ID SC23B_HUMAN Reviewed; 767 AA. AC Q15437; D3DW33; Q503A9; Q5W183; Q9BS15; Q9BSI2; Q9H1D7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 24-JAN-2024, entry version 202. DE RecName: Full=Protein transport protein Sec23B {ECO:0000305}; DE Short=hSec23B {ECO:0000303|PubMed:8898360}; DE AltName: Full=SEC23-related protein B; GN Name=SEC23B {ECO:0000312|HGNC:HGNC:10702}; 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], VARIANT GLN-489, AND TISSUE SPECIFICITY. RC TISSUE=B-cell; RX PubMed=8898360; DOI=10.1091/mbc.7.10.1535; RA Paccaud J.-P., Reith W., Carpentier J.-L., Ravazzola M., Amherdt M., RA Schekman R., Orci L.; RT "Cloning and functional characterization of mammalian homologues of the RT COPII component Sec23."; RL Mol. Biol. Cell 7:1535-1546(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-373 AND LEU-433. RC TISSUE=Cervix, 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 [5] 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 [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [8] 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 [9] RP VARIANTS CDAN2 TRP-14; LYS-109; ALA-348; CYS-497; LEU-603 AND CYS-701, AND RP VARIANT GLN-489. RX PubMed=19621418; DOI=10.1002/humu.21077; RA Bianchi P., Fermo E., Vercellati C., Boschetti C., Barcellini W., Iurlo A., RA Marcello A.P., Righetti P.G., Zanella A.; RT "Congenital dyserythropoietic anemia type II (CDAII) is caused by mutations RT in the SEC23B gene."; RL Hum. Mutat. 30:1292-1298(2009). RN [10] RP VARIANTS CDAN2 TRP-14; LYS-109; GLY-239 AND TRP-530, VARIANTS HIS-18; RP HIS-313; THR-318; ARG-386; ILE-426; CYS-462; CYS-497 AND VAL-524, AND RP CHARACTERIZATION OF VARIANTS CDAN2 TRP-14; LYS-109 AND GLY-239. RX PubMed=19561605; DOI=10.1038/ng.405; RA Schwarz K., Iolascon A., Verissimo F., Trede N.S., Horsley W., Chen W., RA Paw B.H., Hopfner K.-P., Holzmann K., Russo R., Esposito M.R., Spano D., RA De Falco L., Heinrich K., Joggerst B., Rojewski M.T., Perrotta S., RA Denecke J., Pannicke U., Delaunay J., Pepperkok R., Heimpel H.; RT "Mutations affecting the secretory COPII coat component SEC23B cause RT congenital dyserythropoietic anemia type II."; RL Nat. Genet. 41:936-940(2009). RN [11] RP VARIANTS CWS7 LEU-164 AND GLY-594, CHARACTERIZATION OF VARIANT CWS7 RP GLY-594, INTERACTION WITH SAR1A, AND SUBCELLULAR LOCATION. RX PubMed=26522472; DOI=10.1016/j.ajhg.2015.10.001; RA Yehia L., Niazi F., Ni Y., Ngeow J., Sankunny M., Liu Z., Wei W., RA Mester J.L., Keri R.A., Zhang B., Eng C.; RT "Germline heterozygous variants in SEC23B are associated with Cowden RT syndrome and enriched in apparently sporadic thyroid cancer."; RL Am. J. Hum. Genet. 97:661-676(2015). RN [12] RP VARIANTS CDAN2 TRP-14; GLY-239; LEU-436 AND 554-ARG--CYS-767 DEL. RX PubMed=33159567; DOI=10.1007/s00277-020-04319-5; RA Mendez M., Moreno-Carralero M.I., Peri V.L., Camacho-Galan R., RA Bosch-Benitez J.M., Huerta-Aragones J., Sanchez-Calero-Guilarte J., RA Moreno-Risco M.B., Alonso-Dominguez J.M., Moran-Jimenez M.J.; RT "Congenital dyserythropoietic anemia types Ib, II, and III: novel variants RT in the CDIN1 gene and functional study of a novel variant in the KIF23 RT gene."; RL Ann. Hematol. 100:353-364(2021). CC -!- FUNCTION: Component of the coat protein complex II (COPII) which CC promotes the formation of transport vesicles from the endoplasmic CC reticulum (ER). The coat has two main functions, the physical CC deformation of the endoplasmic reticulum membrane into vesicles and the CC selection of cargo molecules for their transport to the Golgi complex. CC {ECO:0000250|UniProtKB:Q15436}. CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24 CC complex, the Sec13/31 complex and Sar1 (By similarity). Interacts with CC SAR1A (PubMed:26522472). {ECO:0000250|UniProtKB:Q15436, CC ECO:0000269|PubMed:26522472}. CC -!- INTERACTION: CC Q15437; Q8N684: CPSF7; NbExp=3; IntAct=EBI-742673, EBI-746909; CC Q15437; Q86UW9: DTX2; NbExp=6; IntAct=EBI-742673, EBI-740376; CC Q15437; Q969F0: FATE1; NbExp=3; IntAct=EBI-742673, EBI-743099; CC Q15437; O43365: HOXA3; NbExp=4; IntAct=EBI-742673, EBI-8643838; CC Q15437; P42858: HTT; NbExp=3; IntAct=EBI-742673, EBI-466029; CC Q15437; Q96M27: PRRC1; NbExp=3; IntAct=EBI-742673, EBI-2560879; CC Q15437; Q13671: RIN1; NbExp=3; IntAct=EBI-742673, EBI-366017; CC Q15437; Q15436: SEC23A; NbExp=3; IntAct=EBI-742673, EBI-81088; CC Q15437; O94855: SEC24D; NbExp=6; IntAct=EBI-742673, EBI-748817; CC Q15437; O94855-2: SEC24D; NbExp=3; IntAct=EBI-742673, EBI-12081096; CC Q15437; P09234: SNRPC; NbExp=3; IntAct=EBI-742673, EBI-766589; CC Q15437; Q8N205: SYNE4; NbExp=3; IntAct=EBI-742673, EBI-7131783; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle CC membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q15436}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:26522472}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q15436}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q15436}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:8898360}. CC -!- DISEASE: Cowden syndrome 7 (CWS7) [MIM:616858]: A form of Cowden CC syndrome, a hamartomatous polyposis syndrome with age-related CC penetrance. Cowden syndrome is characterized by hamartomatous lesions CC affecting derivatives of ectodermal, mesodermal and endodermal layers, CC macrocephaly, facial trichilemmomas (benign tumors of the hair follicle CC infundibulum), acral keratoses, papillomatous papules, and elevated CC risk for development of several types of malignancy, particularly CC breast carcinoma in women and thyroid carcinoma in both men and women. CC Colon cancer and renal cell carcinoma have also been reported. CC Hamartomas can be found in virtually every organ, but most commonly in CC the skin, gastrointestinal tract, breast and thyroid. CWS7 inheritance CC is autosomal dominant. {ECO:0000269|PubMed:26522472}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Anemia, congenital dyserythropoietic, 2 (CDAN2) [MIM:224100]: CC An autosomal recessive blood disorder characterized by morphological CC abnormalities of erythroblasts, ineffective erythropoiesis, normocytic CC anemia, iron overload, jaundice, and variable splenomegaly. CC Ultrastructural features include bi- or multinucleated erythroblasts in CC bone marrow, karyorrhexis, and the presence of Gaucher-like bone marrow CC histiocytes. The main biochemical feature of the disease is defective CC glycosylation of some red blood cells membrane proteins. CC {ECO:0000269|PubMed:19561605, ECO:0000269|PubMed:19621418, CC ECO:0000269|PubMed:33159567}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily. CC {ECO:0000305}. 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; X97065; CAA65775.1; -; mRNA. DR EMBL; AL121893; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121900; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10231.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10232.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10233.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10234.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10235.1; -; Genomic_DNA. DR EMBL; BC005032; AAH05032.1; -; mRNA. DR EMBL; BC005404; AAH05404.1; -; mRNA. DR EMBL; BC095404; AAH95404.1; -; mRNA. DR CCDS; CCDS13137.1; -. DR RefSeq; NP_001166216.1; NM_001172745.1. DR RefSeq; NP_006354.2; NM_006363.4. DR RefSeq; NP_116780.1; NM_032985.4. DR RefSeq; NP_116781.1; NM_032986.3. DR RefSeq; XP_016883082.1; XM_017027593.1. DR AlphaFoldDB; Q15437; -. DR SMR; Q15437; -. DR BioGRID; 115746; 224. DR IntAct; Q15437; 78. DR MINT; Q15437; -. DR STRING; 9606.ENSP00000338844; -. DR GlyGen; Q15437; 15 sites, 1 O-linked glycan (15 sites). DR iPTMnet; Q15437; -. DR MetOSite; Q15437; -. DR PhosphoSitePlus; Q15437; -. DR SwissPalm; Q15437; -. DR BioMuta; SEC23B; -. DR DMDM; 20141794; -. DR EPD; Q15437; -. DR jPOST; Q15437; -. DR MassIVE; Q15437; -. DR MaxQB; Q15437; -. DR PaxDb; 9606-ENSP00000338844; -. DR PeptideAtlas; Q15437; -. DR ProteomicsDB; 60596; -. DR Pumba; Q15437; -. DR Antibodypedia; 1407; 236 antibodies from 24 providers. DR DNASU; 10483; -. DR Ensembl; ENST00000262544.6; ENSP00000262544.2; ENSG00000101310.17. DR Ensembl; ENST00000336714.8; ENSP00000338844.3; ENSG00000101310.17. DR Ensembl; ENST00000377465.6; ENSP00000366685.1; ENSG00000101310.17. DR Ensembl; ENST00000650089.1; ENSP00000497473.1; ENSG00000101310.17. DR GeneID; 10483; -. DR KEGG; hsa:10483; -. DR MANE-Select; ENST00000650089.1; ENSP00000497473.1; NM_006363.6; NP_006354.2. DR UCSC; uc002wqz.3; human. DR AGR; HGNC:10702; -. DR CTD; 10483; -. DR DisGeNET; 10483; -. DR GeneCards; SEC23B; -. DR HGNC; HGNC:10702; SEC23B. DR HPA; ENSG00000101310; Low tissue specificity. DR MalaCards; SEC23B; -. DR MIM; 224100; phenotype. DR MIM; 610512; gene. DR MIM; 616858; phenotype. DR neXtProt; NX_Q15437; -. DR OpenTargets; ENSG00000101310; -. DR Orphanet; 98873; Congenital dyserythropoietic anemia type II. DR Orphanet; 201; Cowden syndrome. DR PharmGKB; PA35625; -. DR VEuPathDB; HostDB:ENSG00000101310; -. DR eggNOG; KOG1986; Eukaryota. DR GeneTree; ENSGT00390000006916; -. DR HOGENOM; CLU_008658_3_0_1; -. DR InParanoid; Q15437; -. DR OMA; PWNIIPV; -. DR OrthoDB; 5474700at2759; -. DR PhylomeDB; Q15437; -. DR TreeFam; TF300693; -. DR PathwayCommons; Q15437; -. DR SignaLink; Q15437; -. DR SIGNOR; Q15437; -. DR BioGRID-ORCS; 10483; 46 hits in 1164 CRISPR screens. DR ChiTaRS; SEC23B; human. DR GeneWiki; SEC23B; -. DR GenomeRNAi; 10483; -. DR Pharos; Q15437; Tbio. DR PRO; PR:Q15437; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q15437; Protein. DR Bgee; ENSG00000101310; Expressed in endothelial cell and 195 other cell types or tissues. DR ExpressionAtlas; Q15437; baseline and differential. DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0012505; C:endomembrane system; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR CDD; cd01478; Sec23-like; 1. DR CDD; cd11287; Sec23_C; 1. DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1. DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1. DR Gene3D; 3.40.20.10; Severin; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1. DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR007123; Gelsolin-like_dom. DR InterPro; IPR036180; Gelsolin-like_dom_sf. DR InterPro; IPR037364; Sec23. DR InterPro; IPR006900; Sec23/24_helical_dom. DR InterPro; IPR036175; Sec23/24_helical_dom_sf. DR InterPro; IPR006896; Sec23/24_trunk_dom. DR InterPro; IPR012990; Sec23_24_beta_S. DR InterPro; IPR037550; Sec23_C. DR InterPro; IPR036465; vWFA_dom_sf. DR InterPro; IPR006895; Znf_Sec23_Sec24. DR InterPro; IPR036174; Znf_Sec23_Sec24_sf. DR PANTHER; PTHR11141; PROTEIN TRANSPORT PROTEIN SEC23; 1. DR PANTHER; PTHR11141:SF10; PROTEIN TRANSPORT PROTEIN SEC23B; 1. DR Pfam; PF00626; Gelsolin; 1. DR Pfam; PF08033; Sec23_BS; 1. DR Pfam; PF04815; Sec23_helical; 1. DR Pfam; PF04811; Sec23_trunk; 1. DR Pfam; PF04810; zf-Sec23_Sec24; 1. DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1. DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1. DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1. DR Genevisible; Q15437; HS. PE 1: Evidence at protein level; KW Acetylation; Congenital dyserythropoietic anemia; Cytoplasm; KW Cytoplasmic vesicle; Disease variant; Endoplasmic reticulum; KW ER-Golgi transport; Hereditary hemolytic anemia; Membrane; Metal-binding; KW Protein transport; Reference proteome; Transport; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..767 FT /note="Protein transport protein Sec23B" FT /id="PRO_0000205148" FT REPEAT 634..720 FT /note="Gelsolin-like" FT /evidence="ECO:0000255" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q15436" FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q15436" FT BINDING 85 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q15436" FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q15436" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 564 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D662" FT VARIANT 14 FT /note="R -> W (in CDAN2; the mutant protein is unstable FT with less than 5% of protein detectable compared to FT wild-type; dbSNP:rs121918222)" FT /evidence="ECO:0000269|PubMed:19561605, FT ECO:0000269|PubMed:19621418, ECO:0000269|PubMed:33159567" FT /id="VAR_062294" FT VARIANT 18 FT /note="R -> H (in dbSNP:rs905074313)" FT /evidence="ECO:0000269|PubMed:19561605" FT /id="VAR_062295" FT VARIANT 109 FT /note="E -> K (in CDAN2; the mutant protein is unstable FT with less than 5% of protein detectable compared to FT wild-type; dbSNP:rs121918221)" FT /evidence="ECO:0000269|PubMed:19561605, FT ECO:0000269|PubMed:19621418" FT /id="VAR_062296" FT VARIANT 164 FT /note="V -> L (in CWS7; uncertain significance; FT dbSNP:rs36023150)" FT /evidence="ECO:0000269|PubMed:26522472" FT /id="VAR_076424" FT VARIANT 239 FT /note="D -> G (in CDAN2; uncertain significance; the mutant FT protein is expressed as the wild-type; dbSNP:rs761034212)" FT /evidence="ECO:0000269|PubMed:19561605, FT ECO:0000269|PubMed:33159567" FT /id="VAR_062297" FT VARIANT 313 FT /note="R -> H (in dbSNP:rs750888081)" FT /evidence="ECO:0000269|PubMed:19561605" FT /id="VAR_062298" FT VARIANT 318 FT /note="I -> T (in dbSNP:rs953079477)" FT /evidence="ECO:0000269|PubMed:19561605" FT /id="VAR_062299" FT VARIANT 348 FT /note="D -> A (in CDAN2)" FT /evidence="ECO:0000269|PubMed:19621418" FT /id="VAR_062300" FT VARIANT 373 FT /note="M -> V (in dbSNP:rs17849992)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_062301" FT VARIANT 386 FT /note="Q -> R" FT /evidence="ECO:0000269|PubMed:19561605" FT /id="VAR_062302" FT VARIANT 426 FT /note="V -> I (in dbSNP:rs41309927)" FT /evidence="ECO:0000269|PubMed:19561605" FT /id="VAR_062303" FT VARIANT 433 FT /note="P -> L (in dbSNP:rs17807673)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_034482" FT VARIANT 436 FT /note="S -> L (in CDAN2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33159567" FT /id="VAR_086961" FT VARIANT 462 FT /note="Y -> C (in dbSNP:rs780978419)" FT /evidence="ECO:0000269|PubMed:19561605" FT /id="VAR_062304" FT VARIANT 489 FT /note="H -> Q (in dbSNP:rs2273526)" FT /evidence="ECO:0000269|PubMed:19621418, FT ECO:0000269|PubMed:8898360" FT /id="VAR_020318" FT VARIANT 497 FT /note="R -> C (in CDAN2; uncertain significance; FT dbSNP:rs727504145)" FT /evidence="ECO:0000269|PubMed:19561605, FT ECO:0000269|PubMed:19621418" FT /id="VAR_062305" FT VARIANT 524 FT /note="A -> V (in dbSNP:rs398124225)" FT /evidence="ECO:0000269|PubMed:19561605" FT /id="VAR_062306" FT VARIANT 530 FT /note="R -> W (in CDAN2; dbSNP:rs121918223)" FT /evidence="ECO:0000269|PubMed:19561605" FT /id="VAR_062307" FT VARIANT 554..767 FT /note="Missing (in CDAN2)" FT /evidence="ECO:0000269|PubMed:33159567" FT /id="VAR_086962" FT VARIANT 594 FT /note="V -> G (in CWS7; aberrant aggregation; causes FT mislocalization of the protein in the cytoplasm; reduces FT interaction with SAR1A; confers endoplasmic reticulum (ER) FT stress-mediated cell growth advantage; dbSNP:rs752366963)" FT /evidence="ECO:0000269|PubMed:26522472" FT /id="VAR_076425" FT VARIANT 603 FT /note="S -> L (in CDAN2)" FT /evidence="ECO:0000269|PubMed:19621418" FT /id="VAR_062308" FT VARIANT 701 FT /note="R -> C (in CDAN2; dbSNP:rs201270568)" FT /evidence="ECO:0000269|PubMed:19621418" FT /id="VAR_062309" SQ SEQUENCE 767 AA; 86479 MW; 1A00DE39D56B0204 CRC64; MATYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPLAC LLTPLKERPD LPPVQYEPVL CSRPTCKAVL NPLCQVDYRA KLWACNFCFQ RNQFPPAYGG ISEVNQPAEL MPQFSTIEYV IQRGAQSPLI FLYVVDTCLE EDDLQALKES LQMSLSLLPP DALVGLITFG RMVQVHELSC EGISKSYVFR GTKDLTAKQI QDMLGLTKPA MPMQQARPAQ PQEHPFASSR FLQPVHKIDM NLTDLLGELQ RDPWPVTQGK RPLRSTGVAL SIAVGLLEGT FPNTGARIML FTGGPPTQGP GMVVGDELKI PIRSWHDIEK DNARFMKKAT KHYEMLANRT AANGHCIDIY ACALDQTGLL EMKCCANLTG GYMVMGDSFN TSLFKQTFQR IFTKDFNGDF RMAFGATLDV KTSRELKIAG AIGPCVSLNV KGPCVSENEL GVGGTSQWKI CGLDPTSTLG IYFEVVNQHN TPIPQGGRGA IQFVTHYQHS STQRRIRVTT IARNWADVQS QLRHIEAAFD QEAAAVLMAR LGVFRAESEE GPDVLRWLDR QLIRLCQKFG QYNKEDPTSF RLSDSFSLYP QFMFHLRRSP FLQVFNNSPD ESSYYRHHFA RQDLTQSLIM IQPILYSYSF HGPPEPVLLD SSSILADRIL LMDTFFQIVI YLGETIAQWR KAGYQDMPEY ENFKHLLQAP LDDAQEILQA RFPMPRYINT EHGGSQARFL LSKVNPSQTH NNLYAWGQET GAPILTDDVS LQVFMDHLKK LAVSSAC //