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Protein

Alpha-1-acid glycoprotein 2

Gene

ORM2

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

Functioni

Functions as transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction.1 Publication

GO - Biological processi

  • acute-phase response Source: ProtInc
  • regulation of immune system process Source: InterPro
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Acute phase, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1-acid glycoprotein 2
Short name:
AGP 2
Alternative name(s):
Orosomucoid-2
Short name:
OMD 2
Gene namesi
Name:ORM2
Synonyms:AGP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:8499. ORM2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32818.

Chemistry

DrugBankiDB00477. Chlorpromazine.
DB00497. Oxycodone.
DB01041. Thalidomide.

Polymorphism and mutation databases

BioMutaiORM2.
DMDMi231458.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 201183Alpha-1-acid glycoprotein 2PRO_0000017861Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Pyrrolidone carboxylic acid1 Publication
Disulfide bondi23 ↔ 165
Glycosylationi33 – 331N-linked (GlcNAc...) (complex)8 Publications
Glycosylationi56 – 561N-linked (GlcNAc...)4 Publications
Glycosylationi72 – 721N-linked (GlcNAc...)3 Publications
Disulfide bondi90 ↔ 183
Glycosylationi93 – 931N-linked (GlcNAc...)5 Publications
Glycosylationi103 – 1031N-linked (GlcNAc...)3 PublicationsCAR_000171

Post-translational modificationi

N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).8 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP19652.
PeptideAtlasiP19652.
PRIDEiP19652.

2D gel databases

DOSAC-COBS-2DPAGEP19652.
SWISS-2DPAGEP19652.

PTM databases

PhosphoSiteiP19652.
UniCarbKBiP19652.

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

BgeeiP19652.
GenevisibleiP19652. HS.

Organism-specific databases

HPAiHPA046438.

Interactioni

Protein-protein interaction databases

BioGridi111047. 5 interactions.
IntActiP19652. 3 interactions.
STRINGi9606.ENSP00000394936.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni20 – 234Combined sources
Helixi24 – 263Combined sources
Helixi33 – 397Combined sources
Beta strandi41 – 5111Combined sources
Helixi53 – 608Combined 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 – 1208Combined sources
Beta strandi127 – 1337Combined sources
Turni137 – 1393Combined sources
Beta strandi141 – 15010Combined sources
Helixi153 – 16513Combined sources
Helixi170 – 1723Combined sources
Helixi178 – 1803Combined sources
Helixi184 – 1918Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3APUX-ray2.10A/B19-201[»]
3APVX-ray2.15A/B19-201[»]
3APWX-ray2.20A/B19-201[»]
3APXX-ray2.20A19-201[»]
ProteinModelPortaliP19652.
SMRiP19652. Positions 19-196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19652.

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

GeneTreeiENSGT00390000012130.
HOGENOMiHOG000125170.
HOVERGENiHBG000035.
InParanoidiP19652.
KOiK17308.
OMAiPGSHEDE.
OrthoDBiEOG7B5WXT.
PhylomeDBiP19652.
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.

P19652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDRIT GKWFYIASAF
60 70 80 90 100
RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQNQC FYNSSYLNVQ
110 120 130 140 150
RENGTVSRYE GGREHVAHLL FLRDTKTLMF GSYLDDEKNW GLSFYADKPE
160 170 180 190 200
TTKEQLGEFY EALDCLCIPR SDVMYTDWKK DKCEPLEKQH EKERKQEEGE

S
Length:201
Mass (Da):23,603
Last modified:April 1, 1993 - v2
Checksum:i49167ABCC22933B9
GO

Sequence cautioni

The sequence CAA29873.2 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAA29874.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321T → I in CAG33211 (Ref. 4) Curated
Sequence conflicti102 – 1021E → D in BAG35159 (PubMed:14702039).Curated
Sequence conflicti125 – 1251T → I in BAG35159 (PubMed:14702039).Curated
Sequence conflicti162 – 1621A → V in BAG35159 (PubMed:14702039).Curated
Sequence conflicti189 – 1891Q → H in BAG35159 (PubMed:14702039).Curated

Polymorphismi

Many different variants of ORM2 are known.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381R → Q.
Corresponds to variant rs17650 [ dbSNP | Ensembl ].
VAR_014667
Natural varianti99 – 991V → A.
Corresponds to variant rs2636889 [ dbSNP | Ensembl ].
VAR_050172
Natural varianti141 – 1411G → R.
Corresponds to variant rs12685968 [ dbSNP | Ensembl ].
VAR_050173
Natural varianti167 – 1671C → R.
Corresponds to variant rs1126777 [ dbSNP | Ensembl ].
VAR_050174
Natural varianti174 – 1741M → V.
Corresponds to variant rs2636890 [ dbSNP | Ensembl ].
VAR_050175

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06675 Genomic DNA. Translation: CAA29874.1. Sequence problems.
X05780 Genomic DNA. No translation available.
X06674
, X06676, X06677, X06678, X06679, X06680 Genomic DNA. Translation: CAA29873.2. Sequence problems.
X05784 Genomic DNA. No translation available.
M21540 Genomic DNA. Translation: AAA51549.1.
AK312226 mRNA. Translation: BAG35159.1.
CR456930 mRNA. Translation: CAG33211.1.
AL356796 Genomic DNA. Translation: CAI16860.1.
CH471090 Genomic DNA. Translation: EAW87417.1.
BC015964 mRNA. Translation: AAH15964.1.
BC056239 mRNA. Translation: AAH56239.1.
CCDSiCCDS6804.1.
PIRiJT0326. OMHU2.
RefSeqiNP_000599.1. NM_000608.2.
UniGeneiHs.719954.

Genome annotation databases

EnsembliENST00000431067; ENSP00000394936; ENSG00000228278.
GeneIDi5005.
KEGGihsa:5005.
UCSCiuc004bil.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06675 Genomic DNA. Translation: CAA29874.1. Sequence problems.
X05780 Genomic DNA. No translation available.
X06674
, X06676, X06677, X06678, X06679, X06680 Genomic DNA. Translation: CAA29873.2. Sequence problems.
X05784 Genomic DNA. No translation available.
M21540 Genomic DNA. Translation: AAA51549.1.
AK312226 mRNA. Translation: BAG35159.1.
CR456930 mRNA. Translation: CAG33211.1.
AL356796 Genomic DNA. Translation: CAI16860.1.
CH471090 Genomic DNA. Translation: EAW87417.1.
BC015964 mRNA. Translation: AAH15964.1.
BC056239 mRNA. Translation: AAH56239.1.
CCDSiCCDS6804.1.
PIRiJT0326. OMHU2.
RefSeqiNP_000599.1. NM_000608.2.
UniGeneiHs.719954.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3APUX-ray2.10A/B19-201[»]
3APVX-ray2.15A/B19-201[»]
3APWX-ray2.20A/B19-201[»]
3APXX-ray2.20A19-201[»]
ProteinModelPortaliP19652.
SMRiP19652. Positions 19-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111047. 5 interactions.
IntActiP19652. 3 interactions.
STRINGi9606.ENSP00000394936.

Chemistry

ChEMBLiCHEMBL5958.
DrugBankiDB00477. Chlorpromazine.
DB00497. Oxycodone.
DB01041. Thalidomide.

PTM databases

PhosphoSiteiP19652.
UniCarbKBiP19652.

Polymorphism and mutation databases

BioMutaiORM2.
DMDMi231458.

2D gel databases

DOSAC-COBS-2DPAGEP19652.
SWISS-2DPAGEP19652.

Proteomic databases

MaxQBiP19652.
PeptideAtlasiP19652.
PRIDEiP19652.

Protocols and materials databases

DNASUi5005.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000431067; ENSP00000394936; ENSG00000228278.
GeneIDi5005.
KEGGihsa:5005.
UCSCiuc004bil.3. human.

Organism-specific databases

CTDi5005.
GeneCardsiGC09P117092.
HGNCiHGNC:8499. ORM2.
HPAiHPA046438.
MIMi138610. gene.
neXtProtiNX_P19652.
PharmGKBiPA32818.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000012130.
HOGENOMiHOG000125170.
HOVERGENiHBG000035.
InParanoidiP19652.
KOiK17308.
OMAiPGSHEDE.
OrthoDBiEOG7B5WXT.
PhylomeDBiP19652.
TreeFamiTF343791.

Miscellaneous databases

EvolutionaryTraceiP19652.
GenomeRNAii5005.
NextBioi19276.
PROiP19652.
SOURCEiSearch...

Gene expression databases

BgeeiP19652.
GenevisibleiP19652. HS.

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.
ProtoNetiSearch...

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. "Structure and characterisation of a duplicated human alpha 1 acid glycoprotein gene."
    Merritt C.M., Board P.G.
    Gene 66:97-106(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Skeletal muscle.
  8. "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.
  9. "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.
  10. "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: PYROGLUTAMATE FORMATION AT GLN-19, GLYCOSYLATION AT ASN-33 AND ASN-93, IDENTIFICATION BY MASS SPECTROMETRY.
  11. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33.
    Tissue: Bile.
  12. "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 AND ASN-93.
    Tissue: Plasma.
  13. "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.
  14. "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-33; ASN-56; ASN-93 AND ASN-103.
    Tissue: Liver.
  15. "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, STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  16. "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.
  17. "Structural insights into differences in drug-binding selectivity between two forms of human {alpha}1-acid glycoprotein genetic variants, the A and F1*S forms."
    Nishi K., Ono T., Nakamura T., Fukunaga N., Izumi M., Watanabe H., Suenaga A., Maruyama T., Yamagata Y., Curry S., Otagiri M.
    J. Biol. Chem. 286:14427-14434(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 19-201 OF VARIANT ARG-167 IN COMPLEXES WITH DISOPYRAMIDE; AMITRIPTYLINE AND CHLORPROMAZINE, FUNCTION, DISULFIDE BONDS, DOMAIN.

Entry informationi

Entry nameiA1AG2_HUMAN
AccessioniPrimary (citable) accession number: P19652
Secondary accession number(s): B2R5L2
, Q16571, Q5T538, Q6IB74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: April 1, 1993
Last modified: June 24, 2015
This is version 159 of the entry and version 2 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.