Search Results

Overview

Uniprot IDQ92797
Protein NameSymplekin
Gene NameSYMPK
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1147 GLRLAQEKALKRQLE
343 ARNMPSSKDTRKRPR
361 DSTLKKMKLEPNLGE
483 PKEEKVVKTESVLIK
490 KTESVLIKRRLSAQG

Function

Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity

Protein Sequence

10 MASGSGDSVT 20 RRSVASQFFT 30 QEEGPGIDGM 40 TTSERVVDLL 50 NQAALITNDS 60 KITVLKQVQE 70 LIINKDPTLL 80 DNFLDEIIAF 90 QADKSIEVRK 100 FVIGFIEEAC 110 KRDIELLLKL 120 IANLNMLLRD 130 ENVNVVKKAI 140 LTMTQLYKVA 150 LQWMVKSRVI 160 SELQEACWDM 170 VSAMAGDIIL 180 LLDSDNDGIR 190 THAIKFVEGL 200 IVTLSPRMAD 210 SEIPRRQEHD 220 ISLDRIPRDH 230 PYIQYNVLWE 240 EGKAALEQLL 250 KFMVHPAISS 260 INLTTALGSL 270 ANIARQRPMF 280 MSEVIQAYET 290 LHANLPPTLA 300 KSQVSSVRKN 310 LKLHLLSVLK 320 HPASLEFQAQ 330 ITTLLVDLGT 340 PQAEIARNMP 350 SSKDTRKRPR 360 DDSDSTLKKM 370 KLEPNLGEDD 380 EDKDLEPGPS 390 GTSKASAQIS 400 GQSDTDITAE 410 FLQPLLTPDN 420 VANLVLISMV 430 YLPEAMPASF 440 QAIYTPVESA 450 GTEAQIKHLA 460 RLMATQMTAA 470 GLGPGVEQTK 480 QCKEEPKEEK 490 VVKTESVLIK 500 RRLSAQGQAI 510 SVVGSLSSMS 520 PLEEEAPQAK 530 RRPEPIIPVT 540 QPRLAGAGGR 550 KKIFRLSDVL 560 KPLTDAQVEA 570 MKLGAVKRIL 580 RAEKAVACSG 590 AAQVRIKILA 600 SLVTQFNSGL 610 KAEVLSFILE 620 DVRARLDLAF 630 AWLYQEYNAY 640 LAAGASGSLD 650 KYEDCLIRLL 660 SGLQEKPDQK 670 DGIFTKVVLE 680 APLITESALE 690 VVRKYCEDES 700 RTYLGMSTLR 710 DLIFKRPSRQ 720 FQYLHVLLDL 730 SSHEKDKVRS 740 QALLFIKRMY 750 EKEQLREYVE 760 KFALNYLQLL 770 VHPNPPSVLF 780 GADKDTEVAA 790 PWTEETVKQC 800 LYLYLALLPQ 810 NHKLIHELAA 820 VYTEAIADIK 830 RTVLRVIEQP 840 IRGMGMNSPE 850 LLLLVENCPK 860 GAETLVTRCL 870 HSLTDKVPPS 880 PELVKRVRDL 890 YHKRLPDVRF 900 LIPVLNGLEK 910 KEVIQALPKL 920 IKLNPIVVKE 930 VFNRLLGTQH 940 GEGNSALSPL 950 NPGELLIALH 960 NIDSVKCDMK 970 SIIKATNLCF 980 AERNVYTSEV 990 LAVVMQQLME 1000 QSPLPMLLMR 1010 TVIQSLTMYP 1020 RLGGFVMNIL 1030 SRLIMKQVWK 1040 YPKVWEGFIK 1050 CCQRTKPQSF 1060 QVILQLPPQQ 1070 LGAVFDKCPE 1080 LREPLLAHVR 1090 SFTPHQQAHI 1100 PNSIMTILEA 1110 SGKQEPEAKE 1120 APAGPLEEDD 1130 LEPLTLAPAP 1140 APRPPQDLIG 1150 LRLAQEKALK 1160 RQLEEEQKLK 1170 PGGVGAPSSS 1180 SPSPSPSARP 1190 GPPPSEEAMD 1200 FREEGPECET 1210 PGIFISMDDD 1220 SGLTEAALLD 1230 SSLEGPLPKE 1240 TAAGGLTLKE 1250 ERSPQTLAPV 1260 GEDAMKTPSP 1270 AAEDAREPEA KGNS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005923 bicellular tight junction
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005847 mRNA cleavage and polyadenylation specificity factor complex
Cellular Component GO:0097165 nuclear stress granule
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Biological Process GO:0007155 cell adhesion
Biological Process GO:0031124 mRNA 3'-end processing
Biological Process GO:0032091 negative regulation of protein binding
Biological Process GO:0071045 nuclear histone mRNA catabolic process

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] 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.

[5] 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.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] 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.