| Tag | Content |
|---|
| CPLM ID | CPLM-013944 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Unconventional myosin-Id |
Protein Synonyms/Alias | |
Gene Name | Myo1d |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 152 | LEAFGNAKTNRNDNS | ubiquitination | [1] | | 495 | RKTCASDKILEFDRD | ubiquitination | [1] | | 811 | VAAMEMLKGQRADLG | ubiquitination | [1] | | 994 | QPQPDFTKNRSGFIL | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). |
Sequence Annotation | DOMAIN 2 682 Myosin head-like.
DOMAIN 699 719 IQ 1.
DOMAIN 721 741 IQ 2.
NP_BIND 102 109 ATP (Potential).
MOD_RES 2 2 N-acetylalanine (By similarity).
MOD_RES 200 200 Phosphoserine (By similarity).
MOD_RES 536 536 Phosphotyrosine. |
Keyword | Acetylation; Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding; Complete proteome; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1006 AA |
Protein Sequence | MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKVLNIYGR 60
DTVEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIMI SGESGAGKTE ASKYIMQYIA 120
AITNPSQRAE IERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH 180
INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSEQMLHSLH LQKSLSSYNY IRVGAQLKSS 240
INDAAEFKVV ADAMKVIGFK PEEIQTVYKI LAVILHLGNL KFIVDGDTPL IENGKVVSVI 300
AELLSTKADM VEKALLYRTV ATGRDIIDKQ HTEQEASYGR DAFAKAIYER LFCWIVTRIN 360
DIIEVKNYDT TIHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ 420
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDGM FLEALNSKLG 480
KHGHFSSRKT CASDKILEFD RDFRIRHYAG DVVYSAIGFI DKNKDTLFQD FKRLMYNSSN 540
PVLKNMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDKKSPQI 600
FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK 660
KLIERCGFQD DVAYGKSKIF IRTPRTLFTL EELRAQMLVR VVLFLQKVWR GTLARMRYKR 720
TKAALTIIRY YRRYKVKSYI HEVARRFHGV KNMRDYGKHV KWPTPPKVLR RFEEALQSIF 780
NRWRASQLIK TIPASDLPQV RAKVAAMEML KGQRADLGLQ RAWEGNYLAS KPDTPQTSGT 840
FVPVANELKR KDKYMNVLFS CHVRKVNRFS KVEDRAIFVT DRHLYKMDPT KQYKVMKTIP 900
LYNLTGLSVS NGKDQLVVFH TKDNKDLIVC LFSKQPTHES RIGELVGVLV NHFKSEKRHL 960
QVNVTNPVQC SLHGKKCTVS VETRLNQPQP DFTKNRSGFI LSVPGN 1006 |
Gene Ontology | GO:0030673; C:axolemma; IEA:Compara. GO:0016459; C:myosin complex; IEA:UniProtKB-KW. GO:0005790; C:smooth endoplasmic reticulum; IEA:Compara. GO:0030898; F:actin-dependent ATPase activity; IEA:Compara. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0000146; F:microfilament motor activity; IEA:Compara. GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |