Search Results

Overview

Uniprot ID	O15027
Protein Name	Protein transport protein Sec16A
Gene Name	SEC16A
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
1313	AFGDRPEKRDNNWRY
2118	RWLPGKKKTEAYLPD

Function

Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17005010, PubMed:17192411, PubMed:17428803, PubMed:21768384, PubMed:22355596). Mediates the recruitment of MIA3/TANGO to ERES (PubMed:28442536). Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (PubMed:28067262). Positively regulates the protein stability of E3 ubiquitin-protein ligases RNF152 and RNF183 and the ER localization of RNF183 (PubMed:29300766). Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the cell membrane in adipocytes (By similarity)

Protein Sequence

10 MQPPPQTVPS 20 GMAGPPPAGN 30 PRSVFWASSP 40 YRRRANNNAA 50 VAPTTCPLQP 60 VTDPFAFSRQ 70 ALQSTPLGSS 80 SKSSPPVLQG 90 PAPAGFSQHP 100 GLLVPHTHAR 110 DSSQGPCEPL 120 PGPLTQPRAH 130 ASPFSGALTP 140 SAPPGPEMNR 150 SAEVGPSSEP 160 EVQTLPYLPH 170 YIPGVDPETS 180 HGGHPHGNMP 190 GLDRPLSRQN 200 PHDGVVTPAA 210 SPSLPQPGLQ 220 MPGQWGPVQG 230 GPQPSGQHRS 240 PCPEGPVPSG 250 VPCATSVPHF 260 PTPSILHQGP 270 GHEQHSPLVA 280 PPAALPSDGR 290 DEVSHLQSGS 300 HLANNSDPES 310 TFRQNPRIVN 320 HWASPELRQN 330 PGVKNEHRPA 340 SALVNPLARG 350 DSPENRTHHP 360 LGAGAGSGCA 370 PLEADSGASG 380 ALAMFFQGGE 390 TENEENLSSE 400 KAGLSGQADF 410 DDFCSSPGLG 420 RPPAPTHVGA 430 GSLCQALLPG 440 PSNEAAGDVW 450 GDTASTGVPD 460 ASGSQYENVE 470 NLEFVQNQEV 480 LPSEPLNLDP 490 SSPSDQFRYG 500 PLPGPAVPRH 510 GAVCHTGAPD 520 ATLHTVHPDS 530 VSSSYSSRSH 540 GRLSGSARPQ 550 ELVGTFIQQE 560 VGKPEDEASG 570 SFFKQIDSSP 580 VGGETDETTV 590 SQNYRGSVSQ 600 PSTPSPPKPT 610 GIFQTSANSS 620 FEPVKSHLVG 630 VKPFEADRAN 640 VVGEVRETCV 650 RQKQCRPAAA 660 LPDASPGNLE 670 QPPDNMETLC 680 APQVCPLPLN 690 STTEAVHMLP 700 HAGAPPLDTV 710 YPAPEKRPSA 720 RTQGPVKCES 730 PATTLWAQSE 740 LPDFGGNVLL 750 APAAPALYVC 760 AKPQPPVVQP 770 PEEAMSGQQS 780 RNPSSAAPVQ 790 SRGGIGASEN 800 LENPPKMGEE 810 EALQSQASSG 820 YASLLSSPPT 830 ESLQNPPVLI 840 AQPDHSYNLA 850 QPINFSVSLS 860 NSHEKNQSWR 870 EALVGDRPAV 880 SSWALGGDSG 890 ENTSLSGIPT 900 SSVLSLSLPS 910 SVAQSNFPQG 920 SGASEMVSNQ 930 PANLLVQPPS 940 QPVPENLVPE 950 SQKDRKAGSA 960 LPGFANSPAG 970 STSVVLVPPA 980 HGTLVPDGNK 990 ANHSSHQEDT 1000 YGALDFTLSR 1010 TLENPVNVYN 1020 PSHSDSLASQ 1030 QSVASHPRQS 1040 GPGAPNLDRF 1050 YQQVTKDAQG 1060 QPGLERAQQE 1070 LVPPQQQASP 1080 PQLPKAMFSE 1090 LSNPESLPAQ 1100 GQAQNSAQSP 1110 ASLVLVDAGQ 1120 QLPPRPPQSS 1130 SVSLVSSGSG 1140 QAAVPSEQPW 1150 PQPVPALAPG 1160 PPPQDLAAYY 1170 YYRPLYDAYQ 1180 PQYSLPYPPE 1190 PGAASLYYQD 1200 VYSLYEPRYR 1210 PYDGAASAYA 1220 QNYRYPEPER 1230 PSSRASHSSE 1240 RPPPRQGYPE 1250 GYYSSKSGWS 1260 SQSDYYASYY 1270 SSQYDYGDPG 1280 HWDRYHYSAR 1290 VRDPRTYDRR 1300 YWCDAEYDAY 1310 RREHSAFGDR 1320 PEKRDNNWRY 1330 DPRFTGSFDD 1340 DPDPHRDPYG 1350 EEVDRRSVHS 1360 EHSARSLHSA 1370 HSLASRRSSL 1380 SSHSHQSQIY 1390 RSHNVAAGSY 1400 EAPLPPGSFH 1410 GDFAYGTYRS 1420 NFSSGPGFPE 1430 YGYPADTVWP 1440 AMEQVSSRPT 1450 SPEKFSVPHV 1460 CARFGPGGQL 1470 IKVIPNLPSE 1480 GQPALVEVHS 1490 MEALLQHTSE 1500 QEEMRAFPGP 1510 LAKDDTHKVD 1520 VINFAQNKAM 1530 KCLQNENLID 1540 KESASLLWNF 1550 IVLLCRQNGT 1560 VVGTDIAELL 1570 LRDHRTVWLP 1580 GKSPNEANLI 1590 DFTNEAVEQV 1600 EEEESGEAQL 1610 SFLTGGPAAA 1620 ASSLERETER 1630 FRELLLYGRK 1640 KDALESAMKN 1650 GLWGHALLLA 1660 SKMDSRTHAR 1670 VMTRFANSLP 1680 INDPLQTVYQ 1690 LMSGRMPAAS 1700 TCCGDEKWGD 1710 WRPHLAMVLS 1720 NLNNNMDVES 1730 RTMATMGDTL 1740 ASRGLLDAAH 1750 FCYLMAQAGF 1760 GVYTKKTTKL 1770 VLIGSNHSLP 1780 FLKFATNEAI 1790 QRTEAYEYAQ 1800 SLGAETCPLP 1810 SFQVFKFIYS 1820 CRLAEMGLAT 1830 QAFHYCEAIA 1840 KSILTQPHLY 1850 SPVLISQLVQ 1860 MASQLRLFDP 1870 QLKEKPEEES 1880 LAAPTWLVHL 1890 QQVERQIKEG 1900 AGVWHQDGAL 1910 PQQCPGTPSS 1920 EMEQLDRPGL 1930 SQPGALGIAN 1940 PLLAVPAPSP 1950 EHSSPSVRLL 1960 PSAPQTLPDG 1970 PLASPARVPM 1980 FPVPLPPGPL 1990 EPGPGCVTPG 2000 PALGFLEPSG 2010 PGLPPGVPPL 2020 QERRHLLQEA 2030 RSPDPGIVPQ 2040 EAPVGNSLSE 2050 LSEENFDGKF 2060 ANLTPSRTVP 2070 DSEAPPGWDR 2080 ADSGPTQPPL 2090 SLSPAPETKR 2100 PGQAAKKETK 2110 EPKKGESWFF 2120 RWLPGKKKTE 2130 AYLPDDKNKS 2140 IVWDEKKNQW 2150 VNLNEPEEEK 2160 KAPPPPPTSM 2170 PKTVQAAPPA 2180 LPGPPGAPVN 2190 MYSRRAAGTR 2200 ARYVDVLNPS 2210 GTQRSEPALA 2220 PADFVAPLAP 2230 LPIPSNLFVP 2240 TPDAEEPQLP 2250 DGTGREGPAA 2260 ARGLANPEPA 2270 PEPKVLSSAA 2280 SLPGSELPSS 2290 RPEGSQGGEL 2300 SRCSSMSSLS 2310 REVSQHFNQA 2320 PGDLPAAGGP 2330 PSGAMPFYNP 2340 AQLAQACATS 2350 GSSRLGRIGQ RKHLVLN

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005783	endoplasmic reticulum
Cellular Component	GO:0070971	endoplasmic reticulum exit site
Cellular Component	GO:0005789	endoplasmic reticulum membrane
Cellular Component	GO:0012507	ER to Golgi transport vesicle membrane
Cellular Component	GO:0005794	Golgi apparatus
Cellular Component	GO:0000139	Golgi membrane
Cellular Component	GO:0031090	organelle membrane
Cellular Component	GO:0048471	perinuclear region of cytoplasm
Molecular Function	GO:0043495	protein-membrane adaptor activity
Biological Process	GO:0007029	endoplasmic reticulum organization
Biological Process	GO:0006888	endoplasmic reticulum to Golgi vesicle-mediated transport
Biological Process	GO:0006893	Golgi to plasma membrane transport
Biological Process	GO:0032527	protein exit from endoplasmic reticulum
Biological Process	GO:0070973	protein localization to endoplasmic reticulum exit site
Biological Process	GO:0072659	protein localization to plasma membrane
Biological Process	GO:0050821	protein stabilization
Biological Process	GO:0003400	regulation of COPII vesicle coating
Biological Process	GO:0034976	response to endoplasmic reticulum stress
Biological Process	GO:0021762	substantia nigra development

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] 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] 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.