GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Protein transport protein Sec23A (hSec23A) (SEC23-related protein A)

 SC23A_HUMAN             Reviewed;         765 AA.
Q15436; B2R5P4; B3KXI2; Q8NE16;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
07-APR-2021, entry version 198.
RecName: Full=Protein transport protein Sec23A {ECO:0000305};
Short=hSec23A {ECO:0000303|PubMed:8898360};
AltName: Full=SEC23-related protein A;
Name=SEC23A {ECO:0000312|HGNC:HGNC:10701};
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), VARIANT VAL-211, FUNCTION,
SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
TISSUE=B-cell;
PubMed=8898360; DOI=10.1091/mbc.7.10.1535;
Paccaud J.-P., Reith W., Carpentier J.-L., Ravazzola M., Amherdt M.,
Schekman R., Orci L.;
"Cloning and functional characterization of mammalian homologues of the
COPII component Sec23.";
Mol. Biol. Cell 7:1535-1546(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
VAL-211.
TISSUE=Hippocampus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-211.
TISSUE=Testis;
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).
[5]
INTERACTION WITH SEC16A.
TISSUE=Liver;
PubMed=17192411; DOI=10.1091/mbc.e06-08-0707;
Bhattacharyya D., Glick B.S.;
"Two mammalian Sec16 homologues have nonredundant functions in endoplasmic
reticulum (ER) export and transitional ER organization.";
Mol. Biol. Cell 18:839-849(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
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).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[10]
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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
INTERACTION WITH MIA3, AND SUBCELLULAR LOCATION.
PubMed=28442536; DOI=10.1083/jcb.201703084;
Maeda M., Katada T., Saito K.;
"TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient
secretion.";
J. Cell Biol. 216:1731-1743(2017).
[13]
INTERACTION WITH TMEM39A AND SACM1L.
PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
Miao G., Zhang Y., Chen D., Zhang H.;
"The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
Mol. Cell 0:0-0(2019).
[14] {ECO:0007744|PDB:2YRC, ECO:0007744|PDB:2YRD}
STRUCTURE BY NMR OF 57-108 IN COMPLEX WITH ZINC.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the ZF-SEC23_SEC24 from human SEC23A.";
Submitted (OCT-2007) to the PDB data bank.
[15] {ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2NUT}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SEC22B; SEC24A AND
ZINC, FUNCTION, SUBUNIT, AND INTERACTION WITH SEC22B.
PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
Mancias J.D., Goldberg J.;
"The transport signal on Sec22 for packaging into COPII-coated vesicles is
a conformational epitope.";
Mol. Cell 26:403-414(2007).
[16] {ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, ECO:0007744|PDB:3EGD, ECO:0007744|PDB:3EGX}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-764 IN COMPLEX WITH CARGO
PEPTIDES; SEC22B; SEC24A; SEC24D AND ZINC, AND FUNCTION.
PubMed=18843296; DOI=10.1038/emboj.2008.208;
Mancias J.D., Goldberg J.;
"Structural basis of cargo membrane protein discrimination by the human
COPII coat machinery.";
EMBO J. 27:2918-2928(2008).
[17] {ECO:0007744|PDB:5KYN, ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYW, ECO:0007744|PDB:5KYX, ECO:0007744|PDB:5KYY}
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH MIA3 PEPTIDE; SEC24D
AND ZINC, FUNCTION, INTERACTION WITH MIA2; MIA3 AND SEC31A, MUTAGENESIS OF
PHE-628; TYR-672; TYR-678 AND PHE-681, AND DOMAIN.
PubMed=27551091; DOI=10.1073/pnas.1605916113;
Ma W., Goldberg J.;
"TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large
COPII coats.";
Proc. Natl. Acad. Sci. U.S.A. 113:10061-10066(2016).
[18]
VARIANT CLSD LEU-382, CHARACTERIZATION OF VARIANT CLSD LEU-382, AND
FUNCTION.
PubMed=16980979; DOI=10.1038/ng1876;
Boyadjiev S.A., Fromme J.C., Ben J., Chong S.S., Nauta C., Hur D.J.,
Zhang G., Hamamoto S., Schekman R., Ravazzola M., Orci L., Eyaid W.;
"Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading
to abnormal endoplasmic-reticulum-to-Golgi trafficking.";
Nat. Genet. 38:1192-1197(2006).
-!- FUNCTION: Component of the coat protein complex II (COPII) which
promotes the formation of transport vesicles from the endoplasmic
reticulum (ER). The coat has two main functions, the physical
deformation of the endoplasmic reticulum membrane into vesicles and the
selection of cargo molecules for their transport to the Golgi complex.
Required for the translocation of insulin-induced glucose transporter
SLC2A4/GLUT4 to the cell membrane (By similarity).
{ECO:0000250|UniProtKB:Q01405, ECO:0000269|PubMed:16980979,
ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296,
ECO:0000269|PubMed:27551091, ECO:0000269|PubMed:8898360}.
-!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
complex, the Sec13/31 complex and Sar1 (PubMed:17499046). Interacts
with SEC23IP. Interacts with HTR4 (By similarity). Interacts with
SEC16A (PubMed:17192411). Interacts with SLC6A4 (By similarity).
Interacts (as part of the Sec23/24 complex) with SEC22B; recruits
SEC22B into COPII-coated vesicles and allows the transport of this
cargo from the endoplasmic reticulum to the Golgi (PubMed:17499046).
Interacts (via Gelsolin-like repeat) with MIA2 and MIA3; specifically
involved in the transport of large cargos like the collagen COL7A1
(PubMed:27551091, PubMed:28442536). Interacts with DDHD1 (By
similarity). Interacts with TMEM39A (PubMed:31806350). Interacts with
SACM1L; this interaction is reduced in the absence of TMEM39A
(PubMed:31806350). {ECO:0000250|UniProtKB:Q01405,
ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:17499046,
ECO:0000269|PubMed:27551091, ECO:0000269|PubMed:28442536,
ECO:0000269|PubMed:31806350}.
-!- INTERACTION:
Q15436; Q12983: BNIP3; NbExp=3; IntAct=EBI-81088, EBI-749464;
Q15436; A2RRN7: CADPS; NbExp=3; IntAct=EBI-81088, EBI-10179719;
Q15436; Q00536: CDK16; NbExp=3; IntAct=EBI-81088, EBI-726261;
Q15436; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-81088, EBI-11977093;
Q15436; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-81088, EBI-25840379;
Q15436; P50570: DNM2; NbExp=3; IntAct=EBI-81088, EBI-346547;
Q15436; Q86UW9: DTX2; NbExp=3; IntAct=EBI-81088, EBI-740376;
Q15436; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-81088, EBI-781551;
Q15436; O75477: ERLIN1; NbExp=3; IntAct=EBI-81088, EBI-359299;
Q15436; P48023: FASLG; NbExp=3; IntAct=EBI-81088, EBI-495538;
Q15436; Q969F0: FATE1; NbExp=3; IntAct=EBI-81088, EBI-743099;
Q15436; P48165: GJA8; NbExp=3; IntAct=EBI-81088, EBI-17458373;
Q15436; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-81088, EBI-11956541;
Q15436; Q5JRA6: MIA3; NbExp=3; IntAct=EBI-81088, EBI-2291868;
Q15436; Q9UPX6: MINAR1; NbExp=3; IntAct=EBI-81088, EBI-11977115;
Q15436; O75928-2: PIAS2; NbExp=3; IntAct=EBI-81088, EBI-348567;
Q15436; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-81088, EBI-2466594;
Q15436; Q15437: SEC23B; NbExp=3; IntAct=EBI-81088, EBI-742673;
Q15436; Q9Y6Y8: SEC23IP; NbExp=3; IntAct=EBI-81088, EBI-1767971;
Q15436; P53992: SEC24C; NbExp=5; IntAct=EBI-81088, EBI-81134;
Q15436; O94855-2: SEC24D; NbExp=3; IntAct=EBI-81088, EBI-12081096;
Q15436; Q15637-4: SF1; NbExp=3; IntAct=EBI-81088, EBI-12223157;
Q15436; P30825: SLC7A1; NbExp=3; IntAct=EBI-81088, EBI-4289564;
Q15436; Q9P2R7: SUCLA2; NbExp=3; IntAct=EBI-81088, EBI-2269898;
Q15436; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-81088, EBI-3923061;
Q15436; O43557: TNFSF14; NbExp=3; IntAct=EBI-81088, EBI-524131;
Q15436; Q9Y2W2: WBP11; NbExp=3; IntAct=EBI-81088, EBI-714455;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
membrane {ECO:0000305|PubMed:8898360}; Peripheral membrane protein
{ECO:0000269|PubMed:8898360}; Cytoplasmic side
{ECO:0000269|PubMed:8898360}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:8898360}; Peripheral membrane protein
{ECO:0000269|PubMed:8898360}; Cytoplasmic side
{ECO:0000269|PubMed:8898360}. Cytoplasm, cytosol
{ECO:0000269|PubMed:8898360}. Note=Enriched at endoplasmic reticulum
exit sites, also known as transitional endoplasmic reticulum (tER).
{ECO:0000269|PubMed:28442536, ECO:0000269|PubMed:8898360}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15436-1; Sequence=Displayed;
Name=2;
IsoId=Q15436-2; Sequence=VSP_056230;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:8898360}.
-!- DOMAIN: The Gelsolin-like repeat mediates interaction with proteins
containing PPP motifs that include MIA2, MIA3 but also SEC31A. These
interactions are probably competitive. {ECO:0000269|PubMed:27551091}.
-!- DISEASE: Craniolenticulosutural dysplasia (CLSD) [MIM:607812]:
Autosomal recessive syndrome characterized by late-closing fontanels,
sutural cataracts, facial dysmorphisms and skeletal defects.
{ECO:0000269|PubMed:16980979}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
{ECO:0000305}.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; X97064; CAA65774.1; -; mRNA.
EMBL; AK127355; BAG54494.1; -; mRNA.
EMBL; AK312259; BAG35191.1; -; mRNA.
EMBL; AL109628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC036649; AAH36649.1; -; mRNA.
CCDS; CCDS9668.1; -. [Q15436-1]
PIR; T09574; T09574.
RefSeq; NP_006355.2; NM_006364.3. [Q15436-1]
PDB; 2NUP; X-ray; 2.80 A; A=1-765.
PDB; 2NUT; X-ray; 2.30 A; A=1-765.
PDB; 2YRC; NMR; -; A=57-108.
PDB; 2YRD; NMR; -; A=57-108.
PDB; 3EFO; X-ray; 2.70 A; A=1-765.
PDB; 3EG9; X-ray; 3.00 A; A=1-764.
PDB; 3EGD; X-ray; 2.70 A; A=1-764.
PDB; 3EGX; X-ray; 3.30 A; A=1-764.
PDB; 5KYN; X-ray; 2.55 A; A/B=1-765.
PDB; 5KYU; X-ray; 3.51 A; A=1-765.
PDB; 5KYW; X-ray; 3.20 A; A=1-765.
PDB; 5KYX; X-ray; 3.52 A; A=1-765.
PDB; 5KYY; X-ray; 3.40 A; A=1-765.
PDB; 5VNE; X-ray; 2.70 A; A=1-764.
PDB; 5VNF; X-ray; 2.41 A; A=1-764.
PDB; 5VNG; X-ray; 2.60 A; A=1-764.
PDB; 5VNH; X-ray; 2.60 A; A=1-764.
PDB; 5VNI; X-ray; 2.79 A; A=1-764.
PDB; 5VNJ; X-ray; 2.81 A; A=1-764.
PDB; 5VNK; X-ray; 2.55 A; A=1-764.
PDB; 5VNL; X-ray; 2.39 A; A=1-764.
PDB; 5VNM; X-ray; 2.77 A; A=1-764.
PDB; 5VNN; X-ray; 2.50 A; A=1-764.
PDB; 5VNO; X-ray; 2.90 A; A=1-764.
PDBsum; 2NUP; -.
PDBsum; 2NUT; -.
PDBsum; 2YRC; -.
PDBsum; 2YRD; -.
PDBsum; 3EFO; -.
PDBsum; 3EG9; -.
PDBsum; 3EGD; -.
PDBsum; 3EGX; -.
PDBsum; 5KYN; -.
PDBsum; 5KYU; -.
PDBsum; 5KYW; -.
PDBsum; 5KYX; -.
PDBsum; 5KYY; -.
PDBsum; 5VNE; -.
PDBsum; 5VNF; -.
PDBsum; 5VNG; -.
PDBsum; 5VNH; -.
PDBsum; 5VNI; -.
PDBsum; 5VNJ; -.
PDBsum; 5VNK; -.
PDBsum; 5VNL; -.
PDBsum; 5VNM; -.
PDBsum; 5VNN; -.
PDBsum; 5VNO; -.
SMR; Q15436; -.
BioGRID; 115747; 158.
CORUM; Q15436; -.
IntAct; Q15436; 71.
MINT; Q15436; -.
STRING; 9606.ENSP00000306881; -.
ChEMBL; CHEMBL4295827; -.
iPTMnet; Q15436; -.
MetOSite; Q15436; -.
PhosphoSitePlus; Q15436; -.
SwissPalm; Q15436; -.
BioMuta; SEC23A; -.
DMDM; 143811354; -.
EPD; Q15436; -.
jPOST; Q15436; -.
MassIVE; Q15436; -.
MaxQB; Q15436; -.
PaxDb; Q15436; -.
PeptideAtlas; Q15436; -.
PRIDE; Q15436; -.
ProteomicsDB; 3813; -.
ProteomicsDB; 60595; -. [Q15436-1]
Antibodypedia; 23326; 156 antibodies.
DNASU; 10484; -.
Ensembl; ENST00000307712; ENSP00000306881; ENSG00000100934. [Q15436-1]
Ensembl; ENST00000537403; ENSP00000444193; ENSG00000100934. [Q15436-2]
GeneID; 10484; -.
KEGG; hsa:10484; -.
UCSC; uc001wup.2; human. [Q15436-1]
CTD; 10484; -.
DisGeNET; 10484; -.
GeneCards; SEC23A; -.
HGNC; HGNC:10701; SEC23A.
HPA; ENSG00000100934; Low tissue specificity.
MalaCards; SEC23A; -.
MIM; 607812; phenotype.
MIM; 610511; gene.
neXtProt; NX_Q15436; -.
OpenTargets; ENSG00000100934; -.
Orphanet; 50814; Craniolenticulosutural dysplasia.
PharmGKB; PA35624; -.
VEuPathDB; HostDB:ENSG00000100934.14; -.
eggNOG; KOG1986; Eukaryota.
GeneTree; ENSGT00390000006916; -.
HOGENOM; CLU_008658_4_0_1; -.
InParanoid; Q15436; -.
OMA; FPPHYAE; -.
OrthoDB; 930591at2759; -.
PhylomeDB; Q15436; -.
TreeFam; TF300693; -.
PathwayCommons; Q15436; -.
Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
BioGRID-ORCS; 10484; 16 hits in 990 CRISPR screens.
ChiTaRS; SEC23A; human.
EvolutionaryTrace; Q15436; -.
GeneWiki; SEC23A; -.
GenomeRNAi; 10484; -.
Pharos; Q15436; Tbio.
PRO; PR:Q15436; -.
Proteomes; UP000005640; Chromosome 14.
RNAct; Q15436; protein.
Bgee; ENSG00000100934; Expressed in jejunal mucosa and 250 other tissues.
ExpressionAtlas; Q15436; baseline and differential.
Genevisible; Q15436; HS.
GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IGI:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
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:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
CDD; cd11287; Sec23_C; 1.
Gene3D; 3.40.20.10; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
InterPro; IPR007123; Gelsolin-like_dom.
InterPro; IPR036180; Gelsolin-like_dom_sf.
InterPro; IPR037364; Sec23.
InterPro; IPR006900; Sec23/24_helical_dom.
InterPro; IPR036175; Sec23/24_helical_dom_sf.
InterPro; IPR006896; Sec23/24_trunk_dom.
InterPro; IPR012990; Sec23_24_beta_S.
InterPro; IPR037550; Sec23_C.
InterPro; IPR036465; vWFA_dom_sf.
InterPro; IPR006895; Znf_Sec23_Sec24.
InterPro; IPR036174; Znf_Sec23_Sec24_sf.
PANTHER; PTHR11141; PTHR11141; 1.
Pfam; PF00626; Gelsolin; 1.
Pfam; PF08033; Sec23_BS; 1.
Pfam; PF04815; Sec23_helical; 1.
Pfam; PF04811; Sec23_trunk; 1.
Pfam; PF04810; zf-Sec23_Sec24; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF81811; SSF81811; 1.
SUPFAM; SSF82754; SSF82754; 1.
SUPFAM; SSF82919; SSF82919; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cytoplasm;
Cytoplasmic vesicle; Disease variant; Endoplasmic reticulum;
ER-Golgi transport; Membrane; Metal-binding; Phosphoprotein;
Protein transport; Reference proteome; Transport; Zinc.
INIT_MET 1
/note="Removed"
/evidence="ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378"
CHAIN 2..765
/note="Protein transport protein Sec23A"
/id="PRO_0000205146"
REPEAT 632..718
/note="Gelsolin-like"
/evidence="ECO:0000255"
METAL 61
/note="Zinc"
/evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2YRD,
ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9,
ECO:0007744|PDB:3EGD, ECO:0007744|PDB:5KYN,
ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX"
METAL 66
/note="Zinc"
/evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2YRD,
ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9,
ECO:0007744|PDB:3EGD, ECO:0007744|PDB:5KYN,
ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX"
METAL 85
/note="Zinc"
/evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2YRD,
ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9,
ECO:0007744|PDB:3EGD, ECO:0007744|PDB:5KYN,
ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX"
METAL 88
/note="Zinc"
/evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2YRD,
ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9,
ECO:0007744|PDB:3EGD, ECO:0007744|PDB:5KYN,
ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX"
MOD_RES 2
/note="N-acetylthreonine"
/evidence="ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378"
MOD_RES 308
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18669648"
VAR_SEQ 1..202
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_056230"
VARIANT 211
/note="L -> V (in dbSNP:rs8018720)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8898360"
/id="VAR_031029"
VARIANT 382
/note="F -> L (in CLSD; loss of COPII vesicle coating;
results in absence of incorporation of cargo proteins into
vesicles; dbSNP:rs118204000)"
/evidence="ECO:0000269|PubMed:16980979"
/id="VAR_031030"
MUTAGEN 628
/note="F->A: Decreased interaction with MIA3; when
associated with A-681."
/evidence="ECO:0000269|PubMed:27551091"
MUTAGEN 672
/note="Y->K: Decreased interaction with MIA3; when
associated with A-678."
/evidence="ECO:0000269|PubMed:27551091"
MUTAGEN 678
/note="Y->A: Decreased interaction with MIA3; when
associated with K-672."
/evidence="ECO:0000269|PubMed:27551091"
MUTAGEN 681
/note="F->A: Decreased interaction with MIA3; when
associated with A-628."
/evidence="ECO:0000269|PubMed:27551091"
CONFLICT 623
/note="L -> M (in Ref. 4; AAH36649)"
/evidence="ECO:0000305"
HELIX 4..15
/evidence="ECO:0007744|PDB:2NUT"
STRAND 16..24
/evidence="ECO:0007744|PDB:2NUT"
HELIX 28..31
/evidence="ECO:0007744|PDB:2NUT"
STRAND 34..36
/evidence="ECO:0007744|PDB:5KYN"
STRAND 39..42
/evidence="ECO:0007744|PDB:2NUT"
STRAND 49..51
/evidence="ECO:0007744|PDB:5KYY"
TURN 64..66
/evidence="ECO:0007744|PDB:5VNL"
STRAND 74..77
/evidence="ECO:0007744|PDB:2NUT"
TURN 78..81
/evidence="ECO:0007744|PDB:2NUT"
STRAND 82..84
/evidence="ECO:0007744|PDB:2NUT"
STRAND 86..88
/evidence="ECO:0007744|PDB:2NUT"
STRAND 91..93
/evidence="ECO:0007744|PDB:2NUT"
HELIX 96..98
/evidence="ECO:0007744|PDB:2NUT"
STRAND 103..105
/evidence="ECO:0007744|PDB:5VNL"
HELIX 108..110
/evidence="ECO:0007744|PDB:2NUT"
HELIX 112..114
/evidence="ECO:0007744|PDB:2NUT"
STRAND 115..121
/evidence="ECO:0007744|PDB:2NUT"
STRAND 130..136
/evidence="ECO:0007744|PDB:2NUT"
HELIX 141..155
/evidence="ECO:0007744|PDB:2NUT"
STRAND 163..179
/evidence="ECO:0007744|PDB:2NUT"
TURN 181..183
/evidence="ECO:0007744|PDB:5VNL"
STRAND 185..190
/evidence="ECO:0007744|PDB:2NUT"
HELIX 198..204
/evidence="ECO:0007744|PDB:2NUT"
STRAND 228..232
/evidence="ECO:0007744|PDB:2NUT"
HELIX 233..246
/evidence="ECO:0007744|PDB:2NUT"
HELIX 264..278
/evidence="ECO:0007744|PDB:2NUT"
STRAND 285..292
/evidence="ECO:0007744|PDB:2NUT"
STRAND 296..299
/evidence="ECO:0007744|PDB:2NUT"
HELIX 313..317
/evidence="ECO:0007744|PDB:2NUT"
HELIX 324..341
/evidence="ECO:0007744|PDB:2NUT"
STRAND 344..350
/evidence="ECO:0007744|PDB:2NUT"
HELIX 357..360
/evidence="ECO:0007744|PDB:2NUT"
HELIX 362..366
/evidence="ECO:0007744|PDB:2NUT"
STRAND 371..375
/evidence="ECO:0007744|PDB:2NUT"
STRAND 377..379
/evidence="ECO:0007744|PDB:2NUT"
HELIX 380..388
/evidence="ECO:0007744|PDB:2NUT"
STRAND 401..410
/evidence="ECO:0007744|PDB:2NUT"
STRAND 414..422
/evidence="ECO:0007744|PDB:2NUT"
STRAND 431..433
/evidence="ECO:0007744|PDB:3EG9"
STRAND 439..442
/evidence="ECO:0007744|PDB:5VNL"
STRAND 444..451
/evidence="ECO:0007744|PDB:2NUT"
STRAND 457..463
/evidence="ECO:0007744|PDB:2NUT"
STRAND 467..469
/evidence="ECO:0007744|PDB:3EG9"
STRAND 477..487
/evidence="ECO:0007744|PDB:2NUT"
STRAND 488..490
/evidence="ECO:0007744|PDB:2NUP"
STRAND 492..501
/evidence="ECO:0007744|PDB:2NUT"
HELIX 506..508
/evidence="ECO:0007744|PDB:2NUT"
HELIX 509..515
/evidence="ECO:0007744|PDB:2NUT"
HELIX 519..534
/evidence="ECO:0007744|PDB:2NUT"
HELIX 542..557
/evidence="ECO:0007744|PDB:2NUT"
STRAND 558..561
/evidence="ECO:0007744|PDB:3EGD"
HELIX 565..567
/evidence="ECO:0007744|PDB:2NUT"
TURN 572..576
/evidence="ECO:0007744|PDB:2NUT"
HELIX 577..586
/evidence="ECO:0007744|PDB:2NUT"
TURN 588..590
/evidence="ECO:0007744|PDB:2NUT"
HELIX 592..594
/evidence="ECO:0007744|PDB:3EFO"
HELIX 597..607
/evidence="ECO:0007744|PDB:2NUT"
HELIX 612..619
/evidence="ECO:0007744|PDB:2NUT"
STRAND 622..626
/evidence="ECO:0007744|PDB:2NUT"
STRAND 628..631
/evidence="ECO:0007744|PDB:2NUT"
STRAND 633..635
/evidence="ECO:0007744|PDB:5VNF"
HELIX 639..641
/evidence="ECO:0007744|PDB:2NUT"
STRAND 647..651
/evidence="ECO:0007744|PDB:2NUT"
STRAND 653..660
/evidence="ECO:0007744|PDB:2NUT"
HELIX 662..670
/evidence="ECO:0007744|PDB:2NUT"
TURN 671..674
/evidence="ECO:0007744|PDB:2NUT"
HELIX 676..678
/evidence="ECO:0007744|PDB:2NUT"
HELIX 679..698
/evidence="ECO:0007744|PDB:2NUT"
STRAND 699..701
/evidence="ECO:0007744|PDB:2NUT"
STRAND 704..709
/evidence="ECO:0007744|PDB:2NUT"
HELIX 713..715
/evidence="ECO:0007744|PDB:5VNL"
HELIX 716..721
/evidence="ECO:0007744|PDB:2NUT"
HELIX 749..760
/evidence="ECO:0007744|PDB:2NUT"
SEQUENCE 765 AA; 86161 MW; 128DF9964B253313 CRC64;
MTTYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPVAA LFTPLKERPD LPPIQYEPVL
CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPSYAG ISELNQPAEL LPQFSSIEYV
VLRGPQMPLI FLYVVDTCME DEDLQALKES MQMSLSLLPP TALVGLITFG RMVQVHELGC
EGISKSYVFR GTKDLSAKQL QEMLGLSKVP LTQATRGPQV QQPPPSNRFL QPVQKIDMNL
TDLLGELQRD PWPVPQGKRP LRSSGVALSI AVGLLECTFP NTGARIMMFI GGPATQGPGM
VVGDELKTPI RSWHDIDKDN AKYVKKGTKH FEALANRAAT TGHVIDIYAC ALDQTGLLEM
KCCPNLTGGY MVMGDSFNTS LFKQTFQRVF TKDMHGQFKM GFGGTLEIKT SREIKISGAI
GPCVSLNSKG PCVSENEIGT GGTCQWKICG LSPTTTLAIY FEVVNQHNAP IPQGGRGAIQ
FVTQYQHSSG QRRIRVTTIA RNWADAQTQI QNIAASFDQE AAAILMARLA IYRAETEEGP
DVLRWLDRQL IRLCQKFGEY HKDDPSSFRF SETFSLYPQF MFHLRRSSFL QVFNNSPDES
SYYRHHFMRQ DLTQSLIMIQ PILYAYSFSG PPEPVLLDSS SILADRILLM DTFFQILIYH
GETIAQWRKS GYQDMPEYEN FRHLLQAPVD DAQEILHSRF PMPRYIDTEH GGSQARFLLS
KVNPSQTHNN MYAWGQESGA PILTDDVSLQ VFMDHLKKLA VSSAA


Related products :

Catalog number Product name Quantity
EIAAB37402 Mouse,Mus musculus,Protein transport protein Sec23A,Sec23,Sec23a,Sec23r,SEC23-related protein A
EIAAB37399 Homo sapiens,Human,Protein transport protein Sec23A,SEC23A,SEC23-related protein A
EIAAB37401 Bos taurus,Bovine,Protein transport protein Sec23A,SEC23A,SEC23-related protein A
EIAAB37400 Chicken,Gallus gallus,Protein transport protein Sec23A,RCJMB04_14a13,SEC23A,SEC23-related protein A
15-288-22818 Protein transport protein Sec23B - SEC23-related protein B Polyclonal 0.1 mg
15-288-22818 Protein transport protein Sec23B - SEC23-related protein B Polyclonal 0.05 mg
SC23A_MOUSE ELISA Kit FOR Protein transport protein Sec23A; organism: Mouse; gene name: Sec23a 96T
SC23A_HUMAN ELISA Kit FOR Protein transport protein Sec23A; organism: Human; gene name: SEC23A 96T
EIAAB37403 Homo sapiens,Human,Protein transport protein Sec23B,SEC23B,SEC23-related protein B
CSB-EL020947MO Mouse Protein transport protein Sec23A(SEC23A) ELISA kit SpeciesMouse 96T
CSB-EL020947BO Bovine Protein transport protein Sec23A(SEC23A) ELISA kit SpeciesBovine 96T
CSB-EL020947HU Human Protein transport protein Sec23A(SEC23A) ELISA kit SpeciesHuman 96T
CSB-EL020947CH Chicken Protein transport protein Sec23A(SEC23A) ELISA kit SpeciesChicken 96T
EIAAB37405 Mouse,Mus musculus,Protein transport protein Sec23B,Sec23b,SEC23-related protein B
EIAAB37404 Bos taurus,Bovine,Protein transport protein Sec23B,SEC23B,SEC23-related protein B
CSB-EL020947BO Bovine Protein transport protein Sec23A(SEC23A) ELISA kit 96T
CSB-EL020947CH Chicken Protein transport protein Sec23A(SEC23A) ELISA kit 96T
CSB-EL020947MO Mouse Protein transport protein Sec23A(SEC23A) ELISA kit 96T
CSB-EL020947HU Human Protein transport protein Sec23A(SEC23A) ELISA kit 96T
G4292 Protein transport protein Sec23A (SEC23A), Mouse, ELISA Kit 96T
G4290 Protein transport protein Sec23A (SEC23A), Chicken, ELISA Kit 96T
G4291 Protein transport protein Sec23A (SEC23A), Human, ELISA Kit 96T
G4289 Protein transport protein Sec23A (SEC23A), Bovine, ELISA Kit 96T
SC23A_HUMAN Human ELISA Kit FOR Protein transport protein Sec23A 96T
SEC23A SEC23A Gene Sec23 homolog A (S. cerevisiae)
Pathways :
WP1616: ABC transporters
WP731: Sterol regulatory element binding protein related
WP2199: Seed Development
WP1689: Porphyrin and chlorophyll metabolism
WP2272: Pathogenic Escherichia coli infection
WP1713: Two-component system
WP1502: Mitochondrial biogenesis
WP1685: Peptidoglycan biosynthesis
WP2218: sGC
WP1624: Bacterial secretion system
WP1909: Signal regulatory protein (SIRP) family interactions
WP813: G Protein Signaling Pathways
WP1650: Fluorobenzoate degradation
WP1692: Protein export
WP232: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1700: Selenoamino acid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1939: Unfolded Protein Response
WP1665: Limonene and pinene degradation
WP525: Mitochondrial Unfolded-Protein Response
WP1675: Nitrogen metabolism
WP210: Cytoplasmic Ribosomal Proteins
WP2203: TSLP Signaling Pathway
WP931: G Protein Signaling Pathways

Related Genes :
[SEC23B] Protein transport protein Sec23B (hSec23B) (SEC23-related protein B)
[SEC24A] Protein transport protein Sec24A (SEC24-related protein A)
[MIA3 KIAA0268 TANGO UNQ6077/PRO20088] Transport and Golgi organization protein 1 homolog (TANGO1) (C219-reactive peptide) (D320) (Melanoma inhibitory activity protein 3)
[YIPF5 FINGER5 YIP1A PP12723 SB140 UNQ3123/PRO10275] Protein YIPF5 (Five-pass transmembrane protein localizing in the Golgi apparatus and the endoplasmic reticulum 5) (Smooth muscle cell-associated protein 5) (SMAP-5) (YIP1 family member 5) (YPT-interacting protein 1 A)
[Mia3 Kiaa0268 Tango] Transport and Golgi organization protein 1 homolog (TANGO1) (Melanoma inhibitory activity protein 3)
[MIA2 CTAGE5 MEA11 MEA6 MGEA11 MGEA6] Melanoma inhibitory activity protein 2 (MIA protein 2) (CTAGE family member 5 ER export factor) (Cutaneous T-cell lymphoma-associated antigen 5) (Meningioma-expressed antigen 6/11)
[SEC22B SEC22L1] Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1)
[SLC6A4 HTT SERT] Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4)
[Slc6a4 Htt Sert] Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4)
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (S31I125) (S31III125) (Tmp-21-I) (Transmembrane protein Tmp21) (p23) (p24 family protein delta-1) (p24delta1) (p24delta)
[DDHD1 KIAA1705] Phospholipase DDHD1 (EC 3.1.1.-) (DDHD domain-containing protein 1) (Phosphatidic acid-preferring phospholipase A1 homolog) (PA-PLA1)
[SUCLA2] Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA)
[Sec22b Sec22l1] Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1) (mSec22b)
[Sec22b Sec22l1] Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1)
[TMED2 RNP24] Transmembrane emp24 domain-containing protein 2 (Membrane protein p24A) (p24) (p24 family protein beta-1) (p24beta1)
[DNM2 DYN2] Dynamin-2 (EC 3.6.5.5)
[Tmed2 Rnp24] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (RNP21.4) (p24 family protein beta-1) (p24beta1)
[Tmed2 Rnp24 Sid394] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (Sid 394) (p24 family protein beta-1) (p24beta1)
[TMEM39A SUSR2] Transmembrane protein 39A
[Slc6a4] Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4)
[DCTN1] Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (p135) (p150-glued)
[SLC6A4 SERT] Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4)
[SLC6A4] Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4)
[Tmed10 Tmp21] Transmembrane emp24 domain-containing protein 10 (Protein Tmed10) (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[Tmed10 Tmp21] Transmembrane emp24 domain-containing protein 10 (Protein Tmed10) (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (Integral membrane protein p23) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (Integral membrane protein p23) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[SACM1L KIAA0851 SAC1] Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Suppressor of actin mutations 1-like protein)
[TMED10 TMP21] Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)

Bibliography :