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Q15437 (SC23B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein transport protein Sec23B
Alternative name(s):
SEC23-related protein B
Gene names
Name:SEC23B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length767 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 By similarity.

Subunit structure

COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and Sar1 By similarity.

Subcellular location

Golgi apparatus membrane By similarity. Endoplasmic reticulum membrane By similarity. Endoplasmic reticulum-Golgi intermediate compartment membrane By similarity.

Involvement in disease

Anemia, congenital dyserythropoietic, 2 (CDAN2) [MIM:224100]: An autosomal recessive blood disorder characterized by morphological abnormalities of erythroblasts, ineffective erythropoiesis, normocytic anemia, iron overload, jaundice, and variable splenomegaly. Ultrastructural features include bi- or multinucleated erythroblasts in bone marrow, karyorrhexis, and the presence of Gaucher-like bone marrow histiocytes. The main biochemical feature of the disease is defective glycosylation of some red blood cells membrane proteins.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9

Sequence similarities

Belongs to the SEC23/SEC24 family. SEC23 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 767766Protein transport protein Sec23B
PRO_0000205148

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.7
Modified residue5641N6-acetyllysine By similarity

Natural variations

Natural variant141R → W in CDAN2; the mutant protein is unstable with less than 5% of protein detectable compared to wild-type. Ref.8 Ref.9
VAR_062294
Natural variant181R → H. Ref.9
VAR_062295
Natural variant1091E → K in CDAN2; the mutant protein is unstable with less than 5% of protein detectable compared to wild-type. Ref.8 Ref.9
VAR_062296
Natural variant2391D → G The mutant protein is expressed as the wild-type. Ref.9
VAR_062297
Natural variant3131R → H. Ref.9
VAR_062298
Natural variant3181I → T. Ref.9
VAR_062299
Natural variant3481D → A in CDAN2. Ref.8
VAR_062300
Natural variant3731M → V. Ref.4
Corresponds to variant rs17849992 [ dbSNP | Ensembl ].
VAR_062301
Natural variant3861Q → R. Ref.9
VAR_062302
Natural variant4261V → I. Ref.9
Corresponds to variant rs41309927 [ dbSNP | Ensembl ].
VAR_062303
Natural variant4331P → L. Ref.4
Corresponds to variant rs17807673 [ dbSNP | Ensembl ].
VAR_034482
Natural variant4621Y → C. Ref.9
VAR_062304
Natural variant4891H → Q. Ref.1 Ref.8
Corresponds to variant rs2273526 [ dbSNP | Ensembl ].
VAR_020318
Natural variant4971R → C in CDAN2; unknown pathological significance. Ref.8 Ref.9
VAR_062305
Natural variant5241A → V. Ref.9
VAR_062306
Natural variant5301R → W in CDAN2. Ref.9
VAR_062307
Natural variant6031S → L in CDAN2. Ref.8
VAR_062308
Natural variant7011R → C in CDAN2. Ref.8
Corresponds to variant rs201270568 [ dbSNP | Ensembl ].
VAR_062309

Sequences

Sequence LengthMass (Da)Tools
Q15437 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 1A00DE39D56B0204

FASTA76786,479
        10         20         30         40         50         60 
MATYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPLAC LLTPLKERPD LPPVQYEPVL 

        70         80         90        100        110        120 
CSRPTCKAVL NPLCQVDYRA KLWACNFCFQ RNQFPPAYGG ISEVNQPAEL MPQFSTIEYV 

       130        140        150        160        170        180 
IQRGAQSPLI FLYVVDTCLE EDDLQALKES LQMSLSLLPP DALVGLITFG RMVQVHELSC 

       190        200        210        220        230        240 
EGISKSYVFR GTKDLTAKQI QDMLGLTKPA MPMQQARPAQ PQEHPFASSR FLQPVHKIDM 

       250        260        270        280        290        300 
NLTDLLGELQ RDPWPVTQGK RPLRSTGVAL SIAVGLLEGT FPNTGARIML FTGGPPTQGP 

       310        320        330        340        350        360 
GMVVGDELKI PIRSWHDIEK DNARFMKKAT KHYEMLANRT AANGHCIDIY ACALDQTGLL 

       370        380        390        400        410        420 
EMKCCANLTG GYMVMGDSFN TSLFKQTFQR IFTKDFNGDF RMAFGATLDV KTSRELKIAG 

       430        440        450        460        470        480 
AIGPCVSLNV KGPCVSENEL GVGGTSQWKI CGLDPTSTLG IYFEVVNQHN TPIPQGGRGA 

       490        500        510        520        530        540 
IQFVTHYQHS STQRRIRVTT IARNWADVQS QLRHIEAAFD QEAAAVLMAR LGVFRAESEE 

       550        560        570        580        590        600 
GPDVLRWLDR QLIRLCQKFG QYNKEDPTSF RLSDSFSLYP QFMFHLRRSP FLQVFNNSPD 

       610        620        630        640        650        660 
ESSYYRHHFA RQDLTQSLIM IQPILYSYSF HGPPEPVLLD SSSILADRIL LMDTFFQIVI 

       670        680        690        700        710        720 
YLGETIAQWR KAGYQDMPEY ENFKHLLQAP LDDAQEILQA RFPMPRYINT EHGGSQARFL 

       730        740        750        760 
LSKVNPSQTH NNLYAWGQET GAPILTDDVS LQVFMDHLKK LAVSSAC 

« 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 GLN-489.
Tissue: B-cell.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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], VARIANTS VAL-373 AND LEU-433.
Tissue: Cervix, Placenta and Uterus.
[5]"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].
[6]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[7]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Congenital dyserythropoietic anemia type II (CDAII) is caused by mutations in the SEC23B gene."
Bianchi P., Fermo E., Vercellati C., Boschetti C., Barcellini W., Iurlo A., Marcello A.P., Righetti P.G., Zanella A.
Hum. Mutat. 30:1292-1298(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDAN2 TRP-14; LYS-109; ALA-348; CYS-497; LEU-603 AND CYS-701, VARIANT GLN-489.
[9]"Mutations affecting the secretory COPII coat component SEC23B cause congenital dyserythropoietic anemia type II."
Schwarz K., Iolascon A., Verissimo F., Trede N.S., Horsley W., Chen W., Paw B.H., Hopfner K.-P., Holzmann K., Russo R., Esposito M.R., Spano D., De Falco L., Heinrich K., Joggerst B., Rojewski M.T., Perrotta S., Denecke J. expand/collapse author list , Pannicke U., Delaunay J., Pepperkok R., Heimpel H.
Nat. Genet. 41:936-940(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDAN2 TRP-14; LYS-109 AND TRP-530, VARIANTS HIS-18; GLY-239; HIS-313; THR-318; ARG-386; ILE-426; CYS-462; CYS-497 AND VAL-524, CHARACTERIZATION OF VARIANTS CDAN2 TRP-14 AND LYS-109, CHARACTERIZATION OF VARIANT GLY-239.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X97065 mRNA. Translation: CAA65775.1.
AL121893, AL121900 Genomic DNA. Translation: CAI12512.1.
AL121900, AL121893 Genomic DNA. Translation: CAH73149.1.
CH471133 Genomic DNA. Translation: EAX10231.1.
CH471133 Genomic DNA. Translation: EAX10232.1.
CH471133 Genomic DNA. Translation: EAX10233.1.
CH471133 Genomic DNA. Translation: EAX10234.1.
CH471133 Genomic DNA. Translation: EAX10235.1.
BC005032 mRNA. Translation: AAH05032.1.
BC005404 mRNA. Translation: AAH05404.1.
BC095404 mRNA. Translation: AAH95404.1.
CCDSCCDS13137.1.
RefSeqNP_001166216.1. NM_001172745.1.
NP_001166217.1. NM_001172746.1.
NP_006354.2. NM_006363.4.
NP_116780.1. NM_032985.4.
NP_116781.1. NM_032986.3.
UniGeneHs.369373.

3D structure databases

ProteinModelPortalQ15437.
SMRQ15437. Positions 3-764.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115746. 25 interactions.
IntActQ15437. 12 interactions.
MINTMINT-3031478.
STRING9606.ENSP00000262544.

PTM databases

PhosphoSiteQ15437.

Polymorphism databases

DMDM20141794.

Proteomic databases

MaxQBQ15437.
PaxDbQ15437.
PeptideAtlasQ15437.
PRIDEQ15437.

Protocols and materials databases

DNASU10483.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262544; ENSP00000262544; ENSG00000101310.
ENST00000336714; ENSP00000338844; ENSG00000101310.
ENST00000377465; ENSP00000366685; ENSG00000101310.
ENST00000377475; ENSP00000366695; ENSG00000101310.
GeneID10483.
KEGGhsa:10483.
UCSCuc002wqz.2. human.

Organism-specific databases

CTD10483.
GeneCardsGC20P018488.
HGNCHGNC:10702. SEC23B.
HPAHPA008216.
MIM224100. phenotype.
610512. gene.
neXtProtNX_Q15437.
Orphanet98873. Congenital dyserythropoietic anemia type II.
PharmGKBPA35625.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5047.
HOVERGENHBG055039.
InParanoidQ15437.
KOK14006.
OMAETIAQWQ.
OrthoDBEOG72C4ZP.
PhylomeDBQ15437.
TreeFamTF300693.

Gene expression databases

ArrayExpressQ15437.
BgeeQ15437.
CleanExHS_SEC23B.
GenevestigatorQ15437.

Family and domain databases

Gene3D3.40.20.10. 1 hit.
3.40.50.410. 1 hit.
InterProIPR029006. 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]
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

ChiTaRSSEC23B. human.
GeneWikiSEC23B.
GenomeRNAi10483.
NextBio39772.
PROQ15437.
SOURCESearch...

Entry information

Entry nameSC23B_HUMAN
AccessionPrimary (citable) accession number: Q15437
Secondary accession number(s): D3DW33 expand/collapse secondary AC list , Q503A9, Q5W183, Q9BS15, Q9BSI2, Q9H1D7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 130 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

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 20

Human chromosome 20: entries, gene names and cross-references to MIM