Reviewed,
UniProtKB/Swiss-Prot P35580 (MYH10_HUMAN)
Last modified
January 19, 2010.
Version 101.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Myosin-10 Alternative name(s): Myosin heavy chain 10 Myosin heavy chain, non-muscle IIb Non-muscle myosin heavy chain IIb Short name=NMMHC II-b Short name=NMMHC-IIB Cellular myosin heavy chain, type B Non-muscle myosin heavy chain B Short name=NMMHC-B | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1976 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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. |
| 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. Ref.7 |
| Tissue specificity | In brain, isoform 1 is predominantly expresssed in cerebellum and spinal chord, isoform 2 in cerebrum and retina; isoform 3 is expressed in the cerebebrum and to a much lower extent in cerebellum. Ref.5 |
| 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 upon DNA damage, probably by ATM or ATR. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 |
| Sequence similarities | Contains 1 IQ domain. Contains 1 myosin head-like domain. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| IKBKE | Q14164 | 1 | EBI-351758,EBI-307369 | |
| LLGL1 | Q15334 | 1 | EBI-351758,EBI-299979 | |
| MCC | P23508 | 1 | EBI-351758,EBI-307531 | |
| PAK2 | Q13177 | 1 | EBI-351758,EBI-1045887 | |
| PRKAB1 | Q9Y478 | 1 | EBI-351758,EBI-719769 | |
| TNFRSF10D | Q9UBN6 | 1 | EBI-351758,EBI-1044859 |
Alternative products
| This entry describes 3 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 | ||||||
| Isoform 3 (identifier: P35580-3) The sequence of this isoform differs from the canonical sequence as follows: 621-621: D → DEIQNIQRASFYDSVSGLHEPP |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 1976 | 1975 | Myosin-10 | PRO_0000123421 | |||||
Regions | |||||||||
| Domain | 2 – 785 | 784 | Myosin head-like | ||||||
| Domain | 786 – 815 | 30 | IQ | ||||||
| Nucleotide binding | 178 – 185 | 8 | ATP Potential | ||||||
| Coiled coil | 845 – 1976 | 1132 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.16 | ||||||
| Modified residue | 442 | 1 | N6-acetyllysine Ref.18 | ||||||
| Modified residue | 552 | 1 | N6-acetyllysine Ref.18 | ||||||
| Modified residue | 1013 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 1247 | 1 | N6-acetyllysine Ref.18 | ||||||
| Modified residue | 1376 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 1415 | 1 | Phosphotyrosine Ref.9 | ||||||
| Modified residue | 1645 | 1 | N6-acetyllysine Ref.18 | ||||||
| Modified residue | 1938 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1939 | 1 | Phosphoserine Ref.13 Ref.17 | ||||||
| Modified residue | 1952 | 1 | Phosphoserine Ref.13 Ref.17 | ||||||
| Modified residue | 1956 | 1 | Phosphoserine Ref.11 Ref.13 Ref.14 Ref.17 | ||||||
| Modified residue | 1960 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 1964 | 1 | Phosphothreonine Ref.16 | ||||||
| Modified residue | 1965 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 1975 | 1 | Phosphoserine Ref.11 Ref.16 | ||||||
Natural variations | |||||||||
| Alternative sequence | 211 | 1 | P → PQESPKPVKHQSGSLLY in isoform 2. | VSP_022013 | |||||
| Alternative sequence | 621 | 1 | D → DEIQNIQRASFYDSVSGLHE PP in isoform 3. | VSP_022014 | |||||
Experimental info | |||||||||
| Sequence conflict | 800 | 1 | Y → C in AAA99177. Ref.1 | ||||||
| Sequence conflict | 1751 | 1 | N → D in AAB28952. Ref.6 | ||||||
Sequences
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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: 7499478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [2] | 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. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). |
| [4] | "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: 1860190] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-722 (ISOFORM 1). |
| [5] | "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: 7782316] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 211-301 (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 3), TISSUE SPECIFICITY. |
| [6] | "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: 7916668] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1751-1976. |
| [7] | "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: 16721066] [Abstract] Cited for: INTERACTION WITH PLEKHG6. |
| [8] | "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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1960, MASS SPECTROMETRY. Tissue: Epithelium. |
| [9] | "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J.Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1415, MASS SPECTROMETRY. |
| [10] | "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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1013, MASS SPECTROMETRY. |
| [11] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956 AND SER-1975, MASS SPECTROMETRY. |
| [12] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1376, MASS SPECTROMETRY. |
| [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND SER-1956, MASS SPECTROMETRY. |
| [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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, MASS SPECTROMETRY. Tissue: Liver. |
| [15] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [16] | "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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1964; SER-1965 AND SER-1975, MASS SPECTROMETRY. |
| [17] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND SER-1956, MASS SPECTROMETRY. Tissue: T-cell. |
| [18] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-442; LYS-552; LYS-1247 AND LYS-1645, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M69181 mRNA. Translation: AAA99177.1. CH471108 Genomic DNA. Translation: EAW90049.1. BC117691 mRNA. Translation: AAI17692.1. U15618 mRNA. Translation: AAA87712.1. S67247 mRNA. Translation: AAB28952.1. |
| IPI | IPI00397526. IPI00479307. IPI00790503. |
| PIR | A59252. I65769. |
| RefSeq | NP_005955.1. |
| UniGene | Hs.16355 |
3D structure databases | |
| SMR | P35580. Positions 7-815, 26-843, 843-964. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P35580. 19 interactions. |
| STRING | P35580. |
PTM databases | |
| PhosphoSite | P35580. |
Proteomic databases | |
| PRIDE | P35580. |
Genome annotation databases | |
| Ensembl | ENST00000269243; ENSP00000269243; ENSG00000133026; Homo sapiens. [Genome view] |
| GeneID | 4628. |
| KEGG | hsa:4628. |
Organism-specific databases | |
| CTD | 4628. |
| GeneCards | GC17M008318. |
| H-InvDB | HIX0013525. |
| HGNC | HGNC:7568. MYH10. |
| HPA | CAB017180. |
| MIM | 160776. gene. |
| PharmGKB | PA31366. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | maNOG15268. |
| HOVERGEN | P35580. |
| PhylomeDB | P35580. |
Enzyme and pathway databases | |
| Reactome | REACT_18266. Axon guidance. |
Gene expression databases | |
| ArrayExpress | P35580. |
| Bgee | P35580. |
| CleanEx | HS_MYH10. |
| Genevestigator | P35580. |
| GermOnline | ENSG00000133026. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR000048. IQ_CaM_bd_region. IPR001609. Myosin_head_motor_dom. IPR004009. Myosin_N. IPR008989. Myosin_S1_N. IPR002928. Myosin_tail. [Graphical view] |
| Pfam | PF00612. IQ. 1 hit. PF00063. Myosin_head. 1 hit. PF02736. Myosin_N. 1 hit. PF01576. Myosin_tail_1. 1 hit. [Graphical view] |
| PRINTS | PR00193. MYOSINHEAVY. |
| SMART | SM00015. IQ. 1 hit. SM00242. MYSc. 1 hit. [Graphical view] |
| PROSITE | PS50096. IQ. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 17814. |
| SOURCE | Search... |
Entry information
| Entry name | MYH10_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P35580 Secondary accession number(s): Q12989, Q149N3, Q16087 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


