Overview
| Uniprot ID | Q5T200 |
| Protein Name | Zinc finger CCCH domain-containing protein 13 |
| Gene Name | ZC3H13 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 102 |
DVDTEPQKRNTEESS |
| 1167 |
CHRTRVEKVETPHVT |
| 1239 |
SRDREKTKSLEITGE |
| 1388 |
SSQIESVKRCEAKLE |
| 1393 |
SVKRCEAKLEGEHER |
| 205 |
SPEVVRSKLSPSPSL |
| 236 |
SASKKDRKTSAVSSP |
| 47 |
TQCRNWLKTGNCLYG |
| 7 |
*MSKIRRKVTVENTK |
| 970 |
QKKPIKKKKEDDVGI |
Function
Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity)
Protein Sequence
10
MSKIRRKVTV
20
ENTKTISDST
30
SRRPSVFERL
40
GPSTGSTAET
50
QCRNWLKTGN
60
CLYGNTCRFV
70
HGPSPRGKGY
80
SSNYRRSPER
90
PTGDLRERMK
100
NKRQDVDTEP
110
QKRNTEESSS
120
PVRKESSRGR
130
HREKEDIKIT
140
KERTPESEEE
150
NVEWETNRDD
160
SDNGDINYDY
170
VHELSLEMKR
180
QKIQRELMKL
190
EQENMEKREE
200
IIIKKEVSPE
210
VVRSKLSPSP
220
SLRKSSKSPK
230
RKSSPKSSSA
240
SKKDRKTSAV
250
SSPLLDQQRN
260
SKTNQSKKKG
270
PRTPSPPPPI
280
PEDIALGKKY
290
KEKYKVKDRI
300
EEKTRDGKDR
310
GRDFERQREK
320
RDKPRSTSPA
330
GQHHSPISSR
340
HHSSSSQSGS
350
SIQRHSPSPR
360
RKRTPSPSYQ
370
RTLTPPLRRS
380
ASPYPSHSLS
390
SPQRKQSPPR
400
HRSPMREKGR
410
HDHERTSQSH
420
DRRHERREDT
430
RGKRDREKDS
440
REEREYEQDQ
450
SSSRDHRDDR
460
EPRDGRDRRD
470
ARDTRDRREL
480
RDSRDMRDSR
490
EMRDYSRDTK
500
ESRDPRDSRS
510
TRDAHDYRDR
520
EGRDTHRKED
530
TYPEESRSYG
540
RNHLREESSR
550
TEIRNESRNE
560
SRSEIRNDRM
570
GRSRGRVPEL
580
PEKGSRGSRG
590
SQIDSHSSNS
600
NYHDSWETRS
610
SYPERDRYPE
620
RDNRDQARDS
630
SFERRHGERD
640
RRDNRERDQR
650
PSSPIRHQGR
660
NDELERDERR
670
EERRVDRVDD
680
RRDERARERD
690
RERERDRERE
700
RERERERDRE
710
REKERELERE
720
RARERERERE
730
KERDRERDRD
740
RDHDRERERE
750
RERDREKERE
760
REREERERER
770
ERERERERER
780
ERERERARER
790
DKERERQRDW
800
EDKDKGRDDR
810
REKREEIRED
820
RNPRDGHDER
830
KSKKRYRNEG
840
SPSPRQSPKR
850
RREHSPDSDA
860
YNSGDDKNEK
870
HRLLSQVVRP
880
QESRSLSPSH
890
LTEDRQGRWK
900
EEDRKPERKE
910
SSRRYEEQEL
920
KEKVSSVDKQ
930
REQTEILESS
940
RMRAQDIIGH
950
HQSEDRETSD
960
RAHDENKKKA
970
KIQKKPIKKK
980
KEDDVGIERG
990
NIETTSEDGQ
1000
VFSPKKGQKK
1010
KSIEKKRKKS
1020
KGDSDISDEE
1030
AAQQSKKKRG
1040
PRTPPITTKE
1050
ELVEMCNGKN
1060
GILEDSQKKE
1070
DTAFSDWSDE
1080
DVPDRTEVTE
1090
AEHTATATTP
1100
GSTPSPLSSL
1110
LPPPPPVATA
1120
TATTVPATLA
1130
ATTAAAATSF
1140
STSAITISTS
1150
ATPTNTTNNT
1160
FANEDSHRKC
1170
HRTRVEKVET
1180
PHVTIEDAQH
1190
RKPMDQKRSS
1200
SLGSNRSNRS
1210
HTSGRLRSPS
1220
NDSAHRSGDD
1230
QSGRKRVLHS
1240
GSRDREKTKS
1250
LEITGERKSR
1260
IDQLKRGEPS
1270
RSTSSDRQDS
1280
RSHSSRRSSP
1290
ESDRQVHSRS
1300
GSFDSRDRLQ
1310
ERDRYEHDRE
1320
RERERRDTRQ
1330
REWDRDADKD
1340
WPRNRDRDRL
1350
RERERERERD
1360
KRRDLDRERE
1370
RLISDSVERD
1380
RDRDRDRTFE
1390
SSQIESVKRC
1400
EAKLEGEHER
1410
DLESTSRDSL
1420
ALDKERMDKD
1430
LGSVQGFEET
1440
NKSERTESLE
1450
GDDESKLDDA
1460
HSLGSGAGEG
1470
YEPISDDELD
1480
EILAGDAEKR
1490
EDQQDEEKMP
1500
DPLDVIDVDW
1510
SGLMPKHPKE
1520
PREPGAALLK
1530
FTPGAVMLRV
1540
GISKKLAGSE
1550
LFAKVKETCQ
1560
RLLEKPKDAD
1570
NLFEHELGAL
1580
NMAALLRKEE
1590
RASLLSNLGP
1600
CCKALCFRRD
1610
SAIRKQLVKN
1620
EKGTIKQAYT
1630
SAPMVDNELL
1640
RLSLRLFKRK
1650
TTCHAPGHEK
1660
TEDNKLSQSS
IQQELCVS
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0016607 |
nuclear speck |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0036396 |
RNA N6-methyladenosine methyltransferase complex |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0006397 |
mRNA processing |
| Biological Process |
GO:2000036 |
regulation of stem cell population maintenance |
| Biological Process |
GO:0008380 |
RNA splicing |
Reference
[1] 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.
[2] 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.