Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O00160 (MYO1F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-If
Alternative name(s):
Myosin-Ie
Gene names
Name:MYO1F
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1098 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 By similarity.

Sequence similarities

Contains 1 IQ domain.

Contains 1 myosin head-like domain.

Contains 1 SH3 domain.

Caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10981098Unconventional myosin-If
PRO_0000123452

Regions

Domain1 – 677677Myosin head-like
Domain693 – 72230IQ
Domain1041 – 109858SH3
Nucleotide binding110 – 1178ATP Potential
Region579 – 58911Actin-binding Potential

Amino acid modifications

Modified residue10231Phosphoserine Ref.6

Natural variations

Natural variant9601P → L.
Corresponds to variant rs2288411 [ dbSNP | Ensembl ].
VAR_056179

Experimental info

Sequence conflict2591A → V in BAC03995. Ref.2
Sequence conflict534 – 5363TSE → SSD in CAA67058. Ref.5
Sequence conflict592 – 5932RP → HA in CAC83948. Ref.1
Sequence conflict592 – 5932RP → HA in CAA67058. Ref.5
Sequence conflict6021K → Q in CAA67058. Ref.5
Sequence conflict7591R → K in CAC83948. Ref.1
Sequence conflict7591R → K in CAA67058. Ref.5
Sequence conflict7971V → M in CAC83948. Ref.1
Sequence conflict7971V → M in CAA67058. Ref.5
Sequence conflict8051Q → P in CAA67058. Ref.5
Sequence conflict8091V → I in CAA67058. Ref.5
Sequence conflict8141V → L in CAA67058. Ref.5
Sequence conflict9221S → N in CAA67058. Ref.5
Sequence conflict9271R → G in CAA67058. Ref.5
Sequence conflict9301M → L in CAA67058. Ref.5
Sequence conflict948 – 9514APPR → GAPQ in CAA67058. Ref.5
Sequence conflict958 – 96710VPPSARGGPL → APLCPQGGAPC in CAA67058. Ref.5
Sequence conflict971 – 99020IMSGG…STSLG → KFIWPRGHPQASPALRPHPW D in CAA67058. Ref.5
Sequence conflict10311Missing in CAA67058. Ref.5
Sequence conflict1090 – 10989FPGNYVEKI → GSPSARSPA in BAC03995. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O00160 [UniParc].

Last modified November 24, 2009. Version 3.
Checksum: 75C2B1306F74C7C5

FASTA1,098124,844
        10         20         30         40         50         60 
MGSKERFHWQ SHNVKQSGVD DMVLLPQITE DAIAANLRKR FMDDYIFTYI GSVLISVNPF 

        70         80         90        100        110        120 
KQMPYFTDRE IDLYQGAAQY ENPPHIYALT DNMYRNMLID CENQCVIISG ESGAGKTVAA 

       130        140        150        160        170        180 
KYIMGYISKV SGGGEKVQHV KDIILQSNPL LEAFGNAKTV RNNNSSRFGK YFEIQFSRGG 

       190        200        210        220        230        240 
EPDGGKISNF LLEKSRVVMQ NENERNFHIY YQLLEGASQE QRQNLGLMTP DYYYYLNQSD 

       250        260        270        280        290        300 
TYQVDGTDDR SDFGETLSAM QVIGIPPSIQ QLVLQLVAGI LHLGNISFCE DGNYARVESV 

       310        320        330        340        350        360 
DLLAFPAYLL GIDSGRLQEK LTSRKMDSRW GGRSESINVT LNVEQAAYTR DALAKGLYAR 

       370        380        390        400        410        420 
LFDFLVEAIN RAMQKPQEEY SIGVLDIYGF EIFQKNGFEQ FCINFVNEKL QQIFIELTLK 

       430        440        450        460        470        480 
AEQEEYVQEG IRWTPIQYFN NKVVCDLIEN KLSPPGIMSV LDDVCATMHA TGGGADQTLL 

       490        500        510        520        530        540 
QKLQAAVGTH EHFNSWSAGF VIHHYAGKVS YDVSGFCERN RDVLFSDLIE LMQTSEQAFL 

       550        560        570        580        590        600 
RMLFPEKLDG DKKGRPSTAG SKIKKQANDL VATLMRCTPH YIRCIKPNET KRPRDWEENR 

       610        620        630        640        650        660 
VKHQVEYLGL KENIRVRRAG FAYRRQFAKF LQRYAILTPE TWPRWRGDER QGVQHLLRAV 

       670        680        690        700        710        720 
NMEPDQYQMG STKVFVKNPE SLFLLEEVRE RKFDGFARTI QKAWRRHVAV RKYEEMREEA 

       730        740        750        760        770        780 
SNILLNKKER RRNSINRNFV GDYLGLEERP ELRQFLGKRE RVDFADSVTK YDRRFKPIKR 

       790        800        810        820        830        840 
DLILTPKCVY VIGREKVKKG PEKGQVCEVL KKKVDIQALR GVSLSTRQDD FFILQEDAAD 

       850        860        870        880        890        900 
SFLESVFKTE FVSLLCKRFE EATRRPLPLT FSDTLQFRVK KEGWGGGGTR SVTFSRGFGD 

       910        920        930        940        950        960 
LAVLKVGGRT LTVSVGDGLP KSSKPTRKGM AKGKPRRSSQ APTRAAPAPP RGMDRNGVPP 

       970        980        990       1000       1010       1020 
SARGGPLPLE IMSGGGTHRP PRGPPSTSLG ASRRPRARPP SEHNTEFLNV PDQGMAGMQR 

      1030       1040       1050       1060       1070       1080 
KRSVGQRPVP GVGRPKPQPR THGPRCRALY QYVGQDVDEL SFNVNEVIEI LMEDPSGWWK 

      1090 
GRLHGQEGLF PGNYVEKI 

« Hide

References

« Hide 'large scale' references
[1]"Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices."
Krugmann S., Anderson K.E., Ridley S.H., Risso N., McGregor A., Coadwell J., Davidson K., Eguinoa A., Ellson C.D., Lipp P., Manifava M., Ktistakis N., Painter G., Thuring J.W., Cooper M.A., Lim Z.-Y., Holmes A.B., Dove S.K. expand/collapse author list , Michell R.H., Grewal A., Nazarian A., Erdjument-Bromage H., Tempst P., Stephens L.R., Hawkins P.T.
Mol. Cell 9:95-108(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Spleen.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Blood.
[5]"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] OF 318-1098.
Tissue: Retina.
[6]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1023, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ310570 mRNA. Translation: CAC83948.1.
AK092877 mRNA. Translation: BAC03995.1.
AC092298 Genomic DNA. No translation available.
AC092316 Genomic DNA. No translation available.
AC124902 Genomic DNA. No translation available.
AC130469 Genomic DNA. No translation available.
BC028071 mRNA. Translation: AAH28071.1.
X98411 mRNA. Translation: CAA67058.1.
RefSeqNP_036467.2. NM_012335.3.
UniGeneHs.465818.

3D structure databases

ProteinModelPortalO00160.
SMRO00160. Positions 18-717, 1044-1098.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110638. 5 interactions.
IntActO00160. 2 interactions.
STRING9606.ENSP00000344871.

PTM databases

PhosphoSiteO00160.

Proteomic databases

PaxDbO00160.
PRIDEO00160.

Protocols and materials databases

DNASU4542.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338257; ENSP00000344871; ENSG00000142347.
ENST00000572880; ENSP00000460038; ENSG00000262149.
GeneID4542.
KEGGhsa:4542.
UCSCuc002mkg.3. human.

Organism-specific databases

CTD4542.
GeneCardsGC19M008585.
H-InvDBHIX0014717.
HGNCHGNC:7600. MYO1F.
HPAHPA055242.
MIM601480. gene.
neXtProtNX_O00160.
PharmGKBPA31402.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOVERGENHBG100702.
KOK10356.
OMARRQFAKF.
PhylomeDBO00160.
TreeFamTF312960.

Gene expression databases

ArrayExpressO00160.
BgeeO00160.
CleanExHS_MYO1F.
GenevestigatorO00160.

Family and domain databases

InterProIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
PR00452. SH3DOMAIN.
SMARTSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50096. IQ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO1F. human.
GeneWikiMYO1F.
GenomeRNAi4542.
NextBio17517.
PROO00160.
SOURCESearch...

Entry information

Entry nameMYO1F_HUMAN
AccessionPrimary (citable) accession number: O00160
Secondary accession number(s): Q8WWN7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 24, 2009
Last modified: April 16, 2014
This is version 139 of the entry and version 3 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

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 19

Human chromosome 19: entries, gene names and cross-references to MIM