| Tag | Content |
|---|
| CPLM ID | CPLM-002720 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Myosin-1 |
Protein Synonyms/Alias | Type II myosin |
Gene Name | MYO1 |
Gene Synonyms/Alias | YHR023W |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1403 | LPVGDIIKNRDSISK | ubiquitination | [1] | | 1684 | IVSLTKIKQELESDL | ubiquitination | [1] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | Required for cell division. |
Sequence Annotation | DOMAIN 1 793 Myosin head-like.
DOMAIN 794 823 IQ.
NP_BIND 180 187 ATP (By similarity).
REGION 460 529 Actin-binding (By similarity). |
Keyword | Actin-binding; ATP-binding; Coiled coil; Complete proteome; Motor protein; Myosin; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1928 AA |
Protein Sequence | MTGGQSCSSN MIVWIPDEKE VFVKGELMST DINKNKFTGQ EEQIGIVHPL DSTEVSNLVQ 60
VRISDVFPVN PSTFDKVENM SELTHLNEPS VLYNLEKRYD CDLIYTYSGL FLVAINPYHN 120
LNLYSEDHIN LYHNKHNRLS KSRLDENSHE KLPPHIFAIA EEAYENLLSE GKDQSILVTG 180
ESGAGKTENT KKILQYLASI TSGSPSNIAP VSGSSIVESF EMKILQSNPI LESFGNAQTV 240
RNNNSSRFGK FIKIEFNEHG MINGAHIEWY LLEKSRIVHQ NSKERNYHIF YQLLSGLDDS 300
ELKNLRLKSR NVKDYKILSN SNQDIIPGIN DVENFKELLS ALNIIGFSKD QIRWIFQVVA 360
IILLIGNIEF VSDRAEQASF KNDVSAICSN LGVDEKDFQT AILRPRSKAG KEWVSQSKNS 420
QQAKFILNAL SRNLYERLFG YIVDMINKNL DHGSATLNYI GLLDIAGFEI FENNSFEQLC 480
INYTNEKLQQ FFNNHMFVLE QSEYLKENIQ WDYIDYGKDL QLTIDLIESK GPPTGVLPLL 540
DEEAVLPKST DESFYSKLIS TWDQNSSKFK RSRLKNGFIL KHYAGDVEYT VEGWLSKNKD 600
PLNDNLLSLL SSSQNDIISK LFQPEGEKSS SAGVEANISN QEVKKSARTS TFKTTSSRHR 660
EQQITLLNQL ASTHPHFVRC IIPNNVKKVK TFNRRLILDQ LRCNGVLEGI RLAREGYPNR 720
IAFQEFFQRY RILYPENSTT TTFSSKLKAS TKQNCEFLLT SLQLDTKVYK IGNTKLFFKA 780
GVLADLEKQK DVKLNNIMIK LTATIRGYTV RKEITYHLQK LKKTRVIGNT FRLYNRLVKE 840
DPWFNLFIRI KPLLTSSNDM TRTKKFNEQI NKLKNDLQEM ESKKKFLEEK NQKTVNELEN 900
TQDLLNQEKE NLRKNESLLN RVKTSSETLQ KQFDDLVSEK DEISREKLEV AQNLEEAHQK 960
IQGLQETIRE REATLEKLHS KNNELIKQIS DLNCDISKEQ SSQSLIKESK LKLENEIKRL 1020
KDVINSKEEE IKSFNDKLSS SEEDLDIKLV TLEKNCNIAM SRLQSLVTEN SDLRSKNENF 1080
KKEKAALNNQ LKNKESELLK MKEKIDNHKK ELATFSKQRD DAVSEHGKIT AELKETRIQL 1140
TEYKSNYQKI KEEYSNFQRE TKEQEQKKRN SLVESLNDSK IKELEARLSQ EISLNQYLNK 1200
RISGNSVETN ISSTRRSTSY SDDPLDKEDI IKKYYDLQLA FTEITRNLEN EIEEKKNLIS 1260
RLRFTETRLA SSSFEDQKIK AQMKKLKKLI QDMDPSIPLD SILNEPLDNC PDKESDINKL 1320
MLEVDYLKRQ LDIETRAHYD AENAISALHS KFRKIQGESS LSSSDIYKLK FEASEERVKS 1380
LEDKLKTMPL RDRTNLPVGD IIKNRDSISK YEEEIRYYKL ENYKLQEILN ESNGKLSQLT 1440
LDLRQSKSKE ALLSEQLDRL QKDLESTERQ KELLSSTIKQ QKQQFENCMD DLQGNELRLR 1500
EHIHALKQAE EDVKNMASII EKLKTQNKQK EKLIWEREME RNDSDMQLQE TLLELKRVQD 1560
VKKILSDDLA HLKERLSAVE DRSQYTDEIN RLKEELNCSL KAETNLKKEF ATLKYKLETS 1620
TNDSEAKISD LLKQLDHYTK VVEMLNNEKD AISLAEKELY QKYEALNTEC ESLKGKIVSL 1680
TKIKQELESD LNQKTDALQI SNAALSSSTQ KNKEITEKIK YLEETLQLQM EQNSRNGELV 1740
KTLQASCNGY KDKFDDEKQK NIDLYEENQT LQKLNTDLQL QLKNLHERLS DTTEKNAWLS 1800
KIHELENMVS LETDLKYEEM KKNKSLERAV EELQTKNSQQ TDVIELANKN RSEFEEATLK 1860
YEAQISDLEK YISQQELEMK KSIRDNSSYR DKVQEMAQEI EFWKSRYEST MIGSKNIDSN 1920
NAQSKIFS 1928 |
Gene Ontology | GO:0005935; C:cellular bud neck; IDA:SGD. GO:0000131; C:incipient cellular bud site; IDA:SGD. GO:0016460; C:myosin II complex; IPI:SGD. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0000146; F:microfilament motor activity; ISS:SGD. GO:0000916; P:actomyosin contractile ring contraction; IMP:SGD. GO:0000915; P:cytokinesis, actomyosin contractile ring assembly; IMP:SGD. GO:0007109; P:cytokinesis, completion of separation; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |