AGBL1

Protein identityUniProt · HPA

UniProt accession

Q96MI9

Gene

AGBL1

Ensembl

ENSG00000273540

Chromosome

15

Canonical length

1112 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Potential drug targets, Predicted intracellular proteins

OverviewNCBI Gene

Polyglutamylation is a reversible posttranslational modification catalyzed by polyglutamylases that results in the addition of glutamate side chains on the modified protein. This gene encodes a glutamate decarboxylase that catalyzes the deglutamylation of polyglutamylated proteins. Mutations in this gene result in dominant late-onset Fuchs corneal dystrophy. [provided by RefSeq, Nov 2013]

Canonical amino-acid sequenceUniProt

1112 residues, UniProt reviewed canonical sequence.

>Q96MI9|AGBL1
     1  MAEQEASGLQ VLLHTLQSSS DKESILTILK VLGDLLSVGT DRRIHYMISK GGSEALLQTL
    61  VDTARTAPPD YDILLPLFRL LAKVGLRDKK IGRKALELEA LDVTLILARK NLSHGQNLLH
   121  CLWALRVFAS SVSMGAMLGI NGAMELLFKV ITPYTRKRTQ AIRAATEVLA ALLKSKSNGR
   181  RAVNRGYVTS LLGLHQDWHS HDTANAYVQI RRGLLLCLRH IAALRSGREA FLAAQGMEIL
   241  FSTTQNCLDD KSMEPVISVV LQILRQCYPT SPLPLVTASS AYAFPVPGCI TTEPPHDLPE
   301  EDFEDDGDDE VDKDSDTEDG KVEDDDLETD VNKLSSKPGL DRPEEELMQY EVMCLELSYS
   361  FEELQSKLGD DLNSEKTQYA NHHHIPAAAS SKQHCYSKDQ SSCGQEREYA VQTSLLCRVK
   421  TGRSTVHLGS KKNPGVNLYQ NVQSNSLRRD SSESEIPDIQ ASPKADAWDV DAIFCPRMSA
   481  SFSNSTRTRE VVKVIDKLLQ THLKRVPFHD PYLYMAKARR TSSVVDFKMM AFPDVWGHCP
   541  PPTTQPMLER KCGVQRIRIF EDIRRLIQPS DVINKVVFSL DEPWPLQDNA SNCLRFFSKF
   601  ESGNLRKAIQ VREFEYDLLV NADVNSTQHQ QWFYFKVSGM QAAIPYHFNI INCEKPNSQF
   661  NYGMQPTLYS VKEALLGKPT WIRTGHEICY YKNHYRQSTA VAGGASGKCY YTLTFAVTFP
   721  HSEDVCYLAY HYPYTYTALM THLDILEKSV NLKEVYFRQD VLCQTLGGNP CPLVTITAMP
   781  ESNSDEHLEQ FRHRPYQVIT ARVHPGESNA SWVMKGTLEF LVSSDPVARL LRENFIFKII
   841  PMLNPDGVIN GNHRCSLSGE DLNRQWLSPS AHLQPTIYHA KGLLYHLSSI GRSPVVFCDF
   901  HGHSQKKNVF LYGCSIKETL WQAACTVGTS TILEEVNYRT LPKILDKLAP AFTMSSCSFL
   961  VEKSRASTAR VVVWREMGVS RSYTMESSYC GCNQGPYQCT QRLLERTKNE RAHPVDGLQG
  1021  LQFGTRELEE MGAMFCLGLL ILELKSASCS HQLLAQAATL LSAEEDALDQ HLQRLKSSNF
  1081  LPKHIWFAYH FFAITNFFKM NLLLHVSPVC DT

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against AGBL1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.29

Highest tissue expression

22 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about AGBL1.

Disease | AllUniProt

Conditions AGBL1 is implicated in, by any mechanism.

• Corneal dystrophy, Fuchs endothelial, 8 (FECD8) MIM:615523

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1.14

gnomAD pLI

0

gnomAD missense Z

-2.23

DepMap mean gene effect

0.04

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• C-terminal protein deglutamylation
• protein side chain deglutamylation
• proteolysis

Molecular functions

• metallocarboxypeptidase activity
• tubulin binding
• zinc ion binding

Cellular components

• cytoplasm
• cytosol
• microtubule cytoskeleton

Protein domainsUniProt · Pfam · InterPro

• Peptidase M14, carboxypeptidase A
• Armadillo-like helical
• Armadillo-type fold
• Cytosolic aminopeptidase 1/4
• Cytosolic carboxypeptidase, N-terminal
• Cytosolic carboxypeptidase
• Zinc carboxypeptidase
• Cytosolic carboxypeptidase N-terminal domain
• CCP1-like, N-terminal TPR repeats

KeywordsUniProt

• Carboxypeptidase
• Corneal dystrophy
• Cytoplasm
• Hydrolase
• Metal-binding
• Metalloprotease
• Protease
• Zinc

InteractionsUniProt · HPA

Protein binding partners of AGBL1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• MYLK
• TCF4