Overview
| Uniprot ID | P57678 |
| Protein Name | Gem-associated protein 4 |
| Gene Name | GEMIN4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 201 |
DEFPHPPKRLRSDPD |
Function
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP
Protein Sequence
10
MDLGPLNICE
20
EMTILHGGFL
30
LAEQLFHPKA
40
LAELTKSDWE
50
RVGRPIVEAL
60
REISSAAAHS
70
QPFAWKKKAL
80
IIIWAKVLQP
90
HPVTPSDTET
100
RWQEDLFFSV
110
GNMIPTINHT
120
ILFELLKSLE
130
ASGLFIQLLM
140
ALPTTICHAE
150
LERFLEHVTV
160
DTSAEDVAFF
170
LDVWWEVMKH
180
KGHPQDPLLS
190
QFSAMAHKYL
200
PALDEFPHPP
210
KRLRSDPDAC
220
PTMPLLAMLL
230
RGLTQIQSRI
240
LGPGRKCCAL
250
ANLADMLTVF
260
ALTEDDPQEV
270
SATVYLDKLA
280
TVISVWNSDT
290
QNPYHQQALA
300
EKVKEAERDV
310
SLTSLAKLPS
320
ETIFVGCEFL
330
HHLLREWGEE
340
LQAVLRSSQG
350
TSYDSYRLCD
360
SLTSFSQNAT
370
LYLNRTSLSK
380
EDRQVVSELA
390
ECVRDFLRKT
400
STVLKNRALE
410
DITASIAMAV
420
IQQKMDRHME
430
VCYIFASEKK
440
WAFSDEWVAC
450
LGSNRALFRQ
460
PDLVLRLLET
470
VIDVSTADRA
480
IPESQIRQVI
490
HLILECYADL
500
SLPGKNKVLA
510
GILRSWGRKG
520
LSEKLLAYVE
530
GFQEDLNTTF
540
NQLTQSASEQ
550
GLAKAVASVA
560
RLVIVHPEVT
570
VKKMCSLAVV
580
NLGTHKFLAQ
590
ILTAFPALRF
600
VEEQGPNSSA
610
TFMVSCLKET
620
VWMKFSTPKE
630
EKQFLELLNC
640
LMSPVKPQGI
650
PVAALLEPDE
660
VLKEFVLPFL
670
RLDVEEVDLS
680
LRIFIQTLEA
690
NACREEYWLQ
700
TCSPFPLLFS
710
LCQLLDRFSK
720
YWQLPKEKRC
730
LSLDRKDLAI
740
HILELLCEIV
750
SANAETFSPD
760
VWIKSLSWLH
770
RKLEQLDWTV
780
GLRLKSFFEG
790
HFKCEVPATL
800
FEICKLSEDE
810
WTSQAHPGYG
820
AGTGLLAWME
830
CCCVSSGISE
840
RMLSLLVVDV
850
GNPEEVRLFS
860
KGFLVALVQV
870
MPWCSPQEWQ
880
RLHQLTRRLL
890
EKQLLHVPYS
900
LEYIQFVPLL
910
NLKPFAQELQ
920
LSVLFLRTFQ
930
FLCSHSCRDW
940
LPLEGWNHVV
950
KLLCGSLTRL
960
LDSVRAIQAA
970
GPWVQGPEQD
980
LTQEALFVYT
990
QVFCHALHIM
1000
AMLHPEVCEP
1010
LYVLALETLT
1020
CYETLSKTNP
1030
SVSSLLQRAH
1040
EQRFLKSIAE
1050
GIGPEERRQT
LLQKMSSF
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0015030 |
Cajal body |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0070062 |
extracellular exosome |
| Cellular Component |
GO:0097504 |
Gemini of Cajal bodies |
| Cellular Component |
GO:0016020 |
membrane |
| Cellular Component |
GO:0016604 |
nuclear body |
| Cellular Component |
GO:0005730 |
nucleolus |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0030532 |
small nuclear ribonucleoprotein complex |
| Cellular Component |
GO:0032797 |
SMN complex |
| Cellular Component |
GO:0034719 |
SMN-Sm protein complex |
| Molecular Function |
GO:0043021 |
ribonucleoprotein complex binding |
| Biological Process |
GO:0006364 |
rRNA processing |
| Biological Process |
GO:0000387 |
spliceosomal snRNP assembly |
Reference
[1] 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.