KEGGhsa:4641.
UCSCuc002fsn.3. human. [O00159-3]
uc002fso.3. human. [O00159-1]

Organism-specific databases

CTD4641.
GeneCardsGC17M001367.
H-InvDBHIX0202539.
HGNCHGNC:7597. MYO1C.
HPACAB037023.
HPA001768.
MIM606538. gene.
neXtProtNX_O00159.
PharmGKBPA31399.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000260264.
InParanoidO00159.
KOK10356.
OMAYAETCPA.
OrthoDBEOG7V49XQ.
PhylomeDBO00159.
TreeFamTF312960.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressO00159.
BgeeO00159.
CleanExHS_MYO1C.
GenevestigatorO00159.

Family and domain databases

InterProIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00612. IQ. 2 hits.
PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS50096. IQ. 2 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO1C. human.
GeneWikiMYO1C.
GenomeRNAi4641.
NextBio17880.
PROO00159.
SOURCESearch...

Entry information

Entry nameMYO1C_HUMAN
AccessionPrimary (citable) accession number: O00159
Secondary accession number(s): Q4LE56, Q6NVJ7, Q86Y95
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM