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P02763 (A1AG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Alpha-1-acid glycoprotein 1

Short name=AGP 1
Alternative name(s):
Orosomucoid-1
Short name=OMD 1
Gene names
Name:ORM1
Synonyms:AGP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SERPINE1P051214EBI-976767,EBI-953978

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.9
Chain19 – 201183Alpha-1-acid glycoprotein 1
PRO_0000017860

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid Ref.9
Glycosylation331N-linked (GlcNAc...) (complex) Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.22 Ref.23
Glycosylation561N-linked (GlcNAc...) Ref.11 Ref.12 Ref.16 Ref.17
Glycosylation721N-linked (GlcNAc...) (complex) Ref.12 Ref.14 Ref.16 Ref.17 Ref.22
Glycosylation931N-linked (GlcNAc...) Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21
Glycosylation1031N-linked (GlcNAc...) Ref.12 Ref.16 Ref.17 Ref.21
CAR_000170
Disulfide bond23 ↔ 165 Ref.11 Ref.24
Disulfide bond90 ↔ 183 Ref.11 Ref.24

Natural variations

Natural variant381Q → R in allele ORM1*S. Ref.6 Ref.7 Ref.8 Ref.25
VAR_013840
Natural variant1671R → C. Ref.8
Corresponds to variant rs3182034 [ dbSNP | Ensembl ].
VAR_056166
Natural variant1741V → M in allele ORM1*F2. Ref.8 Ref.25
Corresponds to variant rs1126801 [ dbSNP | Ensembl ].
VAR_013841

Experimental info

Sequence conflict1701K → R in AAI43315. Ref.8
Sequence conflict1821Missing AA sequence Ref.10
Sequence conflict1931Missing AA sequence Ref.10

Secondary structure

................................. 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02763 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 63292233AD6EAD8B

FASTA20123,512
        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 

« Hide

References

« Hide '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. 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.
[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. 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], 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. 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], 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, PYROGLUTAMATE FORMATION AT GLN-19.
[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, IDENTIFICATION BY 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.
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.
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.
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.
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.
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.
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, IDENTIFICATION BY 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 expand/collapse EMBL AC list , 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.
CCDSCCDS6803.1.
PIROMHU1. A28346.
RefSeqNP_000598.2. NM_000607.2.
UniGeneHs.522356.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KQ0X-ray1.80A19-201[»]
ProteinModelPortalP02763.
SMRP02763. Positions 19-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111046. 7 interactions.
IntActP02763. 7 interactions.
MINTMINT-202382.
STRING9606.ENSP00000259396.

Chemistry

BindingDBP02763.
ChEMBLCHEMBL4285.
DrugBankDB01418. Acenocoumarol.
DB00802. Alfentanil.
DB01429. Aprindine.
DB00280. Disopyramide.
DB01359. Penbutolol.
DB00946. Phenprocoumon.
DB00908. Quinidine.
DB00706. Tamsulosin.

PTM databases

PhosphoSiteP02763.
UniCarbKBP02763.

Polymorphism databases

DMDM112877.

2D gel databases

SWISS-2DPAGEP02763.

Proteomic databases

MaxQBP02763.
PaxDbP02763.
PeptideAtlasP02763.
PRIDEP02763.

Protocols and materials databases

DNASU5004.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259396; ENSP00000259396; ENSG00000229314.
GeneID5004.
KEGGhsa:5004.
UCSCuc004bik.4. human.

Organism-specific databases

CTD5004.
GeneCardsGC09P117085.
HGNCHGNC:8498. ORM1.
HPACAB006265.
HPA046438.
MIM138600. gene.
neXtProtNX_P02763.
PharmGKBPA260.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41523.
HOGENOMHOG000125170.
HOVERGENHBG000035.
InParanoidP02763.
KOK17308.
OrthoDBEOG7B5WXT.
PhylomeDBP02763.
TreeFamTF343791.

Gene expression databases

ArrayExpressP02763.
BgeeP02763.
CleanExHS_ORM1.
GenevestigatorP02763.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR001500. A1A_glycop.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERPTHR11967. PTHR11967. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFPIRSF036899. AGP. 1 hit.
PRINTSPR00708. A1AGLPROTEIN.
SUPFAMSSF50814. SSF50814. 1 hit.
ProtoNetSearch...

Other

ChiTaRSORM1. human.
EvolutionaryTraceP02763.
GeneWikiORM1.
GenomeRNAi5004.
NextBio19272.
PROP02763.
SOURCESearch...

Entry information

Entry nameA1AG1_HUMAN
AccessionPrimary (citable) accession number: P02763
Secondary accession number(s): B7ZKQ5 expand/collapse secondary AC list , Q5T539, Q5U067, Q8TC16
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: July 9, 2014
This is version 162 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

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