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P02760

- AMBP_HUMAN

UniProt

P02760 - AMBP_HUMAN

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Protein
Protein AMBP
Gene
AMBP, HCP, ITIL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization.1 Publication
Trypstatin is a trypsin inhibitor By similarity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Multimeric 3-hydroxykynurenine chromophore (covalent)
Binding sitei111 – 1111Multimeric 3-hydroxykynurenine chromophore (covalent)
Binding sitei137 – 1371Multimeric 3-hydroxykynurenine chromophore (covalent)
Binding sitei149 – 1491Multimeric 3-hydroxykynurenine chromophore (covalent)
Sitei241 – 2422Inhibitory (P1) (chymotrypsin, elastase) By similarity
Sitei297 – 2982Inhibitory (P1) (trypsin) By similarity

GO - Molecular functioni

  1. IgA binding Source: UniProtKB
  2. calcium channel inhibitor activity Source: UniProtKB
  3. calcium oxalate binding Source: UniProtKB
  4. heme binding Source: UniProtKB
  5. protein binding Source: IntAct
  6. protein homodimerization activity Source: UniProtKB
  7. serine-type endopeptidase inhibitor activity Source: UniProtKB
  8. small molecule binding Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB
  2. female pregnancy Source: UniProtKB
  3. heme catabolic process Source: UniProtKB
  4. negative regulation of JNK cascade Source: UniProtKB
  5. negative regulation of endopeptidase activity Source: GOC
  6. negative regulation of immune response Source: UniProtKB
  7. protein catabolic process Source: Ensembl
  8. protein-chromophore linkage Source: UniProtKB-KW
  9. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Chromophore

Enzyme and pathway databases

ReactomeiREACT_160163. Scavenging of heme from plasma.

Protein family/group databases

MEROPSiI02.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein AMBP
Cleaved into the following 3 chains:
Alpha-1-microglobulin
Short name:
Protein HC
Alternative name(s):
Alpha-1 microglycoprotein
Complex-forming glycoprotein heterogeneous in charge
Alternative name(s):
Bikunin
EDC1
HI-30
Uronic-acid-rich protein
Gene namesi
Name:AMBP
Synonyms:HCP, ITIL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:453. AMBP.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. cell surface Source: Ensembl
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProt
  6. intracellular membrane-bounded organelle Source: Ensembl
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24759.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19193 Publications
Add
BLAST
Chaini20 – 203184Alpha-1-microglobulin
PRO_0000017886Add
BLAST
Chaini206 – 352147Inter-alpha-trypsin inhibitor light chain
PRO_0000017887Add
BLAST
Chaini284 – 34461Trypstatin By similarity
PRO_0000318926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241O-linked (GalNAc...)1 Publication
CAR_000172
Glycosylationi36 – 361N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi91 ↔ 188
Glycosylationi115 – 1151N-linked (GlcNAc...) (complex)2 Publications
Glycosylationi215 – 2151O-linked (Xyl...) (chondroitin sulfate)3 Publications
Disulfide bondi231 ↔ 281
Disulfide bondi240 ↔ 264
Glycosylationi250 – 2501N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi256 ↔ 277
Disulfide bondi287 ↔ 337
Disulfide bondi296 ↔ 320
Disulfide bondi312 ↔ 333

Post-translational modificationi

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.5 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP02760.
PaxDbiP02760.
PeptideAtlasiP02760.
PRIDEiP02760.

2D gel databases

SWISS-2DPAGEP02760.

PTM databases

PhosphoSiteiP02760.
UniCarbKBiP02760.

Miscellaneous databases

PMAP-CutDBP02760.

Expressioni

Tissue specificityi

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.

Gene expression databases

ArrayExpressiP02760.
BgeeiP02760.
CleanExiHS_AMBP.
GenevestigatoriP02760.

Organism-specific databases

HPAiHPA001497.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTSBP078584EBI-2115136,EBI-715062

Protein-protein interaction databases

BioGridi106757. 12 interactions.
IntActiP02760. 7 interactions.
MINTiMINT-1367019.
STRINGi9606.ENSP00000265132.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 393
Beta strandi42 – 5110
Helixi54 – 596
Helixi60 – 623
Beta strandi66 – 727
Beta strandi78 – 8710
Beta strandi90 – 10011
Beta strandi106 – 1116
Turni112 – 1154
Beta strandi116 – 12510
Beta strandi127 – 14216
Beta strandi145 – 15511
Helixi159 – 17012
Turni171 – 1733
Helixi176 – 1783
Beta strandi179 – 1813
Beta strandi244 – 2507
Turni251 – 2544
Beta strandi255 – 2617
Beta strandi263 – 2653
Beta strandi271 – 2733
Helixi274 – 2818
Helixi284 – 2885
Beta strandi300 – 3067
Turni307 – 3104
Beta strandi311 – 3177
Beta strandi319 – 3213
Beta strandi327 – 3293
Helixi330 – 3378

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BIKX-ray2.50A206-352[»]
3QKGX-ray2.30A20-202[»]
4ES7X-ray2.00A27-193[»]
ProteinModelPortaliP02760.
SMRiP02760. Positions 28-193, 230-339.

Miscellaneous databases

EvolutionaryTraceiP02760.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini231 – 28151BPTI/Kunitz inhibitor 1
Add
BLAST
Domaini287 – 33751BPTI/Kunitz inhibitor 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni206 – 22621Glycopeptide (secretory piece)
Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the calycin superfamily. Lipocalin family.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG328322.
HOVERGENiHBG000225.
InParanoidiP02760.
OMAiGTSMACE.
OrthoDBiEOG73FQKT.
PhylomeDBiP02760.
TreeFamiTF351222.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
4.10.410.10. 2 hits.
InterProiIPR002968. 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]
PfamiPF00014. Kunitz_BPTI. 2 hits.
PF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01215. A1MCGLOBULIN.
PR00759. BASICPTASE.
PR00179. LIPOCALIN.
SMARTiSM00131. KU. 2 hits.
[Graphical view]
SUPFAMiSSF50814. SSF50814. 1 hit.
SSF57362. SSF57362. 2 hits.
PROSITEiPS00280. BPTI_KUNITZ_1. 2 hits.
PS50279. BPTI_KUNITZ_2. 2 hits.
PS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02760-1 [UniParc]FASTAAdd to Basket

« Hide

MRSLGALLLL LSACLAVSAG PVPTPPDNIQ VQENFNISRI YGKWYNLAIG    50
STCPWLKKIM DRMTVSTLVL GEGATEAEIS MTSTRWRKGV CEETSGAYEK 100
TDTDGKFLYH KSKWNITMES YVVHTNYDEY AIFLTKKFSR HHGPTITAKL 150
YGRAPQLRET LLQDFRVVAQ GVGIPEDSIF TMADRGECVP GEQEPEPILI 200
PRVRRAVLPQ EEEGSGGGQL VTEVTKKEDS CQLGYSAGPC MGMTSRYFYN 250
GTSMACETFQ YGGCMGNGNN FVTEKECLQT CRTVAACNLP IVRGPCRAFI 300
QLWAFDAVKG KCVLFPYGGC QGNGNKFYSE KECREYCGVP GDGDEELLRF 350
SN 352
Length:352
Mass (Da):38,999
Last modified:August 13, 1987 - v1
Checksum:iBC001780094CBD06
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 5710Missing AA sequence 1 Publication
Sequence conflicti57 – 571Missing AA sequence 1 Publication
Sequence conflicti57 – 571Missing AA sequence 1 Publication
Sequence conflicti137 – 1371Missing AA sequence 1 Publication
Sequence conflicti142 – 1421H → T AA sequence 1 Publication
Sequence conflicti145 – 1451Missing AA sequence 1 Publication
Sequence conflicti194 – 1941E → Q AA sequence 1 Publication
Sequence conflicti215 – 2151S → T AA sequence 1 Publication
Sequence conflicti218 – 2181G → T AA sequence 1 Publication
Sequence conflicti291 – 2922IV → VI AA sequence 1 Publication
Sequence conflicti291 – 2922IV → VI AA sequence 1 Publication
Sequence conflicti295 – 2951Missing AA sequence 1 Publication
Sequence conflicti343 – 3431G → E AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6800.1.
PIRiS13433. HCHU.
RefSeqiNP_001624.1. NM_001633.3.
UniGeneiHs.436911.

Genome annotation databases

EnsembliENST00000265132; ENSP00000265132; ENSG00000106927.
GeneIDi259.
KEGGihsa:259.
UCSCiuc004bie.4. human.

Polymorphism databases

DMDMi122801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6800.1.
PIRi S13433. HCHU.
RefSeqi NP_001624.1. NM_001633.3.
UniGenei Hs.436911.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BIK X-ray 2.50 A 206-352 [» ]
3QKG X-ray 2.30 A 20-202 [» ]
4ES7 X-ray 2.00 A 27-193 [» ]
ProteinModelPortali P02760.
SMRi P02760. Positions 28-193, 230-339.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106757. 12 interactions.
IntActi P02760. 7 interactions.
MINTi MINT-1367019.
STRINGi 9606.ENSP00000265132.

Chemistry

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

Protein family/group databases

MEROPSi I02.005.

PTM databases

PhosphoSitei P02760.
UniCarbKBi P02760.

Polymorphism databases

DMDMi 122801.

2D gel databases

SWISS-2DPAGE P02760.

Proteomic databases

MaxQBi P02760.
PaxDbi P02760.
PeptideAtlasi P02760.
PRIDEi P02760.

Protocols and materials databases

DNASUi 259.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265132 ; ENSP00000265132 ; ENSG00000106927 .
GeneIDi 259.
KEGGi hsa:259.
UCSCi uc004bie.4. human.

Organism-specific databases

CTDi 259.
GeneCardsi GC09M116823.
HGNCi HGNC:453. AMBP.
HPAi HPA001497.
MIMi 176870. gene.
neXtProti NX_P02760.
PharmGKBi PA24759.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG328322.
HOVERGENi HBG000225.
InParanoidi P02760.
OMAi GTSMACE.
OrthoDBi EOG73FQKT.
PhylomeDBi P02760.
TreeFami TF351222.

Enzyme and pathway databases

Reactomei REACT_160163. Scavenging of heme from plasma.

Miscellaneous databases

ChiTaRSi AMBP. human.
EvolutionaryTracei P02760.
GeneWikii Alpha-1-microglobulin/bikunin_precursor.
GenomeRNAii 259.
NextBioi 1023.
PMAP-CutDB P02760.
PROi P02760.
SOURCEi Search...

Gene expression databases

ArrayExpressi P02760.
Bgeei P02760.
CleanExi HS_AMBP.
Genevestigatori P02760.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
4.10.410.10. 2 hits.
InterProi 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 ]
Pfami PF00014. Kunitz_BPTI. 2 hits.
PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR01215. A1MCGLOBULIN.
PR00759. BASICPTASE.
PR00179. LIPOCALIN.
SMARTi SM00131. KU. 2 hits.
[Graphical view ]
SUPFAMi SSF50814. SSF50814. 1 hit.
SSF57362. SSF57362. 2 hits.
PROSITEi PS00280. BPTI_KUNITZ_1. 2 hits.
PS50279. BPTI_KUNITZ_2. 2 hits.
PS00213. LIPOCALIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiAMBP_HUMAN
AccessioniPrimary (citable) accession number: P02760
Secondary accession number(s): P00977
, P02759, P78491, Q2TU33, Q5TBD7, Q9UC58, Q9UDI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: September 3, 2014
This is version 179 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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