General Information of Target

Target ID LDTP01959
Target Name Protein AMBP (AMBP)
Gene Name AMBP
Gene ID 259
Synonyms
HCP; ITIL; Protein AMBP; Protein HC) [Cleaved into: Alpha-1-microglobulin; EC 1.6.2.-; Alpha-1 microglycoprotein; Complex-forming glycoprotein heterogeneous in charge; Inter-alpha-trypsin inhibitor light chain; ITI-LC; Bikunin; EDC1; HI-30; Uronic-acid-rich protein; Trypstatin]
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIM
DRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMES
YVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIF
TMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPC
MGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFI
QLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN
Target Bioclass
Other
Family
Calycin superfamily, Lipocalin family
Subcellular location
Secreted
Function
[Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor. Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment.; [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions. Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation. Also inhibits calcium oxalate crystallization.; [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases.
Uniprot ID
P02760
Ensemble ID
ENST00000265132.8
HGNC ID
HGNC:453

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 5 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
TG42
 Probe Info 
51.95  LDD0326  [1]
YN-1
 Probe Info 
100.00  LDD0444  [2]
IPM
 Probe Info 
C53(0.00); C91(0.00); C287(0.00); C188(0.00)  LDD0241  [3]
DBIA
 Probe Info 
C53(3.38)  LDD3418  [4]
W1
 Probe Info 
N.A.  LDD0236  [3]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0367  CL1 PaTu 8988t C91(1.08)  LDD1246  [5]
 LDCM0368  CL10 PaTu 8988t C91(1.59)  LDD1247  [5]
 LDCM0379  CL11 PaTu 8988t C91(1.29)  LDD1258  [5]
 LDCM0390  CL12 PaTu 8988t C91(1.14)  LDD1269  [5]
 LDCM0400  CL13 PaTu 8988t C91(1.49)  LDD1279  [5]
 LDCM0401  CL14 PaTu 8988t C91(1.54)  LDD1280  [5]
 LDCM0402  CL15 PaTu 8988t C91(1.27)  LDD1281  [5]
 LDCM0407  CL2 PaTu 8988t C91(2.75)  LDD1286  [5]
 LDCM0418  CL3 PaTu 8988t C91(1.07)  LDD1297  [5]
 LDCM0420  CL31 PaTu 8988t C91(1.65)  LDD1299  [5]
 LDCM0421  CL32 PaTu 8988t C91(1.46)  LDD1300  [5]
 LDCM0422  CL33 PaTu 8988t C91(1.02)  LDD1301  [5]
 LDCM0423  CL34 PaTu 8988t C91(1.59)  LDD1302  [5]
 LDCM0424  CL35 PaTu 8988t C91(1.69)  LDD1303  [5]
 LDCM0425  CL36 PaTu 8988t C91(0.78)  LDD1304  [5]
 LDCM0426  CL37 PaTu 8988t C91(1.47)  LDD1305  [5]
 LDCM0428  CL39 PaTu 8988t C91(1.55)  LDD1307  [5]
 LDCM0429  CL4 PaTu 8988t C91(2.95)  LDD1308  [5]
 LDCM0430  CL40 PaTu 8988t C91(1.53)  LDD1309  [5]
 LDCM0431  CL41 PaTu 8988t C91(1.67)  LDD1310  [5]
 LDCM0432  CL42 PaTu 8988t C91(1.77)  LDD1311  [5]
 LDCM0433  CL43 PaTu 8988t C91(1.89)  LDD1312  [5]
 LDCM0434  CL44 PaTu 8988t C91(1.34)  LDD1313  [5]
 LDCM0435  CL45 PaTu 8988t C91(1.85)  LDD1314  [5]
 LDCM0436  CL46 PaTu 8988t C91(1.08)  LDD1315  [5]
 LDCM0437  CL47 PaTu 8988t C91(0.91)  LDD1316  [5]
 LDCM0438  CL48 PaTu 8988t C91(0.86)  LDD1317  [5]
 LDCM0439  CL49 PaTu 8988t C91(1.12)  LDD1318  [5]
 LDCM0440  CL5 PaTu 8988t C91(2.39)  LDD1319  [5]
 LDCM0441  CL50 PaTu 8988t C91(1.10)  LDD1320  [5]
 LDCM0442  CL51 PaTu 8988t C91(1.13)  LDD1321  [5]
 LDCM0443  CL52 PaTu 8988t C91(1.69)  LDD1322  [5]
 LDCM0444  CL53 PaTu 8988t C91(3.41)  LDD1323  [5]
 LDCM0445  CL54 PaTu 8988t C91(3.10)  LDD1324  [5]
 LDCM0446  CL55 PaTu 8988t C91(1.67)  LDD1325  [5]
 LDCM0447  CL56 PaTu 8988t C91(1.31)  LDD1326  [5]
 LDCM0448  CL57 PaTu 8988t C91(1.72)  LDD1327  [5]
 LDCM0449  CL58 PaTu 8988t C91(1.50)  LDD1328  [5]
 LDCM0450  CL59 PaTu 8988t C91(1.13)  LDD1329  [5]
 LDCM0451  CL6 PaTu 8988t C91(0.84)  LDD1330  [5]
 LDCM0452  CL60 PaTu 8988t C91(1.15)  LDD1331  [5]
 LDCM0453  CL61 PaTu 8988t C91(0.63)  LDD1332  [5]
 LDCM0454  CL62 PaTu 8988t C91(0.23)  LDD1333  [5]
 LDCM0455  CL63 PaTu 8988t C91(0.38)  LDD1334  [5]
 LDCM0456  CL64 PaTu 8988t C91(0.37)  LDD1335  [5]
 LDCM0457  CL65 PaTu 8988t C91(0.41)  LDD1336  [5]
 LDCM0458  CL66 PaTu 8988t C91(0.48)  LDD1337  [5]
 LDCM0459  CL67 PaTu 8988t C91(0.43)  LDD1338  [5]
 LDCM0460  CL68 PaTu 8988t C91(0.45)  LDD1339  [5]
 LDCM0461  CL69 PaTu 8988t C91(0.52)  LDD1340  [5]
 LDCM0462  CL7 PaTu 8988t C91(1.48)  LDD1341  [5]
 LDCM0463  CL70 PaTu 8988t C91(0.47)  LDD1342  [5]
 LDCM0464  CL71 PaTu 8988t C91(0.28)  LDD1343  [5]
 LDCM0465  CL72 PaTu 8988t C91(0.62)  LDD1344  [5]
 LDCM0466  CL73 PaTu 8988t C91(0.53)  LDD1345  [5]
 LDCM0467  CL74 PaTu 8988t C91(0.32)  LDD1346  [5]
 LDCM0473  CL8 PaTu 8988t C91(1.78)  LDD1352  [5]
 LDCM0484  CL9 PaTu 8988t C91(1.52)  LDD1363  [5]
 LDCM0468  Fragment33 PaTu 8988t C91(0.56)  LDD1347  [5]
 LDCM0427  Fragment51 PaTu 8988t C91(1.67)  LDD1306  [5]
 LDCM0022  KB02 Hep 3B2.1-7 C188(1.69); C53(3.26)  LDD2353  [4]
 LDCM0023  KB03 Hep 3B2.1-7 C188(2.10); C53(2.33)  LDD2770  [4]
 LDCM0024  KB05 SG231 C53(3.38)  LDD3418  [4]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Enzyme
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Cathepsin B (CTSB) Peptidase C1 family P07858
Other
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Four and a half LIM domains protein 3 (FHL3) . Q13643

References

1 Design and synthesis of tailored human caseinolytic protease P inhibitors. Chem Commun (Camb). 2018 Aug 28;54(70):9833-9836. doi: 10.1039/c8cc05265d.
Mass spectrometry data entry: PXD010277
2 Ynamide Electrophile for the Profiling of Ligandable Carboxyl Residues in Live Cells and the Development of New Covalent Inhibitors. J Med Chem. 2022 Aug 11;65(15):10408-10418. doi: 10.1021/acs.jmedchem.2c00272. Epub 2022 Jul 26.
3 Oxidant-Induced Bioconjugation for Protein Labeling in Live Cells. ACS Chem Biol. 2023 Jan 20;18(1):112-122. doi: 10.1021/acschembio.2c00740. Epub 2022 Dec 21.
4 DrugMap: A quantitative pan-cancer analysis of cysteine ligandability. Cell. 2024 May 9;187(10):2536-2556.e30. doi: 10.1016/j.cell.2024.03.027. Epub 2024 Apr 22.
Mass spectrometry data entry: PXD047840
5 Reimagining high-throughput profiling of reactive cysteines for cell-based screening of large electrophile libraries. Nat Biotechnol. 2021 May;39(5):630-641. doi: 10.1038/s41587-020-00778-3. Epub 2021 Jan 4.