Overview
| Uniprot ID | Q14202 |
| Protein Name | Zinc finger MYM-type protein 3 |
| Gene Name | ZMYM3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 1086 |
YANGETSKGDELRFG |
| 308 |
GRSAVGTKMTCAHCR |
| 320 |
HCRTPLQKGQTAYQR |
| 439 |
CSDSCFSKFRANKGL |
| 447 |
FRANKGLKTNCCDQC |
| 804 |
EENGNLGKIPVKTRS |
| 808 |
NLGKIPVKTRSAPTA |
Function
Required for regulation of cell morphology and cytoskeletal organization
Protein Sequence
10
MDPSDFPSPF
20
DPLTLPEKPL
30
AGDLPVDMEF
40
GEDLLESQTA
50
PTRGWAPPGP
60
SPSSGALDLL
70
DTPAGLEKDP
80
GVLDGATELL
90
GLGGLLYKAP
100
SPPEVDHGPE
110
GTLAWDAGDQ
120
TLEPGPGGQT
130
PEVVPPDPGA
140
GANSCSPEGL
150
LEPLAPDSPI
160
TLQSPHIEEE
170
ETTSIATARR
180
GSPGQEEELP
190
QGQPQSPNAP
200
PSPSVGETLG
210
DGINSSQTKP
220
GGSSPPAHPS
230
LPGDGLTAKA
240
SEKPPERKRS
250
ERVRRAEPPK
260
PEVVDSTESI
270
PVSDEDSDAM
280
VDDPNDEDFV
290
PFRPRRSPRM
300
SLRSSVSQRA
310
GRSAVGTKMT
320
CAHCRTPLQK
330
GQTAYQRKGL
340
PQLFCSSSCL
350
TTFSKKPSGK
360
KTCTFCKKEI
370
WNTKDSVVAQ
380
TGSGGSFHEF
390
CTSVCLSLYE
400
AQQQRPIPQS
410
GDPADATRCS
420
ICQKTGEVLH
430
EVSNGSVVHR
440
LCSDSCFSKF
450
RANKGLKTNC
460
CDQCGAYIYT
470
KTGSPGPELL
480
FHEGQQKRFC
490
NTTCLGAYKK
500
KNTRVYPCVW
510
CKTLCKNFEM
520
LSHVDRNGKT
530
SLFCSLCCTT
540
SYKVKQAGLT
550
GPPRPCSFCR
560
RSLSDPCYYN
570
KVDRTVYQFC
580
SPSCWTKFQR
590
TSPEGGIHLS
600
CHYCHSLFSG
610
KPEVLDWQDQ
620
VFQFCCRDCC
630
EDFKRLRGVV
640
SQCEHCRQEK
650
LLHEKLRFSG
660
VEKSFCSEGC
670
VLLYKQDFTK
680
KLGLCCITCT
690
YCSQTCQRGV
700
TEQLDGSTWD
710
FCSEDCKSKY
720
LLWYCKAARC
730
HACKRQGKLL
740
ETIHWRGQIR
750
HFCNQQCLLR
760
FYSQQNQPNL
770
DTQSGPESLL
780
NSQSPESKPQ
790
TPSQTKVENS
800
NTVRTPEENG
810
NLGKIPVKTR
820
SAPTAPTPPP
830
PPPPATPRKN
840
KAAMCKPLMQ
850
NRGVSCKVEM
860
KSKGSQTEEW
870
KPQVIVLPIP
880
VPIFVPVPMH
890
LYCQKVPVPF
900
SMPIPVPVPM
910
FLPTTLESTD
920
KIVETIEELK
930
VKIPSNPLEA
940
DILAMAEMIA
950
EAEELDKASS
960
DLCDLVSNQS
970
AEGLLEDCDL
980
FGPARDDVLA
990
MAVKMANVLD
1000
EPGQDLEADF
1010
PKNPLDINPS
1020
VDFLFDCGLV
1030
GPEDVSTEQD
1040
LPRTMRKGQK
1050
RLVLSESCSR
1060
DSMSSQPSCT
1070
GLNYSYGVNA
1080
WKCWVQSKYA
1090
NGETSKGDEL
1100
RFGPKPMRIK
1110
EDILACSAAE
1120
LNYGLAQFVR
1130
EITRPNGERY
1140
EPDSIYYLCL
1150
GIQQYLLENN
1160
RMVNIFTDLY
1170
YLTFVQELNK
1180
SLSTWQPTLL
1190
PNNTVFSRVE
1200
EEHLWECKQL
1210
GVYSPFVLLN
1220
TLMFFNTKFF
1230
GLQTAEEHMQ
1240
LSFTNVVRQS
1250
RKCTTPRGTT
1260
KVVSIRYYAP
1270
VRQRKGRDTG
1280
PGKRKREDEA
1290
PILEQRENRM
1300
NPLRCPVKFY
1310
EFYLSKCPES
1320
LRTRNDVFYL
1330
QPERSCIAES
1340
PLWYSVIPMD
1350
RSMLESMLNR
1360
ILAVREIYEE
1370
LGRPGEEDLD
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0008270 |
zinc ion binding |
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] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.