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P02763

- A1AG1_HUMAN

UniProt

P02763 - A1AG1_HUMAN

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Protein

Alpha-1-acid glycoprotein 1

Gene

ORM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Biological processi

  1. acute-phase response Source: ProtInc
  2. inflammatory response Source: ProtInc
  3. regulation of immune system process Source: InterPro
  4. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Acute phase, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1-acid glycoprotein 1
Short name:
AGP 1
Alternative name(s):
Orosomucoid-1
Short name:
OMD 1
Gene namesi
Name:ORM1
Synonyms:AGP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:8498. ORM1.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA260.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 201183Alpha-1-acid glycoprotein 1PRO_0000017860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Pyrrolidone carboxylic acid1 Publication
Disulfide bondi23 ↔ 1651 Publication
Glycosylationi33 – 331N-linked (GlcNAc...) (complex)8 Publications
Glycosylationi56 – 561N-linked (GlcNAc...)4 Publications
Glycosylationi72 – 721N-linked (GlcNAc...) (complex)5 Publications
Disulfide bondi90 ↔ 1831 Publication
Glycosylationi93 – 931N-linked (GlcNAc...)8 Publications
Glycosylationi103 – 1031N-linked (GlcNAc...)4 PublicationsCAR_000170

Post-translational modificationi

N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).10 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP02763.
PaxDbiP02763.
PeptideAtlasiP02763.
PRIDEiP02763.

2D gel databases

SWISS-2DPAGEP02763.

PTM databases

PhosphoSiteiP02763.
UniCarbKBiP02763.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Inductioni

Synthesis is controlled by glucocorticoids, interleukin-1 and interleukin-6, It increases 5- to 50-fold upon inflammation.

Gene expression databases

BgeeiP02763.
CleanExiHS_ORM1.
GenevestigatoriP02763.

Organism-specific databases

HPAiCAB006265.
HPA046438.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SERPINE1P051214EBI-976767,EBI-953978

Protein-protein interaction databases

BioGridi111046. 9 interactions.
IntActiP02763. 7 interactions.
MINTiMINT-202382.
STRINGi9606.ENSP00000259396.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi33 – 397Combined sources
Beta strandi41 – 5212Combined sources
Helixi53 – 597Combined sources
Beta strandi62 – 7211Combined sources
Turni73 – 764Combined sources
Beta strandi77 – 8610Combined sources
Beta strandi89 – 10012Combined sources
Turni101 – 1044Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi113 – 1219Combined sources
Beta strandi127 – 1326Combined sources
Helixi137 – 1393Combined sources
Beta strandi141 – 1499Combined sources
Turni153 – 1564Combined sources
Helixi157 – 16610Combined sources
Helixi170 – 1723Combined sources
Helixi178 – 1803Combined sources
Helixi184 – 1929Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KQ0X-ray1.80A19-201[»]
ProteinModelPortaliP02763.
SMRiP02763. Positions 19-193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02763.

Family & Domainsi

Domaini

Contains a beta-barrel that binds various ligands in its interior.1 Publication

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG41523.
GeneTreeiENSGT00390000012130.
HOGENOMiHOG000125170.
HOVERGENiHBG000035.
InParanoidiP02763.
KOiK17308.
OrthoDBiEOG7B5WXT.
PhylomeDBiP02763.
TreeFamiTF343791.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR001500. A1A_glycop.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11967. PTHR11967. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036899. AGP. 1 hit.
PRINTSiPR00708. A1AGLPROTEIN.
SUPFAMiSSF50814. SSF50814. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P02763-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDQIT GKWFYIASAF
60 70 80 90 100
RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQDQC IYNTTYLNVQ
110 120 130 140 150
RENGTISRYV GGQEHFAHLL ILRDTKTYML AFDVNDEKNW GLSVYADKPE
160 170 180 190 200
TTKEQLGEFY EALDCLRIPK SDVVYTDWKK DKCEPLEKQH EKERKQEEGE

S
Length:201
Mass (Da):23,512
Last modified:January 1, 1988 - v1
Checksum:i63292233AD6EAD8B
GO

Sequence cautioni

The sequence CAA29229.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701K → R in AAI43315. (PubMed:15489334)Curated
Sequence conflicti182 – 1821Missing AA sequence (PubMed:4561179)Curated
Sequence conflicti193 – 1931Missing AA sequence (PubMed:4561179)Curated

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381Q → R in allele ORM1*S. 4 Publications
VAR_013840
Natural varianti167 – 1671R → C.1 Publication
Corresponds to variant rs3182034 [ dbSNP | Ensembl ].
VAR_056166
Natural varianti174 – 1741V → M in allele ORM1*F2. 2 Publications
Corresponds to variant rs1126801 [ dbSNP | Ensembl ].
VAR_013841

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6803.1.
PIRiA28346. OMHU1.
RefSeqiNP_000598.2. NM_000607.2.
UniGeneiHs.522356.

Genome annotation databases

EnsembliENST00000259396; ENSP00000259396; ENSG00000229314.
GeneIDi5004.
KEGGihsa:5004.
UCSCiuc004bik.4. human.

Polymorphism databases

DMDMi112877.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS6803.1.
PIRi A28346. OMHU1.
RefSeqi NP_000598.2. NM_000607.2.
UniGenei Hs.522356.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3KQ0 X-ray 1.80 A 19-201 [» ]
ProteinModelPortali P02763.
SMRi P02763. Positions 19-193.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111046. 9 interactions.
IntActi P02763. 7 interactions.
MINTi MINT-202382.
STRINGi 9606.ENSP00000259396.

Chemistry

BindingDBi P02763.
ChEMBLi CHEMBL4285.
DrugBanki DB05812. Abiraterone.
DB01418. Acenocoumarol.
DB01426. Ajmaline.
DB00802. Alfentanil.
DB00321. Amitriptyline.
DB00543. Amoxapine.
DB01429. Aprindine.
DB01156. Bupropion.
DB08907. Canagliflozin.
DB00482. Celecoxib.
DB00477. Chlorpromazine.
DB01151. Desipramine.
DB00280. Disopyramide.
DB00590. Doxazosin.
DB01142. Doxepin.
DB00530. Erlotinib.
DB00472. Fluoxetine.
DB00317. Gefitinib.
DB00619. Imatinib.
DB00458. Imipramine.
DB08820. Ivacaftor.
DB00934. Maprotiline.
DB08893. Mirabegron.
DB00731. Nateglinide.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB00497. Oxycodone.
DB01359. Penbutolol.
DB00454. Pethidine.
DB00946. Phenprocoumon.
DB08860. Pitavastatin.
DB00457. Prazosin.
DB00571. Propranolol.
DB00908. Quinidine.
DB01232. Saquinavir.
DB00864. Tacrolimus.
DB00706. Tamsulosin.
DB05521. Telaprevir.
DB01041. Thalidomide.
DB00656. Trazodone.
DB05294. Vandetanib.
DB08881. Vemurafenib.
DB08828. Vismodegib.
DB00682. Warfarin.

PTM databases

PhosphoSitei P02763.
UniCarbKBi P02763.

Polymorphism databases

DMDMi 112877.

2D gel databases

SWISS-2DPAGE P02763.

Proteomic databases

MaxQBi P02763.
PaxDbi P02763.
PeptideAtlasi P02763.
PRIDEi P02763.

Protocols and materials databases

DNASUi 5004.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259396 ; ENSP00000259396 ; ENSG00000229314 .
GeneIDi 5004.
KEGGi hsa:5004.
UCSCi uc004bik.4. human.

Organism-specific databases

CTDi 5004.
GeneCardsi GC09P117085.
HGNCi HGNC:8498. ORM1.
HPAi CAB006265.
HPA046438.
MIMi 138600. gene.
neXtProti NX_P02763.
PharmGKBi PA260.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41523.
GeneTreei ENSGT00390000012130.
HOGENOMi HOG000125170.
HOVERGENi HBG000035.
InParanoidi P02763.
KOi K17308.
OrthoDBi EOG7B5WXT.
PhylomeDBi P02763.
TreeFami TF343791.

Miscellaneous databases

ChiTaRSi ORM1. human.
EvolutionaryTracei P02763.
GeneWikii ORM1.
GenomeRNAii 5004.
NextBioi 19272.
PROi P02763.
SOURCEi Search...

Gene expression databases

Bgeei P02763.
CleanExi HS_ORM1.
Genevestigatori P02763.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR001500. A1A_glycop.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view ]
PANTHERi PTHR11967. PTHR11967. 1 hit.
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PIRSFi PIRSF036899. AGP. 1 hit.
PRINTSi PR00708. A1AGLPROTEIN.
SUPFAMi SSF50814. SSF50814. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiA1AG1_HUMAN
AccessioniPrimary (citable) accession number: P02763
Secondary accession number(s): B7ZKQ5
, Q5T539, Q5U067, Q8TC16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: November 26, 2014
This is version 166 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

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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3