Reviewed, UniProtKB/Swiss-Prot P02760 (AMBP_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein AMBP
Cleaved into the following 3 chains:
    1- Recommended name:
            Alpha-1-microglobulin
                Short name=Protein HC
        Alternative name(s):
            Complex-forming glycoprotein heterogeneous in charge
            Alpha-1 microglycoprotein
    2- Recommended name:
            Inter-alpha-trypsin inhibitor light chain
                Short name=ITI-LC
        Alternative name(s):
            Bikunin
            HI-30
            Uronic-acid-rich protein
            EDC1
    3- Recommended name:
            Trypstatin

Gene names

Name:	AMBP
Synonyms:	HCP, ITIL

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization. Ref.18 Trypstatin is a trypsin inhibitor By similarity.
Subunit structure	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.
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.
Post-translational modification	The precursor is proteolytically processed into separately functioning proteins. 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'. Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the their C-terminal aspartate By similarity. Addition of glycosaminoglycan chondroitin sulfate, allows cross-linking between the different components.
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.
Sequence similarities	In the N-terminal section; belongs to the calycin superfamily. Lipocalin family. Contains 2 BPTI/Kunitz inhibitor domains.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Chromophore
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell adhesion Non-traceable author statement. Source: UniProtKB female pregnancy Non-traceable author statement. Source: UniProtKB heme catabolic process Non-traceable author statement. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of JNK cascade Traceable author statement. Source: UniProtKB negative regulation of immune response Non-traceable author statement. Source: UniProtKB protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Non-traceable author statement. Source: UniProtKB plasma membrane Inferred from direct assay. Source: UniProtKB
Molecular function	IgA binding Inferred from direct assay. Source: UniProtKB calcium channel inhibitor activity Non-traceable author statement. Source: UniProtKB calcium oxalate binding Non-traceable author statement. Source: UniProtKB heme binding Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase inhibitor activity Traceable author statement. Source: UniProtKB transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.10 Ref.11 Ref.12

Chain

20 – 203

184

Alpha-1-microglobulin

PRO_0000017886

Chain

206 – 352

147

Inter-alpha-trypsin inhibitor light chain

PRO_0000017887

Chain

284 – 344

61

Trypstatin By similarity

PRO_0000318926

Regions

Domain

231 – 281

51

BPTI/Kunitz inhibitor 1

Domain

287 – 337

51

BPTI/Kunitz inhibitor 2

Region

206 – 226

21

Glycopeptide (secretory piece)

Sites

Binding site

53

1

Multimeric 3-hydroxykynurenine chromophore (covalent)

Binding site

111

1

Multimeric 3-hydroxykynurenine chromophore (covalent)

Binding site

137

1

Multimeric 3-hydroxykynurenine chromophore (covalent)

Binding site

149

1

Multimeric 3-hydroxykynurenine chromophore (covalent)

Site

241 – 242

2

Inhibitory (P1) (chymotrypsin, elastase) By similarity

Site

297 – 298

2

Inhibitory (P1) (trypsin) By similarity

Amino acid modifications

Glycosylation

24

1

O-linked (GalNAc...) Ref.22

CAR_000172

Glycosylation

36

1

N-linked (GlcNAc...) (complex) Ref.22

Glycosylation

115

1

N-linked (GlcNAc...) (complex) Ref.22

Glycosylation

215

1

O-linked (Xyl...) (chondroitin sulfate) Ref.16 Ref.17 Ref.20

Glycosylation

250

1

N-linked (GlcNAc...) Ref.20

Disulfide bond

91 ↔ 188

Disulfide bond

231 ↔ 281

Disulfide bond

240 ↔ 264

Disulfide bond

256 ↔ 277

Disulfide bond

287 ↔ 337

Disulfide bond

296 ↔ 320

Disulfide bond

312 ↔ 333

Experimental info

Sequence conflict

48 – 57

10

Missing AA sequence Ref.11

Sequence conflict

57

1

Missing Ref.10

Sequence conflict

57

1

Missing Ref.12

Sequence conflict

137

1

Missing AA sequence Ref.11

Sequence conflict

142

1

H → T AA sequence Ref.11

Sequence conflict

145

1

Missing AA sequence Ref.11

Sequence conflict

194

1

E → Q AA sequence Ref.11

Sequence conflict

215

1

S → T AA sequence Ref.18

Sequence conflict

218

1

G → T AA sequence Ref.18

Sequence conflict

291 – 292

2

IV → VI AA sequence Ref.14

Sequence conflict

291 – 292

2

IV → VI AA sequence Ref.15

Sequence conflict

295

1

Missing AA sequence Ref.15

Sequence conflict

343

1

G → E AA sequence Ref.14

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

352

Helix Strand Turn

Details...

Beta strand

244 – 250

7

Turn

251 – 254

4

Beta strand

255 – 261

7

Beta strand

263 – 265

3

Beta strand

271 – 273

3

Helix

274 – 281

8

Helix

284 – 288

5

Beta strand

300 – 306

7

Turn

307 – 310

4

Beta strand

311 – 317

7

Beta strand

319 – 321

3

Beta strand

327 – 329

3

Helix

330 – 337

8

Sequences

	Sequence		Length	Mass (Da)
	P02760-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: BC001780094CBD06	FASTA	352	38,999
	10 20 30 40 50 60 MRSLGALLLL LSACLAVSAG PVPTPPDNIQ VQENFNISRI YGKWYNLAIG STCPWLKKIM 70 80 90 100 110 120 DRMTVSTLVL GEGATEAEIS MTSTRWRKGV CEETSGAYEK TDTDGKFLYH KSKWNITMES 130 140 150 160 170 180 YVVHTNYDEY AIFLTKKFSR HHGPTITAKL YGRAPQLRET LLQDFRVVAQ GVGIPEDSIF 190 200 210 220 230 240 TMADRGECVP GEQEPEPILI PRVRRAVLPQ EEEGSGGGQL VTEVTKKEDS CQLGYSAGPC 250 260 270 280 290 300 MGMTSRYFYN GTSMACETFQ YGGCMGNGNN FVTEKECLQT CRTVAACNLP IVRGPCRAFI 310 320 330 340 350 QLWAFDAVKG KCVLFPYGGC QGNGNKFYSE KECREYCGVP GDGDEELLRF SN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of a full length cDNA coding for human protein HC (alpha 1 microglobulin)." Traboni C., Cortese R. Nucleic Acids Res. 14:6340-6340(1986) [PubMed: 2428011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC)." Kaumeyer J.F., Polazzi J.O., Kotick M.P. Nucleic Acids Res. 14:7839-7850(1986) [PubMed: 2430261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Structure of the human alpha 1-microglobulin-bikunin gene." Vetr H., Gebhard W. Biol. Chem. Hoppe-Seyler 371:1185-1196(1990) [PubMed: 1708673] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Structural analysis of the human inter-alpha-trypsin inhibitor light-chain gene." Diarra-Mehrpour M., Bourguignon J., Sesboue R., Salier J.-P., Leveillard T., Martin J.-P. Eur. J. Biochem. 191:131-139(1990) [PubMed: 1696200] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[5]	"Identification of a human cell growth inhibition gene." Kim J.W. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[7]	"DNA sequence and analysis of human chromosome 9." 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. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[10]	"The complete amino acid sequence of human complex-forming glycoprotein heterogeneous in charge (protein HC) from one individual." Lopez C., Grubb A.O., Mendez E. Arch. Biochem. Biophys. 228:544-554(1984) [PubMed: 6198962] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-202.
[11]	"Complete amino acid sequence of human alpha 1-microglobulin." Takagi T., Takagi K., Kawai T. Biochem. Biophys. Res. Commun. 98:997-1001(1981) [PubMed: 6164372] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-198.
[12]	"Human protein HC displays variability in its carboxyl-terminal amino acid sequence." Lopez C., Grubb A.O., Mendez E. FEBS Lett. 144:349-353(1982) Cited for: PROTEIN SEQUENCE OF 20-198.
[13]	"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." Calero M., Escribano J., Grubb A., Mendez E. J. Biol. Chem. 269:384-389(1994) [PubMed: 7506257] [Abstract] Cited for: PROTEIN SEQUENCE OF 44-57, BINDING TO CHROMOPHORE.
[14]	"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." Reisinger P., Hochstrasser K., Albrecht G.J., Lempart K., Salier J.-P. Biol. Chem. Hoppe-Seyler 366:479-483(1985) [PubMed: 2408638] [Abstract] Cited for: PROTEIN SEQUENCE OF 206-350.
[15]	"Cancer-related urinary proteinase inhibitor, EDC1: a new method for its isolation and evidence for multiple forms." Chawla R.K., Lawson D.H., Ahmad M., Travis J. J. Cell. Biochem. 50:227-236(1992) [PubMed: 1469060] [Abstract] Cited for: PROTEIN SEQUENCE OF 206-243 AND 275-303. Tissue: Urine.
[16]	"Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor." Enghild J.J., Salvesen G., Hefta S.A., Thoegersen I.B., Rutherfurd S., Pizzo S.V. J. Biol. Chem. 266:747-751(1991) [PubMed: 1898736] [Abstract] Cited for: PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, CROSS-LINK SITE TO HC3.
[17]	"Presence of the protein-glycosaminoglycan-protein covalent cross-link in the inter-alpha-inhibitor-related proteinase inhibitor heavy chain 2/bikunin." Enghild J.J., Salvesen G., Thoegersen I.B., Valnickova Z., Pizzo S.V., Hefta S.A. J. Biol. Chem. 268:8711-8716(1993) [PubMed: 7682553] [Abstract] Cited for: PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, CROSS-LINK SITE TO HC2.
[18]	"Characterization of uronic-acid-rich inhibitor of calcium oxalate crystallization isolated from rat urine." Atmani F., Khan S.R. Urol. Res. 23:95-101(1995) [PubMed: 7676539] [Abstract] Cited for: PROTEIN SEQUENCE OF 206-223, FUNCTION. Tissue: Urine.
[19]	"Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor." Morelle W., Capon C., Balduyck M., Sautiere P., Kouach M., Michalski C., Fournet B., Mizon J. Eur. J. Biochem. 221:881-888(1994) [PubMed: 7513643] [Abstract] Cited for: PROTEIN SEQUENCE OF 206-219, COVALENT LINKAGE WITH CHONDROITIN SULFATE. Tissue: Plasma.
[20]	"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." Hochstrasser K., Schoenberger O.L., Rossmanith I., Wachter E. Hoppe-Seyler's Z. Physiol. Chem. 362:1357-1362(1981) [PubMed: 6171497] [Abstract] Cited for: GLYCOSYLATION AT SER-215 AND ASN-250, STRUCTURE OF CARBOHYDRATES.
[21]	"The reactive site of human inter-alpha-trypsin inhibitor is in the amino-terminal half of the protein." Morii M., Travis J. Biol. Chem. Hoppe-Seyler 366:19-21(1985) [PubMed: 3890890] [Abstract] Cited for: INHIBITORY SITE.
[22]	"Location and characterization of the three carbohydrate prosthetic groups of human protein HC." Escribano J., Lopex-Otin C., Hjerpe A., Grubb A.O., Mendez E. FEBS Lett. 266:167-170(1990) [PubMed: 1694784] [Abstract] Cited for: GLYCOSYLATION AT THR-24; ASN-36 AND ASN-115, STRUCTURE OF CARBOHYDRATES.
[23]	"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." Escribano J., Grubb A.O., Calero M., Mendez E. J. Biol. Chem. 266:15758-15763(1991) [PubMed: 1714898] [Abstract] Cited for: BINDING TO CHROMOPHORE. Tissue: Urine.
[24]	"Alpha1-microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound." Berggaard T., Cohen A., Persson P., Lindqvist A., Cedervall T., Silow M., Thoegersen I.B., Joensson J.A., Enghild J.J., Aakerstroem B. Protein Sci. 8:2611-2620(1999) [PubMed: 10631976] [Abstract] Cited for: BINDING TO CHROMOPHORE.
[25]	"Human alpha-1-microglobulin is covalently bound to kynurenine-derived chromophores." Sala A., Campagnoli M., Perani E., Romano A., Labo S., Monzani E., Minchiotti L., Galliano M. J. Biol. Chem. 279:51033-51041(2004) [PubMed: 15452109] [Abstract] Cited for: CHROMOPHORE CHARACTERIZATION.
[26]	"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." Tyagi S., Surjit M., Roy A.K., Jameel S., Lal S.K. J. Biol. Chem. 279:29308-29319(2004) [PubMed: 15037615] [Abstract] Cited for: INTERACTION OF ALPHA-1-MICROGLOBULIN WITH HEV ORF3 PROTEIN.
[27]	"The 41-amino-acid C-terminal region of the hepatitis E virus ORF3 protein interacts with bikunin, a kunitz-type serine protease inhibitor." Tyagi S., Surjit M., Lal S.K. J. Virol. 79:12081-12087(2005) [PubMed: 16140784] [Abstract] Cited for: INTERACTION OF BIKUNIN WITH HEV ORF3 PROTEIN.
[28]	"The crystal structure of bikunin from the inter-alpha-inhibitor complex: a serine protease inhibitor with two Kunitz domains." Xu Y., Carr P.D., Guss J.M., Ollis D.L. J. Mol. Biol. 276:955-966(1998) [PubMed: 9566199] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 230-339.
[29]	"Alpha(1)-microglobulin: a yellow-brown lipocalin." Aakerstroem B., Loegdberg L., Berggaard T., Osmark P., Lindqvist A. Biochim. Biophys. Acta 1482:172-184(2000) [PubMed: 11058759] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X04225 mRNA. Translation: CAA27803.1.
X04494 mRNA. Translation: CAA28182.1.
X54816, X54817, X54818 Genomic DNA. Translation: CAA38585.1.
X54817 Genomic DNA. Translation: CAA38586.1.
X54818 Genomic DNA. Translation: CAA38587.1.
M88249 , M88165, M88243, M88244, M88246, M88247 Genomic DNA. Translation: AAA59196.1.
AY544123 mRNA. Translation: AAT11154.1.
AK290837 mRNA. Translation: BAF83526.1.
AL137850 Genomic DNA. Translation: CAI15899.1.
CH471090 Genomic DNA. Translation: EAW87404.1.
BC041593 mRNA. Translation: AAH41593.1.

IPI

IPI00022426.

PIR

HCHU. S13433.

RefSeq

NP_001624.1.

UniGene

Hs.436911

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BIK	X-ray	2.50	A	206-352	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P02760. 3 interactions.

STRING

P02760.

Protein family/group databases

MEROPS

I02.005.
I02.006.

PTM databases

GlycoSuiteDB

P02760.

PhosphoSite

P02760.

2-D gel databases

SWISS-2DPAGE

P02760.

Siena-2DPAGE

P02760.

Proteomic databases

PeptideAtlas

P02760.

PRIDE

P02760.

Genome annotation databases

Ensembl

ENST00000265132; ENSP00000265132; ENSG00000106927; Homo sapiens. [Genome view]

GeneID

259.

KEGG

hsa:259.

UCSC

uc004bie.2. human.

Organism-specific databases

CTD

259.

GeneCards

GC09M115862.

H-InvDB

HIX0025747.

HGNC

HGNC:453. AMBP.

HPA

HPA001497.

MIM

176870. gene.

PharmGKB

PA24759.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P02760.

HOVERGEN

P02760.

OMA

GKFLYHK.

Gene expression databases

ArrayExpress

P02760.

Bgee

P02760.

CleanEx

HS_AMBP.

Genevestigator

P02760.

GermOnline

ENSG00000106927. Homo sapiens.

Family and domain databases

InterPro

IPR002968. A1-microglobln.
IPR012674. Calycin.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytFABP.
IPR002223. Prot_inh_Kunz-m.
[Graphical view]

Gene3D

G3DSA:2.40.128.20. Calycin. 1 hit.
G3DSA:4.10.410.10. Prot_inh_Kunz-m. 1 hit.

Pfam

PF00014. Kunitz_BPTI. 2 hits.
PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR01215. A1MCGLOBULIN.
PR00759. BASICPTASE.
PR00179. LIPOCALIN.

ProDom

PD000222. Prot_Inh_Kunz-m. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00131. KU. 2 hits.
[Graphical view]

PROSITE

PS00280. BPTI_KUNITZ_1. 2 hits.
PS50279. BPTI_KUNITZ_2. 2 hits.
PS00213. LIPOCALIN. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

DrugBank

DB00062. Human Serum Albumin.
DB00064. Serum albumin iodonated.

NextBio

1023.

PMAP-CutDB

P02760.

SOURCE

Search...

Entry information

Entry name

AMBP_HUMAN

Accession

Primary (citable) accession number: P02760
Secondary accession number(s): P00977 , P02759, P78491, Q2TU33, Q5TBD7, Q9UC58, Q9UDI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	November 3, 2009
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.