AMBP
Protein AMBP
Also known as: AMBP_HUMAN, EDC1, HCP, HI30, IATIL, ITI, ITIL, ITILC, UTI
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P02760
- Gene
- AMBP
- Ensembl
- ENSG00000106927
- Chromosome
- 9
- Canonical length
- 352 aa
- Protein class
- Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins
- Subcellular location
- Golgi apparatus,Vesicles,Cytosol
- Secretome location
- Secreted to blood
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This gene encodes a complex glycoprotein secreted in plasma. The precursor is proteolytically processed into distinct functioning proteins: alpha-1-microglobulin, which belongs to the superfamily of lipocalin transport proteins and may play a role in the regulation of inflammatory processes, and bikunin, which is a urinary trypsin inhibitor belonging to the superfamily of Kunitz-type protease inhibitors and plays an important role in many physiological and pathological processes. This gene is located on chromosome 9 in a cluster of lipocalin genes. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
352 residues, UniProt reviewed canonical sequence.
>P02760|AMBP
1 MRSLGALLLL LSACLAVSAG PVPTPPDNIQ VQENFNISRI YGKWYNLAIG STCPWLKKIM
61 DRMTVSTLVL GEGATEAEIS MTSTRWRKGV CEETSGAYEK TDTDGKFLYH KSKWNITMES
121 YVVHTNYDEY AIFLTKKFSR HHGPTITAKL YGRAPQLRET LLQDFRVVAQ GVGIPEDSIF
181 TMADRGECVP GEQEPEPILI PRVRRAVLPQ EEEGSGGGQL VTEVTKKEDS CQLGYSAGPC
241 MGMTSRYFYN GTSMACETFQ YGGCMGNGNN FVTEKECLQT CRTVAACNLP IVRGPCRAFI
301 QLWAFDAVKG KCVLFPYGGC QGNGNKFYSE KECREYCGVP GDGDEELLRF SNLocalizationUniProt · AlphaFold · HPA
Whether an antibody against AMBP 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
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.36
- Highest tissue expression
- 10,227 nTPM
Expression across tissuesHPA
Tissue
- liver: 10,227 nTPM
- gallbladder: 151 nTPM
- pancreas: 118 nTPM
- kidney: 10 nTPM
- breast: 6.1 nTPM
- spleen: 2.9 nTPM
Single-cell type
- hepatocytes: 12,897 nCPM
- cholangiocytes: 2,977 nCPM
- pancreatic duct cells: 936 nCPM
- kupffer cells: 128 nCPM
- late spermatids: 94 nCPM
- oocytes: 65 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- cerebellum: 0.7 nTPM
- choroid plexus: 0.7 nTPM
- cerebral cortex: 0.5 nTPM
- midbrain: 0.5 nTPM
- basal ganglia: 0.4 nTPM
- hypothalamus: 0.4 nTPM
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)
- 1.37
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.16
- DepMap mean gene effect
- -0.01
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 2% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cell adhesion
- female pregnancy
- heme catabolic process
- negative regulation of immune response
- negative regulation of JNK cascade
- protein catabolic process
Molecular functions
- calcium channel inhibitor activity
- carbohydrate binding
- heme binding
- IgA binding
- oxidoreductase activity
- protein homodimerization activity
- serine-type endopeptidase inhibitor activity
- calcium oxalate binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Lipocalin/cytosolic fatty-acid binding domain
- Pancreatic trypsin inhibitor Kunitz domain
- Alpha-1-microglobulin
- Calycin
- Proteinase inhibitor I2, Kunitz, conserved site
- Lipocalin family conserved site
- Pancreatic trypsin inhibitor Kunitz domain superfamily
- Kunitz/Bovine pancreatic trypsin inhibitor domain
- Lipocalin / cytosolic fatty-acid binding protein family
- Protein AMBP
KeywordsUniProt
- Cell membrane
- Chromophore
- Cleavage on pair of basic residues
- Cytoplasm
- Disulfide bond
- Endoplasmic reticulum
- Extracellular matrix
- Glycoprotein
- Host-virus interaction
- Membrane
- Mitochondrion
- Mitochondrion inner membrane
- Nucleus
- Oxidoreductase
- Protease inhibitor
- Proteoglycan
- Repeat
- Secreted
- Serine protease inhibitor
- Signal
InteractionsUniProt · HPA
Protein binding partners of AMBP in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads AMBP as an antibody target. Whether an autoantibody or antibody against AMBP could matter depends on whether native AMBP is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
AMBP is annotated at the cell surface, where native AMBP is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label AMBP as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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