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Protein Page:
MYO5A (mouse)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
MYO5A Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. May also be required for some polarization process involved in dendrite formation. May be a homodimer, which associates with multiple calmodulin or myosin light chains. Binds MLPH and MYRIP. Interacts with RIPL2, the interaction is required for its role in dendrite formation. Detected in melanocytes. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Motor protein
Cellular Component: Golgi apparatus; neuron projection; cell; intermediate filament; actomyosin; secretory granule; ruffle; synaptic vesicle; actomyosin, myosin complex part; photoreceptor outer segment; cell soma; axon; cytoplasm; melanosome; myosin complex
Molecular Function: protein dimerization activity; nucleotide binding; motor activity; calcium ion binding; actin binding; calcium-dependent protein binding; calmodulin binding; microfilament motor activity; ATP-dependent protein binding; SNARE binding; protein binding; protein heterodimerization activity; syntaxin-1 binding; ATP binding; Rab GTPase binding
Biological Process: myelination; exocytosis; melanin metabolic process; metabolic process; pigmentation during development; long-chain fatty acid biosynthetic process; locomotion during locomotory behavior; odontogenesis; synaptic transmission; vesicle transport along actin filament; protein transport; visual perception; transport; melanocyte differentiation; synapse organization and biogenesis; regulation of inositol-1,4,5-triphosphate receptor activity; neuromuscular process controlling balance; ER localization; actin filament-based movement; melanosome localization; melanosome transport; vesicle-mediated transport; melanin biosynthetic process; regulation of exocytosis; cellular response to insulin stimulus; pigmentation; insulin secretion; anagen; secretory granule localization
Reference #:  Q99104 (UniProtKB)
Alt. Names/Synonyms: 9630007J19Rik; AI413174; AI661011; d; d-120J; Dbv; Dilute; dilute lethal-20J protein; Dilute myosin heavy chain, non-muscle; flail; flailer; flr; MVa; Myo5; Myo5a; myosin VA; Myosin-Va; MyoVA; Sev-1
Gene Symbols: Myo5a
Molecular weight: 215,538 Da
Basal Isoelectric point: 8.82  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

MYO5A

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
molecular association, regulation: S1650‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 2 Y31 SAELLKDYKPGDKVL
0 1 K210-u MESIGNAkTTRNDNS
0 16 S600-p QDDEKAIsPTSATSS
0 2 K902-a CFRRMMAkRELKKLK
0 2 K941-a RKVDEQNkDYKCLME
0 1 K979-u QLSEEEAkVATGRVL
0 2 S987 VATGRVLSLQEEIAK
0 1 T1032 SNLKEENTLLKQEKE
0 2 T1113-p PKPGHKRtDstHssN
0 12 S1115-p PGHKRtDstHssNEs
0 4 T1116-p GHKRtDstHssNEsE
0 7 S1118-p KRtDstHssNEsEyT
0 2 S1119-p RtDstHssNEsEyTF
0 2 S1122-p stHssNEsEyTFSSE
0 2 Y1124-p HssNEsEyTFSSEFA
0 27 Y1203 IRGAELEYESLkRQE
0 1 K1207-u ELEYESLkRQELESE
0 1 S1213 LkRQELESENKKLKN
0 1 K1232-u LRKALSEkSAPEVTA
0 1 Y1245 TAPGAPAYRVLMEQL
0 2 K1277-u RSQLVSQkEAIQPKD
0 11 S1450-p VGQMENIsPGQIIDE
0 2 S1537 LLTSTINSIKKVLKK
0 3 T1648-p PTGLRKRtssIADEG
0 7 S1649-p TGLRKRtssIADEGt
2 19 S1650-p GLRKRtssIADEGty
0 3 T1656-p ssIADEGtyTLDSIL
0 1 Y1657-p sIADEGtyTLDSILR
0 1 S1668-p SILRQLNsFHsVMCQ
0 1 S1671-p RQLNsFHsVMCQHGM
  human

 
Y31-p SAELLKDyKPGDKVL
K210 MESIGNAKTTRNDNS
S600-p QDDEKAIsPTSATSS
K902-a CFRRMMAkRELKKLK
K941 RKVDEQNKDYKCLVE
K979 QLSEEEAKVATGRVL
S987-p VATGRVLsLQEEIAK
T1032-p SNLKEENtLLKQEKE
T1113-p PKPGHKRtDstHssN
S1115-p PGHKRtDstHssNES
T1116-p GHKRtDstHssNESE
S1118-p KRtDstHssNESEYI
S1119-p RtDstHssNESEYIF
S1122 stHssNESEYIFSSE
Y1124 HssNESEYIFSSEIA
Y1203-p IRGAELEyESLKRQE
K1207 ELEyESLKRQELEsE
S1213-p LKRQELEsENKKLKN
K1232 LRKALSEKSAPEVTA
Y1245-p TAPGAPAyRVLMEQL
K1277 RSQLVSQKEAIQPKD
S1452-p VGQMENIsPGQIIDE
S1539-p LLTSTINsIKKVLKK
T1650-p PTGLRKRtssIADEG
S1651-p TGLRKRtssIADEGt
S1652-p GLRKRtssIADEGty
T1658-p ssIADEGtyTLDSIL
Y1659-p sIADEGtyTLDSILR
S1670 SILRQLNSFHSVMCQ
S1673 RQLNSFHSVMCQHGM
  rat

 
Y31 SAELLKDYKPGDKVL
K210 MESIGNAKTTRNDNS
S600 QDDEKAISPTSATSS
K902 CFRRMMAKRELKKLK
K941 RKVDEQNKDYKCLME
K979 QLSEEEAKVATGRVL
S987 VATGRVLSLQEEIAK
T1032-p SNLKEENtLLKQEKE
T1113 PKPGHKRTDSTHSSN
S1115 PGHKRTDSTHSSNES
T1116 GHKRTDSTHSSNESE
S1118 KRTDSTHSSNESEYT
S1119 RTDSTHSSNESEYTF
S1122 STHSSNESEYTFSSE
Y1124 HSSNESEYTFSSEFA
Y1203 IRGAELGYESLKRQE
K1207 ELGYESLKRQELESE
S1213 LKRQELESENKKLKN
K1232 LRKALSEKSAPEVNA
Y1245 NAPGAPAYRVLMEQL
K1277-u RSQLVSQkEAIQPKD
S1425 VGQMENISPGQIIDE
S1512 LLTSTINSIKKVLKK
T1623 PTGLRKRTSSIADEG
S1624 TGLRKRTSSIADEGT
S1625 GLRKRTSSIADEGTY
T1631 SSIADEGTYTLDSIL
Y1632 SIADEGTYTLDSILR
S1643 SILRQLNSFHSVMCQ
S1646 RQLNSFHSVMCQHGM
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