P25311 · ZA2G_HUMAN
- ProteinZinc-alpha-2-glycoprotein
- GeneAZGP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids298 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | external side of plasma membrane | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | nucleus | |
Molecular Function | protein transmembrane transporter activity | |
Molecular Function | RNA nuclease activity | |
Biological Process | cell adhesion | |
Biological Process | detection of chemical stimulus involved in sensory perception of bitter taste | |
Biological Process | immune response | |
Biological Process | negative regulation of cell population proliferation |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZinc-alpha-2-glycoprotein
- Short namesZn-alpha-2-GP; Zn-alpha-2-glycoprotein
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP25311
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 409 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, modified residue, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MVRMVPVLLSLLLLLGPAVP | ||||||
Modified residue | 21 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000019012 | 21-298 | Zinc-alpha-2-glycoprotein | |||
Sequence: QENQDGRYSLTYIYTGLSKHVEDVPAFQALGSLNDLQFFRYNSKDRKSQPMGLWRQVEGMEDWKQDSQLQKAREDIFMETLKDIVEYYNDSNGSHVLQGRFGCEIENNRSSGAFWKYYYDGKDYIEFNKEIPAWVPFDPAAQITKQKWEAEPVYVQRAKAYLEEECPATLRKYLKYSKNILDRQDPPSVVVTSHQAPGEKKKLKCLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSCHVQHSSLAQPLVVPWEAS | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 112 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 123↔186 | |||||
Sequence: CEIENNRSSGAFWKYYYDGKDYIEFNKEIPAWVPFDPAAQITKQKWEAEPVYVQRAKAYLEEEC | ||||||
Glycosylation | 128 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 225↔280 | |||||
Sequence: CLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSC | ||||||
Glycosylation | 259 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated. N-glycan at Asn-128: Hex5HexNAc4.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Blood plasma, seminal plasma, urine, saliva, sweat, epithelial cells of various human glands, liver.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with PIP.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P25311 | PRNP P04156 | 4 | EBI-2513837, EBI-977302 | |
BINARY | P25311 | UBQLN2 Q9UHD9 | 3 | EBI-2513837, EBI-947187 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 207-292 | Ig-like C1-type | ||||
Sequence: PSVVVTSHQAPGEKKKLKCLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSCHVQHSSLAQPLV |
Sequence similarities
Belongs to the MHC class I family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length298
- Mass (Da)34,259
- Last updated2010-03-23 v2
- Checksum006A153A8E32A0B1
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 1; CAA42438 | ||||
Sequence: V → S | ||||||
Sequence conflict | 5 | in Ref. 1; CAA42438 | ||||
Sequence: V → L | ||||||
Sequence conflict | 33 | in Ref. 7; AAH05306 | ||||
Sequence: I → V | ||||||
Sequence conflict | 85 | in Ref. 9; AA sequence | ||||
Sequence: Q → E | ||||||
Sequence conflict | 96-97 | in Ref. 9; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 244 | in Ref. 9; AA sequence | ||||
Sequence: E → Q |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X59766 EMBL· GenBank· DDBJ | CAA42438.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
D14034 EMBL· GenBank· DDBJ | BAA03123.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
X69953 EMBL· GenBank· DDBJ | CAA49574.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC004522 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH236956 EMBL· GenBank· DDBJ | EAL23862.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471091 EMBL· GenBank· DDBJ | EAW76621.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471091 EMBL· GenBank· DDBJ | EAW76622.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC005306 EMBL· GenBank· DDBJ | AAH05306.1 EMBL· GenBank· DDBJ | mRNA | ||
BC033830 EMBL· GenBank· DDBJ | AAH33830.1 EMBL· GenBank· DDBJ | mRNA | ||
D90427 EMBL· GenBank· DDBJ | BAA14417.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
M76707 EMBL· GenBank· DDBJ | AAA61311.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |