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RecName: Full=Protein transport protein Sec24C; AltName: Full=SEC24-related protein C

UniProtKB/Swiss-Prot: P53992.3

Identical Proteins FASTA Graphics 

LOCUS       SC24C_HUMAN             1094 aa            linear   PRI 27-NOV-2024
DEFINITION  RecName: Full=Protein transport protein Sec24C; AltName:
            Full=SEC24-related protein C.
ACCESSION   P53992
VERSION     P53992.3
DBSOURCE    UniProtKB: locus SC24C_HUMAN, accession P53992;
            class: standard.
            extra accessions:B4DZT4,Q8WV25
            created: Oct 1, 1996.
            sequence updated: Sep 1, 2009.
            annotation updated: Nov 27, 2024.
            xrefs: D38555.1, BAA07558.2, AK303085.1, BAG64196.1, AC022400.9,
            BC018928.2, AAH18928.1, NP_004913.2, NP_940999.1, 3EH2_A, 3EH2_B,
            3EH2_C, 6PU1_B, 8CL3_B
            xrefs (non-sequence databases): CCDS:CCDS7332.1, PDBsum:3EH2,
            PDBsum:6PU1, PDBsum:8CL3, AlphaFoldDB:P53992, EMDB:EMD-16711,
            SMR:P53992, BioGRID:114991, ComplexPortal:CPX-2360, DIP:DIP-30981N,
            IntAct:P53992, MINT:P53992, STRING:9606.ENSP00000343405,
            GlyCosmos:P53992, GlyGen:P53992, iPTMnet:P53992, MetOSite:P53992,
            PhosphoSitePlus:P53992, SwissPalm:P53992, BioMuta:SEC24C,
            DMDM:257051070, jPOST:P53992, MassIVE:P53992,
            PaxDb:9606-ENSP00000343405, PeptideAtlas:P53992, ProteomicsDB:5623,
            ProteomicsDB:56640, Pumba:P53992, Antibodypedia:45407, DNASU:9632,
            Ensembl:ENST00000339365.2, Ensembl:ENSP00000343405.2,
            Ensembl:ENSG00000176986.16, Ensembl:ENST00000345254.9,
            Ensembl:ENSP00000321845.6, GeneID:9632, KEGG:hsa:9632,
            MANE-Select:ENST00000345254.9, UCSC:uc001juw.4, AGR:HGNC:10705,
            CTD:9632, DisGeNET:9632, GeneCards:SEC24C, HGNC:10705,
            HPA:ENSG00000176986, MalaCards:SEC24C, MIM 607185,
            neXtProt:NX_P53992, OpenTargets:ENSG00000176986, Orphanet:567,
            PharmGKB:PA35628, VEuPathDB:HostDB:ENSG00000176986, eggNOG:KOG1984,
            GeneTree:ENSGT01060000248649, HOGENOM:CLU_004589_1_1_1,
            InParanoid:P53992, OMA:INPFMTF, OrthoDB:977017at2759,
            PhylomeDB:P53992, TreeFam:TF300464, PathwayCommons:P53992,
            Reactome:R-HSA-1655829, Reactome:R-HSA-204005,
            Reactome:R-HSA-2132295, Reactome:R-HSA-5694530,
            Reactome:R-HSA-9705671, Reactome:R-HSA-983170, SignaLink:P53992,
            SIGNOR:P53992, BioGRID-ORCS:9632, ChiTaRS:SEC24C,
            EvolutionaryTrace:P53992, GeneWiki:SEC24C, GenomeRNAi:9632,
            Pharos:P53992, PRO:PR:P53992, Proteomes:UP000005640, RNAct:P53992,
            Bgee:ENSG00000176986, ExpressionAtlas:P53992, GO:0030127,
            GO:0005829, GO:0070971, GO:0005789, GO:0012507, GO:0000149,
            GO:0008270, GO:0090110, GO:0006888, GO:0001701, GO:0006886,
            CDD:cd01479, FunFam:1.20.120.730:FF:000002,
            FunFam:3.40.20.10:FF:000023, FunFam:3.40.50.410:FF:000020,
            FunFam:2.30.30.380:FF:000003, Gene3D:2.60.40.1670,
            Gene3D:1.20.120.730, Gene3D:3.40.20.10, Gene3D:3.40.50.410,
            Gene3D:2.30.30.380, InterPro:IPR029006, InterPro:IPR007123,
            InterPro:IPR036180, InterPro:IPR006900, InterPro:IPR036175,
            InterPro:IPR006896, InterPro:IPR012990, InterPro:IPR050550,
            InterPro:IPR041742, InterPro:IPR036465, InterPro:IPR006895,
            InterPro:IPR036174, PANTHER:PTHR13803:SF5, PANTHER:PTHR13803,
            Pfam:PF00626, Pfam:PF08033, Pfam:PF04815, Pfam:PF04811,
            Pfam:PF04810, SUPFAM:SSF81995, SUPFAM:SSF82754, SUPFAM:SSF81811,
            SUPFAM:SSF53300, SUPFAM:SSF82919
KEYWORDS    3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
            Endoplasmic reticulum; ER-Golgi transport; Membrane; Metal-binding;
            Phosphoprotein; Protein transport; Proteomics identification;
            Reference proteome; Transport; Zinc.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
            Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. II.
            The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
            analysis of cDNA clones from human cell line KG-1
  JOURNAL   DNA Res 1 (5), 223-229 (1994)
   PUBMED   7584044
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).;
            TISSUE=Bone marrow
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   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. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).;
            TISSUE=Thymus
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   4  (residues 1 to 1094)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
            SER-109.;
            TISSUE=Muscle
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   5  (residues 1 to 1094)
  AUTHORS   Tani,K., Oyama,Y., Hatsuzawa,K. and Tagaya,M.
  TITLE     Hypothetical protein KIAA0079 is a mammalian homologue of yeast
            Sec24p
  JOURNAL   FEBS Lett 447 (2-3), 247-250 (1999)
   PUBMED   10214955
  REMARK    FUNCTION, AND SUBUNIT.
REFERENCE   6  (residues 1 to 1094)
  AUTHORS   Tang,B.L., Kausalya,J., Low,D.Y., Lock,M.L. and Hong,W.
  TITLE     A family of mammalian proteins homologous to yeast Sec24p
  JOURNAL   Biochem Biophys Res Commun 258 (3), 679-684 (1999)
   PUBMED   10329445
  REMARK    SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
REFERENCE   7  (residues 1 to 1094)
  AUTHORS   Pagano,A., Letourneur,F., Garcia-Estefania,D., Carpentier,J.L.,
            Orci,L. and Paccaud,J.P.
  TITLE     Sec24 proteins and sorting at the endoplasmic reticulum
  JOURNAL   J Biol Chem 274 (12), 7833-7840 (1999)
   PUBMED   10075675
  REMARK    SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
REFERENCE   8  (residues 1 to 1094)
  AUTHORS   Iinuma,T., Shiga,A., Nakamoto,K., O'Brien,M.B., Aridor,M.,
            Arimitsu,N., Tagaya,M. and Tani,K.
  TITLE     Mammalian Sec16/p250 plays a role in membrane traffic from the
            endoplasmic reticulum
  JOURNAL   J Biol Chem 282 (24), 17632-17639 (2007)
   PUBMED   17428803
  REMARK    INTERACTION WITH DDHD1.
REFERENCE   9  (residues 1 to 1094)
  AUTHORS   Mancias,J.D. and Goldberg,J.
  TITLE     The transport signal on Sec22 for packaging into COPII-coated
            vesicles is a conformational epitope
  JOURNAL   Mol Cell 26 (3), 403-414 (2007)
   PUBMED   17499046
  REMARK    FUNCTION, AND SUBUNIT.
REFERENCE   10 (residues 1 to 1094)
  AUTHORS   Dephoure,N., Zhou,C., Villen,J., Beausoleil,S.A., Bakalarski,C.E.,
            Elledge,S.J. and Gygi,S.P.
  TITLE     A quantitative atlas of mitotic phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 105 (31), 10762-10767 (2008)
   PUBMED   18669648
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Cervix carcinoma
REFERENCE   11 (residues 1 to 1094)
  AUTHORS   Bonnon,C., Wendeler,M.W., Paccaud,J.P. and Hauri,H.P.
  TITLE     Selective export of human GPI-anchored proteins from the
            endoplasmic reticulum
  JOURNAL   J Cell Sci 123 (Pt 10), 1705-1715 (2010)
   PUBMED   20427317
  REMARK    FUNCTION, AND INTERACTION WITH TMED2 AND TMED10.
REFERENCE   12 (residues 1 to 1094)
  AUTHORS   Burkard,T.R., Planyavsky,M., Kaupe,I., Breitwieser,F.P.,
            Burckstummer,T., Bennett,K.L., Superti-Furga,G. and Colinge,J.
  TITLE     Initial characterization of the human central proteome
  JOURNAL   BMC Syst Biol 5, 17 (2011)
   PUBMED   21269460
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
            Publication Status: Online-Only
REFERENCE   13 (residues 1 to 1094)
  AUTHORS   Zhou,H., Di Palma,S., Preisinger,C., Peng,M., Polat,A.N., Heck,A.J.
            and Mohammed,S.
  TITLE     Toward a comprehensive characterization of a human cancer cell
            phosphoproteome
  JOURNAL   J Proteome Res 12 (1), 260-271 (2013)
   PUBMED   23186163
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Erythroleukemia
REFERENCE   14 (residues 1 to 1094)
  AUTHORS   Bian,Y., Song,C., Cheng,K., Dong,M., Wang,F., Huang,J., Sun,D.,
            Wang,L., Ye,M. and Zou,H.
  TITLE     An enzyme assisted RP-RPLC approach for in-depth analysis of human
            liver phosphoproteome
  JOURNAL   J Proteomics 96, 253-262 (2014)
   PUBMED   24275569
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Liver
REFERENCE   15 (residues 1 to 1094)
  AUTHORS   Vaca Jacome,A.S., Rabilloud,T., Schaeffer-Reiss,C., Rompais,M.,
            Ayoub,D., Lane,L., Bairoch,A., Van Dorsselaer,A. and Carapito,C.
  TITLE     N-terminome analysis of the human mitochondrial proteome
  JOURNAL   Proteomics 15 (14), 2519-2524 (2015)
   PUBMED   25944712
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
REFERENCE   16 (residues 1 to 1094)
  AUTHORS   Gui,X., Yang,H., Li,T., Tan,X., Shi,P., Li,M., Du,F. and Chen,Z.J.
  TITLE     Autophagy induction via STING trafficking is a primordial function
            of the cGAS pathway
  JOURNAL   Nature 567 (7747), 262-266 (2019)
   PUBMED   30842662
  REMARK    INTERACTION WITH STING1.
REFERENCE   17 (residues 1 to 1094)
  AUTHORS   Mancias,J.D. and Goldberg,J.
  TITLE     Structural basis of cargo membrane protein discrimination by the
            human COPII coat machinery
  JOURNAL   EMBO J 27 (21), 2918-2928 (2008)
   PUBMED   18843296
  REMARK    X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 329-1094 IN COMPLEX WITH
            ZINC, FUNCTION, INTERACTION WITH GOSR2 AND STX5, AND MUTAGENESIS OF
            895-LEU--LEU-897.
COMMENT     On Sep 1, 2009 this sequence version replaced P53992.2.
            [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 (PubMed:10214955, PubMed:17499046, PubMed:18843296,
            PubMed:20427317). Plays a central role in cargo selection within
            the COPII complex and together with SEC24D may have a different
            specificity compared to SEC24A and SEC24B (PubMed:17499046,
            PubMed:18843296, PubMed:20427317). May more specifically package
            GPI-anchored proteins through the cargo receptor TMED10
            (PubMed:20427317). May also be specific for IxM motif-containing
            cargos like the SNAREs GOSR2 and STX5 (PubMed:18843296).
            {ECO:0000269|PubMed:10214955, ECO:0000269|PubMed:17499046,
            ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
            [SUBUNIT] COPII is composed of at least five proteins: the Sec23/24
            complex, the Sec13/31 complex and Sar1 (PubMed:10075675,
            PubMed:10214955, PubMed:17499046). Interacts with TMED2 and TMED10
            (PubMed:20427317). Interacts with GOSR2 (via IxM motif) and STX5
            (via IxM motif); recruits GOSR2 and STX5 into COPII-coated vesicles
            (PubMed:18843296). Interacts with DDHD1 (PubMed:17428803).
            Interacts with STING1; promoting STING1 translocation to the COPII
            vesicles (PubMed:30842662). {ECO:0000269|PubMed:10075675,
            ECO:0000269|PubMed:10214955, ECO:0000269|PubMed:17428803,
            ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296,
            ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:30842662}.
            [INTERACTION] P53992; P00540: MOS; NbExp=4; IntAct=EBI-81134,
            EBI-1757866; P53992; Q15436: SEC23A; NbExp=8; IntAct=EBI-81134,
            EBI-81088; P53992; Q15437: SEC23B; NbExp=5; IntAct=EBI-81134,
            EBI-742673; P53992; O43516: WIPF1; NbExp=3; IntAct=EBI-81134,
            EBI-346356.
            [SUBCELLULAR LOCATION] Cytoplasmic vesicle, COPII-coated vesicle
            membrane {ECO:0000269|PubMed:10075675,
            ECO:0000269|PubMed:10329445}; Peripheral membrane protein
            {ECO:0000269|PubMed:10075675}; Cytoplasmic side
            {ECO:0000269|PubMed:10075675}. Endoplasmic reticulum membrane
            {ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:10329445};
            Peripheral membrane protein {ECO:0000269|PubMed:10075675};
            Cytoplasmic side {ECO:0000269|PubMed:10075675}. Cytoplasm, cytosol
            {ECO:0000269|PubMed:10075675}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=1; IsoId=P53992-1; Sequence=Displayed; Name=2;
            IsoId=P53992-2; Sequence=VSP_056516.
            [TISSUE SPECIFICITY] Ubiquitous. {ECO:0000269|PubMed:10329445}.
            [SIMILARITY] Belongs to the SEC23/SEC24 family. SEC24 subfamily.
            {ECO:0000305}.
            [SEQUENCE CAUTION] Sequence=BAA07558.2; Type=Frameshift;
            Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..1094
                     /gene="SEC24C"
                     /gene_synonym="KIAA0079"
     Protein         1..1094
                     /product="Protein transport protein Sec24C"
                     /note="SEC24-related protein C"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..1094
                     /region_name="Mature chain"
                     /note="Protein transport protein Sec24C.
                     /id=PRO_0000205156."
     Region          1..752
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:14702039. /id=VSP_056516."
     Region          1..338
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          <4..329
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          20..34
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          50..73
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          86..107
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          109
                     /region_name="Variant"
                     /note="P -> S (in dbSNP:rs17851695).
                     /evidence=ECO:0000269|PubMed:15489334. /id=VAR_058690."
     Region          115..129
                     /region_name="Compositionally biased region"
                     /note="Pro residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          131..145
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          161..218
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          181..1090
                     /region_name="COG5028"
                     /note="Vesicle coat complex COPII, subunit SEC24/subunit
                     SFB2/subunit SFB3 [Intracellular trafficking and
                     secretion]"
                     /db_xref="CDD:227361"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648."
     Region          236..255
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          261..275
                     /region_name="Compositionally biased region"
                     /note="Pro residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          276..290
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          305..324
                     /region_name="Compositionally biased region"
                     /note="Pro residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          331..340
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          343..346
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          362..364
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          366..368
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          371..373
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          374..384
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          385..391
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          395..399
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          413..415
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          418..420
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          425..450
                     /region_name="Region of interest in the sequence"
                     /note="Zinc finger-like."
     Region          426..428
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          437..439
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          440..442
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          444..446
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          448..450
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          453..455
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          458..461
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          462..466
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          467..469
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          477..480
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          482..487
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          490..492
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          494..496
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          503..509
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          512..516
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          519..530
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          531..533
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          546..560
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          569..573
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          576..578
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          587..589
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          591..594
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          595..609
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          620..632
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          637..643
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          649..651
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          661..663
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          669..672
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          679..689
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          692..698
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          706..709
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          711..715
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          720..722
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          728..744
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          747..757
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          761..769
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          773..776
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          778..784
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          789..797
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          801..803
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          805..814
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          820..834
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          835..840
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          844..858
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          859..861
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          864..885
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Site            895..897
                     /site_type="mutagenized"
                     /note="LIL->AAA: Loss of packaging into COPII-coated
                     vesicles of the IxM motif-containing cargos GOSR2 and
                     STX5. /evidence=ECO:0000269|PubMed:18843296."
     Region          899..901
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          904..912
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          915..917
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          925..937
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          934
                     /region_name="Variant"
                     /note="L -> P (in dbSNP:rs16930872). /id=VAR_057174."
     Region          940..947
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          950..953
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          962..1034
                     /region_name="Repetitive region"
                     /note="Gelsolin-like. /evidence=ECO:0000255."
     Region          972..974
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          980..984
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          986..993
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          999..1006
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          1011..1013
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          1027..1040
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          1043..1045
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          1048..1056
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          1059..1063
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          1072..1074
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
     Region          1078..1092
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3EH2."
ORIGIN      
        1 mnvnqsvppv ppfgqpqpiy pgyhqssygg qsgstapaip ygayngpvpg yqqtppqgms
       61 rappssgapp astaqapcgq aaygqfgqgd vqngpsstvq mqrlpgsqpf gsplapvgnq
      121 ppvlqpygpp ptsaqvatql sgmqisgava pappssglgf gpptslasas gsfpnsglyg
      181 sypqgqappl sqaqghpgiq tpqrsapsqa ssftppasgg prlpsmtgpl lpgqsfggps
      241 vsqpnhvssp pqalppgtqm tgplgplppm hspqqpgyqp qqngsfgpar gpqsnyggpy
      301 paaptfgsqp gppqplppkr ldpdaipspi qvieddrnnr gtepfvtgvr gqvpplvttn
      361 flvkdqgnas pryirctsyn ipctsdmakq aqvplaavik plarlppeea spyvvdhges
      421 gplrcnrcka ymcpfmqfie ggrrfqccfc scindvppqy fqhldhtgkr vdaydrpels
      481 lgsyeflatv dycknnkfps ppafifmidv synairtglv rllceelksl ldflpregga
      541 eesairvgfv tynkvlhfyn vksslaqpqm mvvsdvadmf vplldgflvn vnesravits
      601 lldqipemfa dtretetvfv pviqagmeal kaaecagklf lfhtslpiae apgklknrdd
      661 rklintdkek tlfqpqtgay qtlakecvaq gccvdlflfp nqyvdvatls vvpqltggsv
      721 ykyasfqven dqerflsdlr rdvqkvvgfd avmrvrtstg iravdffgaf ymsnttdvel
      781 agldgdktvt vefkhddrln eesgallqca llytscagqr rlrihnlaln cctqladlyr
      841 ncetdtliny makfayrgvl nspvkavrdt litqcaqila cyrkncasps sagqlilpec
      901 mkllpvylnc vlksdvlqpg aevttddray vrqlvtsmdv tetnvffypr llpltkspve
      961 stteppavra seerlsngdi yllenglnlf lwvgasvqqg vvqslfsvss fsqitsglsv
     1021 lpvldnplsk kvrglidslr aqrsrymklt vvkqedkmem lfkhflvedk slsggasyvd
     1081 flchmhkeir qlls
//
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Protein 3D Structure

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