P02760 (AMBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. 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 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 Reference proteome
Gene Ontology (GO)
Biological_process	cell 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 immune response Non-traceable author statement PubMed 10097787. Source: UniProtKB protein catabolic process Inferred from electronic annotation. Source: Compara protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara extracellular region Non-traceable author statement PubMed 11877257PubMed 14718574. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara intracellular membrane-bounded organelle Inferred from electronic annotation. Source: Compara plasma membrane Inferred from direct assay PubMed 12817471. Source: UniProtKB
Molecular_function	IgA 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 serine-type endopeptidase inhibitor activity Traceable author statement PubMed 12817471. Source: UniProtKB small molecule binding 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 Ref.28

Glycosylation

215

1

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

Glycosylation

250

1

N-linked (GlcNAc...) (complex) Ref.20 Ref.28

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 AA sequence Ref.10

Sequence conflict

57

1

Missing AA sequence 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...

Helix

37 – 40

4

Beta strand

42 – 52

11

Helix

54 – 59

6

Beta strand

60 – 62

3

Beta strand

66 – 72

7

Beta strand

78 – 86

9

Beta strand

88 – 100

13

Beta strand

106 – 111

6

Turn

112 – 115

4

Beta strand

116 – 125

10

Beta strand

127 – 137

11

Beta strand

140 – 143

4

Beta strand

145 – 155

11

Helix

159 – 171

13

Beta strand

179 – 181

3

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 [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] [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. , 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. , 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. , 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, 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 , 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. NM_001633.3.

UniGene

Hs.436911.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BIK	X-ray	2.50	A	206-352	[»]
3QKG	X-ray	2.30	A	20-202	[»]

ProteinModelPortal

P02760.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02760. 6 interactions.

MINT

MINT-1367019.

STRING

9606.ENSP00000265132.

Protein family/group databases

MEROPS

I02.005.

PTM databases

GlycoSuiteDB

P02760.

PhosphoSite

P02760.

Polymorphism databases

DMDM

122801.

2D gel databases

SWISS-2DPAGE

P02760.

Proteomic databases

PaxDb

P02760.

PeptideAtlas

P02760.

PRIDE

P02760.

Protocols and materials databases

DNASU

259.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265132; ENSP00000265132; ENSG00000106927.

GeneID

259.

KEGG

hsa:259.

UCSC

uc004bie.4. human.

Organism-specific databases

CTD

259.

GeneCards

GC09M116823.

HGNC

HGNC:453. AMBP.

HPA

HPA001497.

MIM

176870. gene.

neXtProt

NX_P02760.

PharmGKB

PA24759.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG328322.

HOVERGEN

HBG000225.

InParanoid

P02760.

OMA

TCPWLKK.

OrthoDB

EOG4XSKQ8.

PhylomeDB

P02760.

Gene expression databases

ArrayExpress

P02760.

Bgee

P02760.

CleanEx

HS_AMBP.

Genevestigator

P02760.

GermOnline

ENSG00000106927. Homo sapiens.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.
4.10.410.10. 2 hits.

InterPro

IPR002968. 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]

Pfam

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

PRINTS

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

SMART

SM00131. KU. 2 hits.
[Graphical view]

SUPFAM

SSF50814. Calycin. 1 hit.
SSF57362. Prot_inh_Kunz-m. 2 hits.

PROSITE

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

ProtoNet

Search...

Other

ChEMBL

CHEMBL1741301.

ChiTaRS

AMBP. human.

DrugBank

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

EvolutionaryTrace

P02760.

GenomeRNAi

259.

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:	May 1, 2013
This is version 165 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.