P02763 (A1AG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-1-acid glycoprotein 1
Short name=AGP 1

Alternative name(s):
Orosomucoid-1
Short name=OMD 1

Gene names

Name:	ORM1
Synonyms:	AGP1

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	201 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	Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction. Ref.18 Ref.20
Subcellular location	Secreted.
Tissue specificity	Expressed by the liver and secreted in plasma.
Induction	Synthesis is controlled by glucocorticoids, interleukin-1 and interleukin-6, It increases 5- to 50-fold upon inflammation.
Domain	Contains a beta-barrel that binds various ligands in its interior. Ref.24
Post-translational modification	N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor). Ref.12 Ref.13 Ref.14 Ref.23
Polymorphism	Three common alleles of ORM1 are known. ORM1*F1 has Gln-38/Val-174; ORM1*F2 has Gln-38/Met-174 and ORM1*S has Arg-38/Val-174. The sequence shown is that of allele ORM1*F1.
Sequence similarities	Belongs to the calycin superfamily. Lipocalin family.
Sequence caution	The sequence CAA29229.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Acute phase Transport
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acute-phase response Traceable author statement Ref.1. Source: ProtInc regulation of immune system process Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular space Traceable author statement PubMed 3360326. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SERPINE1	P05121	4	EBI-976767,EBI-953978

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.9

Chain

19 – 201

183

Alpha-1-acid glycoprotein 1

PRO_0000017860

Amino acid modifications

Modified residue

19

1

Pyrrolidone carboxylic acid Ref.9

Glycosylation

33

1

N-linked (GlcNAc...) (complex) Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.22 Ref.23

Glycosylation

56

1

N-linked (GlcNAc...) Ref.11 Ref.12 Ref.16 Ref.17

Glycosylation

72

1

N-linked (GlcNAc...) (complex) Ref.12 Ref.14 Ref.16 Ref.17 Ref.22

Glycosylation

93

1

N-linked (GlcNAc...) Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21

Glycosylation

103

1

N-linked (GlcNAc...) Ref.12 Ref.16 Ref.17 Ref.21

CAR_000170

Disulfide bond

23 ↔ 165

Ref.11 Ref.24

Disulfide bond

90 ↔ 183

Ref.11 Ref.24

Natural variations

Natural variant

38

1

Q → R in allele ORM1*S. Ref.6 Ref.7 Ref.8 Ref.25

VAR_013840

Natural variant

167

1

R → C. Ref.8
Corresponds to variant rs3182034 [ dbSNP | Ensembl ].

VAR_056166

Natural variant

174

1

V → M in allele ORM1*F2. Ref.8 Ref.25
Corresponds to variant rs1126801 [ dbSNP | Ensembl ].

VAR_013841

Experimental info

Sequence conflict

170

1

K → R in AAI43315. Ref.8

Sequence conflict

182

1

Missing AA sequence Ref.10

Sequence conflict

193

1

Missing AA sequence Ref.10

Secondary structure

1

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201

Helix Strand Turn

Details...

Helix

24 – 26

3

Helix

33 – 39

7

Beta strand

41 – 52

12

Helix

53 – 59

7

Beta strand

62 – 72

11

Turn

73 – 76

4

Beta strand

77 – 86

10

Beta strand

89 – 100

12

Turn

101 – 104

4

Beta strand

105 – 110

6

Beta strand

113 – 121

9

Beta strand

127 – 132

6

Helix

137 – 139

3

Beta strand

141 – 149

9

Turn

153 – 156

4

Helix

157 – 166

10

Helix

170 – 172

3

Helix

178 – 180

3

Helix

184 – 192

9

Sequences

	Sequence		Length	Mass (Da)
	P02763 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 63292233AD6EAD8B	FASTA	201	23,512
	10 20 30 40 50 60 MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDQIT GKWFYIASAF RNEEYNKSVQ 70 80 90 100 110 120 EIQATFFYFT PNKTEDTIFL REYQTRQDQC IYNTTYLNVQ RENGTISRYV GGQEHFAHLL 130 140 150 160 170 180 ILRDTKTYML AFDVNDEKNW GLSVYADKPE TTKEQLGEFY EALDCLRIPK SDVVYTDWKK 190 200 DKCEPLEKQH EKERKQEEGE S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of the genes coding for human alpha 1-acid glycoprotein." Dente L., Pizza M.G., Metspalu A., Cortese R. EMBO J. 6:2289-2296(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular cloning and nucleotide sequence of human alpha 1 acid glycoprotein cDNA." Board P.G., Jones I.M., Bentley A.K. Gene 44:127-131(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure of the human alpha 1-acid glycoprotein gene: sequence homology with other human acute phase protein genes." Dente L., Ciliberto G., Cortese R. Nucleic Acids Res. 13:3941-3952(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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.
[6]	"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], VARIANT ARG-38.
[7]	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], VARIANT ARG-38.
[8]	"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], VARIANTS ARG-38; CYS-167 AND MET-174. Tissue: Liver.
[9]	"Structure of alpha 1-acid glycoprotein. The complete amino acid sequence, multiple amino acid substitutions, and homology with the immunoglobulins." Schmid K., Kaufmann H., Isemura S., Bauer F., Emura J., Motoyama T., Ishiguro M., Nanno S. Biochemistry 12:2711-2724(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-129.
[10]	"Isolation and partial characterization of the cyanogen bromide fragments of alpha 1-acid glycoprotein and the elucidation of the amino acid sequence of the carboxyl-terminal cyanogen bromide fragment." Ikenaka T., Ishiguro M., Emura J., Kaufmann H., Isemura S., Bauer W., Schmid K. Biochemistry 11:3817-3829(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 129-201.
[11]	"The disulfide bonds of alpha1-acid glycoprotein." Schmid K., Buergi W., Collins J.H., Nanno S. Biochemistry 13:2694-2697(1974) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS.
[12]	"Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein." Treuheit M.J., Costello C.E., Halsall H.B. Biochem. J. 283:105-112(1992) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
[13]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-33.
[14]	"A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation." Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P. J. Proteome Res. 3:556-566(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-33; ASN-72 AND ASN-93, MASS SPECTROMETRY.
[15]	"A proteomic analysis of human bile." Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A. Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-93, MASS SPECTROMETRY. Tissue: Bile.
[16]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103, MASS SPECTROMETRY. Tissue: Plasma.
[17]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103, MASS SPECTROMETRY. Tissue: Plasma.
[18]	"Selective binding of imatinib to the genetic variants of human alpha1-acid glycoprotein." Fitos I., Visy J., Zsila F., Mady G., Simonyi M. Biochim. Biophys. Acta 1760:1704-1712(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry." Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A. J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, MASS SPECTROMETRY. Tissue: Saliva.
[20]	"The drug binding site of human alpha1-acid glycoprotein: insight from induced circular dichroism and electronic absorption spectra." Zsila F., Iwao Y. Biochim. Biophys. Acta 1770:797-809(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[21]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93 AND ASN-103, MASS SPECTROMETRY. Tissue: Liver.
[22]	"Enrichment of glycopeptides for glycan structure and attachment site identification." Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G. Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-72, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[23]	"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-33, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
[24]	"The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin." Schonfeld D.L., Ravelli R.B., Mueller U., Skerra A. J. Mol. Biol. 384:393-405(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-201, DOMAIN, DISULFIDE BONDS.
[25]	"Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1*F1, ORM1*F2, and ORM1*S." Yuasa I., Umetsu K., Vogt U., Nakamura H., Nanba E., Tamaki N., Irizawa Y. Hum. Genet. 99:393-398(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-38 AND MET-174.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02544 mRNA. Translation: CAA26397.1.
M13692 mRNA. Translation: AAA35515.1.
X05779 , X05780, X05781, X05782, X05783, X05784 Genomic DNA. Translation: CAA29229.1. Sequence problems.
X06676 Genomic DNA. No translation available.
X06680 Genomic DNA. No translation available.
BT019790 mRNA. Translation: AAV38593.1.
AK312035 mRNA. Translation: BAG34972.1.
AL356796 Genomic DNA. Translation: CAI16859.1.
CH471090 Genomic DNA. Translation: EAW87416.1.
BC104818 mRNA. Translation: AAI04819.1.
BC104820 mRNA. Translation: AAI04821.1.
BC143313 mRNA. Translation: AAI43314.1.
BC143314 mRNA. Translation: AAI43315.1.
BC026238 mRNA. Translation: AAH26238.1.

IPI

IPI00022429.

PIR

OMHU1. A28346.

RefSeq

NP_000598.2. NM_000607.2.

UniGene

Hs.522356.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KQ0	X-ray	1.80	A	20-201	[»]

ProteinModelPortal

P02763.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02763. 7 interactions.

STRING

9606.ENSP00000259396.

PTM databases

GlycoSuiteDB

P02763.

PhosphoSite

P02763.

Polymorphism databases

DMDM

112877.

2D gel databases

SWISS-2DPAGE

P02763.

Proteomic databases

PaxDb

P02763.

PeptideAtlas

P02763.

PRIDE

P02763.

Protocols and materials databases

DNASU

5004.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000259396; ENSP00000259396; ENSG00000229314.

GeneID

5004.

KEGG

hsa:5004.

UCSC

uc004bik.4. human.

Organism-specific databases

CTD

5004.

GeneCards

GC09P117085.

HGNC

HGNC:8498. ORM1.

HPA

CAB006265.
HPA046438.

MIM

138600. gene.

neXtProt

NX_P02763.

PharmGKB

PA260.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41523.

HOGENOM

HOG000125170.

HOVERGEN

HBG000035.

InParanoid

P02763.

OrthoDB

EOG4V9TS3.

Gene expression databases

ArrayExpress

P02763.

Bgee

P02763.

CleanEx

HS_ORM1.

Genevestigator

P02763.

GermOnline

ENSG00000187681. Homo sapiens.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR001500. A1A_glycop.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]

PANTHER

PTHR11967. PTHR11967. 1 hit.

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PIRSF

PIRSF036899. AGP. 1 hit.

PRINTS

PR00708. A1AGLPROTEIN.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00213. LIPOCALIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P02763.

ChEMBL

CHEMBL4285.

ChiTaRS

ORM1. human.

DrugBank

DB01418. Acenocoumarol.
DB00802. Alfentanil.
DB01429. Aprindine.
DB00280. Disopyramide.
DB01359. Penbutolol.
DB00946. Phenprocoumon.
DB00908. Quinidine.
DB00706. Tamsulosin.

EvolutionaryTrace

P02763.

GenomeRNAi

5004.

NextBio

19272.

SOURCE

Search...

Entry information

Entry name

A1AG1_HUMAN

Accession

Primary (citable) accession number: P02763
Secondary accession number(s): B7ZKQ5 , Q5T539, Q5U067, Q8TC16

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 149 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.