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Protein AMBP [Cleaved into: Alpha-1-microglobulin (Protein HC) (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]

 AMBP_HUMAN              Reviewed;         352 AA.
P02760; P00977; P02759; P78491; Q2TU33; Q5TBD7; Q9UC58; Q9UDI8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
27-SEP-2017, entry version 204.
RecName: Full=Protein AMBP;
Contains:
RecName: Full=Alpha-1-microglobulin;
Short=Protein HC;
AltName: Full=Alpha-1 microglycoprotein;
AltName: Full=Complex-forming glycoprotein heterogeneous in charge;
Contains:
RecName: Full=Inter-alpha-trypsin inhibitor light chain;
Short=ITI-LC;
AltName: Full=Bikunin;
AltName: Full=EDC1;
AltName: Full=HI-30;
AltName: Full=Uronic-acid-rich protein;
Contains:
RecName: Full=Trypstatin;
Flags: Precursor;
Name=AMBP; Synonyms=HCP, ITIL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2428011; DOI=10.1093/nar/14.15.6340;
Traboni C., Cortese R.;
"Sequence of a full length cDNA coding for human protein HC (alpha 1
microglobulin).";
Nucleic Acids Res. 14:6340-6340(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2430261; DOI=10.1093/nar/14.20.7839;
Kaumeyer J.F., Polazzi J.O., Kotick M.P.;
"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. 14:7839-7850(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1708673;
Vetr H., Gebhard W.;
"Structure of the human alpha 1-microglobulin-bikunin gene.";
Biol. Chem. Hoppe-Seyler 371:1185-1196(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=1696200; DOI=10.1111/j.1432-1033.1990.tb19102.x;
Diarra-Mehrpour M., Bourguignon J., Sesboue R., Salier J.-P.,
Leveillard T., Martin J.-P.;
"Structural analysis of the human inter-alpha-trypsin inhibitor light-
chain gene.";
Eur. J. Biochem. 191:131-139(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human cell growth inhibition gene.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 20-202.
PubMed=6198962; DOI=10.1016/0003-9861(84)90021-3;
Lopez C., Grubb A.O., Mendez E.;
"The complete amino acid sequence of human complex-forming
glycoprotein heterogeneous in charge (protein HC) from one
individual.";
Arch. Biochem. Biophys. 228:544-554(1984).
[11]
PROTEIN SEQUENCE OF 20-198.
PubMed=6164372; DOI=10.1016/0006-291X(81)91209-2;
Takagi T., Takagi K., Kawai T.;
"Complete amino acid sequence of human alpha 1-microglobulin.";
Biochem. Biophys. Res. Commun. 98:997-1001(1981).
[12]
PROTEIN SEQUENCE OF 20-198.
Lopez C., Grubb A.O., Mendez E.;
"Human protein HC displays variability in its carboxyl-terminal amino
acid sequence.";
FEBS Lett. 144:349-353(1982).
[13]
PROTEIN SEQUENCE OF 44-57, AND BINDING TO CHROMOPHORE.
PubMed=7506257;
Calero M., Escribano J., Grubb A., Mendez E.;
"Location of a novel type of interpolypeptide chain linkage in the
human protein HC-IgA complex (HC-IgA) and identification of a
heterogeneous chromophore associated with the complex.";
J. Biol. Chem. 269:384-389(1994).
[14]
PROTEIN SEQUENCE OF 206-350.
PubMed=2408638;
Reisinger P., Hochstrasser K., Albrecht G.J., Lempart K.,
Salier J.-P.;
"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 366:479-483(1985).
[15]
PROTEIN SEQUENCE OF 206-243 AND 275-303.
TISSUE=Urine;
PubMed=1469060; DOI=10.1002/jcb.240500303;
Chawla R.K., Lawson D.H., Ahmad M., Travis J.;
"Cancer-related urinary proteinase inhibitor, EDC1: a new method for
its isolation and evidence for multiple forms.";
J. Cell. Biochem. 50:227-236(1992).
[16]
PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, AND CROSS-LINK
SITE TO HC3.
PubMed=1898736;
Enghild J.J., Salvesen G., Hefta S.A., Thoegersen I.B., Rutherfurd S.,
Pizzo S.V.;
"Chondroitin 4-sulfate covalently cross-links the chains of the human
blood protein pre-alpha-inhibitor.";
J. Biol. Chem. 266:747-751(1991).
[17]
PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, AND CROSS-LINK
SITE TO HC2.
PubMed=7682553;
Enghild J.J., Salvesen G., Thoegersen I.B., Valnickova Z., Pizzo S.V.,
Hefta S.A.;
"Presence of the protein-glycosaminoglycan-protein covalent cross-link
in the inter-alpha-inhibitor-related proteinase inhibitor heavy chain
2/bikunin.";
J. Biol. Chem. 268:8711-8716(1993).
[18]
PROTEIN SEQUENCE OF 206-223, AND FUNCTION.
TISSUE=Urine;
PubMed=7676539; DOI=10.1007/BF00307939;
Atmani F., Khan S.R.;
"Characterization of uronic-acid-rich inhibitor of calcium oxalate
crystallization isolated from rat urine.";
Urol. Res. 23:95-101(1995).
[19]
PROTEIN SEQUENCE OF 206-219, AND COVALENT LINKAGE WITH CHONDROITIN
SULFATE.
TISSUE=Plasma;
PubMed=7513643; DOI=10.1111/j.1432-1033.1994.tb18803.x;
Morelle W., Capon C., Balduyck M., Sautiere P., Kouach M.,
Michalski C., Fournet B., Mizon J.;
"Chondroitin sulphate covalently cross-links the three polypeptide
chains of inter-alpha-trypsin inhibitor.";
Eur. J. Biochem. 221:881-888(1994).
[20]
GLYCOSYLATION AT SER-215 AND ASN-250, AND STRUCTURE OF CARBOHYDRATES.
PubMed=6171497;
Hochstrasser K., Schoenberger O.L., Rossmanith I., Wachter E.;
"Kunitz-type proteinase inhibitors derived by limited proteolysis of
the inter-alpha-trypsin inhibitor, V. Attachments of carbohydrates in
the human urinary trypsin inhibitor isolated by affinity
chromatography.";
Hoppe-Seyler's Z. Physiol. Chem. 362:1357-1362(1981).
[21]
INHIBITORY SITE.
PubMed=3890890; DOI=10.1515/bchm3.1985.366.1.19;
Morii M., Travis J.;
"The reactive site of human inter-alpha-trypsin inhibitor is in the
amino-terminal half of the protein.";
Biol. Chem. Hoppe-Seyler 366:19-21(1985).
[22]
GLYCOSYLATION AT THR-24; ASN-36 AND ASN-115, AND STRUCTURE OF
CARBOHYDRATES.
PubMed=1694784; DOI=10.1016/0014-5793(90)81531-R;
Escribano J., Lopex-Otin C., Hjerpe A., Grubb A.O., Mendez E.;
"Location and characterization of the three carbohydrate prosthetic
groups of human protein HC.";
FEBS Lett. 266:167-170(1990).
[23]
BINDING TO CHROMOPHORE.
TISSUE=Urine;
PubMed=1714898;
Escribano J., Grubb A.O., Calero M., Mendez E.;
"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. 266:15758-15763(1991).
[24]
BINDING TO CHROMOPHORE.
PubMed=10631976; DOI=10.1110/ps.8.12.2611;
Berggaard T., Cohen A., Persson P., Lindqvist A., Cedervall T.,
Silow M., Thoegersen I.B., Joensson J.A., Enghild J.J.,
Aakerstroem B.;
"Alpha1-microglobulin chromophores are located to three lysine
residues semiburied in the lipocalin pocket and associated with a
novel lipophilic compound.";
Protein Sci. 8:2611-2620(1999).
[25]
CHROMOPHORE CHARACTERIZATION.
PubMed=15452109; DOI=10.1074/jbc.M408242200;
Sala A., Campagnoli M., Perani E., Romano A., Labo S., Monzani E.,
Minchiotti L., Galliano M.;
"Human alpha-1-microglobulin is covalently bound to kynurenine-derived
chromophores.";
J. Biol. Chem. 279:51033-51041(2004).
[26]
INTERACTION OF ALPHA-1-MICROGLOBULIN WITH HEV ORF3 PROTEIN.
PubMed=15037615; DOI=10.1074/jbc.M402017200;
Tyagi S., Surjit M., Roy A.K., Jameel S., Lal S.K.;
"The ORF3 protein of hepatitis E virus interacts with liver-specific
alpha1-microglobulin and its precursor alpha1-microglobulin/bikunin
precursor (AMBP) and expedites their export from the hepatocyte.";
J. Biol. Chem. 279:29308-29319(2004).
[27]
INTERACTION OF BIKUNIN WITH HEV ORF3 PROTEIN.
PubMed=16140784; DOI=10.1128/JVI.79.18.12081-12087.2005;
Tyagi S., Surjit M., Lal S.K.;
"The 41-amino-acid C-terminal region of the hepatitis E virus ORF3
protein interacts with bikunin, a Kunitz-type serine protease
inhibitor.";
J. Virol. 79:12081-12087(2005).
[28]
GLYCOSYLATION AT ASN-115 AND ASN-250, STRUCTURE OF CARBOHYDRATES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 0:0-0(2011).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 230-339.
PubMed=9566199; DOI=10.1006/jmbi.1997.1582;
Xu Y., Carr P.D., Guss J.M., Ollis D.L.;
"The crystal structure of bikunin from the inter-alpha-inhibitor
complex: a serine protease inhibitor with two Kunitz domains.";
J. Mol. Biol. 276:955-966(1998).
[31]
REVIEW.
PubMed=11058759;
Aakerstroem B., Loegdberg L., Berggaard T., Osmark P., Lindqvist A.;
"Alpha(1)-microglobulin: a yellow-brown lipocalin.";
Biochim. Biophys. Acta 1482:172-184(2000).
-!- FUNCTION: Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin,
and lysosomal granulocytic elastase. Inhibits calcium oxalate
crystallization. {ECO:0000269|PubMed:7676539}.
-!- FUNCTION: Trypstatin is a trypsin inhibitor. {ECO:0000250}.
-!- SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from
one or two heavy chains (H1, H2 or H3) and one light chain,
bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2
and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and
bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin.
Alpha-1-microglobulin occurs as a monomer and also in complexes
with IgA and albumin. Alpha-1-microglobulin interacts with FN1.
Trypstatin is a monomer and also occurs as a complex with tryptase
in mast cells (By similarity). Alpha-1-microglobulin and bikunin
interact (via SH3 domain) with HEV ORF3 protein. {ECO:0000250,
ECO:0000269|PubMed:15037615, ECO:0000269|PubMed:16140784}.
-!- INTERACTION:
P07858:CTSB; NbExp=4; IntAct=EBI-2115136, EBI-715062;
Q13643:FHL3; NbExp=3; IntAct=EBI-2115136, EBI-741101;
P69616:ORF3 (xeno); NbExp=4; IntAct=EBI-2115136, EBI-7810260;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
Alpha-1-microglobulin occurs in many physiological fluids
including plasma, urine, and cerebrospinal fluid. Inter-alpha-
trypsin inhibitor is present in plasma and urine.
-!- PTM: The precursor is proteolytically processed into separately
functioning proteins.
-!- PTM: 3-hydroxykynurenine, an oxidized tryptophan metabolite that
is common in biological fluids, reacts with Cys-53, Lys-111, Lys-
137, and Lys-149 to form heterogeneous polycyclic chromophores
including hydroxanthommatin. The reaction by alpha-1-microglobulin
is autocatalytic; the human protein forms chromophore even when
expressed in insect and bacterial cells. The chromophore can react
with accessible cysteines forming non-reducible thioether cross-
links with other molecules of alpha-1-microglobulin or with other
proteins such as Ig alpha-1 chain C region 'Cys-352'.
-!- PTM: Heavy chains are interlinked with bikunin via a chondroitin
4-sulfate bridge to the their C-terminal aspartate. {ECO:0000250}.
-!- PTM: N- and O-glycosylated. N-glycan heterogeneity at Asn-115:
Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5
(minor). N-glycan at Asn-250: Hex5HexNAc4. O-linkage of the
glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-
linking between the three polypeptide chains.
{ECO:0000269|PubMed:1694784, ECO:0000269|PubMed:1898736,
ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:6171497,
ECO:0000269|PubMed:7682553}.
-!- MISCELLANEOUS: In vitro, the first twelve residues of the amino
end of the inhibitor appear to have a reactive site capable of
inhibiting the activity of a number of enzymes. Its in vivo
function is not known.
-!- SIMILARITY: In the N-terminal section; belongs to the calycin
superfamily. Lipocalin family. {ECO:0000305}.
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EMBL; X04225; CAA27803.1; -; mRNA.
EMBL; X04494; CAA28182.1; -; mRNA.
EMBL; X54816; CAA38585.1; -; Genomic_DNA.
EMBL; X54817; CAA38585.1; JOINED; Genomic_DNA.
EMBL; X54818; CAA38585.1; JOINED; Genomic_DNA.
EMBL; X54817; CAA38586.1; -; Genomic_DNA.
EMBL; X54818; CAA38587.1; -; Genomic_DNA.
EMBL; M88249; AAA59196.1; -; Genomic_DNA.
EMBL; M88165; AAA59196.1; JOINED; Genomic_DNA.
EMBL; M88243; AAA59196.1; JOINED; Genomic_DNA.
EMBL; M88244; AAA59196.1; JOINED; Genomic_DNA.
EMBL; M88246; AAA59196.1; JOINED; Genomic_DNA.
EMBL; M88247; AAA59196.1; JOINED; Genomic_DNA.
EMBL; AY544123; AAT11154.1; -; mRNA.
EMBL; AK290837; BAF83526.1; -; mRNA.
EMBL; AL137850; CAI15899.1; -; Genomic_DNA.
EMBL; CH471090; EAW87404.1; -; Genomic_DNA.
EMBL; BC041593; AAH41593.1; -; mRNA.
CCDS; CCDS6800.1; -.
PIR; S13433; HCHU.
RefSeq; NP_001624.1; NM_001633.3.
UniGene; Hs.436911; -.
PDB; 1BIK; X-ray; 2.50 A; A=206-352.
PDB; 3QKG; X-ray; 2.30 A; A=20-202.
PDB; 4ES7; X-ray; 2.00 A; A=27-193.
PDB; 4U30; X-ray; 2.50 A; W/X/Y/Z=283-340.
PDBsum; 1BIK; -.
PDBsum; 3QKG; -.
PDBsum; 4ES7; -.
PDBsum; 4U30; -.
ProteinModelPortal; P02760; -.
SMR; P02760; -.
BioGrid; 106757; 13.
IntAct; P02760; 12.
MINT; MINT-1367019; -.
STRING; 9606.ENSP00000265132; -.
DrugBank; DB00062; Human Serum Albumin.
DrugBank; DB00064; Serum albumin iodonated.
MEROPS; I02.005; -.
iPTMnet; P02760; -.
PhosphoSitePlus; P02760; -.
UniCarbKB; P02760; -.
BioMuta; AMBP; -.
DMDM; 122801; -.
SWISS-2DPAGE; P02760; -.
MaxQB; P02760; -.
PaxDb; P02760; -.
PeptideAtlas; P02760; -.
PRIDE; P02760; -.
DNASU; 259; -.
Ensembl; ENST00000265132; ENSP00000265132; ENSG00000106927.
GeneID; 259; -.
KEGG; hsa:259; -.
UCSC; uc004bie.5; human.
CTD; 259; -.
DisGeNET; 259; -.
EuPathDB; HostDB:ENSG00000106927.11; -.
GeneCards; AMBP; -.
HGNC; HGNC:453; AMBP.
HPA; CAB069436; -.
HPA; HPA001497; -.
MIM; 176870; gene.
neXtProt; NX_P02760; -.
OpenTargets; ENSG00000106927; -.
PharmGKB; PA24759; -.
eggNOG; KOG4295; Eukaryota.
eggNOG; ENOG410XQNP; LUCA.
GeneTree; ENSGT00740000114929; -.
HOVERGEN; HBG000225; -.
InParanoid; P02760; -.
OrthoDB; EOG091G09P2; -.
PhylomeDB; P02760; -.
TreeFam; TF351222; -.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
EvolutionaryTrace; P02760; -.
GeneWiki; Alpha-1-microglobulin/bikunin_precursor; -.
GenomeRNAi; 259; -.
PMAP-CutDB; P02760; -.
PRO; PR:P02760; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000106927; -.
CleanEx; HS_AMBP; -.
ExpressionAtlas; P02760; baseline and differential.
Genevisible; P02760; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0019855; F:calcium channel inhibitor activity; NAS:UniProtKB.
GO; GO:0046904; F:calcium oxalate binding; NAS:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0019862; F:IgA binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:UniProtKB.
GO; GO:0036094; F:small molecule binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
GO; GO:0007565; P:female pregnancy; NAS:UniProtKB.
GO; GO:0042167; P:heme catabolic process; NAS:UniProtKB.
GO; GO:0050777; P:negative regulation of immune response; NAS:UniProtKB.
GO; GO:0046329; P:negative regulation of JNK cascade; TAS:UniProtKB.
GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00109; KU; 2.
Gene3D; 2.40.128.20; -; 1.
Gene3D; 4.10.410.10; -; 2.
InterPro; IPR002968; A1-microglobln.
InterPro; IPR029856; AMBP.
InterPro; IPR012674; Calycin.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR002345; Lipocalin.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR10083:SF281; PTHR10083:SF281; 1.
Pfam; PF00014; Kunitz_BPTI; 2.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR01215; A1MCGLOBULIN.
PRINTS; PR00759; BASICPTASE.
PRINTS; PR00179; LIPOCALIN.
SMART; SM00131; KU; 2.
SUPFAM; SSF50814; SSF50814; 1.
SUPFAM; SSF57362; SSF57362; 2.
PROSITE; PS00280; BPTI_KUNITZ_1; 2.
PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Chromophore; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Host-virus interaction; Protease inhibitor;
Proteoglycan; Reference proteome; Repeat; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:6164372,
ECO:0000269|PubMed:6198962,
ECO:0000269|Ref.12}.
CHAIN 20 203 Alpha-1-microglobulin.
/FTId=PRO_0000017886.
CHAIN 206 352 Inter-alpha-trypsin inhibitor light
chain.
/FTId=PRO_0000017887.
CHAIN 284 344 Trypstatin. {ECO:0000250}.
/FTId=PRO_0000318926.
DOMAIN 231 281 BPTI/Kunitz inhibitor 1.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
DOMAIN 287 337 BPTI/Kunitz inhibitor 2.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
REGION 206 226 Glycopeptide (secretory piece).
BINDING 53 53 Multimeric 3-hydroxykynurenine
chromophore (covalent).
BINDING 111 111 Multimeric 3-hydroxykynurenine
chromophore (covalent).
BINDING 137 137 Multimeric 3-hydroxykynurenine
chromophore (covalent).
BINDING 149 149 Multimeric 3-hydroxykynurenine
chromophore (covalent).
SITE 241 242 Inhibitory (P1) (chymotrypsin, elastase).
{ECO:0000250}.
SITE 297 298 Inhibitory (P1) (trypsin). {ECO:0000250}.
CARBOHYD 24 24 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:1694784}.
/FTId=CAR_000172.
CARBOHYD 36 36 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:1694784}.
CARBOHYD 115 115 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:1694784,
ECO:0000269|PubMed:22171320}.
CARBOHYD 215 215 O-linked (Xyl...) (chondroitin sulfate)
serine. {ECO:0000269|PubMed:1898736,
ECO:0000269|PubMed:6171497,
ECO:0000269|PubMed:7682553}.
CARBOHYD 250 250 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:6171497}.
DISULFID 91 188
DISULFID 231 281
DISULFID 240 264
DISULFID 256 277
DISULFID 287 337
DISULFID 296 320
DISULFID 312 333
CONFLICT 48 57 Missing (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 57 57 Missing (in Ref. 10; AA sequence and 12;
AA sequence). {ECO:0000305}.
CONFLICT 137 137 Missing (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 142 142 H -> T (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 145 145 Missing (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 194 194 E -> Q (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 215 215 S -> T (in Ref. 18; AA sequence).
{ECO:0000305}.
CONFLICT 218 218 G -> T (in Ref. 18; AA sequence).
{ECO:0000305}.
CONFLICT 291 292 IV -> VI (in Ref. 14; AA sequence and 15;
AA sequence). {ECO:0000305}.
CONFLICT 295 295 Missing (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 343 343 G -> E (in Ref. 14; AA sequence).
{ECO:0000305}.
HELIX 37 39 {ECO:0000244|PDB:4ES7}.
STRAND 42 51 {ECO:0000244|PDB:4ES7}.
HELIX 54 59 {ECO:0000244|PDB:4ES7}.
HELIX 60 62 {ECO:0000244|PDB:4ES7}.
STRAND 66 72 {ECO:0000244|PDB:4ES7}.
STRAND 78 87 {ECO:0000244|PDB:4ES7}.
STRAND 90 100 {ECO:0000244|PDB:4ES7}.
STRAND 106 111 {ECO:0000244|PDB:4ES7}.
TURN 112 115 {ECO:0000244|PDB:4ES7}.
STRAND 116 125 {ECO:0000244|PDB:4ES7}.
STRAND 127 142 {ECO:0000244|PDB:4ES7}.
STRAND 145 155 {ECO:0000244|PDB:4ES7}.
HELIX 159 170 {ECO:0000244|PDB:4ES7}.
TURN 171 173 {ECO:0000244|PDB:4ES7}.
HELIX 176 178 {ECO:0000244|PDB:4ES7}.
STRAND 179 181 {ECO:0000244|PDB:4ES7}.
STRAND 244 250 {ECO:0000244|PDB:1BIK}.
TURN 251 254 {ECO:0000244|PDB:1BIK}.
STRAND 255 261 {ECO:0000244|PDB:1BIK}.
STRAND 263 265 {ECO:0000244|PDB:1BIK}.
STRAND 271 273 {ECO:0000244|PDB:1BIK}.
HELIX 274 281 {ECO:0000244|PDB:1BIK}.
HELIX 284 288 {ECO:0000244|PDB:1BIK}.
STRAND 300 306 {ECO:0000244|PDB:1BIK}.
TURN 307 310 {ECO:0000244|PDB:1BIK}.
STRAND 311 317 {ECO:0000244|PDB:1BIK}.
STRAND 319 321 {ECO:0000244|PDB:1BIK}.
STRAND 327 329 {ECO:0000244|PDB:1BIK}.
HELIX 330 337 {ECO:0000244|PDB:1BIK}.
SEQUENCE 352 AA; 38999 MW; BC001780094CBD06 CRC64;
MRSLGALLLL LSACLAVSAG PVPTPPDNIQ VQENFNISRI YGKWYNLAIG STCPWLKKIM
DRMTVSTLVL GEGATEAEIS MTSTRWRKGV CEETSGAYEK TDTDGKFLYH KSKWNITMES
YVVHTNYDEY AIFLTKKFSR HHGPTITAKL YGRAPQLRET LLQDFRVVAQ GVGIPEDSIF
TMADRGECVP GEQEPEPILI PRVRRAVLPQ EEEGSGGGQL VTEVTKKEDS CQLGYSAGPC
MGMTSRYFYN GTSMACETFQ YGGCMGNGNN FVTEKECLQT CRTVAACNLP IVRGPCRAFI
QLWAFDAVKG KCVLFPYGGC QGNGNKFYSE KECREYCGVP GDGDEELLRF SN


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