AMBP

From Wikipedia, the free encyclopedia

Alpha-1-microglobulin/bikunin precursor

PDB rendering based on 1bik.

Available structures: 1bik

Identifiers

Symbol(s)

AMBP; HCP; ITI; ITIL; UTI

External IDs

OMIM: 176870 MGI: 88002 HomoloGene: 1234

Gene ontology
Molecular Function:	• transporter activity • calcium channel inhibitor activity • IgA binding • heme binding • trypsin inhibitor activity • plasmin inhibitor activity • protein homodimerization activity • calcium oxalate binding
Cellular Component:	• extracellular region • plasma membrane
Biological Process:	• transport • cell adhesion • female pregnancy • protein-chromophore linkage • heme catabolic process • negative regulation of JNK cascade • negative regulation of immune response

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001633 (mRNA)
NP_001624 (protein)

NM_007443 (mRNA)
NP_031469 (protein)

Location

Chr 9: 115.86 - 115.88 Mb

Chr 4: 62.63 - 62.64 Mb

Pubmed search

[1]

[2]

Alpha-1-microglobulin/bikunin precursor, also known as AMBP, is a human gene.^[1]

[edit] References

^ Entrez Gene: AMBP alpha-1-microglobulin/bikunin precursor.

[edit] Further reading

Akerström B, Lögdberg L, Berggård T, et al. (2000). "alpha(1)-Microglobulin: a yellow-brown lipocalin.". Biochim. Biophys. Acta 1482 (1-2): 172–84. PMID 11058759.
Kobayashi H, Suzuki M, Hirashima Y, Terao T (2004). "The protease inhibitor bikunin, a novel anti-metastatic agent.". Biol. Chem. 384 (5): 749–54. PMID 12817471.
Ekström B, Berggård I (1977). "Human alpha1-microglobulin. Purification procedure, chemical and physiochemical properties.". J. Biol. Chem. 252 (22): 8048–57. PMID 72071.
Salier JP, Simon D, Rouet P, et al. (1992). "Homologous chromosomal locations of the four genes for inter-alpha-inhibitor and pre-alpha-inhibitor family in human and mouse: assignment of the ancestral gene for the lipocalin superfamily.". Genomics 14 (1): 83–8. PMID 1385302.
Escribano J, Lopex-Otin C, Hjerpe A, et al. (1990). "Location and characterization of the three carbohydrate prosthetic groups of human protein HC.". FEBS Lett. 266 (1-2): 167–70. PMID 1694784.
Diarra-Mehrpour M, Bourguignon J, Sesboüé R, et al. (1990). "Structural analysis of the human inter-alpha-trypsin inhibitor light-chain gene.". Eur. J. Biochem. 191 (1): 131–9. PMID 1696200.
Gebhard W, Schreitmüller T, Vetr H, et al. (1990). "Complementary DNA and deduced amino acid sequences of procine alpha 1-microglobulin and bikunin.". FEBS Lett. 269 (1): 32–6. PMID 1696914.
Falkenberg C, Grubb A, Akerström B (1990). "Isolation of rat serum alpha 1-microglobulin. Identification of a complex with alpha 1-inhibitor-3, a rat alpha 2-macroglobulin homologue.". J. Biol. Chem. 265 (27): 16150–7. PMID 1697852.
Nazimova SV, Akulenko IV, Zaĭtseva IV, et al. (1990). "[Immunoenzyme analysis of placenta-specific alpha(1)-microglobulin in the blood serum in normal and pathological pregnancy]". Akusherstvo i ginekologiia (7): 70–2. PMID 1700638.
Vetr H, Gebhard W (1991). "Structure of the human alpha 1-microglobulin-bikunin gene.". Biol. Chem. Hoppe-Seyler 371 (12): 1185–96. PMID 1708673.
Escribano J, Grubb A, Calero M, Méndez E (1991). "The protein HC chromophore is linked to the cysteine residue at position 34 of the polypeptide chain by a reduction-resistant bond and causes the charge heterogeneity of protein HC.". J. Biol. Chem. 266 (24): 15758–63. PMID 1714898.
Enghild JJ, Salvesen G, Hefta SA, et al. (1991). "Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor.". J. Biol. Chem. 266 (2): 747–51. PMID 1898736.
Reisinger P, Hochstrasser K, Albrecht GJ, et al. (1985). "Human inter-alpha-trypsin inhibitor: localization of the Kunitz-type domains in the N-terminal part of the molecule and their release by a trypsin-like proteinase.". Biol. Chem. Hoppe-Seyler 366 (5): 479–83. PMID 2408638.
Bourguignon J, Diarra-Mehrpour M, Sesboüé R, et al. (1985). "Human inter-alpha-trypsin-inhibitor: characterization and partial nucleotide sequencing of a light chain-encoding cDNA.". Biochem. Biophys. Res. Commun. 131 (3): 1146–53. PMID 2413856.
Méndez E, Fernández-Luna JL, Grubb A, Leyva-Cobián F (1986). "Human protein HC and its IgA complex are inhibitors of neutrophil chemotaxis.". Proc. Natl. Acad. Sci. U.S.A. 83 (5): 1472–5. PMID 2419908.
Traboni C, Cortese R (1986). "Sequence of a full length cDNA coding for human protein HC (alpha 1 microglobulin).". Nucleic Acids Res. 14 (15): 6340. PMID 2428011.
Kaumeyer JF, Polazzi JO, Kotick MP (1986). "The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC).". Nucleic Acids Res. 14 (20): 7839–50. PMID 2430261.
Zaraĭskiĭ EI, Nazimova SV, Olefirenko GA, et al. (1990). "[Immunoenzyme analysis of placenta-specific alpha 1-microglobulin in the serum of blood donors]". Vopr. Med. Khim. 35 (5): 130–2. PMID 2482577.
Schreitmüller T, Hochstrasser K, Reisinger PW, et al. (1987). "cDNA cloning of human inter-alpha-trypsin inhibitor discloses three different proteins.". Biol. Chem. Hoppe-Seyler 368 (8): 963–70. PMID 3663330.
Morii M, Travis J (1985). "The reactive site of human inter-alpha-trypsin inhibitor is in the amino-terminal half of the protein.". Biol. Chem. Hoppe-Seyler 366 (1): 19–21. PMID 3890890.