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Protein

Zinc-alpha-2-glycoprotein

Gene

AZGP1

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

Functioni

Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.

GO - Molecular functioni

  1. antigen binding Source: GO_Central
  2. glycoprotein binding Source: UniProtKB
  3. peptide antigen binding Source: InterPro
  4. protein transmembrane transporter activity Source: UniProtKB
  5. ribonuclease activity Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation Source: GO_Central
  2. antigen processing and presentation of peptide antigen via MHC class I Source: InterPro
  3. cell adhesion Source: UniProtKB
  4. detection of chemical stimulus involved in sensory perception of bitter taste Source: UniProtKB
  5. immune response Source: InterPro
  6. negative regulation of cell proliferation Source: UniProtKB
  7. positive regulation of T cell mediated cytotoxicity Source: InterPro
  8. protein transmembrane transport Source: GOC
  9. retina homeostasis Source: UniProtKB
  10. RNA phosphodiester bond hydrolysis Source: GOC
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc-alpha-2-glycoprotein
Short name:
Zn-alpha-2-GP
Short name:
Zn-alpha-2-glycoprotein
Gene namesi
Name:AZGP1
Synonyms:ZAG, ZNGP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:910. AZGP1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. MHC class I protein complex Source: InterPro
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25203.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20202 PublicationsAdd
BLAST
Chaini21 – 298278Zinc-alpha-2-glycoproteinPRO_0000019012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acid1 Publication
Glycosylationi109 – 1091N-linked (GlcNAc...) (complex)5 Publications
Glycosylationi112 – 1121N-linked (GlcNAc...)5 Publications
Disulfide bondi123 ↔ 186
Glycosylationi128 – 1281N-linked (GlcNAc...) (complex)9 Publications
Disulfide bondi225 ↔ 280
Glycosylationi259 – 2591N-linked (GlcNAc...)3 Publications

Post-translational modificationi

N-glycosylated. N-glycan at Asn-128: Hex5HexNAc4.11 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP25311.
PaxDbiP25311.
PRIDEiP25311.

2D gel databases

REPRODUCTION-2DPAGEIPI00166729.
SWISS-2DPAGEP25311.

PTM databases

PhosphoSiteiP25311.

Expressioni

Tissue specificityi

Blood plasma, seminal plasma, urine, saliva, sweat, epithelial cells of various human glands, liver.

Gene expression databases

BgeeiP25311.
CleanExiHS_AZGP1.
ExpressionAtlasiP25311. baseline and differential.
GenevestigatoriP25311.

Organism-specific databases

HPAiCAB016087.
CAB032276.
HPA012582.

Interactioni

Subunit structurei

Interacts with PIP.1 Publication

Protein-protein interaction databases

BioGridi107040. 9 interactions.
IntActiP25311. 9 interactions.
STRINGi9606.ENSP00000292401.

Structurei

Secondary structure

1
298
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 3913Combined sources
Beta strandi42 – 443Combined sources
Beta strandi46 – 538Combined sources
Beta strandi56 – 627Combined sources
Turni63 – 653Combined sources
Helixi72 – 765Combined sources
Beta strandi79 – 813Combined sources
Helixi83 – 10725Combined sources
Beta strandi116 – 12611Combined sources
Beta strandi129 – 13911Combined sources
Beta strandi142 – 1487Combined sources
Turni149 – 1524Combined sources
Beta strandi153 – 1564Combined sources
Helixi159 – 16810Combined sources
Helixi173 – 18311Combined sources
Helixi185 – 19612Combined sources
Helixi198 – 2014Combined sources
Beta strandi208 – 2158Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi221 – 23313Combined sources
Beta strandi235 – 2417Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi249 – 2568Combined sources
Turni257 – 2604Combined sources
Beta strandi261 – 27010Combined sources
Beta strandi278 – 2847Combined sources
Beta strandi291 – 2944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T7VX-ray1.95A21-298[»]
1T7WX-ray2.70A21-298[»]
1T7XX-ray3.10A21-298[»]
1T7YX-ray2.80A21-298[»]
1T7ZX-ray3.00A21-298[»]
1T80X-ray2.10A21-298[»]
1ZAGX-ray2.80A/B/C/D25-298[»]
3ES6X-ray3.23A21-298[»]
ProteinModelPortaliP25311.
SMRiP25311. Positions 25-298.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25311.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini207 – 29286Ig-like C1-typeAdd
BLAST

Sequence similaritiesi

Belongs to the MHC class I family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG25830.
GeneTreeiENSGT00760000118960.
HOGENOMiHOG000296917.
HOVERGENiHBG016709.
InParanoidiP25311.
OMAiIFMVTLK.
OrthoDBiEOG7JT6WQ.
PhylomeDBiP25311.
TreeFamiTF336617.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR027648. MHC_I_a.
IPR001039. MHC_I_a_a1/a2.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
[Graphical view]
PRINTSiPR01638. MHCCLASSI.
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25311-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRMVPVLLS LLLLLGPAVP QENQDGRYSL TYIYTGLSKH VEDVPAFQAL
60 70 80 90 100
GSLNDLQFFR YNSKDRKSQP MGLWRQVEGM EDWKQDSQLQ KAREDIFMET
110 120 130 140 150
LKDIVEYYND SNGSHVLQGR FGCEIENNRS SGAFWKYYYD GKDYIEFNKE
160 170 180 190 200
IPAWVPFDPA AQITKQKWEA EPVYVQRAKA YLEEECPATL RKYLKYSKNI
210 220 230 240 250
LDRQDPPSVV VTSHQAPGEK KKLKCLAYDF YPGKIDVHWT RAGEVQEPEL
260 270 280 290
RGDVLHNGNG TYQSWVVVAV PPQDTAPYSC HVQHSSLAQP LVVPWEAS
Length:298
Mass (Da):34,259
Last modified:March 23, 2010 - v2
Checksum:i006A153A8E32A0B1
GO

Sequence cautioni

The sequence AAA61311.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA03123.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA14417.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA42438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21V → S in CAA42438 (PubMed:1915885).Curated
Sequence conflicti5 – 51V → L in CAA42438 (PubMed:1915885).Curated
Sequence conflicti33 – 331I → V in AAH05306 (PubMed:15489334).Curated
Sequence conflicti85 – 851Q → E AA sequence (PubMed:3422450).Curated
Sequence conflicti96 – 972Missing AA sequence (PubMed:3422450).Curated
Sequence conflicti244 – 2441E → Q AA sequence (PubMed:3422450).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59766 mRNA. Translation: CAA42438.1. Different initiation.
D14034 Genomic DNA. Translation: BAA03123.1. Different initiation.
X69953 Genomic DNA. Translation: CAA49574.1.
AC004522 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23862.1.
CH471091 Genomic DNA. Translation: EAW76621.1.
CH471091 Genomic DNA. Translation: EAW76622.1.
BC005306 mRNA. Translation: AAH05306.1.
BC033830 mRNA. Translation: AAH33830.1.
D90427 mRNA. Translation: BAA14417.1. Different initiation.
M76707 mRNA. Translation: AAA61311.1. Different initiation.
CCDSiCCDS5680.1.
PIRiA54175.
RefSeqiNP_001176.1. NM_001185.3.
UniGeneiHs.546239.

Genome annotation databases

EnsembliENST00000292401; ENSP00000292401; ENSG00000160862.
GeneIDi563.
KEGGihsa:563.
UCSCiuc003ush.3. human.

Polymorphism databases

DMDMi292495049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59766 mRNA. Translation: CAA42438.1. Different initiation.
D14034 Genomic DNA. Translation: BAA03123.1. Different initiation.
X69953 Genomic DNA. Translation: CAA49574.1.
AC004522 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23862.1.
CH471091 Genomic DNA. Translation: EAW76621.1.
CH471091 Genomic DNA. Translation: EAW76622.1.
BC005306 mRNA. Translation: AAH05306.1.
BC033830 mRNA. Translation: AAH33830.1.
D90427 mRNA. Translation: BAA14417.1. Different initiation.
M76707 mRNA. Translation: AAA61311.1. Different initiation.
CCDSiCCDS5680.1.
PIRiA54175.
RefSeqiNP_001176.1. NM_001185.3.
UniGeneiHs.546239.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T7VX-ray1.95A21-298[»]
1T7WX-ray2.70A21-298[»]
1T7XX-ray3.10A21-298[»]
1T7YX-ray2.80A21-298[»]
1T7ZX-ray3.00A21-298[»]
1T80X-ray2.10A21-298[»]
1ZAGX-ray2.80A/B/C/D25-298[»]
3ES6X-ray3.23A21-298[»]
ProteinModelPortaliP25311.
SMRiP25311. Positions 25-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107040. 9 interactions.
IntActiP25311. 9 interactions.
STRINGi9606.ENSP00000292401.

PTM databases

PhosphoSiteiP25311.

Polymorphism databases

DMDMi292495049.

2D gel databases

REPRODUCTION-2DPAGEIPI00166729.
SWISS-2DPAGEP25311.

Proteomic databases

MaxQBiP25311.
PaxDbiP25311.
PRIDEiP25311.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000292401; ENSP00000292401; ENSG00000160862.
GeneIDi563.
KEGGihsa:563.
UCSCiuc003ush.3. human.

Organism-specific databases

CTDi563.
GeneCardsiGC07M099564.
HGNCiHGNC:910. AZGP1.
HPAiCAB016087.
CAB032276.
HPA012582.
MIMi194460. gene.
neXtProtiNX_P25311.
PharmGKBiPA25203.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG25830.
GeneTreeiENSGT00760000118960.
HOGENOMiHOG000296917.
HOVERGENiHBG016709.
InParanoidiP25311.
OMAiIFMVTLK.
OrthoDBiEOG7JT6WQ.
PhylomeDBiP25311.
TreeFamiTF336617.

Miscellaneous databases

ChiTaRSiAZGP1. human.
EvolutionaryTraceiP25311.
GeneWikiiAZGP1.
GenomeRNAii563.
NextBioi2301.
PROiP25311.
SOURCEiSearch...

Gene expression databases

BgeeiP25311.
CleanExiHS_AZGP1.
ExpressionAtlasiP25311. baseline and differential.
GenevestigatoriP25311.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR027648. MHC_I_a.
IPR001039. MHC_I_a_a1/a2.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
[Graphical view]
PRINTSiPR01638. MHCCLASSI.
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human Zn-alpha 2-glycoprotein cDNA cloning and expression analysis in benign and malignant breast tissues."
    Freije J.P., Fueyo A., Uria J., Lopez-Otin C.
    FEBS Lett. 290:247-249(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  2. "Molecular cloning and chromosomal assignment of the gene for human Zn-alpha 2-glycoprotein."
    Ueyama H., Deng H.X., Ohkubo I.
    Biochemistry 32:12968-12976(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Human Zn-alpha 2-glycoprotein: complete genomic sequence, identification of a related pseudogene and relationship to class I major histocompatibility complex genes."
    Freije J.P., Fueyo A., Uria J.A., Velasco G., Sanchez L.M., Lopez-Boado Y.S., Lopez-Otin C.
    Genomics 18:575-587(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Leukocyte.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [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: Colon and Prostate.
  8. "Cloning and nucleotide sequence of a human Zn-alpha 2-glycoprotein cDNA and chromosomal assignment of its gene."
    Ueyama H., Niwa M., Tada T., Sasaki M., Ohkubo I.
    Biochem. Biophys. Res. Commun. 177:696-703(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-298.
    Tissue: Liver and Prostate.
  9. "Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens."
    Araki T., Gejyo F., Takagaki K., Haupt H., Schwick H.G., Buergi W., Marti T., Schaller J., Rickli E., Brossmer R., Atkinson P.H., Putnam F.W., Schmid K.
    Proc. Natl. Acad. Sci. U.S.A. 85:679-683(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-298, PYROGLUTAMATE FORMATION AT GLN-21.
    Tissue: Plasma.
  10. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-35.
  11. "Biochemical characterization and crystallization of human Zn-alpha2-glycoprotein, a soluble class I major histocompatibility complex homolog."
    Sanchez L.M., Lopez-Otin C., Bjorkman P.J.
    Proc. Natl. Acad. Sci. U.S.A. 94:4626-4630(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, CRYSTALLIZATION.
  12. "Hydrophobic ligand binding by Zn-alpha 2-glycoprotein, a soluble fat-depleting factor related to major histocompatibility complex proteins."
    Kennedy M.W., Heikema A.P., Cooper A., Bjorkman P.J., Sanchez L.M.
    J. Biol. Chem. 276:35008-35013(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IN VITRO BINDING OF FATTY ACID.
  13. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128.
    Tissue: Bile.
  14. "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-112 AND ASN-128.
    Tissue: Plasma.
  15. "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-112.
    Tissue: Plasma.
  16. "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-109; ASN-112 AND ASN-128.
    Tissue: Saliva.
  17. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
    Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
    Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128.
    Tissue: Milk.
  18. "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-109; ASN-112 AND ASN-128.
    Tissue: Liver.
  19. Cited for: GLYCOSYLATION AT ASN-109 AND ASN-128.
  20. "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-128, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules."
    Sanchez L.M., Chirino A.J., Bjorkman P.J.
    Science 283:1914-1919(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-109; ASN-128 AND ASN-259.
  23. "Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein."
    Delker S.L., West A.P. Jr., McDermott L., Kennedy M.W., Bjorkman P.J.
    J. Struct. Biol. 148:205-213(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 21-298, DISULFIDE BONDS, GLYCOSYLATION AT ASN-128 AND ASN-259.
  24. "Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma."
    Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P., Singh T.P.
    J. Mol. Biol. 384:663-672(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 32-149 IN COMPLEX WITH PIP, DISULFIDE BONDS, GLYCOSYLATION AT ASN-259.

Entry informationi

Entry nameiZA2G_HUMAN
AccessioniPrimary (citable) accession number: P25311
Secondary accession number(s): D6W5T8
, O60386, Q5XKQ4, Q8N4N0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 23, 2010
Last modified: March 4, 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

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.Curated

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

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.