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P35580

- MYH10_HUMAN

UniProt

P35580 - MYH10_HUMAN

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Protein

Myosin-10

Gene

MYH10

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. actin binding Source: UniProtKB
  2. actin-dependent ATPase activity Source: MGI
  3. actin filament binding Source: MGI
  4. ADP binding Source: MGI
  5. ATP binding Source: UniProtKB
  6. microfilament motor activity Source: MGI

GO - Biological processi

  1. actin filament-based movement Source: MGI
  2. actomyosin structure organization Source: UniProt
  3. adult heart development Source: Ensembl
  4. ATP catabolic process Source: UniProt
  5. axon guidance Source: Reactome
  6. cardiac myofibril assembly Source: Ensembl
  7. cell adhesion Source: UniProtKB-KW
  8. cell proliferation Source: Ensembl
  9. cerebellar Purkinje cell layer development Source: Ensembl
  10. exocytosis Source: Ensembl
  11. fourth ventricle development Source: Ensembl
  12. in utero embryonic development Source: Ensembl
  13. lateral ventricle development Source: Ensembl
  14. mitotic cytokinesis Source: MGI
  15. neuromuscular process controlling balance Source: Ensembl
  16. neuron migration Source: Ensembl
  17. nuclear migration Source: Ensembl
  18. plasma membrane repair Source: Ensembl
  19. regulation of cell shape Source: UniProtKB-KW
  20. retina development in camera-type eye Source: Ensembl
  21. substrate-dependent cell migration, cell extension Source: Ensembl
  22. third ventricle development Source: Ensembl
  23. ventricular cardiac muscle cell development Source: Ensembl
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.

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: Chromosome 17

Organism-specific databases

HGNCiHGNC:7568. MYH10.

Subcellular locationi

Cell projectionlamellipodium 2 Publications
Note: Colocalizes with MCC at the leading edge of migrating cells.

GO - Cellular componenti

  1. actomyosin Source: UniProt
  2. axon Source: Ensembl
  3. cell cortex Source: UniProtKB
  4. cleavage furrow Source: UniProtKB
  5. cytoplasm Source: UniProtKB
  6. dendritic spine Source: Ensembl
  7. extracellular vesicular exosome Source: UniProtKB
  8. growth cone Source: Ensembl
  9. midbody Source: UniProtKB
  10. myosin complex Source: UniProtKB
  11. myosin II complex Source: UniProt
  12. myosin II filament Source: UniProt
  13. neuromuscular junction Source: Ensembl
  14. neuronal cell body Source: Ensembl
  15. nucleus Source: UniProt
  16. plasma membrane Source: Ensembl
  17. spindle Source: Ensembl
  18. stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31366.

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 residuei442 – 4421N6-acetyllysine1 Publication
Modified residuei1145 – 11451Phosphoserine1 Publication
Modified residuei1241 – 12411N6-acetyllysineBy similarity
Modified residuei1301 – 13011N6-acetyllysineBy similarity
Modified residuei1645 – 16451N6-acetyllysine1 Publication
Modified residuei1938 – 19381Phosphoserine1 Publication
Modified residuei1939 – 19391Phosphoserine2 Publications
Modified residuei1952 – 19521Phosphoserine1 Publication
Modified residuei1956 – 19561Phosphoserine5 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.
GenevestigatoriP35580.

Organism-specific databases

HPAiCAB017180.

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

3D structure databases

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.
OMAiASNMESQ.
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. Align

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

Note: Contains a phosphoserine at position 214.

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. Contains a phosphoserine at position 214.

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti800 – 8001Y → C in AAA99177. (PubMed:7499478)Curated
Sequence conflicti943 – 9442NE → KK in AAH08968. 1 PublicationCurated
Sequence conflicti1429 – 14291L → P in AAI17691. 1 PublicationCurated
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:
EMBL
GenBank
DDBJ
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]
XP_005256709.1. XM_005256652.2. [P35580-3]
UniGeneiHs.16355.

Genome annotation databases

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

Polymorphism databases

DMDMi215274129.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11144.1. [P35580-1 ]
CCDS58515.1. [P35580-4 ]
CCDS73984.1. [P35580-5 ]
PIRi A59252.
I65769.
RefSeqi NP_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 ]
XP_005256709.1. XM_005256652.2. [P35580-3 ]
UniGenei Hs.16355.

3D structure databases

ProteinModelPortali P35580.
SMRi P35580. Positions 7-904.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110713. 58 interactions.
DIPi DIP-31110N.
IntActi P35580. 19 interactions.
MINTi MINT-7901694.
STRINGi 9606.ENSP00000269243.

PTM databases

PhosphoSitei P35580.

Polymorphism databases

DMDMi 215274129.

Proteomic databases

MaxQBi P35580.
PaxDbi P35580.
PRIDEi P35580.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269243 ; ENSP00000269243 ; ENSG00000133026 . [P35580-1 ]
ENST00000360416 ; ENSP00000353590 ; ENSG00000133026 . [P35580-4 ]
ENST00000379980 ; ENSP00000369315 ; ENSG00000133026 . [P35580-5 ]
GeneIDi 4628.
KEGGi hsa:4628.
UCSCi uc002gll.4. human. [P35580-1 ]
uc010cnx.4. human.

Organism-specific databases

CTDi 4628.
GeneCardsi GC17M008318.
H-InvDB HIX0013525.
HGNCi HGNC:7568. MYH10.
HPAi CAB017180.
MIMi 160776. gene.
neXtProti NX_P35580.
PharmGKBi PA31366.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5022.
GeneTreei ENSGT00760000118919.
HOGENOMi HOG000173958.
HOVERGENi HBG004704.
InParanoidi P35580.
KOi K10352.
OMAi ASNMESQ.
PhylomeDBi P35580.
TreeFami TF333601.

Enzyme and pathway databases

Reactomei REACT_19277. Sema4D induced cell migration and growth-cone collapse.

Miscellaneous databases

ChiTaRSi MYH10. human.
GeneWikii MYH10.
GenomeRNAii 4628.
NextBioi 17814.
PROi P35580.
SOURCEi Search...

Gene expression databases

Bgeei P35580.
CleanExi HS_MYH10.
ExpressionAtlasi P35580. baseline and differential.
Genevestigatori P35580.

Family and domain databases

Gene3Di 4.10.270.10. 1 hit.
InterProi IPR000048. 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 ]
Pfami PF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view ]
PRINTSi PR00193. MYOSINHEAVY.
SMARTi SM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view ]
SUPFAMi SSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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; SER-1938 AND SER-1956, 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.

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: October 29, 2014
This is version 150 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

Keywords - Technical termi

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3