Search Results
Overview
| Uniprot ID | Q9UKX2 |
|---|---|
| Protein Name | Myosin-2 |
| Gene Name | MYH2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1762 | RNAEEKAKKAITDAA |
| 1885 | QAKVKSYKRQAEEAE |
| 1901 | QSNTNLAKFRKLQHE |
| 568 | GKSANFQKPKVVKGK |
| 871 | KIKDELAKSEAKRKE |
Function
Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction
Protein Sequence
10
MSSDSELAVF
20
GEAAPFLRKS
30
ERERIEAQNR
40
PFDAKTSVFV
50
AEPKESFVKG
60
TIQSREGGKV
70
TVKTEGGATL
80
TVKDDQVFPM
90
NPPKYDKIED
100
MAMMTHLHEP
110
AVLYNLKERY
120
AAWMIYTYSG
130
LFCVTVNPYK
140
WLPVYKPEVV
150
TAYRGKKRQE
160
APPHIFSISD
170
NAYQFMLTDR
180
ENQSILITGE
190
SGAGKTVNTK
200
RVIQYFATIA
210
VTGEKKKEEI
220
TSGKIQGTLE
230
DQIISANPLL
240
EAFGNAKTVR
250
NDNSSRFGKF
260
IRIHFGTTGK
270
LASADIETYL
280
LEKSRVVFQL
290
KAERSYHIFY
300
QITSNKKPEL
310
IEMLLITTNP
320
YDYPFVSQGE
330
ISVASIDDQE
340
ELMATDSAID
350
ILGFTNEEKV
360
SIYKLTGAVM
370
HYGNLKFKQK
380
QREEQAEPDG
390
TEVADKAAYL
400
QSLNSADLLK
410
ALCYPRVKVG
420
NEYVTKGQTV
430
EQVSNAVGAL
440
AKAVYEKMFL
450
WMVARINQQL
460
DTKQPRQYFI
470
GVLDIAGFEI
480
FDFNSLEQLC
490
INFTNEKLQQ
500
FFNHHMFVLE
510
QEEYKKEGIE
520
WTFIDFGMDL
530
AACIELIEKP
540
MGIFSILEEE
550
CMFPKATDTS
560
FKNKLYDQHL
570
GKSANFQKPK
580
VVKGKAEAHF
590
ALIHYAGVVD
600
YNITGWLEKN
610
KDPLNETVVG
620
LYQKSAMKTL
630
AQLFSGAQTA
640
EGEGAGGGAK
650
KGGKKKGSSF
660
QTVSALFREN
670
LNKLMTNLRS
680
THPHFVRCII
690
PNETKTPGAM
700
EHELVLHQLR
710
CNGVLEGIRI
720
CRKGFPSRIL
730
YADFKQRYKV
740
LNASAIPEGQ
750
FIDSKKASEK
760
LLASIDIDHT
770
QYKFGHTKVF
780
FKAGLLGLLE
790
EMRDDKLAQL
800
ITRTQARCRG
810
FLARVEYQRM
820
VERREAIFCI
830
QYNIRSFMNV
840
KHWPWMKLFF
850
KIKPLLKSAE
860
TEKEMATMKE
870
EFQKIKDELA
880
KSEAKRKELE
890
EKMVTLLKEK
900
NDLQLQVQAE
910
AEGLADAEER
920
CDQLIKTKIQ
930
LEAKIKEVTE
940
RAEDEEEINA
950
ELTAKKRKLE
960
DECSELKKDI
970
DDLELTLAKV
980
EKEKHATENK
990
VKNLTEEMAG
1000
LDETIAKLTK
1010
EKKALQEAHQ
1020
QTLDDLQAEE
1030
DKVNTLTKAK
1040
IKLEQQVDDL
1050
EGSLEQEKKL
1060
RMDLERAKRK
1070
LEGDLKLAQE
1080
SIMDIENEKQ
1090
QLDEKLKKKE
1100
FEISNLQSKI
1110
EDEQALGIQL
1120
QKKIKELQAR
1130
IEELEEEIEA
1140
ERASRAKAEK
1150
QRSDLSRELE
1160
EISERLEEAG
1170
GATSAQIEMN
1180
KKREAEFQKM
1190
RRDLEEATLQ
1200
HEATAATLRK
1210
KHADSVAELG
1220
EQIDNLQRVK
1230
QKLEKEKSEM
1240
KMEIDDLASN
1250
VETVSKAKGN
1260
LEKMCRTLED
1270
QLSELKSKEE
1280
EQQRLINDLT
1290
AQRGRLQTES
1300
GEFSRQLDEK
1310
EALVSQLSRG
1320
KQAFTQQIEE
1330
LKRQLEEEIK
1340
AKNALAHALQ
1350
SSRHDCDLLR
1360
EQYEEEQESK
1370
AELQRALSKA
1380
NTEVAQWRTK
1390
YETDAIQRTE
1400
ELEEAKKKLA
1410
QRLQAAEEHV
1420
EAVNAKCASL
1430
EKTKQRLQNE
1440
VEDLMLDVER
1450
TNAACAALDK
1460
KQRNFDKILA
1470
EWKQKCEETH
1480
AELEASQKEA
1490
RSLGTELFKI
1500
KNAYEESLDQ
1510
LETLKRENKN
1520
LQQEISDLTE
1530
QIAEGGKRIH
1540
ELEKIKKQVE
1550
QEKCELQAAL
1560
EEAEASLEHE
1570
EGKILRIQLE
1580
LNQVKSEVDR
1590
KIAEKDEEID
1600
QLKRNHIRIV
1610
ESMQSTLDAE
1620
IRSRNDAIRL
1630
KKKMEGDLNE
1640
MEIQLNHANR
1650
MAAEALRNYR
1660
NTQGILKDTQ
1670
IHLDDALRSQ
1680
EDLKEQLAMV
1690
ERRANLLQAE
1700
IEELRATLEQ
1710
TERSRKIAEQ
1720
ELLDASERVQ
1730
LLHTQNTSLI
1740
NTKKKLETDI
1750
SQMQGEMEDI
1760
LQEARNAEEK
1770
AKKAITDAAM
1780
MAEELKKEQD
1790
TSAHLERMKK
1800
NMEQTVKDLQ
1810
LRLDEAEQLA
1820
LKGGKKQIQK
1830
LEARVRELEG
1840
EVESEQKRNA
1850
EAVKGLRKHE
1860
RRVKELTYQT
1870
EEDRKNILRL
1880
QDLVDKLQAK
1890
VKSYKRQAEE
1900
AEEQSNTNLA
1910
KFRKLQHELE
1920
EAEERADIAE
1930
SQVNKLRVKS
1940
REVHTKVISE
E
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005911 | cell-cell junction |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005859 | muscle myosin complex |
| Cellular Component | GO:0030016 | myofibril |
| Cellular Component | GO:0032982 | myosin filament |
| Cellular Component | GO:0016460 | myosin II complex |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0030017 | sarcomere |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0005516 | calmodulin binding |
| Molecular Function | GO:0000146 | microfilament motor activity |
| Biological Process | GO:0006936 | muscle contraction |
| Biological Process | GO:0030049 | muscle filament sliding |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.