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P35580 (MYH10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MYH10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1976 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.19 Ref.20

Subunit structure

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. Ref.11 Ref.18 Ref.19 Ref.24

Subcellular location

Cell projectionlamellipodium. Note: Colocalizes with MCC at the leading edge of migrating cells. Ref.20 Ref.24

Tissue specificity

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. Ref.8

Domain

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.

Post-translational modification

Phosphorylated by ABL2 By similarity.

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Contains 1 IQ domain.

Contains 1 myosin motor domain.

Caution

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

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
Cell shape
   Cellular componentCell projection
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from mutant phenotype PubMed 24072716. Source: UniProt

actin filament-based movement

Inferred from direct assay PubMed 15845534. Source: MGI

actomyosin structure organization

Inferred from mutant phenotype PubMed 24072716. Source: UniProt

adult heart development

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

cardiac myofibril assembly

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cerebellar Purkinje cell layer development

Inferred from electronic annotation. Source: Ensembl

exocytosis

Inferred from electronic annotation. Source: Ensembl

fourth ventricle development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

lateral ventricle development

Inferred from electronic annotation. Source: Ensembl

mitotic cytokinesis

Inferred from direct assay PubMed 15774463. Source: MGI

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

nuclear migration

Inferred from electronic annotation. Source: Ensembl

plasma membrane repair

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

substrate-dependent cell migration, cell extension

Inferred from electronic annotation. Source: Ensembl

third ventricle development

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactomyosin

Inferred from direct assay PubMed 24072716. Source: UniProt

axon

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from direct assay PubMed 7699007. Source: UniProtKB

cleavage furrow

Inferred from direct assay PubMed 11029059PubMed 7699007. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 7699007. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: Ensembl

growth cone

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay PubMed 11029059. Source: UniProtKB

myosin II complex

Inferred from direct assay PubMed 24072716. Source: UniProt

myosin II filament

Inferred from direct assay PubMed 24072716. Source: UniProt

myosin complex

Non-traceable author statement Ref.1. Source: UniProtKB

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

plasma membrane

Inferred from electronic annotation. Source: Ensembl

spindle

Inferred from electronic annotation. Source: Ensembl

stress fiber

Inferred from direct assay PubMed 7699007. Source: UniProtKB

   Molecular_functionADP binding

Inferred from direct assay PubMed 15845534. Source: MGI

ATP binding

Non-traceable author statement Ref.8. Source: UniProtKB

actin binding

Non-traceable author statement Ref.8. Source: UniProtKB

actin filament binding

Inferred from direct assay PubMed 15845534. Source: MGI

actin-dependent ATPase activity

Inferred from direct assay PubMed 15845534. Source: MGI

microfilament motor activity

Inferred from direct assay PubMed 15845534. Source: MGI

protein binding

Inferred from physical interaction PubMed 7542763. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35580-1)

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.
Isoform 2 (identifier: P35580-2)

The sequence of this isoform differs from the canonical sequence as follows:
     211-211: P → PQESPKPVKHQSGSLLY
Note: Contains a phosphoserine at position 214.
Isoform 3 (identifier: P35580-3)

The sequence of this isoform differs from the canonical sequence as follows:
     621-621: D → DEIQNIQRASFYDSVSGLHEPP
Isoform 4 (identifier: P35580-4)

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.
Isoform 5 (identifier: P35580-5)

The sequence of this isoform differs from the canonical sequence as follows:
     211-211: P → PESPKPVKHQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19761976Myosin-10
PRO_0000123421

Regions

Domain85 – 783699Myosin motor
Domain786 – 81530IQ
Nucleotide binding178 – 1858ATP Potential
Coiled coil845 – 19761132 Potential

Amino acid modifications

Modified residue4421N6-acetyllysine Ref.17
Modified residue11451Phosphoserine Ref.23
Modified residue12411N6-acetyllysine By similarity
Modified residue13011N6-acetyllysine By similarity
Modified residue16451N6-acetyllysine Ref.17
Modified residue19381Phosphoserine Ref.23
Modified residue19391Phosphoserine Ref.13 Ref.16
Modified residue19521Phosphoserine Ref.13
Modified residue19561Phosphoserine Ref.13 Ref.14 Ref.16 Ref.21 Ref.23

Natural variations

Alternative sequence2111P → PQESPKPVKHQSGSLLY in isoform 2.
VSP_022013
Alternative sequence2111P → PQESPKPVKHQ in isoform 4.
VSP_046033
Alternative sequence2111P → PESPKPVKHQ in isoform 5.
VSP_054974
Alternative sequence6211D → DEIQNIQRASFYDSVSGLHE PP in isoform 3 and isoform 4.
VSP_022014

Experimental info

Sequence conflict8001Y → C in AAA99177. Ref.1
Sequence conflict943 – 9442NE → KK in AAH08968. Ref.5
Sequence conflict14291L → P in AAI17691. Ref.5
Sequence conflict17511N → D in AAB28952. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: A7C91944EBC2368F

FASTA1,976228,999
        10         20         30         40         50         60 
MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVMV 

        70         80         90        100        110        120 
ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL 

       130        140        150        160        170        180 
FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQDRE DQSILCTGES 

       190        200        210        220        230        240 
GAGKTENTKK VIQYLAHVAS SHKGRKDHNI PGELERQLLQ ANPILESFGN AKTVKNDNSS 

       250        260        270        280        290        300 
RFGKFIRINF DVTGYIVGAN IETYLLEKSR AVRQAKDERT FHIFYQLLSG AGEHLKSDLL 

       310        320        330        340        350        360 
LEGFNNYRFL SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV SSVLQFGNIS 

       370        380        390        400        410        420 
FKKERNTDQA SMPENTVAQK LCHLLGMNVM EFTRAILTPR IKVGRDYVQK AQTKEQADFA 

       430        440        450        460        470        480 
VEALAKATYE RLFRWLVHRI NKALDRTKRQ GASFIGILDI AGFEIFELNS FEQLCINYTN 

       490        500        510        520        530        540 
EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCID LIERPANPPG VLALLDEECW 

       550        560        570        580        590        600 
FPKATDKTFV EKLVQEQGSH SKFQKPRQLK DKADFCIIHY AGKVDYKADE WLMKNMDPLN 

       610        620        630        640        650        660 
DNVATLLHQS SDRFVAELWK DVDRIVGLDQ VTGMTETAFG SAYKTKKGMF RTVGQLYKES 

       670        680        690        700        710        720 
LTKLMATLRN TNPNFVRCII PNHEKRAGKL DPHLVLDQLR CNGVLEGIRI CRQGFPNRIV 

       730        740        750        760        770        780 
FQEFRQRYEI LTPNAIPKGF MDGKQACERM IRALELDPNL YRIGQSKIFF RAGVLAHLEE 

       790        800        810        820        830        840 
ERDLKITDII IFFQAVCRGY LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR HWQWWRVFTK 

       850        860        870        880        890        900 
VKPLLQVTRQ EEELQAKDEE LLKVKEKQTK VEGELEEMER KHQQLLEEKN ILAEQLQAET 

       910        920        930        940        950        960 
ELFAEAEEMR ARLAAKKQEL EEILHDLESR VEEEEERNQI LQNEKKKMQA HIQDLEEQLD 

       970        980        990       1000       1010       1020 
EEEGARQKLQ LEKVTAEAKI KKMEEEILLL EDQNSKFIKE KKLMEDRIAE CSSQLAEEEE 

      1030       1040       1050       1060       1070       1080 
KAKNLAKIRN KQEVMISDLE ERLKKEEKTR QELEKAKRKL DGETTDLQDQ IAELQAQIDE 

      1090       1100       1110       1120       1130       1140 
LKLQLAKKEE ELQGALARGD DETLHKNNAL KVVRELQAQI AELQEDFESE KASRNKAEKQ 

      1150       1160       1170       1180       1190       1200 
KRDLSEELEA LKTELEDTLD TTAAQQELRT KREQEVAELK KALEEETKNH EAQIQDMRQR 

      1210       1220       1230       1240       1250       1260 
HATALEELSE QLEQAKRFKA NLEKNKQGLE TDNKELACEV KVLQQVKAES EHKRKKLDAQ 

      1270       1280       1290       1300       1310       1320 
VQELHAKVSE GDRLRVELAE KASKLQNELD NVSTLLEEAE KKGIKFAKDA ASLESQLQDT 

      1330       1340       1350       1360       1370       1380 
QELLQEETRQ KLNLSSRIRQ LEEEKNSLQE QQEEEEEARK NLEKQVLALQ SQLADTKKKV 

      1390       1400       1410       1420       1430       1440 
DDDLGTIESL EEAKKKLLKD AEALSQRLEE KALAYDKLEK TKNRLQQELD DLTVDLDHQR 

      1450       1460       1470       1480       1490       1500 
QVASNLEKKQ KKFDQLLAEE KSISARYAEE RDRAEAEARE KETKALSLAR ALEEALEAKE 

      1510       1520       1530       1540       1550       1560 
EFERQNKQLR ADMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE LEDELQATED 

      1570       1580       1590       1600       1610       1620 
AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK KRLLIKQVRE LEAELEDERK QRALAVASKK 

      1630       1640       1650       1660       1670       1680 
KMEIDLKDLE AQIEAANKAR DEVIKQLRKL QAQMKDYQRE LEEARASRDE IFAQSKESEK 

      1690       1700       1710       1720       1730       1740 
KLKSLEAEIL QLQEELASSE RARRHAEQER DELADEITNS ASGKSALLDE KRRLEARIAQ 

      1750       1760       1770       1780       1790       1800 
LEEELEEEQS NMELLNDRFR KTTLQVDTLN AELAAERSAA QKSDNARQQL ERQNKELKAK 

      1810       1820       1830       1840       1850       1860 
LQELEGAVKS KFKATISALE AKIGQLEEQL EQEAKERAAA NKLVRRTEKK LKEIFMQVED 

      1870       1880       1890       1900       1910       1920 
ERRHADQYKE QMEKANARMK QLKRQLEEAE EEATRANASR RKLQRELDDA TEANEGLSRE 

      1930       1940       1950       1960       1970 
VSTLKNRLRR GGPISFSSSR SGRRQLHLEG ASLELSDDDT ESKTSDVNET QPPQSE 

« Hide

Isoform 2 [UniParc].

Checksum: 2FCF86A36AB04BC5
Show »

FASTA1,992230,779
Isoform 3 [UniParc].

Checksum: 59FCA83F827E415E
Show »

FASTA1,997231,369
Isoform 4 [UniParc].

Checksum: D56BDA1A873045A2
Show »

FASTA2,007232,528
Isoform 5 [UniParc].

Checksum: 493EC32CF0F26E58
Show »

FASTA1,985230,030

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11144.1. [P35580-1]
CCDS58515.1. [P35580-4]
PIRA59252.
I65769.
RefSeqNP_001242941.1. NM_001256012.1. [P35580-4]
NP_001243024.1. NM_001256095.1.
NP_005955.3. NM_005964.3. [P35580-1]
XP_005256708.1. XM_005256651.2. [P35580-4]
XP_005256709.1. XM_005256652.2. [P35580-3]
UniGeneHs.16355.

3D structure databases

ProteinModelPortalP35580.
SMRP35580. Positions 7-963, 1899-1926.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110713. 60 interactions.
DIPDIP-31110N.
IntActP35580. 17 interactions.
MINTMINT-7901694.
STRING9606.ENSP00000269243.

PTM databases

PhosphoSiteP35580.

Polymorphism databases

DMDM215274129.

Proteomic databases

MaxQBP35580.
PaxDbP35580.
PRIDEP35580.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269243; ENSP00000269243; ENSG00000133026. [P35580-1]
ENST00000360416; ENSP00000353590; ENSG00000133026. [P35580-4]
ENST00000396239; ENSP00000379539; ENSG00000133026. [P35580-3]
GeneID4628.
KEGGhsa:4628.
UCSCuc002gll.4. human. [P35580-1]

Organism-specific databases

CTD4628.
GeneCardsGC17M008318.
H-InvDBHIX0013525.
HGNCHGNC:7568. MYH10.
HPACAB017180.
MIM160776. gene.
neXtProtNX_P35580.
PharmGKBPA31366.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000173958.
HOVERGENHBG004704.
KOK10352.
OMAASNMESQ.
PhylomeDBP35580.
TreeFamTF333601.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressP35580.
BgeeP35580.
CleanExHS_MYH10.
GenevestigatorP35580.

Family and domain databases

Gene3D4.10.270.10. 1 hit.
InterProIPR000048. 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]
PfamPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYH10. human.
GeneWikiMYH10.
GenomeRNAi4628.
NextBio17814.
PROP35580.
SOURCESearch...

Entry information

Entry nameMYH10_HUMAN
AccessionPrimary (citable) accession number: P35580
Secondary accession number(s): B2RWP9 expand/collapse secondary AC list , D3DTS1, F8VTL3, Q12989, Q149N3, Q149N4, Q16087, Q4LE45, Q6PK16, Q9BWG0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM