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Protein

Myosin-10

Gene

MYH10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi178 – 1858ATPSequence Analysis

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin-dependent ATPase activity Source: MGI
  • actin filament binding Source: MGI
  • ADP binding Source: MGI
  • ATP binding Source: UniProtKB
  • microfilament motor activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Cell adhesion, Cell shape

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_264548. EPHA-mediated growth cone collapse.
REACT_355192. RHO GTPases Activate ROCKs.
REACT_355303. RHO GTPases activate CIT.
REACT_355347. RHO GTPases activate PAKs.
REACT_355542. RHO GTPases activate PKNs.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-10
Alternative name(s):
Cellular myosin heavy chain, type B
Myosin heavy chain 10
Myosin heavy chain, non-muscle IIb
Non-muscle myosin heavy chain B
Short name:
NMMHC-B
Non-muscle myosin heavy chain IIb
Short name:
NMMHC II-b
Short name:
NMMHC-IIB
Gene namesi
Name:MYH10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7568. MYH10.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • actomyosin Source: UniProtKB
  • axon Source: Ensembl
  • brush border Source: Ensembl
  • cell cortex Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • dendritic spine Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • growth cone Source: Ensembl
  • lamellipodium Source: UniProtKB-SubCell
  • midbody Source: UniProtKB
  • mitochondrion Source: HPA
  • myosin complex Source: UniProtKB
  • myosin II complex Source: UniProtKB
  • myosin II filament Source: UniProtKB
  • neuromuscular junction Source: Ensembl
  • neuronal cell body Source: Ensembl
  • nucleus Source: UniProtKB
  • plasma membrane Source: Ensembl
  • spindle Source: Ensembl
  • stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31366.

Polymorphism and mutation databases

BioMutaiMYH10.
DMDMi215274129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19761976Myosin-10PRO_0000123421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei442 – 4421N6-acetyllysine1 Publication
Modified residuei1145 – 11451Phosphoserine1 Publication
Modified residuei1241 – 12411N6-acetyllysineBy similarity
Modified residuei1301 – 13011N6-acetyllysineBy similarity
Modified residuei1645 – 16451N6-acetyllysine1 Publication
Modified residuei1935 – 19351Phosphoserine1 Publication
Modified residuei1938 – 19381Phosphoserine1 Publication
Modified residuei1939 – 19391Phosphoserine3 Publications
Modified residuei1952 – 19521Phosphoserine2 Publications
Modified residuei1956 – 19561Phosphoserine5 Publications
Modified residuei1960 – 19601Phosphothreonine1 Publication
Isoform 2 (identifier: P35580-2)
Modified residuei214 – 2141Phosphoserine3 Publications
Isoform 4 (identifier: P35580-4)
Modified residuei214 – 2141Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated by ABL2.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35580.
PaxDbiP35580.
PRIDEiP35580.

PTM databases

PhosphoSiteiP35580.

Expressioni

Tissue specificityi

Isoform 1 is expressed in cerebellum and spinal chord. Isoform 2 is expressed in cerebrum and retina. Isoform 3 is expressed in the cerebrum and to a much lower extent in cerebellum.1 Publication

Gene expression databases

BgeeiP35580.
CleanExiHS_MYH10.
ExpressionAtlasiP35580. baseline and differential.
GenevisibleiP35580. HS.

Organism-specific databases

HPAiCAB017180.
HPA047541.
HPA057198.

Interactioni

Subunit structurei

Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with PLEKHG6. Interacts with ECM29. Interacts with KIF26B (By similarity). Interacts with LARP6. Interacts with MCC.By similarity4 Publications

Protein-protein interaction databases

BioGridi110713. 58 interactions.
DIPiDIP-31110N.
IntActiP35580. 19 interactions.
MINTiMINT-7901694.
STRINGi9606.ENSP00000269243.

Structurei

Secondary structure

1
1976
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni9 – 146Combined sources
Beta strandi36 – 394Combined sources
Beta strandi41 – 499Combined sources
Beta strandi57 – 659Combined sources
Beta strandi68 – 758Combined sources
Helixi82 – 843Combined sources
Helixi90 – 923Combined sources
Helixi98 – 10912Combined sources
Turni110 – 1123Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi121 – 1255Combined sources
Helixi136 – 1416Combined sources
Helixi154 – 16714Combined sources
Beta strandi172 – 1787Combined sources
Helixi180 – 1823Combined sources
Helixi184 – 19815Combined sources
Helixi216 – 2183Combined sources
Helixi221 – 2299Combined sources
Beta strandi237 – 2404Combined sources
Beta strandi242 – 2509Combined sources
Beta strandi256 – 2649Combined sources
Helixi269 – 2724Combined sources
Helixi282 – 2909Combined sources
Helixi293 – 2986Combined sources
Helixi304 – 3063Combined sources
Helixi322 – 33514Combined sources
Helixi340 – 35718Combined sources
Helixi379 – 3846Combined sources
Helixi389 – 3979Combined sources
Helixi414 – 44229Combined sources
Beta strandi453 – 4619Combined sources
Helixi471 – 50131Combined sources
Helixi511 – 5144Combined sources
Helixi516 – 5227Combined sources
Helixi531 – 5388Combined sources
Helixi546 – 55611Combined sources
Beta strandi567 – 5693Combined sources
Beta strandi572 – 5787Combined sources
Beta strandi583 – 5864Combined sources
Helixi591 – 5944Combined sources
Helixi601 – 6088Combined sources
Helixi613 – 6186Combined sources
Helixi653 – 66816Combined sources
Beta strandi671 – 6799Combined sources
Helixi692 – 70211Combined sources
Helixi704 – 7118Combined sources
Beta strandi717 – 7204Combined sources
Helixi721 – 7288Combined sources
Helixi729 – 7313Combined sources
Turni733 – 7353Combined sources
Helixi745 – 75410Combined sources
Beta strandi760 – 7634Combined sources
Beta strandi765 – 7706Combined sources
Helixi774 – 7829Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PD3X-ray2.84A/B1-782[»]
ProteinModelPortaliP35580.
SMRiP35580. Positions 7-904.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 783699Myosin motorAdd
BLAST
Domaini786 – 81530IQPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili845 – 19761132Sequence AnalysisAdd
BLAST

Domaini

The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiP35580.
KOiK10352.
OMAiRHKHAQE.
PhylomeDBiP35580.
TreeFamiTF333601.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR008989. Myosin_S1_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35580-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI
60 70 80 90 100
KEERGDEVMV ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS
110 120 130 140 150
VLHNLKDRYY SGLIYTYSGL FCVVINPYKN LPIYSENIIE MYRGKKRHEM
160 170 180 190 200
PPHIYAISES AYRCMLQDRE DQSILCTGES GAGKTENTKK VIQYLAHVAS
210 220 230 240 250
SHKGRKDHNI PGELERQLLQ ANPILESFGN AKTVKNDNSS RFGKFIRINF
260 270 280 290 300
DVTGYIVGAN IETYLLEKSR AVRQAKDERT FHIFYQLLSG AGEHLKSDLL
310 320 330 340 350
LEGFNNYRFL SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV
360 370 380 390 400
SSVLQFGNIS FKKERNTDQA SMPENTVAQK LCHLLGMNVM EFTRAILTPR
410 420 430 440 450
IKVGRDYVQK AQTKEQADFA VEALAKATYE RLFRWLVHRI NKALDRTKRQ
460 470 480 490 500
GASFIGILDI AGFEIFELNS FEQLCINYTN EKLQQLFNHT MFILEQEEYQ
510 520 530 540 550
REGIEWNFID FGLDLQPCID LIERPANPPG VLALLDEECW FPKATDKTFV
560 570 580 590 600
EKLVQEQGSH SKFQKPRQLK DKADFCIIHY AGKVDYKADE WLMKNMDPLN
610 620 630 640 650
DNVATLLHQS SDRFVAELWK DVDRIVGLDQ VTGMTETAFG SAYKTKKGMF
660 670 680 690 700
RTVGQLYKES LTKLMATLRN TNPNFVRCII PNHEKRAGKL DPHLVLDQLR
710 720 730 740 750
CNGVLEGIRI CRQGFPNRIV FQEFRQRYEI LTPNAIPKGF MDGKQACERM
760 770 780 790 800
IRALELDPNL YRIGQSKIFF RAGVLAHLEE ERDLKITDII IFFQAVCRGY
810 820 830 840 850
LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR HWQWWRVFTK VKPLLQVTRQ
860 870 880 890 900
EEELQAKDEE LLKVKEKQTK VEGELEEMER KHQQLLEEKN ILAEQLQAET
910 920 930 940 950
ELFAEAEEMR ARLAAKKQEL EEILHDLESR VEEEEERNQI LQNEKKKMQA
960 970 980 990 1000
HIQDLEEQLD EEEGARQKLQ LEKVTAEAKI KKMEEEILLL EDQNSKFIKE
1010 1020 1030 1040 1050
KKLMEDRIAE CSSQLAEEEE KAKNLAKIRN KQEVMISDLE ERLKKEEKTR
1060 1070 1080 1090 1100
QELEKAKRKL DGETTDLQDQ IAELQAQIDE LKLQLAKKEE ELQGALARGD
1110 1120 1130 1140 1150
DETLHKNNAL KVVRELQAQI AELQEDFESE KASRNKAEKQ KRDLSEELEA
1160 1170 1180 1190 1200
LKTELEDTLD TTAAQQELRT KREQEVAELK KALEEETKNH EAQIQDMRQR
1210 1220 1230 1240 1250
HATALEELSE QLEQAKRFKA NLEKNKQGLE TDNKELACEV KVLQQVKAES
1260 1270 1280 1290 1300
EHKRKKLDAQ VQELHAKVSE GDRLRVELAE KASKLQNELD NVSTLLEEAE
1310 1320 1330 1340 1350
KKGIKFAKDA ASLESQLQDT QELLQEETRQ KLNLSSRIRQ LEEEKNSLQE
1360 1370 1380 1390 1400
QQEEEEEARK NLEKQVLALQ SQLADTKKKV DDDLGTIESL EEAKKKLLKD
1410 1420 1430 1440 1450
AEALSQRLEE KALAYDKLEK TKNRLQQELD DLTVDLDHQR QVASNLEKKQ
1460 1470 1480 1490 1500
KKFDQLLAEE KSISARYAEE RDRAEAEARE KETKALSLAR ALEEALEAKE
1510 1520 1530 1540 1550
EFERQNKQLR ADMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE
1560 1570 1580 1590 1600
LEDELQATED AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK KRLLIKQVRE
1610 1620 1630 1640 1650
LEAELEDERK QRALAVASKK KMEIDLKDLE AQIEAANKAR DEVIKQLRKL
1660 1670 1680 1690 1700
QAQMKDYQRE LEEARASRDE IFAQSKESEK KLKSLEAEIL QLQEELASSE
1710 1720 1730 1740 1750
RARRHAEQER DELADEITNS ASGKSALLDE KRRLEARIAQ LEEELEEEQS
1760 1770 1780 1790 1800
NMELLNDRFR KTTLQVDTLN AELAAERSAA QKSDNARQQL ERQNKELKAK
1810 1820 1830 1840 1850
LQELEGAVKS KFKATISALE AKIGQLEEQL EQEAKERAAA NKLVRRTEKK
1860 1870 1880 1890 1900
LKEIFMQVED ERRHADQYKE QMEKANARMK QLKRQLEEAE EEATRANASR
1910 1920 1930 1940 1950
RKLQRELDDA TEANEGLSRE VSTLKNRLRR GGPISFSSSR SGRRQLHLEG
1960 1970
ASLELSDDDT ESKTSDVNET QPPQSE
Length:1,976
Mass (Da):228,999
Last modified:November 25, 2008 - v3
Checksum:iA7C91944EBC2368F
GO
Isoform 2 (identifier: P35580-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     211-211: P → PQESPKPVKHQSGSLLY

Show »
Length:1,992
Mass (Da):230,779
Checksum:i2FCF86A36AB04BC5
GO
Isoform 3 (identifier: P35580-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     621-621: D → DEIQNIQRASFYDSVSGLHEPP

Show »
Length:1,997
Mass (Da):231,369
Checksum:i59FCA83F827E415E
GO
Isoform 4 (identifier: P35580-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     211-211: P → PQESPKPVKHQ
     621-621: D → DEIQNIQRASFYDSVSGLHEPP

Note: No experimental confirmation available.3 Publications
Show »
Length:2,007
Mass (Da):232,528
Checksum:iD56BDA1A873045A2
GO
Isoform 5 (identifier: P35580-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     211-211: P → PESPKPVKHQ

Note: No experimental confirmation available.
Show »
Length:1,985
Mass (Da):230,030
Checksum:i493EC32CF0F26E58
GO

Sequence cautioni

The sequence BAE06108.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti800 – 8001Y → C in AAA99177 (PubMed:7499478).Curated
Sequence conflicti943 – 9442NE → KK in AAH08968 (Ref. 5) Curated
Sequence conflicti1429 – 14291L → P in AAI17691 (Ref. 5) Curated
Sequence conflicti1751 – 17511N → D in AAB28952 (PubMed:7916668).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei211 – 2111P → PQESPKPVKHQSGSLLY in isoform 2. 1 PublicationVSP_022013
Alternative sequencei211 – 2111P → PQESPKPVKHQ in isoform 4. 1 PublicationVSP_046033
Alternative sequencei211 – 2111P → PESPKPVKHQ in isoform 5. 1 PublicationVSP_054974
Alternative sequencei621 – 6211D → DEIQNIQRASFYDSVSGLHE PP in isoform 3 and isoform 4. 1 PublicationVSP_022014

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69181 mRNA. Translation: AAA99177.1.
AB210026 mRNA. Translation: BAE06108.1. Different initiation.
AC011061 Genomic DNA. No translation available.
AC025518 Genomic DNA. No translation available.
AC026130 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90046.1.
CH471108 Genomic DNA. Translation: EAW90047.1.
CH471108 Genomic DNA. Translation: EAW90048.1.
CH471108 Genomic DNA. Translation: EAW90049.1.
BC000280 mRNA. Translation: AAH00280.1.
BC008968 mRNA. Translation: AAH08968.1.
BC117690 mRNA. Translation: AAI17691.1.
BC117691 mRNA. Translation: AAI17692.1.
BC144668 mRNA. Translation: AAI44669.1.
BC150634 mRNA. Translation: AAI50635.1.
U15618 mRNA. Translation: AAA87712.1.
S67247 mRNA. Translation: AAB28952.1.
CCDSiCCDS11144.1. [P35580-1]
CCDS58515.1. [P35580-4]
CCDS73984.1. [P35580-5]
PIRiA59252.
I65769.
RefSeqiNP_001242941.1. NM_001256012.1. [P35580-4]
NP_001243024.1. NM_001256095.1. [P35580-5]
NP_005955.3. NM_005964.3. [P35580-1]
XP_005256708.1. XM_005256651.2. [P35580-4]
UniGeneiHs.16355.

Genome annotation databases

EnsembliENST00000269243; ENSP00000269243; ENSG00000133026.
ENST00000360416; ENSP00000353590; ENSG00000133026. [P35580-4]
ENST00000379980; ENSP00000369315; ENSG00000133026. [P35580-5]
GeneIDi4628.
KEGGihsa:4628.
UCSCiuc002gll.4. human. [P35580-1]
uc010cnx.4. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69181 mRNA. Translation: AAA99177.1.
AB210026 mRNA. Translation: BAE06108.1. Different initiation.
AC011061 Genomic DNA. No translation available.
AC025518 Genomic DNA. No translation available.
AC026130 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90046.1.
CH471108 Genomic DNA. Translation: EAW90047.1.
CH471108 Genomic DNA. Translation: EAW90048.1.
CH471108 Genomic DNA. Translation: EAW90049.1.
BC000280 mRNA. Translation: AAH00280.1.
BC008968 mRNA. Translation: AAH08968.1.
BC117690 mRNA. Translation: AAI17691.1.
BC117691 mRNA. Translation: AAI17692.1.
BC144668 mRNA. Translation: AAI44669.1.
BC150634 mRNA. Translation: AAI50635.1.
U15618 mRNA. Translation: AAA87712.1.
S67247 mRNA. Translation: AAB28952.1.
CCDSiCCDS11144.1. [P35580-1]
CCDS58515.1. [P35580-4]
CCDS73984.1. [P35580-5]
PIRiA59252.
I65769.
RefSeqiNP_001242941.1. NM_001256012.1. [P35580-4]
NP_001243024.1. NM_001256095.1. [P35580-5]
NP_005955.3. NM_005964.3. [P35580-1]
XP_005256708.1. XM_005256651.2. [P35580-4]
UniGeneiHs.16355.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PD3X-ray2.84A/B1-782[»]
ProteinModelPortaliP35580.
SMRiP35580. Positions 7-904.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110713. 58 interactions.
DIPiDIP-31110N.
IntActiP35580. 19 interactions.
MINTiMINT-7901694.
STRINGi9606.ENSP00000269243.

PTM databases

PhosphoSiteiP35580.

Polymorphism and mutation databases

BioMutaiMYH10.
DMDMi215274129.

Proteomic databases

MaxQBiP35580.
PaxDbiP35580.
PRIDEiP35580.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269243; ENSP00000269243; ENSG00000133026.
ENST00000360416; ENSP00000353590; ENSG00000133026. [P35580-4]
ENST00000379980; ENSP00000369315; ENSG00000133026. [P35580-5]
GeneIDi4628.
KEGGihsa:4628.
UCSCiuc002gll.4. human. [P35580-1]
uc010cnx.4. human.

Organism-specific databases

CTDi4628.
GeneCardsiGC17M008318.
H-InvDBHIX0013525.
HGNCiHGNC:7568. MYH10.
HPAiCAB017180.
HPA047541.
HPA057198.
MIMi160776. gene.
neXtProtiNX_P35580.
PharmGKBiPA31366.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiP35580.
KOiK10352.
OMAiRHKHAQE.
PhylomeDBiP35580.
TreeFamiTF333601.

Enzyme and pathway databases

ReactomeiREACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_264548. EPHA-mediated growth cone collapse.
REACT_355192. RHO GTPases Activate ROCKs.
REACT_355303. RHO GTPases activate CIT.
REACT_355347. RHO GTPases activate PAKs.
REACT_355542. RHO GTPases activate PKNs.

Miscellaneous databases

ChiTaRSiMYH10. human.
GeneWikiiMYH10.
GenomeRNAii4628.
NextBioi17814.
PROiP35580.
SOURCEiSearch...

Gene expression databases

BgeeiP35580.
CleanExiHS_MYH10.
ExpressionAtlasiP35580. baseline and differential.
GenevisibleiP35580. HS.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR008989. Myosin_S1_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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  1. "Cloning of the cDNA encoding human nonmuscle myosin heavy chain-B and analysis of human tissues with isoform-specific antibodies."
    Phillips C.L., Yamakawa K., Adelstein R.S.
    J. Muscle Res. Cell Motil. 16:379-389(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Leukophysin: an RNA helicase A-related molecule identified in cytotoxic T cell granules and vesicles."
    Abdelhaleem M.M., Hameed S., Klassen D., Greenberg A.H.
    J. Immunol. 156:2026-2035(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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 4).
    Tissue: Brain.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 5).
    Tissue: Eye and Muscle.
  7. "Human nonmuscle myosin heavy chains are encoded by two genes located on different chromosomes."
    Simons M., Wang M., McBride O.W., Kawamoto S., Yamakawa K., Gdula D., Adelstein R.S., Weir L.
    Circ. Res. 69:530-539(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-722 (ISOFORM 1).
  8. "Neuronal cell expression of inserted isoforms of vertebrate nonmuscle myosin heavy chain II-B."
    Itoh K., Adelstein R.S.
    J. Biol. Chem. 270:14533-14540(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 211-301 (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 3), TISSUE SPECIFICITY.
  9. "Human smooth muscle myosin heavy chain isoforms as molecular markers for vascular development and atherosclerosis."
    Aikawa M., Sivam P.N., Kuro-O M., Kimura K., Nakahara K., Takewaki S., Ueda M., Yamaguchi H., Yazaki Y., Periasamy M.
    Circ. Res. 73:1000-1012(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1751-1976.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "A novel guanine nucleotide exchange factor MyoGEF is required for cytokinesis."
    Wu D., Asiedu M., Adelstein R.S., Wei Q.
    Cell Cycle 5:1234-1239(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLEKHG6.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND SER-1956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939 AND SER-1956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-442 AND LYS-1645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
    Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
    J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ECM29.
  19. "Nonmuscle myosin-dependent synthesis of type I collagen."
    Cai L., Fritz D., Stefanovic L., Stefanovic B.
    J. Mol. Biol. 401:564-578(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LARP6.
  20. "Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading."
    Betapudi V.
    PLoS ONE 5:E8560-E8560(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  21. "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-1956, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 (ISOFORMS 2 AND 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145 AND SER-1938, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 (ISOFORMS 2 AND 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "The PDZ-binding motif of MCC is phosphorylated at position -1 and controls lamellipodia formation in colon epithelial cells."
    Pangon L., Van Kralingen C., Abas M., Daly R.J., Musgrove E.A., Kohonen-Corish M.R.
    Biochim. Biophys. Acta 1823:1058-1067(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCC, SUBCELLULAR LOCATION.
  25. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1935; SER-1939; SER-1952; SER-1956 AND THR-1960, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 (ISOFORMS 2 AND 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMYH10_HUMAN
AccessioniPrimary (citable) accession number: P35580
Secondary accession number(s): B2RWP9
, D3DTS1, F8VTL3, Q12989, Q149N3, Q149N4, Q16087, Q4LE45, Q6PK16, Q9BWG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 25, 2008
Last modified: July 22, 2015
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Represents a conventional non-muscle myosin. This protein should not be confused with the unconventional myosin-10 (MYO10).Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.