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Q15436

- SC23A_HUMAN

UniProt

Q15436 - SC23A_HUMAN

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Protein

Protein transport protein Sec23A

Gene
SEC23A
Organism
Homo sapiens (Human)
Status
Reviewed - 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. protein binding Source: IntAct
  2. 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; Peripheral membrane protein Reviewed prediction
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 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.1 Publication
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 – 11Removed1 Publication
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

ArrayExpressiQ15436.
BgeeiQ15436.
CleanExiHS_SEC23A.
GenevestigatoriQ15436.

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.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi115747. 63 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 – 1512
Beta strandi16 – 249
Helixi28 – 314
Beta strandi39 – 424
Turni64 – 663
Beta strandi74 – 774
Turni78 – 814
Beta strandi82 – 843
Beta strandi86 – 883
Beta strandi91 – 933
Helixi96 – 983
Helixi102 – 1054
Helixi108 – 1103
Helixi112 – 1143
Beta strandi115 – 1217
Beta strandi130 – 1367
Helixi141 – 15515
Beta strandi163 – 17917
Turni181 – 1833
Beta strandi185 – 1906
Helixi198 – 2047
Beta strandi228 – 2325
Helixi233 – 24614
Helixi264 – 27815
Beta strandi285 – 2928
Beta strandi296 – 2994
Helixi313 – 3175
Helixi324 – 34118
Beta strandi344 – 3507
Helixi357 – 3604
Helixi362 – 3665
Beta strandi371 – 3755
Beta strandi377 – 3793
Helixi380 – 3889
Beta strandi401 – 41010
Beta strandi414 – 4229
Beta strandi431 – 4333
Beta strandi439 – 4424
Beta strandi444 – 4518
Beta strandi457 – 4637
Beta strandi467 – 4693
Beta strandi477 – 48711
Beta strandi488 – 4903
Beta strandi492 – 50110
Helixi506 – 5083
Helixi509 – 5157
Helixi519 – 53416
Helixi542 – 55716
Beta strandi558 – 5614
Helixi565 – 5673
Turni572 – 5765
Helixi577 – 58610
Turni588 – 5903
Helixi592 – 5943
Helixi597 – 60711
Helixi612 – 6198
Beta strandi622 – 6265
Beta strandi628 – 6314
Beta strandi633 – 6353
Helixi639 – 6413
Beta strandi647 – 6515
Beta strandi653 – 6608
Helixi662 – 6709
Turni671 – 6744
Helixi676 – 6783
Helixi679 – 69820
Beta strandi699 – 7013
Beta strandi704 – 7096
Turni713 – 7153
Helixi716 – 7216
Helixi749 – 76012

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ15436.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5047.
HOGENOMiHOG000231690.
HOVERGENiHBG055039.
InParanoidiQ15436.
KOiK14006.
OMAiQFYLQFL.
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.

Sequencei

Sequence statusi: Complete.

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

Q15436-1 [UniParc]FASTAAdd to Basket

« Hide

MTTYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPVAA LFTPLKERPD    50
LPPIQYEPVL CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPSYAG 100
ISELNQPAEL LPQFSSIEYV VLRGPQMPLI FLYVVDTCME DEDLQALKES 150
MQMSLSLLPP TALVGLITFG RMVQVHELGC EGISKSYVFR GTKDLSAKQL 200
QEMLGLSKVP LTQATRGPQV QQPPPSNRFL QPVQKIDMNL TDLLGELQRD 250
PWPVPQGKRP LRSSGVALSI AVGLLECTFP NTGARIMMFI GGPATQGPGM 300
VVGDELKTPI RSWHDIDKDN AKYVKKGTKH FEALANRAAT TGHVIDIYAC 350
ALDQTGLLEM KCCPNLTGGY MVMGDSFNTS LFKQTFQRVF TKDMHGQFKM 400
GFGGTLEIKT SREIKISGAI GPCVSLNSKG PCVSENEIGT GGTCQWKICG 450
LSPTTTLAIY FEVVNQHNAP IPQGGRGAIQ FVTQYQHSSG QRRIRVTTIA 500
RNWADAQTQI QNIAASFDQE AAAILMARLA IYRAETEEGP DVLRWLDRQL 550
IRLCQKFGEY HKDDPSSFRF SETFSLYPQF MFHLRRSSFL QVFNNSPDES 600
SYYRHHFMRQ DLTQSLIMIQ PILYAYSFSG PPEPVLLDSS SILADRILLM 650
DTFFQILIYH GETIAQWRKS GYQDMPEYEN FRHLLQAPVD DAQEILHSRF 700
PMPRYIDTEH GGSQARFLLS KVNPSQTHNN MYAWGQESGA PILTDDVSLQ 750
VFMDHLKKLA VSSAA 765
Length:765
Mass (Da):86,161
Last modified:March 6, 2007 - v2
Checksum:i128DF9964B253313
GO

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti623 – 6231L → M in AAH36649. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97064 mRNA. Translation: CAA65774.1.
AK312259 mRNA. Translation: BAG35191.1.
AL109628 Genomic DNA. No translation available.
BC036649 mRNA. Translation: AAH36649.1.
CCDSiCCDS9668.1.
PIRiT09574.
RefSeqiNP_006355.2. NM_006364.2.
UniGeneiHs.272927.

Genome annotation databases

EnsembliENST00000307712; ENSP00000306881; ENSG00000100934.
GeneIDi10484.
KEGGihsa:10484.
UCSCiuc001wup.1. human.

Polymorphism databases

DMDMi143811354.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97064 mRNA. Translation: CAA65774.1 .
AK312259 mRNA. Translation: BAG35191.1 .
AL109628 Genomic DNA. No translation available.
BC036649 mRNA. Translation: AAH36649.1 .
CCDSi CCDS9668.1.
PIRi T09574.
RefSeqi NP_006355.2. NM_006364.2.
UniGenei Hs.272927.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NUP X-ray 2.80 A 1-765 [» ]
2NUT X-ray 2.30 A 1-765 [» ]
2YRC NMR - A 57-108 [» ]
2YRD NMR - A 57-108 [» ]
3EFO X-ray 2.70 A 1-765 [» ]
3EG9 X-ray 3.00 A 1-764 [» ]
3EGD X-ray 2.70 A 1-764 [» ]
3EGX X-ray 3.30 A 1-764 [» ]
ProteinModelPortali Q15436.
SMRi Q15436. Positions 3-762.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115747. 63 interactions.
IntActi Q15436. 26 interactions.
MINTi MINT-4998885.
STRINGi 9606.ENSP00000306881.

PTM databases

PhosphoSitei Q15436.

Polymorphism databases

DMDMi 143811354.

Proteomic databases

MaxQBi Q15436.
PaxDbi Q15436.
PRIDEi Q15436.

Protocols and materials databases

DNASUi 10484.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307712 ; ENSP00000306881 ; ENSG00000100934 .
GeneIDi 10484.
KEGGi hsa:10484.
UCSCi uc001wup.1. human.

Organism-specific databases

CTDi 10484.
GeneCardsi GC14M039501.
H-InvDB HIX0011611.
HGNCi HGNC:10701. SEC23A.
HPAi HPA043806.
MIMi 607812. phenotype.
610511. gene.
neXtProti NX_Q15436.
Orphaneti 50814. Craniolenticulosutural dysplasia.
PharmGKBi PA35624.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5047.
HOGENOMi HOG000231690.
HOVERGENi HBG055039.
InParanoidi Q15436.
KOi K14006.
OMAi QFYLQFL.
PhylomeDBi Q15436.
TreeFami TF300693.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi SEC23A. human.
EvolutionaryTracei Q15436.
GeneWikii SEC23A.
GenomeRNAii 10484.
NextBioi 39780.
PROi Q15436.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15436.
Bgeei Q15436.
CleanExi HS_SEC23A.
Genevestigatori Q15436.

Family and domain databases

Gene3Di 3.40.20.10. 1 hit.
3.40.50.410. 1 hit.
InterProi IPR029006. 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 ]
Pfami PF00626. 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 ]
SUPFAMi SSF53300. SSF53300. 1 hit.
SSF81811. SSF81811. 1 hit.
SSF82919. SSF82919. 1 hit.
ProtoNeti Search...

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], 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], 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.
    , 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. 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].
  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.

Entry informationi

Entry nameiSC23A_HUMAN
AccessioniPrimary (citable) accession number: Q15436
Secondary accession number(s): B2R5P4, Q8NE16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 6, 2007
Last modified: September 3, 2014
This is version 138 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

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