O00159 (MYO1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Unconventional myosin-Ic

Alternative name(s):
Myosin I beta
Short name=MMI-beta
Short name=MMIb

Gene names

Name:

MYO1C

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1063 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. 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.
Subunit structure	Interacts (via its IQ motifs) with calmodulin. 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 calmodulin. 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 By similarity. Interacts with RPS6 and actin. Ref.9 Ref.10
Subcellular location	Cytoplasm. Cell membrane By similarity. Cell projection › stereocilium membrane 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 in actin-based membranes. 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 Isoform 3: Nucleus › nucleoplasm. Nucleus › nucleolus. Nucleus › nuclear 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
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	Contains 2 IQ domains. Contains 1 myosin head-like domain.
Caution	Represents a 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 process	Protein transport Translocation Transport mRNA transport
Cellular component	Cell membrane Cell projection Cytoplasm Membrane Nuclear pore complex Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW 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 to membrane Inferred from direct assay PubMed 21402783. Source: UniProtKB regulation of tight junction assembly Inferred from mutant phenotype PubMed 21402783. Source: UniProtKB
Cellular_component	basal plasma membrane Inferred from direct assay PubMed 9858156. Source: UniProtKB brush border Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay PubMed 21402783PubMed 9858156. Source: UniProtKB 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 raft Inferred from direct assay PubMed 23262137. Source: UniProtKB microvillus Inferred from direct assay PubMed 9858156. Source: UniProtKB myosin I complex Inferred from electronic annotation. Source: Compara nuclear pore Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm 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_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW motor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O00159-1)

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)

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: Nuclear myosin 1; NM1;

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

Note: Gene prediction based on EST data.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1063	1063	Unconventional myosin-Ic		PRO_0000123445
Regions
	Domain	36 – 718	683	Myosin head-like
	Domain	734 – 757	24	IQ 1
	Domain	758 – 786	29	IQ 2
	Nucleotide binding	140 – 147	8	ATP Potential
Amino acid modifications
	Modified residue	383	1	N6-methyllysine Ref.7
	Modified residue	408	1	Phosphoserine Ref.11 Ref.12
Natural variations
	Alternative sequence	1 – 35	35	Missing in isoform 2.		VSP_036861
	Alternative sequence	1 – 25	25	MALQV…RPCKL → MRYRAS in isoform 3.		VSP_036862
	Natural variant	795	1	V → I. Ref.1 Ref.2 Ref.3 Ref.5 Corresponds to variant rs8081370 [ dbSNP | Ensembl ].		VAR_054855
	Natural variant	826	1	Q → R. Ref.1 Ref.2 Ref.3 Ref.5 Corresponds to variant rs9905106 [ dbSNP | Ensembl ].		VAR_054856
Experimental info
	Sequence conflict	37	1	E → D in CAA67131. Ref.1
	Sequence conflict	152	1	R → K in CAA67131. Ref.1
	Sequence conflict	165	1	E → Q in CAA67131. Ref.1
	Sequence conflict	200	1	K → E in BU855623. Ref.6
	Sequence conflict	324	1	E → D in CAA67131. Ref.1
	Sequence conflict	379	1	D → N in CAA67131. Ref.1
	Sequence conflict	453	1	T → P in CAA67131. Ref.1
	Sequence conflict	832	1	S → Y in CAA67131. Ref.1
	Sequence conflict	986	1	N → I in CAA67131. Ref.1
	Sequence conflict	1062	1	S → Y in CAA67131. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 4. Checksum: B105197BA07317B8	FASTA	1,063	121,682
	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
	Isoform 2 [UniParc]. Checksum: 06D3340F7D2A199F	FASTA	1,028	117,907
	10 20 30 40 50 60 MESALTARDR VGVQDFVLLE NFTSEAAFIE NLRRRFRENL IYTYIGPVLV SVNPYRDLQI 70 80 90 100 110 120 YSRQHMERYR GVSFYEVPPH LFAVADTVYR ALRTERRDQA VMISGESGAG KTEATKRLLQ 130 140 150 160 170 180 FYAETCPAPE RGGAVRDRLL QSNPVLEAFG NAKTLRNDNS SRFGKYMDVQ FDFKGAPVGG 190 200 210 220 230 240 HILSYLLEKS RVVHQNHGER NFHIFYQLLE GGEEETLRRL GLERNPQSYL YLVKGQCAKV 250 260 270 280 290 300 SSINDKSDWK VVRKALTVID FTEDEVEDLL SIVASVLHLG NIHFAANEES NAQVTTENQL 310 320 330 340 350 360 KYLTRLLSVE GSTLREALTH RKIIAKGEEL LSPLNLEQAA YARDALAKAV YSRTFTWLVG 370 380 390 400 410 420 KINRSLASKD VESPSWRSTT VLGLLDIYGF EVFQHNSFEQ FCINYCNEKL QQLFIELTLK 430 440 450 460 470 480 SEQEEYEAEG IAWEPVQYFN NKIICDLVEE KFKGIISILD EECLRPGEAT DLTFLEKLED 490 500 510 520 530 540 TVKHHPHFLT HKLADQRTRK SLGRGEFRLL HYAGEVTYSV TGFLDKNNDL LFRNLKETMC 550 560 570 580 590 600 SSKNPIMSQC FDRSELSDKK RPETVATQFK MSLLQLVEIL QSKEPAYVRC IKPNDAKQPG 610 620 630 640 650 660 RFDEVLIRHQ VKYLGLLENL RVRRAGFAYR RKYEAFLQRY KSLCPETWPT WAGRPQDGVA 670 680 690 700 710 720 VLVRHLGYKP EEYKMGRTKI FIRFPKTLFA TEDALEVRRQ SLATKIQAAW RGFHWRQKFL 730 740 750 760 770 780 RVKRSAICIQ SWWRGTLGRR KAAKRKWAAQ TIRRLIRGFV LRHAPRCPEN AFFLDHVRTS 790 800 810 820 830 840 FLLNLRRQLP QNVLDTSWPT PPPALREASE LLRELCIKNM VWKYCRSISP EWKQQLQQKA 850 860 870 880 890 900 VASEIFKGKK DNYPQSVPRL FISTRLGTDE ISPRVLQALG SEPIQYAVPV VKYDRKGYKP 910 920 930 940 950 960 RSRQLLLTPN AVVIVEDAKV KQRIDYANLT GISVSSLSDS LFVLHVQRAD NKQKGDVVLQ 970 980 990 1000 1010 1020 SDHVIETLTK TALSANRVNS ININQGSITF AGGPGRDGTI DFTPGSELLI TKAKNGHLAV VAPRLNSR
	Isoform 3 (Nuclear myosin 1) (NM1) [UniParc]. Checksum: E78D68A46592DC89	FASTA	1,044	119,628
	10 20 30 40 50 60 MRYRASALGS DGVRVTMESA LTARDRVGVQ DFVLLENFTS EAAFIENLRR RFRENLIYTY 70 80 90 100 110 120 IGPVLVSVNP YRDLQIYSRQ HMERYRGVSF YEVPPHLFAV ADTVYRALRT ERRDQAVMIS 130 140 150 160 170 180 GESGAGKTEA TKRLLQFYAE TCPAPERGGA VRDRLLQSNP VLEAFGNAKT LRNDNSSRFG 190 200 210 220 230 240 KYMDVQFDFK GAPVGGHILS YLLEKSRVVH QNHGERNFHI FYQLLEGGEE ETLRRLGLER 250 260 270 280 290 300 NPQSYLYLVK GQCAKVSSIN DKSDWKVVRK ALTVIDFTED EVEDLLSIVA SVLHLGNIHF 310 320 330 340 350 360 AANEESNAQV TTENQLKYLT RLLSVEGSTL REALTHRKII AKGEELLSPL NLEQAAYARD 370 380 390 400 410 420 ALAKAVYSRT FTWLVGKINR SLASKDVESP SWRSTTVLGL LDIYGFEVFQ HNSFEQFCIN 430 440 450 460 470 480 YCNEKLQQLF IELTLKSEQE EYEAEGIAWE PVQYFNNKII CDLVEEKFKG IISILDEECL 490 500 510 520 530 540 RPGEATDLTF LEKLEDTVKH HPHFLTHKLA DQRTRKSLGR GEFRLLHYAG EVTYSVTGFL 550 560 570 580 590 600 DKNNDLLFRN LKETMCSSKN PIMSQCFDRS ELSDKKRPET VATQFKMSLL QLVEILQSKE 610 620 630 640 650 660 PAYVRCIKPN DAKQPGRFDE VLIRHQVKYL GLLENLRVRR AGFAYRRKYE AFLQRYKSLC 670 680 690 700 710 720 PETWPTWAGR PQDGVAVLVR HLGYKPEEYK MGRTKIFIRF PKTLFATEDA LEVRRQSLAT 730 740 750 760 770 780 KIQAAWRGFH WRQKFLRVKR SAICIQSWWR GTLGRRKAAK RKWAAQTIRR LIRGFVLRHA 790 800 810 820 830 840 PRCPENAFFL DHVRTSFLLN LRRQLPQNVL DTSWPTPPPA LREASELLRE LCIKNMVWKY 850 860 870 880 890 900 CRSISPEWKQ QLQQKAVASE IFKGKKDNYP QSVPRLFIST RLGTDEISPR VLQALGSEPI 910 920 930 940 950 960 QYAVPVVKYD RKGYKPRSRQ LLLTPNAVVI VEDAKVKQRI DYANLTGISV SSLSDSLFVL 970 980 990 1000 1010 1020 HVQRADNKQK GDVVLQSDHV IETLTKTALS ANRVNSININ QGSITFAGGP GRDGTIDFTP 1030 1040 GSELLITKAK NGHLAVVAPR LNSR

References

	« Hide 'large scale' referencesShow '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. , 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-36, METHYLATION AT LYS-383, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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].
+	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.
IPI	IPI00010418. IPI00743335. IPI00829992.
PIR	A59253.
RefSeq	NP_001074248.1. NM_001080779.1. NP_001074419.1. NM_001080950.1. NP_203693.3. NM_033375.4.
UniGene	Hs.286226.
3D structure databases
ProteinModelPortal	O00159.
SMR	O00159. Positions 47-732.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33109N.
IntAct	O00159. 13 interactions.
MINT	MINT-1149702.
STRING	9606.ENSP00000352834.
PTM databases
PhosphoSite	O00159.
Proteomic databases
PaxDb	O00159.
PeptideAtlas	O00159.
PRIDE	O00159.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000359786; ENSP00000352834; ENSG00000197879. ENST00000361007; ENSP00000354283; ENSG00000197879. ENST00000438665; ENSP00000412197; ENSG00000197879. ENST00000575158; ENSP00000459174; ENSG00000197879.
GeneID	4641.
KEGG	hsa:4641.
UCSC	uc002fsn.3. human. uc002fso.3. human.
Organism-specific databases
CTD	4641.
GeneCards	GC17M001367.
H-InvDB	HIX0202539.
HGNC	HGNC:7597. MYO1C.
HPA	HPA001768.
MIM	606538. gene.
neXtProt	NX_O00159.
PharmGKB	PA31399.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5022.
HOGENOM	HOG000260264.
InParanoid	O00159.
KO	K10356.
OMA	WAGRPQD.
OrthoDB	EOG4C5CHM.
PhylomeDB	O00159.
Enzyme and pathway databases
Reactome	REACT_11123. Membrane Trafficking.
Gene expression databases
ArrayExpress	O00159.
Bgee	O00159.
CleanEx	HS_MYO1C.
Genevestigator	O00159.
GermOnline	ENSG00000197879. Homo sapiens.
Family and domain databases
InterPro	IPR000048. IQ_motif_EF-hand-BS. IPR001609. Myosin_head_motor_dom. IPR010926. Myosin_tail_2. [Graphical view]
Pfam	PF00612. IQ. 2 hits. PF00063. Myosin_head. 1 hit. PF06017. Myosin_TH1. 1 hit. [Graphical view]
PRINTS	PR00193. MYOSINHEAVY.
SMART	SM00015. IQ. 3 hits. SM00242. MYSc. 1 hit. [Graphical view]
PROSITE	PS50096. IQ. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MYO1C. human.
GenomeRNAi	4641.
NextBio	17880.
SOURCE	Search...

Entry information

Entry name

MYO1C_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.