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Protein

Protein transport protein Sec23A

Gene

SEC23A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100934-MONOMER.
ReactomeiR-HSA-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein Sec23A
Alternative name(s):
SEC23-related protein A
Gene namesi
Name:SEC23A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:10701. SEC23A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Craniolenticulosutural dysplasia (CLSD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects.
See also OMIM:607812
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031030382F → L in CLSD; loss of function mutation; cargo proteins retained in the endoplasmic reticulum. 1 PublicationCorresponds to variant rs118204000dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi10484.
MalaCardsiSEC23A.
MIMi607812. phenotype.
OpenTargetsiENSG00000100934.
Orphaneti50814. Craniolenticulosutural dysplasia.
PharmGKBiPA35624.

Polymorphism and mutation databases

BioMutaiSEC23A.
DMDMi143811354.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002051462 – 765Protein transport protein Sec23AAdd BLAST764

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Modified residuei308PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15436.
MaxQBiQ15436.
PaxDbiQ15436.
PeptideAtlasiQ15436.
PRIDEiQ15436.

PTM databases

iPTMnetiQ15436.
PhosphoSitePlusiQ15436.
SwissPalmiQ15436.

Expressioni

Gene expression databases

BgeeiENSG00000100934.
CleanExiHS_SEC23A.
ExpressionAtlasiQ15436. baseline and differential.
GenevisibleiQ15436. HS.

Organism-specific databases

HPAiHPA043806.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK16Q005363EBI-81088,EBI-726261
SEC24CP539925EBI-81088,EBI-81134

Protein-protein interaction databases

BioGridi115747. 83 interactors.
IntActiQ15436. 47 interactors.
MINTiMINT-4998885.
STRINGi9606.ENSP00000306881.

Structurei

Secondary structure

1765
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 15Combined sources12
Beta strandi16 – 24Combined sources9
Helixi28 – 31Combined sources4
Beta strandi34 – 36Combined sources3
Beta strandi39 – 42Combined sources4
Beta strandi49 – 51Combined sources3
Turni64 – 66Combined sources3
Beta strandi74 – 77Combined sources4
Turni78 – 81Combined sources4
Beta strandi82 – 84Combined sources3
Beta strandi86 – 88Combined sources3
Beta strandi91 – 93Combined sources3
Helixi96 – 98Combined sources3
Beta strandi103 – 105Combined sources3
Helixi108 – 110Combined sources3
Helixi112 – 114Combined sources3
Beta strandi115 – 121Combined sources7
Beta strandi130 – 136Combined sources7
Helixi141 – 155Combined sources15
Beta strandi163 – 179Combined sources17
Turni181 – 183Combined sources3
Beta strandi185 – 190Combined sources6
Helixi198 – 204Combined sources7
Beta strandi228 – 232Combined sources5
Helixi233 – 246Combined sources14
Helixi264 – 278Combined sources15
Beta strandi285 – 292Combined sources8
Beta strandi296 – 299Combined sources4
Helixi313 – 317Combined sources5
Helixi324 – 341Combined sources18
Beta strandi344 – 350Combined sources7
Helixi357 – 360Combined sources4
Helixi362 – 366Combined sources5
Beta strandi371 – 375Combined sources5
Beta strandi377 – 379Combined sources3
Helixi380 – 388Combined sources9
Beta strandi401 – 410Combined sources10
Beta strandi414 – 422Combined sources9
Beta strandi431 – 433Combined sources3
Beta strandi439 – 442Combined sources4
Beta strandi444 – 451Combined sources8
Beta strandi457 – 463Combined sources7
Beta strandi467 – 469Combined sources3
Beta strandi477 – 487Combined sources11
Beta strandi488 – 490Combined sources3
Beta strandi492 – 501Combined sources10
Helixi506 – 508Combined sources3
Helixi509 – 515Combined sources7
Helixi519 – 534Combined sources16
Helixi542 – 557Combined sources16
Beta strandi558 – 561Combined sources4
Helixi565 – 567Combined sources3
Turni572 – 576Combined sources5
Helixi577 – 586Combined sources10
Turni588 – 590Combined sources3
Helixi592 – 594Combined sources3
Helixi597 – 607Combined sources11
Helixi612 – 619Combined sources8
Beta strandi622 – 626Combined sources5
Beta strandi628 – 631Combined sources4
Beta strandi633 – 635Combined sources3
Helixi639 – 641Combined sources3
Beta strandi647 – 651Combined sources5
Beta strandi653 – 660Combined sources8
Helixi662 – 670Combined sources9
Turni671 – 674Combined sources4
Helixi676 – 678Combined sources3
Helixi679 – 698Combined sources20
Beta strandi699 – 701Combined sources3
Beta strandi704 – 709Combined sources6
Turni713 – 715Combined sources3
Helixi716 – 721Combined sources6
Helixi749 – 760Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5KYNX-ray2.55A/B1-765[»]
5KYUX-ray3.51A1-765[»]
5KYWX-ray3.20A1-765[»]
5KYXX-ray3.52A1-765[»]
5KYYX-ray3.40A1-765[»]
ProteinModelPortaliQ15436.
SMRiQ15436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15436.

Family & Domainsi

Sequence similaritiesi

Belongs to the SEC23/SEC24 family. SEC23 subfamily.Curated

Phylogenomic databases

eggNOGiKOG1986. Eukaryota.
COG5047. LUCA.
GeneTreeiENSGT00390000006916.
HOGENOMiHOG000231690.
HOVERGENiHBG055039.
InParanoidiQ15436.
KOiK14006.
OMAiGDYHKDD.
OrthoDBiEOG091G063R.
PhylomeDBiQ15436.
TreeFamiTF300693.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. 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]
PfamiPF00626. 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]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF81811. SSF81811. 1 hit.
SSF82754. SSF82754. 1 hit.
SSF82919. SSF82919. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15436-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTTYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPVAA LFTPLKERPD
60 70 80 90 100
LPPIQYEPVL CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPSYAG
110 120 130 140 150
ISELNQPAEL LPQFSSIEYV VLRGPQMPLI FLYVVDTCME DEDLQALKES
160 170 180 190 200
MQMSLSLLPP TALVGLITFG RMVQVHELGC EGISKSYVFR GTKDLSAKQL
210 220 230 240 250
QEMLGLSKVP LTQATRGPQV QQPPPSNRFL QPVQKIDMNL TDLLGELQRD
260 270 280 290 300
PWPVPQGKRP LRSSGVALSI AVGLLECTFP NTGARIMMFI GGPATQGPGM
310 320 330 340 350
VVGDELKTPI RSWHDIDKDN AKYVKKGTKH FEALANRAAT TGHVIDIYAC
360 370 380 390 400
ALDQTGLLEM KCCPNLTGGY MVMGDSFNTS LFKQTFQRVF TKDMHGQFKM
410 420 430 440 450
GFGGTLEIKT SREIKISGAI GPCVSLNSKG PCVSENEIGT GGTCQWKICG
460 470 480 490 500
LSPTTTLAIY FEVVNQHNAP IPQGGRGAIQ FVTQYQHSSG QRRIRVTTIA
510 520 530 540 550
RNWADAQTQI QNIAASFDQE AAAILMARLA IYRAETEEGP DVLRWLDRQL
560 570 580 590 600
IRLCQKFGEY HKDDPSSFRF SETFSLYPQF MFHLRRSSFL QVFNNSPDES
610 620 630 640 650
SYYRHHFMRQ DLTQSLIMIQ PILYAYSFSG PPEPVLLDSS SILADRILLM
660 670 680 690 700
DTFFQILIYH GETIAQWRKS GYQDMPEYEN FRHLLQAPVD DAQEILHSRF
710 720 730 740 750
PMPRYIDTEH GGSQARFLLS KVNPSQTHNN MYAWGQESGA PILTDDVSLQ
760
VFMDHLKKLA VSSAA
Length:765
Mass (Da):86,161
Last modified:March 6, 2007 - v2
Checksum:i128DF9964B253313
GO
Isoform 2 (identifier: Q15436-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-202: Missing.

Note: No experimental confirmation available.
Show »
Length:563
Mass (Da):63,101
Checksum:iC50E45D0FC9B7300
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti623L → M in AAH36649 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031029211L → V.3 PublicationsCorresponds to variant rs8018720dbSNPEnsembl.1
Natural variantiVAR_031030382F → L in CLSD; loss of function mutation; cargo proteins retained in the endoplasmic reticulum. 1 PublicationCorresponds to variant rs118204000dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0562301 – 202Missing in isoform 2. 1 PublicationAdd BLAST202

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97064 mRNA. Translation: CAA65774.1.
AK127355 mRNA. Translation: BAG54494.1.
AK312259 mRNA. Translation: BAG35191.1.
AL109628 Genomic DNA. No translation available.
BC036649 mRNA. Translation: AAH36649.1.
CCDSiCCDS9668.1. [Q15436-1]
PIRiT09574.
RefSeqiNP_006355.2. NM_006364.3. [Q15436-1]
UniGeneiHs.272927.

Genome annotation databases

EnsembliENST00000307712; ENSP00000306881; ENSG00000100934. [Q15436-1]
ENST00000537403; ENSP00000444193; ENSG00000100934. [Q15436-2]
GeneIDi10484.
KEGGihsa:10484.
UCSCiuc001wup.2. human. [Q15436-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97064 mRNA. Translation: CAA65774.1.
AK127355 mRNA. Translation: BAG54494.1.
AK312259 mRNA. Translation: BAG35191.1.
AL109628 Genomic DNA. No translation available.
BC036649 mRNA. Translation: AAH36649.1.
CCDSiCCDS9668.1. [Q15436-1]
PIRiT09574.
RefSeqiNP_006355.2. NM_006364.3. [Q15436-1]
UniGeneiHs.272927.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5KYNX-ray2.55A/B1-765[»]
5KYUX-ray3.51A1-765[»]
5KYWX-ray3.20A1-765[»]
5KYXX-ray3.52A1-765[»]
5KYYX-ray3.40A1-765[»]
ProteinModelPortaliQ15436.
SMRiQ15436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115747. 83 interactors.
IntActiQ15436. 47 interactors.
MINTiMINT-4998885.
STRINGi9606.ENSP00000306881.

PTM databases

iPTMnetiQ15436.
PhosphoSitePlusiQ15436.
SwissPalmiQ15436.

Polymorphism and mutation databases

BioMutaiSEC23A.
DMDMi143811354.

Proteomic databases

EPDiQ15436.
MaxQBiQ15436.
PaxDbiQ15436.
PeptideAtlasiQ15436.
PRIDEiQ15436.

Protocols and materials databases

DNASUi10484.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307712; ENSP00000306881; ENSG00000100934. [Q15436-1]
ENST00000537403; ENSP00000444193; ENSG00000100934. [Q15436-2]
GeneIDi10484.
KEGGihsa:10484.
UCSCiuc001wup.2. human. [Q15436-1]

Organism-specific databases

CTDi10484.
DisGeNETi10484.
GeneCardsiSEC23A.
H-InvDBHIX0011611.
HGNCiHGNC:10701. SEC23A.
HPAiHPA043806.
MalaCardsiSEC23A.
MIMi607812. phenotype.
610511. gene.
neXtProtiNX_Q15436.
OpenTargetsiENSG00000100934.
Orphaneti50814. Craniolenticulosutural dysplasia.
PharmGKBiPA35624.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1986. Eukaryota.
COG5047. LUCA.
GeneTreeiENSGT00390000006916.
HOGENOMiHOG000231690.
HOVERGENiHBG055039.
InParanoidiQ15436.
KOiK14006.
OMAiGDYHKDD.
OrthoDBiEOG091G063R.
PhylomeDBiQ15436.
TreeFamiTF300693.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100934-MONOMER.
ReactomeiR-HSA-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSiSEC23A. human.
EvolutionaryTraceiQ15436.
GeneWikiiSEC23A.
GenomeRNAii10484.
PROiQ15436.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100934.
CleanExiHS_SEC23A.
ExpressionAtlasiQ15436. baseline and differential.
GenevisibleiQ15436. HS.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. 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]
PfamiPF00626. 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]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF81811. SSF81811. 1 hit.
SSF82754. SSF82754. 1 hit.
SSF82919. SSF82919. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSC23A_HUMAN
AccessioniPrimary (citable) accession number: Q15436
Secondary accession number(s): B2R5P4, B3KXI2, Q8NE16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 6, 2007
Last modified: November 30, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.