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Protein

Myosin-2

Gene

MYO2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Essential for the delivery of secretory vesicles to sites of active growth during bud emergence and cytokinesis. Required for segregation and inheritance of peroxisomes, late Golgi compartments, mitochondria and the vacuole to the daughter cell during cell division. Also required for correct alignment of the spindle during mitosis.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi164 – 1718ATPBy similarity

GO - Molecular functioni

  • actin filament binding Source: SGD
  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: SGD
  • microfilament motor activity Source: SGD

GO - Biological processi

  • budding cell apical bud growth Source: SGD
  • establishment of mitotic spindle orientation Source: SGD
  • Golgi inheritance Source: SGD
  • membrane addition at site of cytokinesis Source: SGD
  • mitochondrion inheritance Source: SGD
  • peroxisome inheritance Source: SGD
  • protein transport Source: UniProtKB-KW
  • unidimensional cell growth Source: SGD
  • vacuole inheritance Source: SGD
  • vesicle-mediated transport Source: SGD
  • vesicle transport along actin filament Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Cell cycle, Cell division, Protein transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciYEAST:G3O-33803-MONOMER.
ReactomeiR-SCE-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-2
Alternative name(s):
Cell division control protein 66
Class V unconventional myosin MYO2
Type V myosin heavy chain MYO2
Short name:
Myosin V MYO2
Gene namesi
Name:MYO2
Synonyms:CDC66
Ordered Locus Names:YOR326W
ORF Names:O6167
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR326W.
SGDiS000005853. MYO2.

Subcellular locationi

  • Bud neck 1 Publication
  • Bud tip 1 Publication

  • Note: Concentrates to sites of polarized growth, namely to the bud tip during S and G2 phases of the cell cycle and to the bud neck during cytokinesis.

GO - Cellular componenti

  • actin filament bundle Source: SGD
  • cellular bud neck Source: SGD
  • cellular bud tip Source: SGD
  • filamentous actin Source: SGD
  • incipient cellular bud site Source: SGD
  • mating projection tip Source: SGD
  • Myo2p-Vac17p-Vac8p transport complex Source: SGD
  • myosin complex Source: UniProtKB-KW
  • transport vesicle Source: SGD
  • vesicle Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi511 – 5111E → K in MYO2-66; disrupts actin binding. 1 Publication
Mutagenesisi1189 – 11891V → A in MYO2-573; causes a mitochondria inheritance defect; when associated with G-1288; M-1500; S-1529; G-1546 and R-1559. 1 Publication
Mutagenesisi1247 – 12471S → G: Intragenic suppressor of MYO2-2. 1 Publication
Mutagenesisi1248 – 12481G → D in MYO2-2; causes a vacuole inheritance defect. 1 Publication
Mutagenesisi1262 – 12621V → A: Intragenic suppressor of MYO2-2. 1 Publication
Mutagenesisi1264 – 12641F → S: Intragenic suppressor of MYO2-2. 1 Publication
Mutagenesisi1268 – 12681S → P: Intragenic suppressor of MYO2-2. 1 Publication
Mutagenesisi1274 – 12741T → M: Intragenic suppressor of MYO2-2. 1 Publication
Mutagenesisi1275 – 12751F → S: Intragenic suppressor of MYO2-2. 1 Publication
Mutagenesisi1288 – 12881V → A: Intragenic suppressor of MYO2-2. 2 Publications
Mutagenesisi1288 – 12881V → G in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; M-1500; S-1529; G-1546 and R-1559. 2 Publications
Mutagenesisi1297 – 12971D → G, N or V: Causes a vacuole inheritance defect. 1 Publication
Mutagenesisi1301 – 13011L → P: Causes a vacuole inheritance defect. 1 Publication
Mutagenesisi1304 – 13041N → D or S: Causes a vacuole inheritance defect. 1 Publication
Mutagenesisi1307 – 13071N → D: Causes a vacuole inheritance defect. 1 Publication
Mutagenesisi1474 – 14741L → S in MYO2-338; abolishes interaction with YPT11; when associated with G-1484 and G-1511. 1 Publication
Mutagenesisi1484 – 14841E → G in MYO2-338; abolishes interaction with YPT11; when associated with S-1474 and G-1511. 1 Publication
Mutagenesisi1500 – 15001K → M in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; S-1529; G-1546 and R-1559. 1 Publication
Mutagenesisi1511 – 15111D → G in MYO2-338; abolishes interaction with YPT11; when associated with S-1474 and G-1484. 1 Publication
Mutagenesisi1529 – 15291P → S in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; G-1546 and R-1559. 1 Publication
Mutagenesisi1546 – 15461E → G in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; S-1529 and R-1559. 1 Publication
Mutagenesisi1559 – 15591K → R in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; S-1529 and G-1546. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 15741573Myosin-2PRO_0000123489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei1097 – 10971PhosphothreonineCombined sources
Modified residuei1121 – 11211PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP19524.

PTM databases

iPTMnetiP19524.

Interactioni

Subunit structurei

Homodimer. Interacts with calmodulin (CMD1) and the myosin light chain MLC1 through its IQ repeats. Binds to the membrane receptors SEC4 and VAC17 to transport secretory vesicles and the vacuole, respectively. Binds to KAR9, which transports BIM1-coated cytoplasmic microtubules that are attached to the spindle pole body into the emerging bud, thereby correctly orienting the mitotic spindle. Interacts with YPT11 and MMR1 to accelerate mitochondrial distribution to the bud. Interacts with SHE4 and localizes it to the bud tip. Interacts with RHO3 and SMY1, putative regulators of MYO2 function. Interacts with SRO7.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
INP2Q038243EBI-11659,EBI-27354
KAR9P325262EBI-11659,EBI-9516
SHE4P515343EBI-11659,EBI-17086

GO - Molecular functioni

  • actin filament binding Source: SGD
  • calmodulin binding Source: SGD

Protein-protein interaction databases

BioGridi34711. 220 interactions.
DIPiDIP-2308N.
IntActiP19524. 45 interactions.
MINTiMINT-440498.

Structurei

Secondary structure

1
1574
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi807 – 82923Combined sources
Helixi855 – 87723Combined sources
Helixi1153 – 116513Combined sources
Helixi1167 – 117610Combined sources
Turni1177 – 11815Combined sources
Helixi1195 – 11984Combined sources
Helixi1200 – 121415Combined sources
Helixi1218 – 123720Combined sources
Helixi1241 – 12433Combined sources
Helixi1244 – 127128Combined sources
Helixi1281 – 132545Combined sources
Turni1332 – 13354Combined sources
Helixi1355 – 137117Combined sources
Helixi1376 – 139924Combined sources
Helixi1407 – 142620Combined sources
Helixi1432 – 14354Combined sources
Helixi1437 – 14459Combined sources
Helixi1453 – 146210Combined sources
Turni1463 – 14653Combined sources
Helixi1468 – 147710Combined sources
Helixi1489 – 150416Combined sources
Helixi1505 – 15073Combined sources
Helixi1533 – 15364Combined sources
Helixi1556 – 156712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M45X-ray1.65B806-830[»]
1M46X-ray2.10B854-878[»]
1N2DX-ray2.00C806-853[»]
2F6HX-ray2.25X1152-1570[»]
ProteinModelPortaliP19524.
SMRiP19524. Positions 8-879, 1152-1570.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19524.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 781712Myosin motorAdd
BLAST
Domaini784 – 80623IQ 1PROSITE-ProRule annotationAdd
BLAST
Domaini807 – 83125IQ 2PROSITE-ProRule annotationAdd
BLAST
Domaini832 – 85524IQ 3PROSITE-ProRule annotationAdd
BLAST
Domaini856 – 87924IQ 4PROSITE-ProRule annotationAdd
BLAST
Domaini880 – 90223IQ 5PROSITE-ProRule annotationAdd
BLAST
Domaini903 – 93230IQ 6PROSITE-ProRule annotationAdd
BLAST
Domaini1226 – 1501276DilutePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni443 – 52381Actin-bindingBy similarityAdd
BLAST
Regioni1087 – 1574488Non alpha-helical, tail domainAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili933 – 1088156Add
BLAST

Domaini

The myosin motor domain binds to actin.
The IQ domains provide the interaction surface for the myosin light chain MLC1.
The coiled-coiled domain is necessary for dimerization.
The tail domain is a globular cargo-binding domain involved in vectorial vesicle transport.

Sequence similaritiesi

Contains 1 dilute domain.PROSITE-ProRule annotation
Contains 6 IQ domains.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00840000129687.
HOGENOMiHOG000171839.
InParanoidiP19524.
KOiK10357.
OMAiWLANVRE.
OrthoDBiEOG77T1CS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR002710. Dilute_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR008989. Myosin_S1_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM01132. DIL. 1 hit.
SM00015. IQ. 4 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19524-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFEVGTRCW YPHKELGWIG AEVIKNEFND GKYHLELQLE DDEIVSVDTK
60 70 80 90 100
DLNNDKDQSL PLLRNPPILE ATEDLTSLSY LNEPAVLHAI KQRYSQLNIY
110 120 130 140 150
TYSGIVLIAT NPFDRVDQLY TQDMIQAYAG KRRGELEPHL FAIAEEAYRL
160 170 180 190 200
MKNDKQNQTI VVSGESGAGK TVSAKYIMRY FASVEEENSA TVQHQVEMSE
210 220 230 240 250
TEQKILATNP IMEAFGNAKT TRNDNSSRFG KYLEILFDKD TSIIGARIRT
260 270 280 290 300
YLLERSRLVY QPPIERNYHI FYQLMAGLPA QTKEELHLTD ASDYFYMNQG
310 320 330 340 350
GDTKINGIDD AKEYKITVDA LTLVGITKET QHQIFKILAA LLHIGNIEIK
360 370 380 390 400
KTRNDASLSA DEPNLKLACE LLGIDAYNFA KWVTKKQIIT RSEKIVSNLN
410 420 430 440 450
YSQALVAKDS VAKFIYSALF DWLVENINTV LCNPAVNDQI SSFIGVLDIY
460 470 480 490 500
GFEHFEKNSF EQFCINYANE KLQQEFNQHV FKLEQEEYVK EEIEWSFIEF
510 520 530 540 550
NDNQPCIDLI ENKLGILSLL DEESRLPAGS DESWTQKLYQ TLDKSPTNKV
560 570 580 590 600
FSKPRFGQTK FIVSHYALDV AYDVEGFIEK NRDTVSDGHL EVLKASTNET
610 620 630 640 650
LINILEGLEK AAKKLEEAKK LELEQAGSKK PGPIRTVNRK PTLGSMFKQS
660 670 680 690 700
LIELMNTINS TNVHYIRCIK PNADKEAWQF DNLMVLSQLR ACGVLETIRI
710 720 730 740 750
SCAGFPSRWT FEEFVLRYYI LIPHEQWDLI FKKKETTEED IISVVKMILD
760 770 780 790 800
ATVKDKSKYQ IGNTKIFFKA GMLAYLEKLR SNKMHNSIVM IQKKIRAKYY
810 820 830 840 850
RKQYLQISQA IKYLQNNIKG FIIRQRVNDE MKVNCATLLQ AAYRGHSIRA
860 870 880 890 900
NVFSVLRTIT NLQKKIRKEL KQRQLKQEHE YNAAVTIQSK VRTFEPRSRF
910 920 930 940 950
LRTKKDTVVV QSLIRRRAAQ RKLKQLKADA KSVNHLKEVS YKLENKVIEL
960 970 980 990 1000
TQNLASKVKE NKEMTERIKE LQVQVEESAK LQETLENMKK EHLIDIDNQK
1010 1020 1030 1040 1050
SKDMELQKTI ENNLQSTEQT LKDAQLELED MVKQHDELKE ESKKQLEELE
1060 1070 1080 1090 1100
QTKKTLVEYQ TLNGDLQNEV KSLKEEIARL QTAMSLGTVT TSVLPQTPLK
1110 1120 1130 1140 1150
DVMGGGASNF NNMMLENSDL SPNDLNLKSR STPSSGNNHI DSLSVDRENG
1160 1170 1180 1190 1200
VNATQINEEL YRLLEDTEIL NQEITEGLLK GFEVPDAGVA IQLSKRDVVY
1210 1220 1230 1240 1250
PARILIIVLS EMWRFGLTKQ SESFLAQVLT TIQKVVTQLK GNDLIPSGVF
1260 1270 1280 1290 1300
WLANVRELYS FVVFALNSIL TEETFKNGMT DEEYKEYVSL VTELKDDFEA
1310 1320 1330 1340 1350
LSYNIYNIWL KKLQKQLQKK AINAVVISES LPGFSAGETS GFLNKIFANT
1360 1370 1380 1390 1400
EEYTMDDILT FFNSIYWCMK SFHIENEVFH AVVTTLLNYV DAICFNELIM
1410 1420 1430 1440 1450
KRNFLSWKRG LQLNYNVTRL EEWCKTHGLT DGTECLQHLI QTAKLLQVRK
1460 1470 1480 1490 1500
YTIEDIDILR GICYSLTPAQ LQKLISQYQV ADYESPIPQE ILRYVADIVK
1510 1520 1530 1540 1550
KEAALSSSGN DSKGHEHSSS IFITPETGPF TDPFSLIKTR KFDQVEAYIP
1560 1570
AWLSLPSTKR IVDLVAQQVV QDGH
Length:1,574
Mass (Da):180,680
Last modified:February 1, 1991 - v1
Checksum:i1F7E2887C1E59D54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35532 Genomic DNA. Translation: AAA34810.1.
Z75234 Genomic DNA. Translation: CAA99646.1.
Z75235 Genomic DNA. Translation: CAA99648.1.
X90565 Genomic DNA. Translation: CAA62184.1.
Z49821 Genomic DNA. Translation: CAA89973.1.
BK006948 Genomic DNA. Translation: DAA11089.1.
PIRiA38454.
RefSeqiNP_014971.1. NM_001183746.1.

Genome annotation databases

EnsemblFungiiYOR326W; YOR326W; YOR326W.
GeneIDi854504.
KEGGisce:YOR326W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35532 Genomic DNA. Translation: AAA34810.1.
Z75234 Genomic DNA. Translation: CAA99646.1.
Z75235 Genomic DNA. Translation: CAA99648.1.
X90565 Genomic DNA. Translation: CAA62184.1.
Z49821 Genomic DNA. Translation: CAA89973.1.
BK006948 Genomic DNA. Translation: DAA11089.1.
PIRiA38454.
RefSeqiNP_014971.1. NM_001183746.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M45X-ray1.65B806-830[»]
1M46X-ray2.10B854-878[»]
1N2DX-ray2.00C806-853[»]
2F6HX-ray2.25X1152-1570[»]
ProteinModelPortaliP19524.
SMRiP19524. Positions 8-879, 1152-1570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34711. 220 interactions.
DIPiDIP-2308N.
IntActiP19524. 45 interactions.
MINTiMINT-440498.

PTM databases

iPTMnetiP19524.

Proteomic databases

MaxQBiP19524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR326W; YOR326W; YOR326W.
GeneIDi854504.
KEGGisce:YOR326W.

Organism-specific databases

EuPathDBiFungiDB:YOR326W.
SGDiS000005853. MYO2.

Phylogenomic databases

GeneTreeiENSGT00840000129687.
HOGENOMiHOG000171839.
InParanoidiP19524.
KOiK10357.
OMAiWLANVRE.
OrthoDBiEOG77T1CS.

Enzyme and pathway databases

BioCyciYEAST:G3O-33803-MONOMER.
ReactomeiR-SCE-194840. Rho GTPase cycle.

Miscellaneous databases

EvolutionaryTraceiP19524.
PROiP19524.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR002710. Dilute_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR008989. Myosin_S1_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM01132. DIL. 1 hit.
SM00015. IQ. 4 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles."
    Johnston G.C., Prendergast J.A., Singer R.A.
    J. Cell Biol. 113:539-551(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / GRF88.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII."
    Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A., Schweizer M.
    Yeast 12:1021-1031(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-748.
    Strain: ATCC 96604 / S288c / FY1679.
  5. "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces cerevisiae chromosome XV: similarity to part of chromosome I."
    Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.
    Yeast 12:999-1004(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 677-1574.
  6. "The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae."
    Brockerhoff S.E., Stevens R.C., Davis T.N.
    J. Cell Biol. 124:315-323(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CMD1.
  7. "Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae."
    Lillie S.H., Brown S.S.
    J. Cell Biol. 125:825-842(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-511.
  8. "Mlc1p is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae."
    Stevens R.C., Davis T.N.
    J. Cell Biol. 142:711-722(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MLC1.
  9. "The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth."
    Catlett N.L., Weisman L.S.
    Proc. Natl. Acad. Sci. U.S.A. 95:14799-14804(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-1248.
  10. "Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70."
    Robinson N.G.G., Guo L., Imai J., Toh-e A., Matsui Y., Tamanoi F.
    Mol. Cell. Biol. 19:3580-3587(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHO3.
  11. "Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes."
    Catlett N.L., Duex J.E., Tang F., Weisman L.S.
    J. Cell Biol. 150:513-526(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-1297; LEU-1301; ASN-1304 AND ASN-1307.
  12. "The yeast kinesin-related protein Smy1p exerts its effects on the class V myosin Myo2p via a physical interaction."
    Beningo K.A., Lillie S.H., Brown S.S.
    Mol. Biol. Cell 11:691-702(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMY1.
  13. "Myosin V orientates the mitotic spindle in yeast."
    Yin H., Pruyne D., Huffaker T.C., Bretscher A.
    Nature 406:1013-1015(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAR9.
  14. "A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae."
    Rossanese O.W., Reinke C.A., Bevis B.J., Hammond A.T., Sears I.B., O'Connor J., Glick B.S.
    J. Cell Biol. 153:47-62(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin-based motors."
    Reck-Peterson S.L., Tyska M.J., Novick P.J., Mooseker M.S.
    J. Cell Biol. 153:1121-1126(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Erratum
    Reck-Peterson S.L., Tyska M.J., Novick P.J., Mooseker M.S.
    J. Cell Biol. 153:1521-1521(2001)
  17. "A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae."
    Hoepfner D., van den Berg M., Philippsen P., Tabak H.F., Hettema E.H.
    J. Cell Biol. 155:979-990(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Mlc1p promotes septum closure during cytokinesis via the IQ motifs of the vesicle motor Myo2p."
    Wagner W., Bielli P., Wacha S., Ragnini-Wilson A.
    EMBO J. 21:6397-6408(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MLC1 AND SEC4.
  19. "Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length."
    Schott D.H., Collins R.N., Bretscher A.
    J. Cell Biol. 156:35-39(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Complex formation with Ypt11p, a rab-type small GTPase, is essential to facilitate the function of Myo2p, a class V myosin, in mitochondrial distribution in Saccharomyces cerevisiae."
    Itoh T., Watabe A., Toh-e A., Matsui Y.
    Mol. Cell. Biol. 22:7744-7757(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YPT11, MUTAGENESIS OF VAL-1189; VAL-1288; LEU-1474; GLU-1484; LYS-1500; ASP-1511; PRO-1529; GLU-1546 AND LYS-1559.
  21. "The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function."
    Wesche S., Arnold M., Jansen R.-P.
    Curr. Biol. 13:715-724(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHE4.
  22. "Identification of an organelle-specific myosin V receptor."
    Ishikawa K., Catlett N.L., Novak J.L., Tang F., Nau J.J., Weisman L.S.
    J. Cell Biol. 160:887-897(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VAC17, MUTAGENESIS OF SER-1247; VAL-1262; PHE-1264; SER-1268; THR-1274; PHE-1275 AND VAL-1288.
  23. "Spindle orientation in Saccharomyces cerevisiae depends on the transport of microtubule ends along polarized actin cables."
    Hwang E., Kusch J., Barral Y., Huffaker T.C.
    J. Cell Biol. 161:483-488(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  25. "Mmr1p is a mitochondrial factor for Myo2p-dependent inheritance of mitochondria in the budding yeast."
    Itoh T., Toh-e A., Matsui Y.
    EMBO J. 23:2520-2530(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MMR1.
  26. "Structurally conserved interaction of Lgl family with SNAREs is critical to their cellular function."
    Gangar A., Rossi G., Andreeva A., Hales R., Brennwald P.
    Curr. Biol. 15:1136-1142(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRO7.
  27. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  28. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1097 AND SER-1121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis."
    Rossi G., Brennwald P.
    Mol. Biol. Cell 22:842-857(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SRO7.
  31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Crystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound to IQ motifs from myosin V."
    Terrak M., Otterbein L.R., Wu G., Palecanda L.A., Lu R.C., Dominguez R.
    Acta Crystallogr. D 58:1882-1885(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 806-878 IN COMPLEX WITH MLC1.
  33. "Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications."
    Terrak M., Wu G., Stafford W.F., Lu R.C., Dominguez R.
    EMBO J. 22:362-371(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 806-830 AND 854-878 IN COMPLEX WITH MLC1.

Entry informationi

Entry nameiMYO2_YEAST
AccessioniPrimary (citable) accession number: P19524
Secondary accession number(s): D6W323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 6, 2016
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4339 molecules/cell in log phase SD medium.1 Publication
Moves with an average velocity of 3 um/s along actin cables.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.