ID SEC13_HUMAN Reviewed; 322 AA. AC P55735; A8MV37; B4DXJ1; Q5BJF0; Q9BRM6; Q9BUG7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 217. DE RecName: Full=Protein SEC13 homolog {ECO:0000305}; DE AltName: Full=GATOR2 complex protein SEC13 {ECO:0000305}; DE AltName: Full=SEC13-like protein 1; DE AltName: Full=SEC13-related protein; GN Name=SEC13 {ECO:0000303|PubMed:35831510, ECO:0000303|PubMed:36528027, GN ECO:0000312|HGNC:HGNC:10697}; GN Synonyms=D3S1231E, SEC13A {ECO:0000303|PubMed:25201882}, SEC13L1, GN SEC13R; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=7987303; DOI=10.1093/hmg/3.8.1281; RA Swaroop A., Yang-Feng T.L., Liu W., Gieser L., Barrow L.L., Chen K.C., RA Agarwal N., Meisler M.H., Smith D.I.; RT "Molecular characterization of a novel human gene, SEC13R, related to the RT yeast secretory pathway gene SEC13, and mapping to a conserved linkage RT group on human chromosome 3p24-p25 and mouse chromosome 6."; RL Hum. Mol. Genet. 3:1281-1286(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=9110174; DOI=10.1101/gr.7.4.353; RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.; RT "Large-scale concatenation cDNA sequencing."; RL Genome Res. 7:353-358(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Placenta, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 2-27. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP PROTEIN SEQUENCE OF 2-27; 44-54; 217-256 AND 291-322, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT VAL-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 182-192; 217-239 AND 291-322, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8972206; DOI=10.1128/mcb.17.1.256; RA Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.; RT "The mammalian homolog of yeast Sec13p is enriched in the intermediate RT compartment and is essential for protein transport from the endoplasmic RT reticulum to the Golgi apparatus."; RL Mol. Cell. Biol. 17:256-266(1997). RN [10] RP SUBCELLULAR LOCATION, AND INTERACTION WITH NUP96. RX PubMed=14517296; DOI=10.1128/mcb.23.20.7271-7284.2003; RA Enninga J., Levay A., Fontoura B.M.; RT "Sec13 shuttles between the nucleus and the cytoplasm and stably interacts RT with Nup96 at the nuclear pore complex."; RL Mol. Cell. Biol. 23:7271-7284(2003). RN [11] RP INTERACTION WITH SEC31B. RX PubMed=16495487; DOI=10.1242/jcs.02751; RA Stankewich M.C., Stabach P.R., Morrow J.S.; RT "Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that RT associate with the COPII coat."; RL J. Cell Sci. 119:958-969(2006). RN [12] RP INTERACTION WITH SEC31A. RX PubMed=16957052; DOI=10.1091/mbc.e06-05-0444; RA Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.; RT "The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit RT sites by Sec31A and stabilizes the localization of Sec31A."; RL Mol. Biol. Cell 17:4876-4887(2006). RN [13] RP INTERACTION WITH SEC16A. RX PubMed=17428803; DOI=10.1074/jbc.m611237200; RA Iinuma T., Shiga A., Nakamoto K., O'Brien M.B., Aridor M., Arimitsu N., RA Tagaya M., Tani K.; RT "Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic RT reticulum."; RL J. Biol. Chem. 282:17632-17639(2007). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP INTERACTION WITH SEC16A. RX PubMed=19638414; DOI=10.1242/jcs.044032; RA Hughes H., Budnik A., Schmidt K., Palmer K.J., Mantell J., Noakes C., RA Johnson A., Carter D.A., Verkade P., Watson P., Stephens D.J.; RT "Organisation of human ER-exit sites: requirements for the localisation of RT Sec16 to transitional ER."; RL J. Cell Sci. 122:2924-2934(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP INTERACTION WITH SEC16B. RX PubMed=22355596; DOI=10.1038/srep00077; RA Budnik A., Heesom K.J., Stephens D.J.; RT "Characterization of human Sec16B: indications of specialized, non- RT redundant functions."; RL Sci. Rep. 1:77-77(2011). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP INTERACTION WITH SESN1; SESN2 AND SESN3. RX PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014; RA Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M., RA Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.; RT "The Sestrins interact with GATOR2 to negatively regulate the amino-acid- RT sensing pathway upstream of mTORC1."; RL Cell Rep. 9:1-8(2014). RN [22] RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SESN2. RX PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019; RA Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C., Akopiants K., RA Guan K.L., Karin M., Budanov A.V.; RT "Sestrins inhibit mTORC1 kinase activation through the GATOR complex."; RL Cell Rep. 9:1281-1291(2014). RN [23] RP FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND INTERACTION WITH RRAG RP PROTEINS. RX PubMed=23723238; DOI=10.1126/science.1232044; RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A., RA Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.; RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that RT signal amino acid sufficiency to mTORC1."; RL Science 340:1100-1106(2013). RN [24] RP INTERACTION WITH SEC16A. RX PubMed=25201882; DOI=10.15252/embj.201487807; RA Cho H.J., Yu J., Xie C., Rudrabhatla P., Chen X., Wu J., Parisiadou L., RA Liu G., Sun L., Ma B., Ding J., Liu Z., Cai H.; RT "Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow RT ER-Golgi export."; RL EMBO J. 33:2314-2331(2014). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [26] RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH CASTOR2 AND CASTOR1. RX PubMed=26972053; DOI=10.1016/j.cell.2016.02.035; RA Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K., Wyant G.A., RA Wang T., Harper J.W., Gygi S.P., Sabatini D.M.; RT "The CASTOR proteins are arginine sensors for the mTORC1 pathway."; RL Cell 165:153-164(2016). RN [27] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=27487210; DOI=10.1038/nature19079; RA Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U., RA Sabatini D.M.; RT "Mechanism of arginine sensing by CASTOR1 upstream of mTORC1."; RL Nature 536:229-233(2016). RN [28] RP SUBCELLULAR LOCATION. RX PubMed=28199306; DOI=10.1038/nature21423; RA Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M., Shen K., RA Condon K.J., Petri S., Kedir J., Scaria S.M., Abu-Remaileh M., RA Frankel W.N., Sabatini D.M.; RT "KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to RT regulate mTORC1."; RL Nature 543:438-442(2017). RN [29] RP FUNCTION, AND IDENTIFICATION IN GATOR2 COMPLEX. RX PubMed=36528027; DOI=10.1016/j.molcel.2022.11.021; RA Jiang C., Dai X., He S., Zhou H., Fang L., Guo J., Liu S., Zhang T., RA Pan W., Yu H., Fu T., Li D., Inuzuka H., Wang P., Xiao J., Wei W.; RT "Ring domains are essential for GATOR2-dependent mTORC1 activation."; RL Mol. Cell 83:74-89(2023). RN [30] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-316 IN COMPLEX WITH YEAST RP NUP145C, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=18160040; DOI=10.1016/j.cell.2007.11.038; RA Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.; RT "Architecture of a coat for the nuclear pore membrane."; RL Cell 131:1313-1326(2007). RN [31] {ECO:0007744|PDB:7UHY} RP STRUCTURE BY ELECTRON MICROSCOPY (3.66 ANGSTROMS) IN COMPLEX WITH WDR24; RP WDR59; MIOS AND SEH1L, FUNCTION, AND IDENTIFICATION IN GATOR2 COMPLEX. RX PubMed=35831510; DOI=10.1038/s41586-022-04939-z; RA Valenstein M.L., Rogala K.B., Lalgudi P.V., Brignole E.J., Gu X., RA Saxton R.A., Chantranupong L., Kolibius J., Quast J.P., Sabatini D.M.; RT "Structure of the nutrient-sensing hub GATOR2."; RL Nature 607:610-616(2022). CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC) CC and the COPII coat (PubMed:8972206). At the endoplasmic reticulum, CC SEC13 is involved in the biogenesis of COPII-coated vesicles CC (PubMed:8972206). Required for the exit of adipsin (CFD/ADN), an CC adipocyte-secreted protein from the endoplasmic reticulum (By CC similarity). {ECO:0000250|UniProtKB:Q9D1M0, CC ECO:0000269|PubMed:8972206}. CC -!- FUNCTION: As a component of the GATOR2 complex, functions as an CC activator of the amino acid-sensing branch of the mTORC1 signaling CC pathway (PubMed:25457612, PubMed:23723238, PubMed:27487210, CC PubMed:36528027, PubMed:35831510). The GATOR2 complex indirectly CC activates mTORC1 through the inhibition of the GATOR1 subcomplex CC (PubMed:23723238, PubMed:27487210, PubMed:36528027, PubMed:35831510). CC GATOR2 probably acts as an E3 ubiquitin-protein ligase toward GATOR1 CC (PubMed:36528027). In the presence of abundant amino acids, the GATOR2 CC complex mediates ubiquitination of the NPRL2 core component of the CC GATOR1 complex, leading to GATOR1 inactivation (PubMed:36528027). In CC the absence of amino acids, GATOR2 is inhibited, activating the GATOR1 CC complex (PubMed:25457612, PubMed:26972053, PubMed:27487210). Within the CC GATOR2 complex, SEC13 and SEH1L are required to stabilize the complex CC (PubMed:35831510). {ECO:0000269|PubMed:23723238, CC ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:26972053, CC ECO:0000269|PubMed:27487210, ECO:0000269|PubMed:35831510, CC ECO:0000269|PubMed:36528027}. CC -!- ACTIVITY REGULATION: The GATOR2 complex is negatively regulated by the CC upstream amino acid sensors CASTOR1 and SESN2, which sequester the CC GATOR2 complex in absence of amino acids (PubMed:26972053, CC PubMed:25457612, PubMed:27487210). In the presence of abundant amino CC acids, GATOR2 is released from CASTOR1 and SESN2 and activated CC (PubMed:26972053, PubMed:25457612, PubMed:27487210). CC {ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:26972053, CC ECO:0000269|PubMed:27487210}. CC -!- SUBUNIT: At the nuclear pore: component of the Y-shaped Nup107-160 CC subcomplex of the nuclear pore complex (NPC) (PubMed:14517296, CC PubMed:18160040, PubMed:36528027, PubMed:35831510). The Nup107-160 CC subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, CC SEH1 and SEC13 (PubMed:18160040). At the COPII coat complex: interacts CC with SEC31A and SEC31B (PubMed:16495487, PubMed:16957052). Interacts CC with SEC16A (PubMed:17428803, PubMed:19638414, PubMed:25201882). CC Interacts with SEC16B (PubMed:22355596). Component of the GATOR2 CC subcomplex, composed of MIOS, SEC13, SEH1L, WDR24 and WDR59 CC (PubMed:23723238). The GATOR2 complex interacts with CASTOR1 and CC CASTOR2; the interaction is negatively regulated by arginine CC (PubMed:26972053). The GATOR2 complex interacts with SESN1, SESN2 and CC SESN3; the interaction is negatively regulated by amino acids CC (PubMed:25263562, PubMed:25457612). {ECO:0000269|PubMed:14517296, CC ECO:0000269|PubMed:16495487, ECO:0000269|PubMed:16957052, CC ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:18160040, CC ECO:0000269|PubMed:19638414, ECO:0000269|PubMed:22355596, CC ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25201882, CC ECO:0000269|PubMed:25263562, ECO:0000269|PubMed:25457612, CC ECO:0000269|PubMed:26972053, ECO:0000269|PubMed:35831510, CC ECO:0000269|PubMed:36528027}. CC -!- INTERACTION: CC P55735; Q8NFH4: NUP37; NbExp=3; IntAct=EBI-1046596, EBI-2563158; CC P55735; P55735: SEC13; NbExp=3; IntAct=EBI-1046596, EBI-1046596; CC P55735; Q96JE7-2: SEC16B; NbExp=6; IntAct=EBI-1046596, EBI-10215083; CC P55735; Q96EE3: SEH1L; NbExp=3; IntAct=EBI-1046596, EBI-922818; CC P55735; O00463: TRAF5; NbExp=3; IntAct=EBI-1046596, EBI-523498; CC P55735; P49687: NUP145; Xeno; NbExp=15; IntAct=EBI-1046596, EBI-11730; CC P55735-1; O94979-1: SEC31A; NbExp=9; IntAct=EBI-10045850, EBI-15564399; CC P55735-3; Q8IZF2: ADGRF5; NbExp=3; IntAct=EBI-12235008, EBI-7600130; CC P55735-3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12235008, EBI-742054; CC P55735-3; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-12235008, EBI-11956675; CC P55735-3; P42858: HTT; NbExp=15; IntAct=EBI-12235008, EBI-466029; CC P55735-3; E9PK14: SEC16B; NbExp=6; IntAct=EBI-12235008, EBI-12372595; CC P55735-3; O00463: TRAF5; NbExp=3; IntAct=EBI-12235008, EBI-523498; CC P55735-3; B4DHB6; NbExp=3; IntAct=EBI-12235008, EBI-14692289; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle CC membrane {ECO:0000269|PubMed:8972206}; Peripheral membrane protein CC {ECO:0000269|PubMed:8972206}; Cytoplasmic side CC {ECO:0000269|PubMed:8972206}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:8972206}; Peripheral membrane protein CC {ECO:0000269|PubMed:8972206}; Cytoplasmic side CC {ECO:0000269|PubMed:8972206}. Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:14517296, ECO:0000269|PubMed:18160040}. Lysosome CC membrane {ECO:0000269|PubMed:28199306}. Note=In interphase, localizes CC at both sides of the NPC. {ECO:0000269|PubMed:14517296}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P55735-1; Sequence=Displayed; CC Name=2; CC IsoId=P55735-2; Sequence=VSP_046191; CC Name=3; CC IsoId=P55735-3; Sequence=VSP_054695; CC Name=4; CC IsoId=P55735-4; Sequence=VSP_058966; CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}. CC -!- CAUTION: The E3 ubiquitin-protein ligase activity of the GATOR2 complex CC is subject to discussion (PubMed:35831510, PubMed:36528027). According CC to a report, the GATOR2 complex does not catalyze ubiquitination of the CC GATOR1 complex (PubMed:35831510). In contrast, another publication CC showed that the GATOR2 complex mediates ubiquitination of the NPRL2 CC core component of the GATOR1 complex, leading to GATOR1 inactivation CC (PubMed:36528027). {ECO:0000269|PubMed:35831510, CC ECO:0000269|PubMed:36528027}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L09260; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF052155; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK301999; BAG63403.1; -; mRNA. DR EMBL; AC022384; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002634; AAH02634.2; -; mRNA. DR EMBL; BC006167; AAH06167.1; -; mRNA. DR EMBL; BC091506; AAH91506.1; -; mRNA. DR CCDS; CCDS2599.1; -. [P55735-1] DR CCDS; CCDS46751.1; -. [P55735-2] DR CCDS; CCDS63540.1; -. [P55735-3] DR RefSeq; NP_001129498.1; NM_001136026.2. [P55735-3] DR RefSeq; NP_001129704.1; NM_001136232.2. [P55735-2] DR RefSeq; NP_109598.2; NM_030673.3. [P55735-4] DR RefSeq; NP_899195.1; NM_183352.2. [P55735-1] DR RefSeq; XP_005265436.1; XM_005265379.2. DR RefSeq; XP_016862508.1; XM_017007019.1. DR PDB; 3BG0; X-ray; 3.15 A; A/D/E/H=1-316. DR PDB; 3BG1; X-ray; 3.00 A; A/D/E/H=1-316. DR PDB; 5A9Q; EM; 23.00 A; 6/F/O/X=1-322. DR PDB; 7PEQ; EM; 35.00 A; AF/BF/CF/DF=1-322. DR PDB; 7R5J; EM; 50.00 A; N0/N1/N2/N3=1-322. DR PDB; 7R5K; EM; 12.00 A; N0/N1/N2/N3=1-322. DR PDB; 7UHY; EM; 3.66 A; H=1-322. DR PDBsum; 3BG0; -. DR PDBsum; 3BG1; -. DR PDBsum; 5A9Q; -. DR PDBsum; 7PEQ; -. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR PDBsum; 7UHY; -. DR AlphaFoldDB; P55735; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR EMDB; EMD-26519; -. DR SMR; P55735; -. DR BioGRID; 112296; 194. DR ComplexPortal; CPX-2360; COPII vesicle coat complex. DR ComplexPortal; CPX-6227; GATOR2 complex. DR ComplexPortal; CPX-873; Nuclear pore complex. DR CORUM; P55735; -. DR DIP; DIP-39091N; -. DR IntAct; P55735; 105. DR MINT; P55735; -. DR STRING; 9606.ENSP00000373312; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; P55735; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P55735; -. DR PhosphoSitePlus; P55735; -. DR SwissPalm; P55735; -. DR BioMuta; SEC13; -. DR DMDM; 50403748; -. DR EPD; P55735; -. DR jPOST; P55735; -. DR MassIVE; P55735; -. DR MaxQB; P55735; -. DR PaxDb; 9606-ENSP00000373312; -. DR PeptideAtlas; P55735; -. DR ProteomicsDB; 2150; -. DR ProteomicsDB; 56858; -. [P55735-1] DR Pumba; P55735; -. DR Antibodypedia; 25962; 275 antibodies from 34 providers. DR DNASU; 6396; -. DR Ensembl; ENST00000337354.8; ENSP00000336566.4; ENSG00000157020.18. [P55735-4] DR Ensembl; ENST00000350697.8; ENSP00000312122.4; ENSG00000157020.18. [P55735-1] DR Ensembl; ENST00000383801.6; ENSP00000373312.2; ENSG00000157020.18. [P55735-3] DR Ensembl; ENST00000397109.7; ENSP00000380298.3; ENSG00000157020.18. [P55735-2] DR GeneID; 6396; -. DR KEGG; hsa:6396; -. DR MANE-Select; ENST00000350697.8; ENSP00000312122.4; NM_183352.3; NP_899195.1. DR UCSC; uc003bvm.5; human. [P55735-1] DR AGR; HGNC:10697; -. DR CTD; 6396; -. DR DisGeNET; 6396; -. DR GeneCards; SEC13; -. DR HGNC; HGNC:10697; SEC13. DR HPA; ENSG00000157020; Low tissue specificity. DR MIM; 600152; gene. DR neXtProt; NX_P55735; -. DR OpenTargets; ENSG00000157020; -. DR PharmGKB; PA35620; -. DR VEuPathDB; HostDB:ENSG00000157020; -. DR eggNOG; KOG1332; Eukaryota. DR GeneTree; ENSGT00940000153393; -. DR HOGENOM; CLU_032441_0_1_1; -. DR InParanoid; P55735; -. DR OrthoDB; 177928at2759; -. DR PhylomeDB; P55735; -. DR TreeFam; TF300815; -. DR PathwayCommons; P55735; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA. DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA. DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript. DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript. DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA. DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus. DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways. DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis. DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery. DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein. DR Reactome; R-HSA-180746; Nuclear import of Rev protein. DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs. DR Reactome; R-HSA-191859; snRNP Assembly. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins. DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly. DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins. DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC). DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-6784531; tRNA processing in the nucleus. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9610379; HCMV Late Events. DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation. DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SignaLink; P55735; -. DR SIGNOR; P55735; -. DR BioGRID-ORCS; 6396; 804 hits in 1139 CRISPR screens. DR ChiTaRS; SEC13; human. DR EvolutionaryTrace; P55735; -. DR GeneWiki; SEC13; -. DR GenomeRNAi; 6396; -. DR Pharos; P55735; Tbio. DR PRO; PR:P55735; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P55735; Protein. DR Bgee; ENSG00000157020; Expressed in stromal cell of endometrium and 213 other cell types or tissues. DR ExpressionAtlas; P55735; baseline and differential. DR GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0061700; C:GATOR2 complex; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005643; C:nuclear pore; NAS:ComplexPortal. DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central. DR GO; GO:0031669; P:cellular response to nutrient levels; IDA:UniProtKB. DR GO; GO:0090114; P:COPII-coated vesicle budding; IBA:GO_Central. DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; NAS:ComplexPortal. DR GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal. DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:SGD. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IDA:UniProtKB. DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central. DR DisProt; DP01236; -. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR037363; Sec13/Seh1_fam. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR11024; NUCLEAR PORE COMPLEX PROTEIN SEC13 / SEH1 FAMILY MEMBER; 1. DR PANTHER; PTHR11024:SF2; PROTEIN SEC13 HOMOLOG; 1. DR Pfam; PF00400; WD40; 5. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; P55735; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle; KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport; KW Lysosome; Membrane; mRNA transport; Nuclear pore complex; Nucleus; KW Phosphoprotein; Protein transport; Reference proteome; Repeat; KW Translocation; Transport; WD repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895" FT CHAIN 2..322 FT /note="Protein SEC13 homolog" FT /id="PRO_0000051203" FT REPEAT 11..50 FT /note="WD 1" FT REPEAT 55..96 FT /note="WD 2" FT REPEAT 101..144 FT /note="WD 3" FT REPEAT 148..204 FT /note="WD 4" FT REPEAT 210..253 FT /note="WD 5" FT REPEAT 260..299 FT /note="WD 6" FT MOD_RES 2 FT /note="N-acetylvaline" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT VAR_SEQ 1..14 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9110174" FT /id="VSP_046191" FT VAR_SEQ 1 FT /note="M -> MREPVLTWCVPLELLCSHPLPLSAFLKSQVKLYTYRACAGKDEMGKM FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054695" FT VAR_SEQ 1 FT /note="M -> MGKM (in isoform 4)" FT /id="VSP_058966" FT VARIANT 172 FT /note="S -> L (in dbSNP:rs34078590)" FT /id="VAR_053413" FT CONFLICT 51 FT /note="A -> V (in Ref. 1; L09260)" FT /evidence="ECO:0000305" FT STRAND 16..21 FT /evidence="ECO:0007829|PDB:3BG1" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 27..32 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 35..43 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 46..54 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:3BG1" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:3BG1" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 129..134 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 193..196 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 230..235 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 239..244 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 246..249 FT /evidence="ECO:0007829|PDB:3BG0" FT STRAND 257..260 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 265..270 FT /evidence="ECO:0007829|PDB:3BG1" FT TURN 272..274 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 277..284 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 286..291 FT /evidence="ECO:0007829|PDB:3BG1" FT STRAND 297..302 FT /evidence="ECO:0007829|PDB:3BG1" SQ SEQUENCE 322 AA; 35541 MW; 18E29627D87FB3DD CRC64; MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI ADLRGHEGPV WQVAWAHPMY GNILASCSYD RKVIIWREEN GTWEKSHEHA GHDSSVNSVC WAPHDYGLIL ACGSSDGAIS LLTYTGEGQW EVKKINNAHT IGCNAVSWAP AVVPGSLIDH PSGQKPNYIK RFASGGCDNL IKLWKEEEDG QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV FIWTCDDASS NTWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI SDVNKGQGSV SASVTEGQQN EQ //