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Q15436 (SC23A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein transport protein Sec23A
Alternative name(s):
SEC23-related protein A
Gene names
Name:SEC23A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length765 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.

Subunit structure

COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and Sar1. Interacts with SEC23IP. Interacts with HTR4 By similarity. Interacts with SLC6A4 By similarity. Interacts with SEC16A. Ref.5

Subcellular location

Smooth endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein Potential. Note: In the ribosome-free transitional face of the ER and associated vesicles.

Involvement in disease

Craniolenticulosutural dysplasia (CLSD) [MIM:607812]: Autosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the SEC23/SEC24 family. SEC23 subfamily.

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCOPII vesicle coating

Traceable author statement. Source: Reactome

ER to Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

membrane organization

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

vesicle-mediated transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentCOPII vesicle coat

Inferred from electronic annotation. Source: InterPro

ER to Golgi transport vesicle membrane

Traceable author statement. Source: Reactome

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Traceable author statement Ref.1. Source: ProtInc

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

smooth endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionzinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDK16Q005363EBI-81088,EBI-726261
SEC24CP539925EBI-81088,EBI-81134

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 765764Protein transport protein Sec23A
PRO_0000205146

Amino acid modifications

Modified residue21N-acetylthreonine Ref.8 Ref.9
Modified residue3081Phosphothreonine Ref.6

Natural variations

Natural variant2111L → V. Ref.1 Ref.2 Ref.4
Corresponds to variant rs8018720 [ dbSNP | Ensembl ].
VAR_031029
Natural variant3821F → L in CLSD; loss of function mutation; cargo proteins retained in the endoplasmic reticulum. Ref.11
VAR_031030

Experimental info

Sequence conflict6231L → M in AAH36649. Ref.4

Secondary structure

................................................................................................................................. 765
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15436 [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: 128DF9964B253313

FASTA76586,161
        10         20         30         40         50         60 
MTTYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPVAA LFTPLKERPD LPPIQYEPVL 

        70         80         90        100        110        120 
CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPSYAG ISELNQPAEL LPQFSSIEYV 

       130        140        150        160        170        180 
VLRGPQMPLI FLYVVDTCME DEDLQALKES MQMSLSLLPP TALVGLITFG RMVQVHELGC 

       190        200        210        220        230        240 
EGISKSYVFR GTKDLSAKQL QEMLGLSKVP LTQATRGPQV QQPPPSNRFL QPVQKIDMNL 

       250        260        270        280        290        300 
TDLLGELQRD PWPVPQGKRP LRSSGVALSI AVGLLECTFP NTGARIMMFI GGPATQGPGM 

       310        320        330        340        350        360 
VVGDELKTPI RSWHDIDKDN AKYVKKGTKH FEALANRAAT TGHVIDIYAC ALDQTGLLEM 

       370        380        390        400        410        420 
KCCPNLTGGY MVMGDSFNTS LFKQTFQRVF TKDMHGQFKM GFGGTLEIKT SREIKISGAI 

       430        440        450        460        470        480 
GPCVSLNSKG PCVSENEIGT GGTCQWKICG LSPTTTLAIY FEVVNQHNAP IPQGGRGAIQ 

       490        500        510        520        530        540 
FVTQYQHSSG QRRIRVTTIA RNWADAQTQI QNIAASFDQE AAAILMARLA IYRAETEEGP 

       550        560        570        580        590        600 
DVLRWLDRQL IRLCQKFGEY HKDDPSSFRF SETFSLYPQF MFHLRRSSFL QVFNNSPDES 

       610        620        630        640        650        660 
SYYRHHFMRQ DLTQSLIMIQ PILYAYSFSG PPEPVLLDSS SILADRILLM DTFFQILIYH 

       670        680        690        700        710        720 
GETIAQWRKS GYQDMPEYEN FRHLLQAPVD DAQEILHSRF PMPRYIDTEH GGSQARFLLS 

       730        740        750        760 
KVNPSQTHNN MYAWGQESGA PILTDDVSLQ VFMDHLKKLA VSSAA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and functional characterization of mammalian homologues of the COPII component Sec23."
Paccaud J.-P., Reith W., Carpentier J.-L., Ravazzola M., Amherdt M., Schekman R., Orci L.
Mol. Biol. Cell 7:1535-1546(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-211.
Tissue: B-cell.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-211.
[3]"The DNA sequence and analysis of human chromosome 14."
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. expand/collapse author list , 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.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-211.
Tissue: Testis.
[5]"Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization."
Bhattacharyya D., Glick B.S.
Mol. Biol. Cell 18:839-849(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEC16A.
Tissue: Liver.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Solution structure of the ZF-SEC23_SEC24 from human SEC23A."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 57-108.
[11]"Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking."
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.
Nat. Genet. 38:1192-1197(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLSD LEU-382, CHARACTERIZATION OF VARIANT CLSD LEU-382.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X97064 mRNA. Translation: CAA65774.1.
AK312259 mRNA. Translation: BAG35191.1.
AL109628 Genomic DNA. No translation available.
BC036649 mRNA. Translation: AAH36649.1.
PIRT09574.
RefSeqNP_006355.2. NM_006364.2.
UniGeneHs.272927.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NUPX-ray2.80A1-765[»]
2NUTX-ray2.30A1-765[»]
2YRCNMR-A57-108[»]
2YRDNMR-A57-108[»]
3EFOX-ray2.70A1-765[»]
3EG9X-ray3.00A1-764[»]
3EGDX-ray2.70A1-764[»]
3EGXX-ray3.30A1-764[»]
ProteinModelPortalQ15436.
SMRQ15436. Positions 3-762.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115747. 62 interactions.
IntActQ15436. 26 interactions.
MINTMINT-4998885.
STRING9606.ENSP00000306881.

PTM databases

PhosphoSiteQ15436.

Polymorphism databases

DMDM143811354.

Proteomic databases

PaxDbQ15436.
PRIDEQ15436.

Protocols and materials databases

DNASU10484.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307712; ENSP00000306881; ENSG00000100934.
GeneID10484.
KEGGhsa:10484.
UCSCuc001wup.1. human.

Organism-specific databases

CTD10484.
GeneCardsGC14M039501.
H-InvDBHIX0011611.
HGNCHGNC:10701. SEC23A.
HPAHPA043806.
MIM607812. phenotype.
610511. gene.
neXtProtNX_Q15436.
Orphanet50814. Craniolenticulosutural dysplasia.
PharmGKBPA35624.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5047.
HOGENOMHOG000231690.
HOVERGENHBG055039.
InParanoidQ15436.
KOK14006.
OMANYTGGYM.
PhylomeDBQ15436.
TreeFamTF300693.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ15436.
BgeeQ15436.
CleanExHS_SEC23A.
GenevestigatorQ15436.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR007123. Gelsolin-like_dom.
IPR006900. Sec23/24_helical_dom.
IPR006896. Sec23/24_trunk_dom.
IPR012990. Sec23_24_beta_S.
IPR002035. VWF_A.
IPR006895. Znf_Sec23_Sec24.
[Graphical view]
PfamPF00626. Gelsolin. 1 hit.
PF08033. Sec23_BS. 1 hit.
PF04815. Sec23_helical. 1 hit.
PF04811. Sec23_trunk. 1 hit.
PF04810. zf-Sec23_Sec24. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
SSF81811. SSF81811. 1 hit.
SSF82919. SSF82919. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSEC23A. human.
EvolutionaryTraceQ15436.
GeneWikiSEC23A.
GenomeRNAi10484.
NextBio39780.
PROQ15436.
SOURCESearch...

Entry information

Entry nameSC23A_HUMAN
AccessionPrimary (citable) accession number: Q15436
Secondary accession number(s): B2R5P4, Q8NE16
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 6, 2007
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM