Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

  1. zinc ion binding Source: InterPro

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  3. cellular protein metabolic process Source: Reactome
  4. COPII vesicle coating Source: Reactome
  5. ER to Golgi vesicle-mediated transport Source: Reactome
  6. intracellular protein transport Source: InterPro
  7. membrane organization Source: Reactome
  8. post-translational protein modification Source: Reactome
  9. protein N-linked glycosylation via asparagine Source: Reactome
  10. small molecule metabolic process Source: Reactome
  11. vesicle-mediated transport Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_75795. 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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:10701. SEC23A.

Subcellular locationi

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

GO - Cellular componenti

  1. COPII vesicle coat Source: InterPro
  2. cytosol Source: Reactome
  3. endoplasmic reticulum Source: ProtInc
  4. endoplasmic reticulum membrane Source: Reactome
  5. ER to Golgi transport vesicle membrane Source: Reactome
  6. Golgi membrane Source: UniProtKB-SubCell
  7. perinuclear region of cytoplasm Source: Ensembl
  8. smooth endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Craniolenticulosutural dysplasia1 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti382 – 3821F → L in CLSD; loss of function mutation; cargo proteins retained in the endoplasmic reticulum. 1 Publication
VAR_031030

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi607812. phenotype.
Orphaneti50814. Craniolenticulosutural dysplasia.
PharmGKBiPA35624.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 765764Protein transport protein Sec23APRO_0000205146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine2 Publications
Modified residuei308 – 3081Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15436.
PaxDbiQ15436.
PRIDEiQ15436.

PTM databases

PhosphoSiteiQ15436.

Expressioni

Gene expression databases

BgeeiQ15436.
CleanExiHS_SEC23A.
ExpressionAtlasiQ15436. baseline and differential.
GenevestigatoriQ15436.

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. 67 interactions.
IntActiQ15436. 26 interactions.
MINTiMINT-4998885.
STRINGi9606.ENSP00000306881.

Structurei

Secondary structure

1
765
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1512Combined sources
Beta strandi16 – 249Combined sources
Helixi28 – 314Combined sources
Beta strandi39 – 424Combined sources
Turni64 – 663Combined sources
Beta strandi74 – 774Combined sources
Turni78 – 814Combined sources
Beta strandi82 – 843Combined sources
Beta strandi86 – 883Combined sources
Beta strandi91 – 933Combined sources
Helixi96 – 983Combined sources
Helixi102 – 1054Combined sources
Helixi108 – 1103Combined sources
Helixi112 – 1143Combined sources
Beta strandi115 – 1217Combined sources
Beta strandi130 – 1367Combined sources
Helixi141 – 15515Combined sources
Beta strandi163 – 17917Combined sources
Turni181 – 1833Combined sources
Beta strandi185 – 1906Combined sources
Helixi198 – 2047Combined sources
Beta strandi228 – 2325Combined sources
Helixi233 – 24614Combined sources
Helixi264 – 27815Combined sources
Beta strandi285 – 2928Combined sources
Beta strandi296 – 2994Combined sources
Helixi313 – 3175Combined sources
Helixi324 – 34118Combined sources
Beta strandi344 – 3507Combined sources
Helixi357 – 3604Combined sources
Helixi362 – 3665Combined sources
Beta strandi371 – 3755Combined sources
Beta strandi377 – 3793Combined sources
Helixi380 – 3889Combined sources
Beta strandi401 – 41010Combined sources
Beta strandi414 – 4229Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi439 – 4424Combined sources
Beta strandi444 – 4518Combined sources
Beta strandi457 – 4637Combined sources
Beta strandi467 – 4693Combined sources
Beta strandi477 – 48711Combined sources
Beta strandi488 – 4903Combined sources
Beta strandi492 – 50110Combined sources
Helixi506 – 5083Combined sources
Helixi509 – 5157Combined sources
Helixi519 – 53416Combined sources
Helixi542 – 55716Combined sources
Beta strandi558 – 5614Combined sources
Helixi565 – 5673Combined sources
Turni572 – 5765Combined sources
Helixi577 – 58610Combined sources
Turni588 – 5903Combined sources
Helixi592 – 5943Combined sources
Helixi597 – 60711Combined sources
Helixi612 – 6198Combined sources
Beta strandi622 – 6265Combined sources
Beta strandi628 – 6314Combined sources
Beta strandi633 – 6353Combined sources
Helixi639 – 6413Combined sources
Beta strandi647 – 6515Combined sources
Beta strandi653 – 6608Combined sources
Helixi662 – 6709Combined sources
Turni671 – 6744Combined sources
Helixi676 – 6783Combined sources
Helixi679 – 69820Combined sources
Beta strandi699 – 7013Combined sources
Beta strandi704 – 7096Combined sources
Turni713 – 7153Combined sources
Helixi716 – 7216Combined sources
Helixi749 – 76012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ15436.
SMRiQ15436. Positions 3-762.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15436.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5047.
GeneTreeiENSGT00390000006916.
HOGENOMiHOG000231690.
HOVERGENiHBG055039.
InParanoidiQ15436.
KOiK14006.
OMAiALIMIQP.
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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti623 – 6231L → M in AAH36649 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti211 – 2111L → V.3 Publications
Corresponds to variant rs8018720 [ dbSNP | Ensembl ].
VAR_031029
Natural varianti382 – 3821F → L in CLSD; loss of function mutation; cargo proteins retained in the endoplasmic reticulum. 1 Publication
VAR_031030

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 202202Missing in isoform 2. 1 PublicationVSP_056230Add
BLAST

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_006364.2. [Q15436-1]
UniGeneiHs.272927.

Genome annotation databases

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

Polymorphism databases

DMDMi143811354.

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_006364.2. [Q15436-1]
UniGeneiHs.272927.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ15436.
SMRiQ15436. Positions 3-762.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115747. 67 interactions.
IntActiQ15436. 26 interactions.
MINTiMINT-4998885.
STRINGi9606.ENSP00000306881.

PTM databases

PhosphoSiteiQ15436.

Polymorphism databases

DMDMi143811354.

Proteomic databases

MaxQBiQ15436.
PaxDbiQ15436.
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.1. human. [Q15436-1]

Organism-specific databases

CTDi10484.
GeneCardsiGC14M039501.
H-InvDBHIX0011611.
HGNCiHGNC:10701. SEC23A.
MIMi607812. phenotype.
610511. gene.
neXtProtiNX_Q15436.
Orphaneti50814. Craniolenticulosutural dysplasia.
PharmGKBiPA35624.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5047.
GeneTreeiENSGT00390000006916.
HOGENOMiHOG000231690.
HOVERGENiHBG055039.
InParanoidiQ15436.
KOiK14006.
OMAiALIMIQP.
PhylomeDBiQ15436.
TreeFamiTF300693.

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSiSEC23A. human.
EvolutionaryTraceiQ15436.
GeneWikiiSEC23A.
GenomeRNAii10484.
NextBioi39780.
PROiQ15436.
SOURCEiSearch...

Gene expression databases

BgeeiQ15436.
CleanExiHS_SEC23A.
ExpressionAtlasiQ15436. baseline and differential.
GenevestigatoriQ15436.

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.
SSF82919. SSF82919. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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.
    , 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] (ISOFORMS 1 AND 2), VARIANT VAL-211.
    Tissue: Hippocampus.
  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.
    , 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] (ISOFORM 1), 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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.
  12. "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.

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: March 4, 2015
This is version 144 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

External Data

Dasty 3

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 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.