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Protein

Corticosteroid-binding globulin

Gene

SERPINA6

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

Functioni

Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei250Conserved cysteine within steroid binding domain1
Binding sitei254Corticosteroid1
Binding sitei286Corticosteroid1
Binding sitei390Corticosteroid1
Binding sitei393Corticosteroid1

GO - Molecular functioni

  • serine-type endopeptidase inhibitor activity Source: ProtInc
  • steroid binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processTransport
LigandLipid-binding, Steroid-binding

Protein family/group databases

MEROPSiI04.954

Names & Taxonomyi

Protein namesi
Recommended name:
Corticosteroid-binding globulin
Short name:
CBG
Alternative name(s):
Serpin A6
Transcortin
Gene namesi
Name:SERPINA6
Synonyms:CBG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000170099.5
HGNCiHGNC:1540 SERPINA6
MIMi122500 gene
neXtProtiNX_P08185

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Corticosteroid-binding globulin deficiency (CBG deficiency)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionExtremely rare hereditary disorder characterized by reduced corticosteroid-binding capacity with normal or low plasma corticosteroid-binding globulin concentration, and normal or low basal cortisol levels associated with hypo/hypertension and muscle fatigue.
See also OMIM:611489
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007111115L → H in CBG deficiency; Leuven; decreased cortisol-binding affinity. 2 PublicationsCorresponds to variant dbSNP:rs113418909EnsemblClinVar.1
Natural variantiVAR_016223389D → N in CBG deficiency; Lyon; decreased cortisol-binding affinity. 2 PublicationsCorresponds to variant dbSNP:rs28929488EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi866
MalaCardsiSERPINA6
MIMi611489 phenotype
OpenTargetsiENSG00000170099
Orphaneti199247 Corticosteroid-binding globulin deficiency
PharmGKBiPA35033

Chemistry databases

ChEMBLiCHEMBL2421
DrugBankiDB00240 Alclometasone
DB00394 Beclomethasone dipropionate
DB01410 Ciclesonide
DB05688 CRx-119
DB00663 Flumethasone
DB00180 Flunisolide
DB00591 Fluocinolone Acetonide
DB01047 Fluocinonide
DB00324 Fluorometholone
DB00846 Flurandrenolide
DB00588 Fluticasone Propionate
DB00741 Hydrocortisone
DB00253 Medrysone
DB00648 Mitotane
DB01384 Paramethasone
DB00860 Prednisolone
DB00896 Rimexolone
DB00620 Triamcinolone
DB00596 Ulobetasol

Polymorphism and mutation databases

BioMutaiSERPINA6
DMDMi115851

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000003242923 – 405Corticosteroid-binding globulinAdd BLAST383

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi31N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi96N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi176N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi260N-linked (GlcNAc...) asparagine1
Glycosylationi330N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi369N-linked (GlcNAc...) asparagine1 Publication1

Post-translational modificationi

N-glycosylated; binds 5 oligosaccharide chains.
Glycosylation in position Asn-260 is needed for steroid binding.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP08185
PaxDbiP08185
PeptideAtlasiP08185
PRIDEiP08185

PTM databases

GlyConnecti788
iPTMnetiP08185
PhosphoSitePlusiP08185

Expressioni

Tissue specificityi

Plasma; synthesized in liver. Has also been identified in a number of glycocorticoid responsive cells.

Gene expression databases

BgeeiENSG00000170099
CleanExiHS_SERPINA6
ExpressionAtlasiP08185 baseline and differential
GenevisibleiP08185 HS

Organism-specific databases

HPAiHPA017864

Interactioni

Protein-protein interaction databases

BioGridi107314, 9 interactors
STRINGi9606.ENSP00000342850

Structurei

Secondary structure

1405
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi39 – 57Combined sources19
Beta strandi59 – 61Combined sources3
Beta strandi63 – 65Combined sources3
Helixi67 – 78Combined sources12
Helixi83 – 92Combined sources10
Turni97 – 99Combined sources3
Helixi102 – 117Combined sources16
Helixi119 – 122Combined sources4
Beta strandi123 – 134Combined sources12
Helixi141 – 151Combined sources11
Beta strandi154 – 158Combined sources5
Helixi163 – 177Combined sources15
Turni178 – 180Combined sources3
Beta strandi188 – 190Combined sources3
Beta strandi194 – 209Combined sources16
Helixi213 – 215Combined sources3
Beta strandi217 – 224Combined sources8
Beta strandi227 – 244Combined sources18
Beta strandi246 – 257Combined sources12
Turni258 – 260Combined sources3
Beta strandi261 – 268Combined sources8
Helixi273 – 279Combined sources7
Helixi282 – 291Combined sources10
Beta strandi293 – 302Combined sources10
Beta strandi304 – 311Combined sources8
Helixi313 – 318Combined sources6
Helixi323 – 325Combined sources3
Turni332 – 334Combined sources3
Beta strandi336 – 338Combined sources3
Beta strandi340 – 353Combined sources14
Beta strandi355 – 370Combined sources16
Beta strandi375 – 378Combined sources4
Beta strandi383 – 389Combined sources7
Turni390 – 393Combined sources4
Beta strandi394 – 402Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VDXX-ray1.84A/B33-357[»]
A/B372-405[»]
2VDYX-ray2.30A/B33-405[»]
4BB2X-ray2.48A33-371[»]
B372-405[»]
4C41X-ray1.80A33-405[»]
4C49X-ray2.70A/B/C/D33-405[»]
ProteinModelPortaliP08185
SMRiP08185
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08185

Family & Domainsi

Domaini

Proteolytic cleavage leads to an important conformation change. This reduces the affinity for steroids.1 Publication

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2392 Eukaryota
COG4826 LUCA
GeneTreeiENSGT00760000118839
HOGENOMiHOG000238521
HOVERGENiHBG005957
InParanoidiP08185
KOiK04525
OMAiLPCQLVQ
OrthoDBiEOG091G0ION
PhylomeDBiP08185
TreeFamiTF343201

Family and domain databases

InterProiView protein in InterPro
IPR023795 Serpin_CS
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf
PANTHERiPTHR11461 PTHR11461, 1 hit
PfamiView protein in Pfam
PF00079 Serpin, 1 hit
SMARTiView protein in SMART
SM00093 SERPIN, 1 hit
SUPFAMiSSF56574 SSF56574, 1 hit
PROSITEiView protein in PROSITE
PS00284 SERPIN, 1 hit

Sequencei

Sequence statusi: Complete.

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

P08185-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLLLYTCLL WLPTSGLWTV QAMDPNAAYV NMSNHHRGLA SANVDFAFSL
60 70 80 90 100
YKHLVALSPK KNIFISPVSI SMALAMLSLG TCGHTRAQLL QGLGFNLTER
110 120 130 140 150
SETEIHQGFQ HLHQLFAKSD TSLEMTMGNA LFLDGSLELL ESFSADIKHY
160 170 180 190 200
YESEVLAMNF QDWATASRQI NSYVKNKTQG KIVDLFSGLD SPAILVLVNY
210 220 230 240 250
IFFKGTWTQP FDLASTREEN FYVDETTVVK VPMMLQSSTI SYLHDSELPC
260 270 280 290 300
QLVQMNYVGN GTVFFILPDK GKMNTVIAAL SRDTINRWSA GLTSSQVDLY
310 320 330 340 350
IPKVTISGVY DLGDVLEEMG IADLFTNQAN FSRITQDAQL KSSKVVHKAV
360 370 380 390 400
LQLNEEGVDT AGSTGVTLNL TSKPIILRFN QPFIIMIFDH FTWSSLFLAR

VMNPV
Length:405
Mass (Da):45,141
Last modified:August 1, 1988 - v1
Checksum:iF0E36EFC3B3C08A1
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007111115L → H in CBG deficiency; Leuven; decreased cortisol-binding affinity. 2 PublicationsCorresponds to variant dbSNP:rs113418909EnsemblClinVar.1
Natural variantiVAR_024350246S → A1 PublicationCorresponds to variant dbSNP:rs2228541Ensembl.1
Natural variantiVAR_016223389D → N in CBG deficiency; Lyon; decreased cortisol-binding affinity. 2 PublicationsCorresponds to variant dbSNP:rs28929488EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02943 mRNA Translation: AAB59523.1
AK290821 mRNA Translation: BAF83510.1
CH471061 Genomic DNA Translation: EAW81568.1
BC056259 mRNA Translation: AAH56259.1
BC058021 mRNA Translation: AAH58021.1
CCDSiCCDS9924.1
PIRiA28321
RefSeqiNP_001747.2, NM_001756.3
UniGeneiHs.532635

Genome annotation databases

EnsembliENST00000341584; ENSP00000342850; ENSG00000170099
ENST00000621384; ENSP00000484501; ENSG00000277405
GeneIDi866
KEGGihsa:866
UCSCiuc001ycv.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCBG_HUMAN
AccessioniPrimary (citable) accession number: P08185
Secondary accession number(s): A8K456, Q7Z2Q9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 25, 2018
This is version 179 of the entry and version 1 of the sequence. See 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, Direct protein sequencing, 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

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