P19524 (MYO2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myosin-2

Alternative name(s):
Cell divison control protein 66
Class V unconventional myosin MYO2
Type V myosin heavy chain MYO2
Short name=Myosin V MYO2

Gene names

Name:	MYO2
Synonyms:	CDC66
Ordered Locus Names:	YOR326W
ORF Names:	O6167

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1574 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.23 Ref.29
Subunit structure	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. Ref.6 Ref.8 Ref.10 Ref.12 Ref.13 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26 Ref.29
Subcellular location	Bud neck. Bud tip. 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. Ref.7
Domain	The myosin head-like domain binds to actin and constitutes the motor domain. The IQ domains serve as interaction surface for the myosin light chains. The coiled-coiled domain is necessary for dimerization. The tail domain is a globular cargo-binding domain involved in vectorial vesicle transport.
Miscellaneous	Present with 4339 molecules/cell in log phase SD medium. Ref.24 Moves with an average velocity of 3 um/s along actin cables.
Sequence similarities	Contains 1 dilute domain. Contains 6 IQ domains. Contains 1 myosin head-like domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Protein transport Transport
Domain	Coiled coil Repeat
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Golgi inheritance Inferred from mutant phenotype Ref.14. Source: SGD budding cell apical bud growth Inferred from mutant phenotype Ref.1. Source: SGD establishment of mitotic spindle orientation Inferred from mutant phenotype Ref.13. Source: SGD membrane addition at site of cytokinesis Inferred from mutant phenotype Ref.18. Source: SGD mitochondrion inheritance Inferred from mutant phenotype Ref.20. Source: SGD peroxisome inheritance Inferred from mutant phenotype Ref.17. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW unidimensional cell growth Inferred from mutant phenotype. Source: SGD vacuole inheritance Inferred from genetic interaction. Source: SGD vesicle transport along actin filament Inferred from mutant phenotype. Source: SGD vesicle-mediated transport Inferred from mutant phenotype Ref.1. Source: SGD
Cellular component	actin filament bundle Inferred from mutant phenotype. Source: SGD cellular bud neck Inferred from direct assay Ref.7. Source: SGD cellular bud tip Inferred from direct assay Ref.7. Source: SGD filamentous actin Inferred from direct assay Ref.15. Source: SGD incipient cellular bud site Inferred from direct assay Ref.7. Source: SGD mating projection tip Inferred from direct assay Ref.7. Source: SGD myosin complex Inferred from electronic annotation. Source: UniProtKB-KW vesicle Inferred from direct assay Ref.18. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin filament binding Inferred from direct assay Ref.15. Source: SGD calmodulin binding Inferred from direct assay Ref.6. Source: SGD microfilament motor activity Inferred from direct assay Ref.15. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
INP2	Q03824	3	EBI-11659,EBI-27354
KAR9	P32526	2	EBI-11659,EBI-9516
SHE4	P51534	3	EBI-11659,EBI-17086

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1574

1574

Myosin-2

PRO_0000123489

Regions

Domain

72 – 769

698

Myosin head-like

Domain

784 – 806

23

IQ 1

Domain

807 – 831

25

IQ 2

Domain

832 – 855

24

IQ 3

Domain

856 – 879

24

IQ 4

Domain

880 – 902

23

IQ 5

Domain

903 – 932

30

IQ 6

Domain

1226 – 1501

276

Dilute

Nucleotide binding

164 – 171

8

ATP By similarity

Region

443 – 523

81

Actin-binding By similarity

Region

1087 – 1574

488

Non alpha-helical, tail domain

Coiled coil

933 – 1088

156

Amino acid modifications

Modified residue

545

1

Phosphoserine Ref.27 Ref.28

Modified residue

1097

1

Phosphothreonine Ref.28

Modified residue

1121

1

Phosphoserine Ref.28

Modified residue

1135

1

Phosphoserine Ref.28

Modified residue

1144

1

Phosphoserine Ref.28

Experimental info

Mutagenesis

511

1

E → K in MYO2-66; disrupts actin binding. Ref.7

Mutagenesis

1189

1

V → A in MYO2-573; causes a mitochondria inheritance defect; when associated with G-1288; M-1500; S-1529; G-1546 and R-1559. Ref.20

Mutagenesis

1247

1

S → G: Intragenic suppressor of MYO2-2. Ref.22

Mutagenesis

1248

1

G → D in MYO2-2; causes a vacuole inheritance defect. Ref.9

Mutagenesis

1262

1

V → A: Intragenic suppressor of MYO2-2. Ref.22

Mutagenesis

1264

1

F → S: Intragenic suppressor of MYO2-2. Ref.22

Mutagenesis

1268

1

S → P: Intragenic suppressor of MYO2-2. Ref.22

Mutagenesis

1274

1

T → M: Intragenic suppressor of MYO2-2. Ref.22

Mutagenesis

1275

1

F → S: Intragenic suppressor of MYO2-2. Ref.22

Mutagenesis

1288

1

V → A: Intragenic suppressor of MYO2-2. Ref.20 Ref.22

Mutagenesis

1288

1

V → G in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; M-1500; S-1529; G-1546 and R-1559. Ref.20 Ref.22

Mutagenesis

1297

1

D → G, N or V: Causes a vacuole inheritance defect. Ref.11

Mutagenesis

1301

1

L → P: Causes a vacuole inheritance defect. Ref.11

Mutagenesis

1304

1

N → D or S: Causes a vacuole inheritance defect. Ref.11

Mutagenesis

1307

1

N → D: Causes a vacuole inheritance defect. Ref.11

Mutagenesis

1474

1

L → S in MYO2-338; abolishes interaction with YPT11; when associated with G-1484 and G-1511. Ref.20

Mutagenesis

1484

1

E → G in MYO2-338; abolishes interaction with YPT11; when associated with S-1474 and G-1511. Ref.20

Mutagenesis

1500

1

K → M in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; S-1529; G-1546 and R-1559. Ref.20

Mutagenesis

1511

1

D → G in MYO2-338; abolishes interaction with YPT11; when associated with S-1474 and G-1484. Ref.20

Mutagenesis

1529

1

P → S in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; G-1546 and R-1559. Ref.20

Mutagenesis

1546

1

E → G in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; S-1529 and R-1559. Ref.20

Mutagenesis

1559

1

K → R in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; S-1529 and G-1546. Ref.20

Secondary structure

1

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1574

Helix Strand Turn

Details...

Helix

807 – 829

23

Helix

831 – 852

22

Helix

855 – 877

23

Helix

1153 – 1165

13

Helix

1167 – 1176

10

Turn

1177 – 1181

5

Helix

1195 – 1198

4

Helix

1200 – 1214

15

Helix

1218 – 1237

20

Helix

1241 – 1243

3

Helix

1244 – 1271

28

Helix

1281 – 1325

45

Turn

1332 – 1335

4

Helix

1355 – 1371

17

Helix

1376 – 1399

24

Helix

1407 – 1426

20

Helix

1432 – 1435

4

Helix

1437 – 1445

9

Helix

1453 – 1462

10

Turn

1463 – 1465

3

Helix

1468 – 1477

10

Helix

1489 – 1504

16

Helix

1505 – 1507

3

Helix

1533 – 1536

4

Helix

1556 – 1567

12

Sequences

	Sequence		Length	Mass (Da)
	P19524 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 1F7E2887C1E59D54	FASTA	1,574	180,680
	10 20 30 40 50 60 MSFEVGTRCW YPHKELGWIG AEVIKNEFND GKYHLELQLE DDEIVSVDTK DLNNDKDQSL 70 80 90 100 110 120 PLLRNPPILE ATEDLTSLSY LNEPAVLHAI KQRYSQLNIY TYSGIVLIAT NPFDRVDQLY 130 140 150 160 170 180 TQDMIQAYAG KRRGELEPHL FAIAEEAYRL MKNDKQNQTI VVSGESGAGK TVSAKYIMRY 190 200 210 220 230 240 FASVEEENSA TVQHQVEMSE TEQKILATNP IMEAFGNAKT TRNDNSSRFG KYLEILFDKD 250 260 270 280 290 300 TSIIGARIRT YLLERSRLVY QPPIERNYHI FYQLMAGLPA QTKEELHLTD ASDYFYMNQG 310 320 330 340 350 360 GDTKINGIDD AKEYKITVDA LTLVGITKET QHQIFKILAA LLHIGNIEIK KTRNDASLSA 370 380 390 400 410 420 DEPNLKLACE LLGIDAYNFA KWVTKKQIIT RSEKIVSNLN YSQALVAKDS VAKFIYSALF 430 440 450 460 470 480 DWLVENINTV LCNPAVNDQI SSFIGVLDIY GFEHFEKNSF EQFCINYANE KLQQEFNQHV 490 500 510 520 530 540 FKLEQEEYVK EEIEWSFIEF NDNQPCIDLI ENKLGILSLL DEESRLPAGS DESWTQKLYQ 550 560 570 580 590 600 TLDKSPTNKV FSKPRFGQTK FIVSHYALDV AYDVEGFIEK NRDTVSDGHL EVLKASTNET 610 620 630 640 650 660 LINILEGLEK AAKKLEEAKK LELEQAGSKK PGPIRTVNRK PTLGSMFKQS LIELMNTINS 670 680 690 700 710 720 TNVHYIRCIK PNADKEAWQF DNLMVLSQLR ACGVLETIRI SCAGFPSRWT FEEFVLRYYI 730 740 750 760 770 780 LIPHEQWDLI FKKKETTEED IISVVKMILD ATVKDKSKYQ IGNTKIFFKA GMLAYLEKLR 790 800 810 820 830 840 SNKMHNSIVM IQKKIRAKYY RKQYLQISQA IKYLQNNIKG FIIRQRVNDE MKVNCATLLQ 850 860 870 880 890 900 AAYRGHSIRA NVFSVLRTIT NLQKKIRKEL KQRQLKQEHE YNAAVTIQSK VRTFEPRSRF 910 920 930 940 950 960 LRTKKDTVVV QSLIRRRAAQ RKLKQLKADA KSVNHLKEVS YKLENKVIEL TQNLASKVKE 970 980 990 1000 1010 1020 NKEMTERIKE LQVQVEESAK LQETLENMKK EHLIDIDNQK SKDMELQKTI ENNLQSTEQT 1030 1040 1050 1060 1070 1080 LKDAQLELED MVKQHDELKE ESKKQLEELE QTKKTLVEYQ TLNGDLQNEV KSLKEEIARL 1090 1100 1110 1120 1130 1140 QTAMSLGTVT TSVLPQTPLK DVMGGGASNF NNMMLENSDL SPNDLNLKSR STPSSGNNHI 1150 1160 1170 1180 1190 1200 DSLSVDRENG VNATQINEEL YRLLEDTEIL NQEITEGLLK GFEVPDAGVA IQLSKRDVVY 1210 1220 1230 1240 1250 1260 PARILIIVLS EMWRFGLTKQ SESFLAQVLT TIQKVVTQLK GNDLIPSGVF WLANVRELYS 1270 1280 1290 1300 1310 1320 FVVFALNSIL TEETFKNGMT DEEYKEYVSL VTELKDDFEA LSYNIYNIWL KKLQKQLQKK 1330 1340 1350 1360 1370 1380 AINAVVISES LPGFSAGETS GFLNKIFANT EEYTMDDILT FFNSIYWCMK SFHIENEVFH 1390 1400 1410 1420 1430 1440 AVVTTLLNYV DAICFNELIM KRNFLSWKRG LQLNYNVTRL EEWCKTHGLT DGTECLQHLI 1450 1460 1470 1480 1490 1500 QTAKLLQVRK YTIEDIDILR GICYSLTPAQ LQKLISQYQV ADYESPIPQE ILRYVADIVK 1510 1520 1530 1540 1550 1560 KEAALSSSGN DSKGHEHSSS IFITPETGPF TDPFSLIKTR KFDQVEAYIP AWLSLPSTKR 1570 IVDLVAQQVV QDGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2016335] [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: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 8896266] [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: 8896263] [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: 8294515] [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: 8188749] [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: 9700160] [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: 9843969] [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: 10207081] [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: 10931864] [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: 10679024] [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: 10984058] [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: 11285273] [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: 11381095] [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: 11733545] [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: 12456647] [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: 11781333] [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: 12391144] [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: 12725728] [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: 12642614] [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: 12743102] [Abstract] Cited for: FUNCTION.
[24]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] 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: 15201867] [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: 15964280] [Abstract] Cited for: INTERACTION WITH SRO7.
[27]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545; THR-1097; SER-1121; SER-1135 AND SER-1144, MASS SPECTROMETRY.
[29]	"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: 21248204] [Abstract] Cited for: FUNCTION, INTERACTION WITN SRO7.
[30]	"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: 12351846] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 806-878 IN COMPLEX WITH MLC1.
[31]	"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: 12554638] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 806-830 AND 854-878 IN COMPLEX WITH MLC1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A38454.

RefSeq

NP_014971.1. NM_001183746.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M45	X-ray	1.65	B	806-830	[»]
1M46	X-ray	2.10	B	854-878	[»]
1N2D	X-ray	2.00	C	806-853	[»]
2F6H	X-ray	2.25	X	1152-1570	[»]

ProteinModelPortal

P19524.

SMR

P19524. Positions 3-853, 1152-1570.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2308N.

IntAct

P19524. 48 interactions.

MINT

MINT-440498.

STRING

P19524.

Proteomic databases

PeptideAtlas

P19524.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR326W; YOR326W; YOR326W.

GeneID

854504.

KEGG

sce:YOR326W.

NMPDR

fig|4932.3.peg.6086.

Organism-specific databases

CYGD

YOR326w.

SGD

S000005853. MYO2.

Phylogenomic databases

eggNOG

fuNOG07209.

GeneTree

EFGT00050000000497.

HOGENOM

HBG717149.

OMA

RYSQLNI.

OrthoDB

EOG4H1F3S.

Gene expression databases

ArrayExpress

P19524.

Genevestigator

P19524.

GermOnline

YOR326W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR018444. Dil_domain.
IPR002710. Dilute.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
[Graphical view]

Pfam

PF01843. DIL. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]

PRINTS

PR00193. MYOSINHEAVY.

SMART

SM00015. IQ. 4 hits.
SM00242. MYSc. 1 hit.
[Graphical view]

PROSITE

PS51126. DILUTE. 1 hit.
PS50096. IQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

976849.

Entry information

Entry name

MYO2_YEAST

Accession

Primary (citable) accession number: P19524
Secondary accession number(s): D6W323

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	December 14, 2011
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program