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P02760 (AMBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein AMBP

Cleaved into the following 3 chains:

  1. Alpha-1-microglobulin
    Short name=Protein HC
    Alternative name(s):
    Alpha-1 microglycoprotein
    Complex-forming glycoprotein heterogeneous in charge
  2. Inter-alpha-trypsin inhibitor light chain
    Short name=ITI-LC
    Alternative name(s):
    Bikunin
    EDC1
    HI-30
    Uronic-acid-rich protein
  3. Trypstatin
Gene names
Name:AMBP
Synonyms:HCP, ITIL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.18

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. Ref.26 Ref.27

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.

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. Ref.16 Ref.17 Ref.20 Ref.22 Ref.28

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 processHost-virus interaction
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandChromophore
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Non-traceable author statement PubMed 9570066. Source: UniProtKB

female pregnancy

Non-traceable author statement PubMed 10097787. Source: UniProtKB

heme catabolic process

Non-traceable author statement PubMed 11877257. Source: UniProtKB

negative regulation of JNK cascade

Traceable author statement PubMed 12817471. Source: UniProtKB

negative regulation of endopeptidase activity

Traceable author statement PubMed 12817471. Source: GOC

negative regulation of immune response

Non-traceable author statement PubMed 10097787. Source: UniProtKB

protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein-chromophore linkage

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cell surface

Inferred from electronic annotation. Source: Ensembl

extracellular region

Non-traceable author statement PubMed 11877257PubMed 14718574. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

intracellular membrane-bounded organelle

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 12817471. Source: UniProtKB

   Molecular_functionIgA binding

Inferred from direct assay PubMed 11877257. Source: UniProtKB

calcium channel inhibitor activity

Non-traceable author statement PubMed 12817471. Source: UniProtKB

calcium oxalate binding

Non-traceable author statement PubMed 14516400. Source: UniProtKB

heme binding

Inferred from direct assay PubMed 11877257. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16364318. Source: IntAct

protein homodimerization activity

Inferred from physical interaction PubMed 11883904. Source: UniProtKB

serine-type endopeptidase inhibitor activity

Traceable author statement PubMed 12817471. Source: UniProtKB

small molecule binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTSBP078584EBI-2115136,EBI-715062

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.10 Ref.11 Ref.12
Chain20 – 203184Alpha-1-microglobulin
PRO_0000017886
Chain206 – 352147Inter-alpha-trypsin inhibitor light chain
PRO_0000017887
Chain284 – 34461Trypstatin By similarity
PRO_0000318926

Regions

Domain231 – 28151BPTI/Kunitz inhibitor 1
Domain287 – 33751BPTI/Kunitz inhibitor 2
Region206 – 22621Glycopeptide (secretory piece)

Sites

Binding site531Multimeric 3-hydroxykynurenine chromophore (covalent)
Binding site1111Multimeric 3-hydroxykynurenine chromophore (covalent)
Binding site1371Multimeric 3-hydroxykynurenine chromophore (covalent)
Binding site1491Multimeric 3-hydroxykynurenine chromophore (covalent)
Site241 – 2422Inhibitory (P1) (chymotrypsin, elastase) By similarity
Site297 – 2982Inhibitory (P1) (trypsin) By similarity

Amino acid modifications

Glycosylation241O-linked (GalNAc...) Ref.22
CAR_000172
Glycosylation361N-linked (GlcNAc...) (complex) Ref.22
Glycosylation1151N-linked (GlcNAc...) (complex) Ref.22 Ref.28
Glycosylation2151O-linked (Xyl...) (chondroitin sulfate) Ref.16 Ref.17 Ref.20
Glycosylation2501N-linked (GlcNAc...) (complex) Ref.20 Ref.28
Disulfide bond91 ↔ 188
Disulfide bond231 ↔ 281
Disulfide bond240 ↔ 264
Disulfide bond256 ↔ 277
Disulfide bond287 ↔ 337
Disulfide bond296 ↔ 320
Disulfide bond312 ↔ 333

Experimental info

Sequence conflict48 – 5710Missing AA sequence Ref.11
Sequence conflict571Missing AA sequence Ref.10
Sequence conflict571Missing AA sequence Ref.12
Sequence conflict1371Missing AA sequence Ref.11
Sequence conflict1421H → T AA sequence Ref.11
Sequence conflict1451Missing AA sequence Ref.11
Sequence conflict1941E → Q AA sequence Ref.11
Sequence conflict2151S → T AA sequence Ref.18
Sequence conflict2181G → T AA sequence Ref.18
Sequence conflict291 – 2922IV → VI AA sequence Ref.14
Sequence conflict291 – 2922IV → VI AA sequence Ref.15
Sequence conflict2951Missing AA sequence Ref.15
Sequence conflict3431G → E AA sequence Ref.14

Secondary structure

................................................ 352
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02760 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: BC001780094CBD06

FASTA35238,999
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION OF BIKUNIN WITH HEV ORF3 PROTEIN.
[28]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-115 AND ASN-250, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[29]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 230-339.
[30]"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] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , 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.
CCDSCCDS6800.1.
PIRHCHU. S13433.
RefSeqNP_001624.1. NM_001633.3.
UniGeneHs.436911.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BIKX-ray2.50A206-352[»]
3QKGX-ray2.30A20-202[»]
4ES7X-ray2.00A27-193[»]
ProteinModelPortalP02760.
SMRP02760. Positions 28-193, 230-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106757. 12 interactions.
IntActP02760. 7 interactions.
MINTMINT-1367019.
STRING9606.ENSP00000265132.

Chemistry

DrugBankDB00062. Human Serum Albumin.
DB00064. Serum albumin iodonated.

Protein family/group databases

MEROPSI02.005.

PTM databases

PhosphoSiteP02760.
UniCarbKBP02760.

Polymorphism databases

DMDM122801.

2D gel databases

SWISS-2DPAGEP02760.

Proteomic databases

MaxQBP02760.
PaxDbP02760.
PeptideAtlasP02760.
PRIDEP02760.

Protocols and materials databases

DNASU259.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265132; ENSP00000265132; ENSG00000106927.
GeneID259.
KEGGhsa:259.
UCSCuc004bie.4. human.

Organism-specific databases

CTD259.
GeneCardsGC09M116823.
HGNCHGNC:453. AMBP.
HPAHPA001497.
MIM176870. gene.
neXtProtNX_P02760.
PharmGKBPA24759.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG328322.
HOVERGENHBG000225.
InParanoidP02760.
OMAGTSMACE.
OrthoDBEOG73FQKT.
PhylomeDBP02760.
TreeFamTF351222.

Enzyme and pathway databases

ReactomeREACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP02760.
BgeeP02760.
CleanExHS_AMBP.
GenevestigatorP02760.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
4.10.410.10. 2 hits.
InterProIPR002968. A1-microglobln.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamPF00014. Kunitz_BPTI. 2 hits.
PF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR01215. A1MCGLOBULIN.
PR00759. BASICPTASE.
PR00179. LIPOCALIN.
SMARTSM00131. KU. 2 hits.
[Graphical view]
SUPFAMSSF50814. SSF50814. 1 hit.
SSF57362. SSF57362. 2 hits.
PROSITEPS00280. BPTI_KUNITZ_1. 2 hits.
PS50279. BPTI_KUNITZ_2. 2 hits.
PS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAMBP. human.
EvolutionaryTraceP02760.
GeneWikiAlpha-1-microglobulin/bikunin_precursor.
GenomeRNAi259.
NextBio1023.
PMAP-CutDBP02760.
PROP02760.
SOURCESearch...

Entry information

Entry nameAMBP_HUMAN
AccessionPrimary (citable) accession number: P02760
Secondary accession number(s): P00977 expand/collapse secondary AC list , P02759, P78491, Q2TU33, Q5TBD7, Q9UC58, Q9UDI8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 178 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM