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Protein SEC13 homolog (GATOR complex protein SEC13) (SEC13-like protein 1) (SEC13-related protein)

 SEC13_HUMAN             Reviewed;         322 AA.
P55735; A8MV37; B4DXJ1; Q5BJF0; Q9BRM6; Q9BUG7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 181.
RecName: Full=Protein SEC13 homolog {ECO:0000305};
AltName: Full=GATOR complex protein SEC13 {ECO:0000305};
AltName: Full=SEC13-like protein 1;
AltName: Full=SEC13-related protein;
Name=SEC13; Synonyms=D3S1231E, SEC13L1, SEC13R;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7987303; DOI=10.1093/hmg/3.8.1281;
Swaroop A., Yang-Feng T.L., Liu W., Gieser L., Barrow L.L., Chen K.C.,
Agarwal N., Meisler M.H., Smith D.I.;
"Molecular characterization of a novel human gene, SEC13R, related to
the yeast secretory pathway gene SEC13, and mapping to a conserved
linkage group on human chromosome 3p24-p25 and mouse chromosome 6.";
Hum. Mol. Genet. 3:1281-1286(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9110174;
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-27.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
PROTEIN SEQUENCE OF 2-27; 44-54; 217-256 AND 291-322, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 182-192; 217-239 AND 291-322, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8972206; DOI=10.1128/MCB.17.1.256;
Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G.,
Hong W.;
"The mammalian homolog of yeast Sec13p is enriched in the intermediate
compartment and is essential for protein transport from the
endoplasmic reticulum to the Golgi apparatus.";
Mol. Cell. Biol. 17:256-266(1997).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH NUP96.
PubMed=14517296; DOI=10.1128/MCB.23.20.7271-7284.2003;
Enninga J., Levay A., Fontoura B.M.;
"Sec13 shuttles between the nucleus and the cytoplasm and stably
interacts with Nup96 at the nuclear pore complex.";
Mol. Cell. Biol. 23:7271-7284(2003).
[11]
INTERACTION WITH SEC31B.
PubMed=16495487; DOI=10.1242/jcs.02751;
Stankewich M.C., Stabach P.R., Morrow J.S.;
"Human Sec31B: a family of new mammalian orthologues of yeast Sec31p
that associate with the COPII coat.";
J. Cell Sci. 119:958-969(2006).
[12]
INTERACTION WITH SEC31A.
PubMed=16957052; DOI=10.1091/mbc.E06-05-0444;
Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.;
"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum
exit sites by Sec31A and stabilizes the localization of Sec31A.";
Mol. Biol. Cell 17:4876-4887(2006).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
INTERACTION WITH SESN1; SESN2 AND SESN3.
PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014;
Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M.,
Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.;
"The Sestrins interact with GATOR2 to negatively regulate the amino-
acid-sensing pathway upstream of mTORC1.";
Cell Rep. 9:1-8(2014).
[19]
FUNCTION, AND INTERACTION WITH SESN2.
PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019;
Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C.,
Akopiants K., Guan K.L., Karin M., Budanov A.V.;
"Sestrins inhibit mTORC1 kinase activation through the GATOR
complex.";
Cell Rep. 9:1281-1291(2014).
[20]
FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND INTERACTION WITH RRAG
PROTEINS.
PubMed=23723238; DOI=10.1126/science.1232044;
Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W.,
Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M.,
Sabatini D.M.;
"A Tumor suppressor complex with GAP activity for the Rag GTPases that
signal amino acid sufficiency to mTORC1.";
Science 340:1100-1106(2013).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
INTERACTION WITH CASTOR2 AND CASTOR1.
PubMed=26972053; DOI=10.1016/j.cell.2016.02.035;
Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K.,
Wyant G.A., Wang T., Harper J.W., Gygi S.P., Sabatini D.M.;
"The CASTOR proteins are arginine sensors for the mTORC1 pathway.";
Cell 165:153-164(2016).
[23]
FUNCTION.
PubMed=27487210; DOI=10.1038/nature19079;
Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U.,
Sabatini D.M.;
"Mechanism of arginine sensing by CASTOR1 upstream of mTORC1.";
Nature 536:229-233(2016).
[24]
SUBCELLULAR LOCATION.
PubMed=28199306; DOI=10.1038/nature21423;
Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M.,
Shen K., Condon K.J., Petri S., Kedir J., Scaria S.M.,
Abu-Remaileh M., Frankel W.N., Sabatini D.M.;
"KICSTOR recruits GATOR1 to the lysosome and is necessary for
nutrients to regulate mTORC1.";
Nature 543:438-442(2017).
[25]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-316 IN COMPLEX WITH YEAST
NUP145C, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=18160040; DOI=10.1016/j.cell.2007.11.038;
Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.;
"Architecture of a coat for the nuclear pore membrane.";
Cell 131:1313-1326(2007).
-!- FUNCTION: Functions as a component of the nuclear pore complex
(NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is
involved in the biogenesis of COPII-coated vesicles.
{ECO:0000269|PubMed:8972206}.
-!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
within the amino acid-sensing branch of the TORC1 signaling
pathway. Indirectly activates mTORC1 and the TORC1 signaling
pathway through the inhibition of the GATOR1 subcomplex
(PubMed:23723238). It is negatively regulated by the upstream
amino acid sensors SESN2 and CASTOR1 (PubMed:25457612,
PubMed:27487210). {ECO:0000269|PubMed:23723238,
ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}.
-!- SUBUNIT: At the nuclear pore: component of the Y-shaped Nup107-160
subcomplex of the nuclear pore complex (NPC). The Nup107-160
subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43,
NUP37, SEH1 and SEC13. At the COPII coat complex: interacts with
SEC31A and SEC31B. Within the GATOR complex, component of the
GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59.
The GATOR complex strongly interacts with RRAGA/RRAGC and
RRAGB/RRAGC heterodimers (PubMed:14517296, PubMed:16495487,
PubMed:16957052, PubMed:18160040, PubMed:23723238). The GATOR2
complex interacts with CASTOR2 and CASTOR1; the interaction is
negatively regulated by arginine (PubMed:26972053). The GATOR2
complex interacts with SESN1, SESN2 and SESN3; the interaction is
negatively regulated by amino acids (PubMed:25263562,
PubMed:25457612). {ECO:0000269|PubMed:14517296,
ECO:0000269|PubMed:16495487, ECO:0000269|PubMed:16957052,
ECO:0000269|PubMed:18160040, ECO:0000269|PubMed:23723238,
ECO:0000269|PubMed:25263562, ECO:0000269|PubMed:25457612,
ECO:0000269|PubMed:26972053}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1046596, EBI-1046596;
P49687:NUP145 (xeno); NbExp=15; IntAct=EBI-1046596, EBI-11730;
E9PK14:SEC16B; NbExp=4; IntAct=EBI-12235008, EBI-12372595;
Q96JE7-2:SEC16B; NbExp=5; IntAct=EBI-1046596, EBI-10215083;
O94979-1:SEC31A; NbExp=9; IntAct=EBI-10045850, EBI-15564399;
Q96EE3:SEH1L; NbExp=3; IntAct=EBI-1046596, EBI-922818;
O00463:TRAF5; NbExp=3; IntAct=EBI-1046596, EBI-523498;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
membrane {ECO:0000269|PubMed:8972206}; Peripheral membrane protein
{ECO:0000269|PubMed:8972206}; Cytoplasmic side
{ECO:0000269|PubMed:8972206}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:8972206}; Peripheral membrane protein
{ECO:0000269|PubMed:8972206}; Cytoplasmic side
{ECO:0000269|PubMed:8972206}. Nucleus, nuclear pore complex
{ECO:0000269|PubMed:14517296, ECO:0000269|PubMed:18160040}.
Lysosome membrane {ECO:0000269|PubMed:28199306}. Note=In
interphase, localizes at both sides of the NPC.
{ECO:0000269|PubMed:14517296}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P55735-1; Sequence=Displayed;
Name=2;
IsoId=P55735-2; Sequence=VSP_046191;
Note=No experimental confirmation available.;
Name=3;
IsoId=P55735-3; Sequence=VSP_054695;
Note=No experimental confirmation available.;
Name=4;
IsoId=P55735-4; Sequence=VSP_058966;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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EMBL; L09260; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF052155; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK301999; BAG63403.1; -; mRNA.
EMBL; AC022384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002634; AAH02634.2; -; mRNA.
EMBL; BC006167; AAH06167.1; -; mRNA.
EMBL; BC091506; AAH91506.1; -; mRNA.
CCDS; CCDS2599.1; -. [P55735-1]
CCDS; CCDS46751.1; -. [P55735-2]
CCDS; CCDS63540.1; -. [P55735-3]
RefSeq; NP_001129498.1; NM_001136026.2. [P55735-3]
RefSeq; NP_001129704.1; NM_001136232.2. [P55735-2]
RefSeq; NP_109598.2; NM_030673.3. [P55735-4]
RefSeq; NP_899195.1; NM_183352.2. [P55735-1]
RefSeq; XP_005265436.1; XM_005265379.2. [P55735-4]
RefSeq; XP_016862508.1; XM_017007019.1. [P55735-3]
UniGene; Hs.166924; -.
UniGene; Hs.672979; -.
PDB; 3BG0; X-ray; 3.15 A; A/D/E/H=1-316.
PDB; 3BG1; X-ray; 3.00 A; A/D/E/H=1-316.
PDB; 5A9Q; EM; 23.00 A; 6/F/O/X=1-322.
PDBsum; 3BG0; -.
PDBsum; 3BG1; -.
PDBsum; 5A9Q; -.
ProteinModelPortal; P55735; -.
SMR; P55735; -.
BioGrid; 112296; 83.
CORUM; P55735; -.
DIP; DIP-39091N; -.
IntAct; P55735; 66.
MINT; P55735; -.
STRING; 9606.ENSP00000312122; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P55735; -.
PhosphoSitePlus; P55735; -.
SwissPalm; P55735; -.
DMDM; 50403748; -.
EPD; P55735; -.
MaxQB; P55735; -.
PaxDb; P55735; -.
PeptideAtlas; P55735; -.
PRIDE; P55735; -.
ProteomicsDB; 56858; -.
DNASU; 6396; -.
Ensembl; ENST00000337354; ENSP00000336566; ENSG00000157020. [P55735-4]
Ensembl; ENST00000350697; ENSP00000312122; ENSG00000157020. [P55735-1]
Ensembl; ENST00000383801; ENSP00000373312; ENSG00000157020. [P55735-3]
Ensembl; ENST00000397109; ENSP00000380298; ENSG00000157020. [P55735-2]
GeneID; 6396; -.
KEGG; hsa:6396; -.
UCSC; uc003bvm.5; human. [P55735-1]
CTD; 6396; -.
DisGeNET; 6396; -.
EuPathDB; HostDB:ENSG00000157020.17; -.
GeneCards; SEC13; -.
HGNC; HGNC:10697; SEC13.
HPA; HPA035292; -.
HPA; HPA057943; -.
MIM; 600152; gene.
neXtProt; NX_P55735; -.
OpenTargets; ENSG00000157020; -.
PharmGKB; PA35620; -.
eggNOG; KOG1332; Eukaryota.
eggNOG; ENOG410XPFM; LUCA.
GeneTree; ENSGT00550000075049; -.
HOGENOM; HOG000216895; -.
HOVERGEN; HBG057343; -.
InParanoid; P55735; -.
KO; K14004; -.
OMA; REDNDRW; -.
OrthoDB; EOG091G0DTE; -.
PhylomeDB; P55735; -.
TreeFam; TF300815; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SignaLink; P55735; -.
SIGNOR; P55735; -.
ChiTaRS; SEC13; human.
EvolutionaryTrace; P55735; -.
GeneWiki; SEC13; -.
GenomeRNAi; 6396; -.
PRO; PR:P55735; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000157020; -.
CleanEx; HS_SEC13; -.
ExpressionAtlas; P55735; baseline and differential.
Genevisible; P55735; HS.
GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0061700; C:GATOR2 complex; IDA:SGD.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0090110; P:cargo loading into COPII-coated vesicle; IDA:UniProtKB.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:SGD.
GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:InterPro.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR037596; Sec13.
InterPro; IPR037363; Sec13/Seh1_fam.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR11024; PTHR11024; 1.
PANTHER; PTHR11024:SF2; PTHR11024:SF2; 1.
Pfam; PF00400; WD40; 5.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50082; WD_REPEATS_2; 3.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum;
ER-Golgi transport; Lysosome; Membrane; mRNA transport;
Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Repeat; Translocation;
Transport; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.7}.
CHAIN 2 322 Protein SEC13 homolog.
/FTId=PRO_0000051203.
REPEAT 11 50 WD 1.
REPEAT 55 96 WD 2.
REPEAT 101 144 WD 3.
REPEAT 148 204 WD 4.
REPEAT 210 253 WD 5.
REPEAT 260 299 WD 6.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.7}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 14 Missing (in isoform 2).
{ECO:0000303|PubMed:9110174}.
/FTId=VSP_046191.
VAR_SEQ 1 1 M -> MREPVLTWCVPLELLCSHPLPLSAFLKSQVKLYTYR
ACAGKDEMGKM (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054695.
VAR_SEQ 1 1 M -> MGKM (in isoform 4).
/FTId=VSP_058966.
VARIANT 172 172 S -> L (in dbSNP:rs34078590).
/FTId=VAR_053413.
CONFLICT 51 51 A -> V (in Ref. 1; L09260).
{ECO:0000305}.
STRAND 16 21 {ECO:0000244|PDB:3BG1}.
HELIX 23 25 {ECO:0000244|PDB:3BG1}.
STRAND 27 32 {ECO:0000244|PDB:3BG1}.
STRAND 35 43 {ECO:0000244|PDB:3BG1}.
STRAND 46 54 {ECO:0000244|PDB:3BG1}.
STRAND 60 65 {ECO:0000244|PDB:3BG1}.
HELIX 68 70 {ECO:0000244|PDB:3BG1}.
STRAND 74 78 {ECO:0000244|PDB:3BG1}.
STRAND 83 86 {ECO:0000244|PDB:3BG1}.
STRAND 89 91 {ECO:0000244|PDB:3BG1}.
STRAND 95 99 {ECO:0000244|PDB:3BG1}.
STRAND 108 111 {ECO:0000244|PDB:3BG1}.
TURN 114 116 {ECO:0000244|PDB:3BG1}.
STRAND 120 123 {ECO:0000244|PDB:3BG1}.
STRAND 125 127 {ECO:0000244|PDB:3BG1}.
STRAND 129 134 {ECO:0000244|PDB:3BG1}.
STRAND 136 138 {ECO:0000244|PDB:3BG1}.
STRAND 140 142 {ECO:0000244|PDB:3BG1}.
STRAND 148 151 {ECO:0000244|PDB:3BG1}.
STRAND 181 183 {ECO:0000244|PDB:3BG1}.
STRAND 193 196 {ECO:0000244|PDB:3BG1}.
STRAND 202 206 {ECO:0000244|PDB:3BG1}.
STRAND 215 219 {ECO:0000244|PDB:3BG1}.
STRAND 230 235 {ECO:0000244|PDB:3BG1}.
STRAND 239 244 {ECO:0000244|PDB:3BG1}.
STRAND 246 249 {ECO:0000244|PDB:3BG0}.
STRAND 257 260 {ECO:0000244|PDB:3BG1}.
STRAND 265 270 {ECO:0000244|PDB:3BG1}.
TURN 272 274 {ECO:0000244|PDB:3BG1}.
STRAND 277 284 {ECO:0000244|PDB:3BG1}.
STRAND 286 291 {ECO:0000244|PDB:3BG1}.
STRAND 297 302 {ECO:0000244|PDB:3BG1}.
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


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