ALB

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0003677 DNA binding	IDA PMID:16405401 DNA interaction with human serum albumin studied by affinity...	KEEP AS NON CORE	Summary: Purified human albumin binds DNA in solution. Reason: The source directly measures complexes with calf-thymus DNA by FTIR and affinity capillary electrophoresis. This is a biochemical ligand interaction under the tested solution conditions; it does not establish a nuclear DNA-regulatory role for circulating albumin. Supporting Evidence: PMID:16405401 Spectroscopic evidence showed two types of HSA-DNA complexes
GO:0005504 fatty acid binding	IDA PMID:16289007 Determining molecular binding sites on human serum albumin b...	ACCEPT	Summary: Oleate displacement and NMR identify human albumin fatty-acid sites. Reason: Human albumin binds oleate at multiple sites. Competitive displacement by drugs identifies site overlap and is direct evidence for the fatty-acid-binding component of its circulating carrier function. Supporting Evidence: PMID:16289007 seven distinct resonances were observed for the (13)C-methyl-labeled oleic acid as a result of its binding to HSA.
GO:0005504 fatty acid binding	IDA PMID:16413837 Structural changes accompanying human serum albumin's bindin...	ACCEPT	Summary: Myristate binding induces concerted changes in human albumin. Reason: The source measures fatty-acid binding and associated conformational changes in human albumin. This is central ligand-binding chemistry rather than a downstream cellular phenotype. Supporting Evidence: PMID:16413837 five strong, interacting, binding sites
GO:0005504 fatty acid binding	NAS PMID:9731778 Crystal structure of human serum albumin complexed with fatt...	ACCEPT	Summary: The human albumin crystal structure resolves multiple fatty-acid sites. Reason: The source reports a human albumin-myristate structure. Its experimentally resolved fatty-acid binding supports the existing NAS assertion without changing the seeded evidence code. Supporting Evidence: PMID:9731778 We have now determined the crystal structure of HSA complexed with five molecules of myristate at 2.5 A resolution.
GO:0005507 copper ion binding	NAS PMID:14726550 Human serum albumin and its N-terminal tetrapeptide (DAHK) b...	ACCEPT	Summary: The N-terminal copper-binding region contributes to albumin antioxidant function. Reason: The cited paper explicitly describes the copper-binding capacity of human albumin and its DAHK peptide; its neuronal protection experiment uses murine cortical cultures. Retain the NAS binding assertion, while distinguishing the stated metal-binding mechanism from the paper's direct cell-survival measurements. Supporting Evidence: PMID:14726550 HSA is a potent antioxidant, in part because of its strong copper-binding capacity.
GO:0005515 protein binding	IPI PMID:16099937 Analysis of albumin-associated peptides and proteins from ov...	REMOVE	Summary: Albumin-associated BRCA2 fragments are real, but generic protein binding is uninformative. Reason: Native albumin affinity isolation and peptide immunocompetition establish circulating BRCA2 fragments, not intact nuclear BRCA2, among albumin-associated cargo. Remove the generic molecular-function assertion for lack of functional precision; this does not reject the measured association. The experiment does not demonstrate delivery to a defined protein acceptor or location sufficient to substitute protein carrier activity solely from this pair. Supporting Evidence: PMID:16099937 series of specific fragments bound to albumin
GO:0005515 protein binding	IPI PMID:23384347 The transferrin receptor-1 membrane stub undergoes intramemb...	REMOVE	Summary: Generic binding to transferrin receptor does not specify an albumin function. Reason: The source is an experimental study of transferrin-receptor processing. Its cached abstract does not resolve the albumin pair assay. The generic protein-binding term adds no defined albumin molecular activity and is removed on that basis; the interaction is not declared false, and no receptor-regulator activity is inferred.
GO:0005515 protein binding	IPI PMID:9183005 Prothrombin, albumin and immunoglobulin A form covalent comp...	REMOVE	Summary: Covalent albumin-alpha1-microglobulin complexes do not define a specific molecular activity. Reason: Human plasma affinity isolation and immunoblotting support the covalent complex. The observed association is retained in the source assessment, but generic protein binding does not explain an albumin function. No catalytic or adaptor activity is inferred from complex formation. Supporting Evidence: PMID:9183005 Albumin x alpha1-microglobulin, corresponding to 7% of total plasma alpha1-microglobulin, was a mixture between 1:1 and 1:2 complexes
GO:0005576 extracellular region	HDA PMID:22664934 Comparison of tear protein levels in breast cancer patients ...	ACCEPT	Summary: The extracellular-region assertion agrees with albumin secretion. Reason: This human tear proteome study supplies a broad extracellular annotation. The cached full body does not resolve the specific ALB peptide entry, so it is not treated as a fresh target-level assay verification. Independent human albumin plasma evidence and UniProt secretion support this same broad location; no narrower tear-specific localization is claimed. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted.
GO:0005576 extracellular region	HDA PMID:23580065 Shotgun proteomics reveals specific modulated protein patter...	ACCEPT	Summary: The tear-proteome location agrees with the established extracellular albumin pool. Reason: The original source compares human tear proteomes in glaucoma. Its abstract does not enumerate the ALB-specific peptide evidence. Retain the broad extracellular assertion with curator deference and independent evidence for secreted human albumin, without claiming a verified disease-specific redistribution. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted.
GO:0005576 extracellular region	IDA PMID:19996109 Identification of human plasma proteins as major clients for...	ACCEPT	Summary: Human plasma albumin forms extracellular complexes with clusterin. Reason: The study identifies albumin by mass spectrometry and detects clusterin-albumin complexes in stressed human plasma. It directly supports the extracellular location; albumin is the chaperone client in this experiment. Supporting Evidence: PMID:19996109 These proteins were identified by mass spectrometry as ceruloplasmin, fibrinogen, and albumin.
GO:0005576 extracellular region	IDA PMID:21805676 Innate immunity proteins and a new truncated form of SPLUNC1...	ACCEPT	Summary: Human airway-fluid proteomics is consistent with extracellular albumin. Reason: The source analyzes nasopharyngeal aspirates from infants. The cached abstract foregrounds other innate-immune proteins rather than enumerating ALB peptides. The broad location is independently established for human albumin and is retained; this is not a claim that albumin has the specific SPLUNC1 mechanism. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted.
GO:0005576 extracellular region	IEA GO_REF:0000120	ACCEPT	Summary: The combined electronic evidence places albumin in its functional extracellular compartment. Reason: Albumin is a secreted ligand carrier, and the UniProt secretion record and albumin-family/domain mappings agree with that location. The mouse ortholog is correctly identified; none of the combined mappings is treated as an independent direct experiment. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00027128 UNRESOLVED Preserved combined mapping; its individual rule/donor experiment was not independently reconstructed. Target secretion provides independent support. UniProtKB:P07724 UNRESOLVED Preserved combined mapping; its individual rule/donor experiment was not independently reconstructed. Target secretion provides independent support. ensembl:ENSMUSP00000031314 UNRESOLVED Preserved combined mapping; its individual rule/donor experiment was not independently reconstructed. Target secretion provides independent support. InterPro:IPR000264 UNRESOLVED Preserved combined mapping; its individual rule/donor experiment was not independently reconstructed. Target secretion provides independent support. InterPro:IPR014760 UNRESOLVED Preserved combined mapping; its individual rule/donor experiment was not independently reconstructed. Target secretion provides independent support. InterPro:IPR020858 UNRESOLVED Preserved combined mapping; its individual rule/donor experiment was not independently reconstructed. Target secretion provides independent support. InterPro:IPR021177 UNRESOLVED Preserved combined mapping; its individual rule/donor experiment was not independently reconstructed. Target secretion provides independent support. UniProtKB-SubCell:SL-0243 SUPPORTS TRANSFER The secretion mapping agrees with the target UniProt record. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted.
GO:0005576 extracellular region	NAS PMID:14718574 The human plasma proteome: a nonredundant list developed by ...	ACCEPT	Summary: The human plasma proteome supports extracellular albumin. Reason: The cited plasma survey provides the NAS context. Albumin secretion and direct biochemical work in human serum establish the broad location independently, while the specific survey identification is not re-created from its abstract. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. PMID:1157293 The tight binding capacity of a pool of normal adult human serum was found to be 20 mg/dl of serum.
GO:0005576 extracellular region	TAS Reactome:R-HSA-2168887	ACCEPT	Summary: Heme transfer from albumin to hemopexin occurs extracellularly. Reason: Albumin acts as a soluble heme donor to hemopexin in the explicitly modeled extracellular transfer event. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-2168887 Despite the lower affinity of ferriheme for albumin than for hemopexin, ferriheme initially associates with albumin, presumably because the molar concentration of albumin in plasma is considerably greater than that of hemopexin.
GO:0005576 extracellular region	TAS Reactome:R-HSA-264679	ACCEPT	Summary: Albumin binds lysophosphatidylcholine in the extracellular compartment. Reason: The event models extracellular lipid binding by human albumin, consistent with its circulating carrier role. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-264679 Serum albumin binds 2-lysophosphatidylcholine (lysolecithin) to form a complex.
GO:0005576 extracellular region	TAS Reactome:R-HSA-481007	ACCEPT	Summary: Platelet granule exocytosis releases albumin into extracellular fluid. Reason: Albumin is a granule cargo in the release event, not the exocytosis machinery. The extracellular output agrees with its established secreted location. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-481007 Alpha granules contain mainly polypeptides such as fibrinogen, von Willebrand factor, growth factors and protease inhibitors that supplement thrombin generation at the site of injury.
GO:0005576 extracellular region	TAS Reactome:R-HSA-9661419	ACCEPT	Summary: Albumin captures extracellular heme. Reason: The event represents ligand capture by extracellular human albumin, not heme biosynthesis. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9661419 Circulating free heme is cytotoxic.
GO:0005576 extracellular region	TAS Reactome:R-HSA-9661425	ACCEPT	Summary: Bilirubin is released from extracellular albumin. Reason: The ligand-release event places the carrier in extracellular fluid before bilirubin uptake into hepatocytes. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9661425 When the bilirubin-albumin complex (BIL:ALB) reaches the liver, the highly permeable hepatic circulation facilitates the complex to reach the sinusoidal side of the hepatocyte.
GO:0005576 extracellular region	TAS Reactome:R-HSA-9661432	ACCEPT	Summary: Extracellular albumin binds bilirubin. Reason: This is the ligand-binding step of the circulating bilirubin carrier. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9661432 The serum protein albumin (ALB) binds unconjugated bilirubin (BIL), preventing BIL toxicity (Griffiths et al. 1975, Weisiger et al. 2001).
GO:0005576 extracellular region	TAS Reactome:R-HSA-9709883	ACCEPT	Summary: Albumin-bound bilirubin participates in extracellular oxidant scavenging. Reason: The modeled bilirubin-albumin complex reacts with superoxide in extracellular fluid. The location is supported without assigning bilirubin oxidoreductase catalysis to albumin. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9709883 Like unbound bilirubin (BIL) the bilirubin-albumin complex (BlL:ALB) scavenges superoxide.
GO:0005576 extracellular region	TAS Reactome:R-HSA-9733545	ACCEPT	Summary: Albumin binds circulating bile salts and acids. Reason: The event models extracellular ligand binding by human albumin. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9733545 Bile salts and acids are transported in the blood primarily bound to serum albumin (ALB) (Rudman & Kendall 1957, Roda et al. 1982).
GO:0005576 extracellular region	TAS Reactome:R-HSA-9733960	ACCEPT	Summary: Bile salts and acids dissociate from extracellular albumin. Reason: The reversible carrier-ligand release occurs in the circulating compartment. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9733960 Bile salts and acids exist in the blood as complexes with serum albumin (ALB) (Rudman & Kendall 1957, Roda et al. 1982), and their uptake by hepatocytes must involve disruption of this complex, but the molecular mechanism coupling release of a bile salt or acid from ALB is unknown.
GO:0005576 extracellular region	TAS Reactome:R-HSA-9749590	ACCEPT	Summary: Aspirin acetylates extracellular albumin. Reason: The event describes albumin acetylation and slow deacetylation in plasma. Retaining its extracellular location does not manufacture an enzymatic esterase annotation. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9749590 Acetylsalicylate (ASA-) acetylates several lysine residues on albumin, which subsequently release their acetate over a long time span.
GO:0005576 extracellular region	TAS Reactome:R-HSA-9750666	ACCEPT	Summary: Salicylate binds extracellular albumin. Reason: Human albumin binds the drug metabolite in the circulating compartment. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9750666 Salicylate binds to multiple sites on serum albumin, but at therapeutic doses only one site seems relevant, for kinetic reason.
GO:0005576 extracellular region	TAS Reactome:R-HSA-9757574	ACCEPT	Summary: Albumin binds prednisolone in plasma. Reason: The event assigns extracellular drug binding to human albumin and distinguishes its binding sites from corticosteroid-binding globulin. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9757574 Distribution and free concentration of various drugs can be significantly altered as a result of their binding to serum albumin (ALB).
GO:0005576 extracellular region	TAS Reactome:R-HSA-9757578	ACCEPT	Summary: Albumin binds prednisone in plasma. Reason: The event models extracellular prednisone association with human albumin. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9757578 Distribution and free concentration of various drugs can be significantly altered as a result of their binding to serum albumin (ALB).
GO:0005576 extracellular region	TAS Reactome:R-HSA-9762343	ACCEPT	Summary: Prednisolone dissociates from extracellular albumin. Reason: Reversible prednisolone carriage occurs in the extracellular pool. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9762343 Binding of prednisolone (PREDL) to albumin (ALB) is high-capacity but weak affinity.
GO:0005576 extracellular region	TAS Reactome:R-HSA-9762345	ACCEPT	Summary: Prednisone dissociates from extracellular albumin. Reason: Reversible prednisone carriage occurs in the extracellular pool. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9762345 Binding of prednisone (PREDN) to albumin (ALB) is high-capacity but weak affinity.
GO:0005576 extracellular region	TAS Reactome:R-HSA-9794444	ACCEPT	Summary: Albumin binds ciprofloxacin extracellularly. Reason: The event models drug binding by human albumin. Its summary separately identifies bovine studies used for some conformational observations; these are not recast as human assays. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9794444 Distribution and free concentration of various drugs can be significantly altered as a result of their binding to serum albumin (ALB).
GO:0005576 extracellular region	TAS Reactome:R-HSA-9794475	ACCEPT	Summary: Ciprofloxacin is released from extracellular albumin. Reason: The carrier-release step maintains the extracellular location established by the corresponding binding event. The live official event participants and compartment were checked; the normal cached summary is retained unchanged. Supporting Evidence: file:human/ALB/ALB-uniprot.txt SUBCELLULAR LOCATION: Secreted. Reactome:R-HSA-9794475 Distribution and free concentration of various drugs can be significantly altered as a result of their binding to serum albumin (ALB).
GO:0005634 nucleus	HDA PMID:21630459 Proteomic characterization of the human sperm nucleus.	UNDECIDED	Summary: The albumin-specific sperm nuclear identification remains unresolved. Reason: The original study purified human sperm nuclei to greater than 99.9% purity and identified hundreds of proteins. Its cached abstract does not expose ALB peptides or the target-level result. A secreted major plasma protein is not automatically a contaminant; the exact nuclear assignment requires the original target table or localization evidence. Supporting Evidence: PMID:21630459 403 different proteins have been identified from the isolated sperm nuclei.
GO:0005737 cytoplasm	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: The broad cytoplasmic donor annotation is compatible with intracellular albumin pools. Reason: The mouse donor P07724 is Alb, and MGI records experimental cytoplasmic localizations. Cached primary evidence for mouse embryonic and teratocarcinoma structures establishes albumin immunostaining and cellular uptake. Retain the broad location as contextual; cytoplasm includes secretory organelles and is not a claim of constitutive human cytosolic function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P07724 SUPPORTS TRANSFER Verified mouse Alb identity and MGI cytoplasmic evidence; cached mouse primary study supports intracellular expression/uptake. This does not imply a constitutive human cytosolic carrier pool. ensembl:ENSMUSP00000031314 SUPPORTS TRANSFER Cross-reference of the same mouse Alb protein, not a second independent experiment. Supporting Evidence: PMID:8607965 Only SA protein was detectable by immunostaining.
GO:0005788 endoplasmic reticulum lumen	TAS Reactome:R-HSA-8952289	KEEP AS NON CORE	Summary: Albumin passes through the secretory lumen as a FAM20C substrate. Reason: Reactome models albumin among FAM20C substrates in the ER lumen. This is a valid biosynthetic/processing compartment for secreted albumin, distinct from the extracellular site of mature carrier function. It does not make albumin a kinase. Supporting Evidence: Reactome:R-HSA-8952289 can phosphorylate a broad range of secreted protein
GO:0006783 heme biosynthetic process	TAS Reactome:R-HSA-189451	REMOVE	Summary: Extracellular acceptance of completed heme is not a heme-synthetic step. Reason: Reactome groups albumin with porphyrin transport accompanying heme biosynthesis. The actual human-albumin assay in the ABCG2 source demonstrates uptake of already formed hemin from the extracellular loop, whereas the GO term concerns formation of heme from less complex precursors. This carrier endpoint does not establish that albumin performs heme synthesis. Preserve heme binding and carriage rather than transferring the broad pathway label as a biosynthetic function. Supporting Evidence: PMID:20705604 human serum albumin could be one of these possible partners as it removes hemin bound to ECL3 Reactome:R-HSA-189451 Eight enzymes are involved in heme biosynthesis
GO:0009267 cellular response to starvation	IDA PMID:16245148 Production of human serum albumin by sugar starvation induce...	REMOVE	Summary: The starvation response belongs to the rice expression system. Reason: The full primary Methods and Figures 1 and 3-6 place mature human albumin cDNA behind the rice alphaAmy3 promoter and signal sequence. Sucrose removal induces production and secretion of the recombinant output protein; albumin is not shown to execute the host starvation response. This is a source-specific role error established from the full experiment, not rejection based on a plant host alone. Supporting Evidence: PMID:16245148 Mature form of HSA was expressed under the control of the sucrose starvation-inducible rice alpha Amy3 promoter
GO:0015643 toxic substance binding	IDA PMID:16169013 Structural basis of the drug-binding specificity of human se...	ACCEPT	Summary: Human albumin directly binds drugs and toxic ligands. Reason: The study resolves multiple human albumin-drug/toxin crystal complexes. Binding these molecules is part of albumin's circulating sequestration and carrier chemistry; binding is not equated with complete detoxification or drug metabolism. Supporting Evidence: PMID:16169013 17 different complexes of HSA with a wide variety of drugs and small-molecule toxins reveals the precise architecture of the two primary drug-binding sites on the protein
GO:0015723 bilirubin transport	IEA GO_REF:0000107	ACCEPT	Summary: Albumin directly carries unconjugated bilirubin in blood. Reason: The mouse ortholog transfer agrees with human serum bilirubin-binding experiments and Reactome binding/release steps. Albumin performs the carrier work; hepatocyte uptake and glucuronidation are separate activities. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P07724 UNRESOLVED Mouse Alb identity verified; the exact donor experimental chain was not reconstructed. Human bilirubin/hemin carrier experiments independently support the target assertion. ensembl:ENSMUSP00000031314 UNRESOLVED Same mouse Alb product cross-reference; not counted as an independent donor experiment. Supporting Evidence: PMID:1157293 The tight binding capacity of a pool of normal adult human serum was found to be 20 mg/dl of serum. Reactome:R-HSA-9661432 ALB-bound BIL is a water-soluble complex and is transported to the liver where it is selectively absorbed by hepatocytes.
GO:0016209 antioxidant activity	NAS PMID:14726550 Human serum albumin and its N-terminal tetrapeptide (DAHK) b...	ACCEPT	Summary: Human albumin protects cells from oxidant toxicity. Reason: Human albumin and its DAHK peptide protect murine cortical cultures from hydrogen-peroxide and copper/ascorbate challenges. Metal sequestration is a proposed contributor and is not presented as direct measurement of every protective mechanism. The antioxidant activity is a distinct biochemical function of the extracellular protein. Supporting Evidence: PMID:14726550 HSA provided complete protection at a concentration of 37.5 micromol/L and 50% protection at 3.75 micromol/L. PMID:14726550 HSA and DAHK were also equally effective in preventing neuronal death induced by CuCl(2)/ascorbic acid.
GO:0019825 oxygen binding	IDA PMID:16283771 Albumin clusters: structurally defined protein tetramer and ...	MARK AS OVER ANNOTATED	Summary: Oxygen binding is demonstrated for an engineered albumin-porphyrin assembly. Reason: The source chemically crosslinks recombinant human albumin and loads synthetic iron(II) porphyrins. Its reversible oxygen carriage is positive evidence for that artificial construct. The retained contributes_to flag is respected: albumin supports the engineered assembly, but that weaker claim still does not establish a native albumin oxygen-binding function. The annotation overextends a designed material to the unmodified gene product. Supporting Evidence: PMID:16283771 These albumin-heme clusters can reversibly bind and release O2 under physiological conditions PMID:16283771 24 and 32 molecules of the synthetic iron(II) porphyrins (FePs) are incorporated into the hydrophobic cavities of the rHSA trimer and tetramer, respectively
GO:0020037 heme binding	EXP PMID:20705604 ABCG2 transports and transfers heme to albumin through its l...	ACCEPT	Summary: Human albumin accepts hemin from ABCG2. Reason: The primary study measures hemin transfer from purified ECL3 or full ABCG2 to human albumin. Indexed original Figure 8 resolves fluorescence and Soret-band changes with apoalbumin and hemin-loaded controls. Albumin is the extracellular ligand acceptor; ABCG2 performs membrane transport. Supporting Evidence: PMID:20705604 human serum albumin could be one of these possible partners as it removes hemin bound to ECL3
GO:0020037 heme binding	EXP PMID:36979511 Heme Scavenging and Delivery: The Role of Human Serum Albumi...	ACCEPT	Summary: Heme binding is a well-supported albumin carrier property. Reason: The cited 2023 article is a narrative review, despite the seeded EXP code. Its heme-scavenging synthesis agrees with the independently inspected primary human-albumin transfer experiment. Retain the correct molecular function without relabeling the machine evidence code or treating the review as a new direct assay. Supporting Evidence: PMID:36979511 HSA slowly removes most of the heme from HDL and LDL and transfers it to Hx PMID:20705604 human serum albumin could be one of these possible partners as it removes hemin bound to ECL3
GO:0030170 pyridoxal phosphate binding	IDA PMID:16201370 [The interaction of vitamin B6 with the human serum albumin]...	UNDECIDED	Summary: The exact vitamin B6 species in the original binding assay remains unresolved. Reason: The English abstract reports human albumin interaction with vitamin B6 by spectroscopy, but it does not identify the assayed chemical form as pyridoxal phosphate. The original Chinese full text was not recovered. This prevents a source-specific decision on the phosphate-specific term; it does not show albumin cannot bind PLP. Supporting Evidence: PMID:16201370 After the vitamin B6 (B6) was added into HSA solution the fluorescence of HSA was quenched partially.
GO:0031093 platelet alpha granule lumen	TAS Reactome:R-HSA-481007	KEEP AS NON CORE	Summary: Albumin is cargo in platelet alpha-granule lumen. Reason: The official Reactome event identifies the albumin-containing platelet granule pool and its release. This contextual storage location is retained without assigning albumin a role in building granules or driving exocytosis. Supporting Evidence: Reactome:R-HSA-481007 Alpha granules contain mainly polypeptides
GO:0031667 response to nutrient levels	IBA GO_REF:0000033	UNDECIDED	Summary: The nutrient-response ancestral assertion needs its descendant evidence resolved. Reason: The cached PAINT family explicitly places this IBD at PTN000147344. Human ALB appearing among the descendant evidences is legitimate, not circular. However, the separately curated human starvation study is a rice-promoter expression experiment, and the other descendant nutrient-response assays have not been reconstructed sufficiently to adjudicate this ancestral process placement. Neither donor count nor that one source defect is used to reject the whole node. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000147344 UNRESOLVED Cached PTHR11385 PAINT record confirms the GO:0031667 IBD. The target rice-promoter source cannot itself establish native participation; the remaining descendant assays and node scope require further review. No donor-count or self-evidence objection is made.
GO:0032991 protein-containing complex	IDA PMID:16283771 Albumin clusters: structurally defined protein tetramer and ...	MARK AS OVER ANNOTATED	Summary: The cited complex is a chemically engineered albumin oligomer. Reason: The experiment constructs structurally defined recombinant albumin trimers/tetramers with chemical crosslinking. Such assemblies are real, but they do not establish an endogenous protein-containing complex for the ordinary human gene product. Other native albumin associations are assessed on their own sources. Supporting Evidence: PMID:16283771 Cross-linking between the Lys groups of the core albumin and a unique Cys-34 of the shell albumins
GO:0034599 cellular response to oxidative stress	TAS Reactome:R-HSA-9707564	KEEP AS NON CORE	Summary: Albumin participates in extracellular protection associated with the HMOX1 pathway. Reason: Within the Reactome pathway, albumin binds bilirubin and the bilirubin-albumin complex scavenges superoxide. The protein supplies the carrier context for the protective reaction, while heme oxygenase and biliverdin reductase perform the upstream chemistry. Retain this contextual stress response without assigning albumin transcriptional sensing or those enzyme activities. Supporting Evidence: Reactome:R-HSA-9709883 the bilirubin-albumin complex (BlL:ALB) scavenges superoxide.
GO:0042167 heme catabolic process	TAS Reactome:R-HSA-189483	MODIFY	Summary: The specified albumin step carries bilirubin after heme breakdown. Reason: The source pathway distinguishes heme-ring cleavage and biliverdin reduction from downstream bilirubin handling. Albumin binds and releases the resulting bilirubin for transport; it does not perform the degradation reactions in this cited branch. Refine to the already supported bilirubin transport process, retaining the pathway context without an albumin heme-cleavage claim. Proposed replacements: bilirubin transport Supporting Evidence: Reactome:R-HSA-189483 cleavage of the heme ring by a microsomal heme oxygenase producing biliverdin Reactome:R-HSA-9661432 ALB-bound BIL is a water-soluble complex and is transported to the liver where it is selectively absorbed by hepatocytes.
GO:0042802 identical protein binding	IPI PMID:15174051 An investigation into the human serum "interactome".	UNDECIDED	Summary: The serum-interactome experiment does not expose the specific self-binding evidence. Reason: The source uses immunoprecipitation and mass spectrometry to identify serum-protein partners. The accessible abstract does not resolve controls that distinguish ALB self-association from recovery of the albumin bait itself. Genuine albumin dimerization in another study does not reconstruct this particular experiment; the IPI assertion remains unresolved. Supporting Evidence: PMID:15174051 immunoprecipitation was combined with microcapillary reversed-phase liquid chromatography
GO:0042802 identical protein binding	IPI PMID:26554815 New insights into in vitro amyloidogenic properties of human...	KEEP AS NON CORE	Summary: Human albumin can homodimerize through Cys34 in vitro. Reason: The source explicitly produces human-albumin homodimers via its free cysteine and studies aggregation/self-seeding. Retain the demonstrated self-association as a conditional biochemical property, without presenting circulating albumin as an obligate dimer or native amyloid. Supporting Evidence: PMID:26554815 HSA was homodimerized via free cysteine-34
GO:0051087 protein-folding chaperone binding	IPI PMID:19996109 Identification of human plasma proteins as major clients for...	KEEP AS NON CORE	Summary: Stressed human albumin binds the extracellular chaperone clusterin. Reason: The paper directly identifies ALB in CLU-client complexes and confirms complexes by sandwich ELISA after shear stress. This is specific chaperone binding by a client, not protein-folding chaperone activity performed by albumin. Supporting Evidence: PMID:19996109 sandwich enzyme-linked immunosorbent assay detected complexes containing CLU and ceruloplasmin, fibrinogen, or albumin
GO:0051902 negative regulation of mitochondrial depolarization	IDA PMID:16153637 Albumin prevents mitochondrial depolarization and apoptosis ...	UNDECIDED	Summary: Albumin protects mitochondrial polarization in the reported culture assay, but human-protein attribution is unresolved. Reason: The abstract reports TMRE protection in human SH-SY5Y cells. PubMed indexing and the same authors' original conference report identify bovine serum albumin; the complete journal Methods were not recovered to determine whether human albumin was also tested. Preserve the positive protective result but leave the human gene annotation unresolved rather than infer species from the host cells. Supporting Evidence: PMID:16153637 depolarization was inhibited by cytoprotective concentrations of albumin
GO:0070062 extracellular exosome	HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos...	UNDECIDED	Summary: The albumin-specific exosome assignment remains unresolved in human urine. Reason: The abstract reports urinary-exosome proteomics and phosphoproteomics. These methods support the study's vesicle characterization, not independent verification of this target. Albumin abundance or extracellular secretion is not treated as proof of contamination or as evidence against vesicle association. The specific source table or assay is needed.
GO:0070062 extracellular exosome	HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote...	UNDECIDED	Summary: The albumin-specific exosome assignment remains unresolved in human B-cell exosomes. Reason: The abstract reports a B-cell vesicle proteome and selected MHC-II associations. These methods support the study's vesicle characterization, not independent verification of this target. Albumin abundance or extracellular secretion is not treated as proof of contamination or as evidence against vesicle association. The specific source table or assay is needed.
GO:0070062 extracellular exosome	HDA PMID:21362503 Protein profile of exosomes from trabecular meshwork cells.	UNDECIDED	Summary: The albumin-specific exosome assignment remains unresolved in cultured human trabecular-meshwork cells. Reason: The cached body describes vesicle isolation and the protein survey, but the ALB-specific supplement entry was not recovered. These methods support the study's vesicle characterization, not independent verification of this target. Albumin abundance or extracellular secretion is not treated as proof of contamination or as evidence against vesicle association. The specific source table or assay is needed.
GO:0070062 extracellular exosome	HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres...	UNDECIDED	Summary: The albumin-specific exosome assignment remains unresolved in expressed prostatic secretions in human urine. Reason: The cached body documents ultracentrifugation, washing and MS/FDR procedures; the ALB-specific supplement hit remains uninspected. These methods support the study's vesicle characterization, not independent verification of this target. Albumin abundance or extracellular secretion is not treated as proof of contamination or as evidence against vesicle association. The specific source table or assay is needed.
GO:0070062 extracellular exosome	IDA PMID:21276792 Morphologic and proteomic characterization of exosomes relea...	UNDECIDED	Summary: The albumin-specific exosome assignment remains unresolved in cultured human Swan71 trophoblast cells. Reason: The abstract reports vesicle density, morphology, size and proteomics, but does not expose the ALB identification. These methods support the study's vesicle characterization, not independent verification of this target. Albumin abundance or extracellular secretion is not treated as proof of contamination or as evidence against vesicle association. The specific source table or assay is needed.
GO:0072562 blood microparticle	HDA PMID:22516433 Proteomic analysis of microvesicles from plasma of healthy d...	UNDECIDED	Summary: The albumin-specific plasma-microparticle identification remains unresolved. Reason: The study identifies proteins in healthy-donor plasma microvesicles, but the cached abstract does not expose ALB peptides, particle association or target controls. The normal presence of soluble albumin in plasma does not establish either contamination or genuine particle association, so no confident deletion or confirmation is made.
GO:0072732 cellular response to calcium ion starvation	IDA PMID:16153637 Albumin prevents mitochondrial depolarization and apoptosis ...	UNDECIDED	Summary: The calcium-starvation process and human albumin attribution are not sufficiently resolved. Reason: The experiment perturbs ER calcium stores in human cells and observes albumin-mediated protection without changing calcium-release kinetics. Its original conference report identifies bovine albumin, and the journal full Methods remain unavailable. The exact human-protein participation and calcium-starvation interpretation are therefore unresolved; a generic response-to-depletion phenotype is not substituted for the specific source evidence. Supporting Evidence: PMID:16153637 Albumin did not modify the kinetic parameters of such increase.
GO:0098869 cellular oxidant detoxification	IEA GO_REF:0000108	ACCEPT	Summary: Albumin antioxidant activity supports the logical oxidant-detoxification mapping. Reason: Live GO places antioxidant activity part_of cellular oxidant detoxification; this is the stated inter-ontology inference. Human albumin protects cultured cells from hydrogen-peroxide and copper-associated toxicity. The process definition does not require the protein to reside inside the cytosol, and extracellular metal/oxidant buffering is not recast as an intracellular enzyme. Propagation Review Root cause: NO FAILURE CORE Sources checked: GO:0016209 SUPPORTS TRANSFER Live ontology explicitly relates antioxidant activity part_of cellular oxidant detoxification. The target human protein has positive antioxidant evidence. Supporting Evidence: PMID:14726550 HSA provided complete protection at a concentration of 37.5 micromol/L and 50% protection at 3.75 micromol/L. PMID:14726550 HSA and DAHK were also equally effective in preventing neuronal death induced by CuCl(2)/ascorbic acid.
GO:0140104 molecular carrier activity	EXP PMID:11397817 Affinity of human serum albumin for bilirubin varies with al...	ACCEPT	Summary: Human albumin binds bilirubin as a molecular carrier. Reason: Ultrafiltration directly measures the albumin-bilirubin binding equilibrium, with affinity dependent on assay conditions. Together with defined binding/release events, this supports carrier activity without assigning a universal affinity or a membrane-transporter mechanism. Supporting Evidence: PMID:11397817 The apparent binding affinity of human serum albumin for [(14)C]bilirubin was strongly dependent on assay conditions
GO:0140104 molecular carrier activity	EXP PMID:1157293 The albumin binding of unconjugated bilirubin in serum.	ACCEPT	Summary: Human serum albumin provides bilirubin-carrying capacity. Reason: Dextran-coated-charcoal titration measures bilirubin binding in normal human adult serum. The direct binding result supports the carrier function synthesized with the bilirubin-release pathway; no ATP-driven membrane movement is implied. Supporting Evidence: PMID:1157293 The tight binding capacity of a pool of normal adult human serum was found to be 20 mg/dl of serum.
GO:0140104 molecular carrier activity	IEA GO_REF:0000107	ACCEPT	Summary: The mouse-ortholog transfer agrees with direct human carrier evidence. Reason: Human albumin binds bilirubin and fatty acids and accepts hemin from an extracellular donor. These target experiments independently establish molecular carrier activity and support the mouse-to-human transfer, while the exact donor assay chain is not treated as independently re-read. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P07724 UNRESOLVED Mouse Alb identity verified; the exact donor experimental chain was not reconstructed. Human bilirubin/hemin carrier experiments independently support the target assertion. ensembl:ENSMUSP00000031314 UNRESOLVED Same mouse Alb product cross-reference; not counted as an independent donor experiment. Supporting Evidence: PMID:20705604 human serum albumin could be one of these possible partners as it removes hemin bound to ECL3 PMID:1157293 The tight binding capacity of a pool of normal adult human serum was found to be 20 mg/dl of serum. Reactome:R-HSA-9661432 ALB-bound BIL is a water-soluble complex and is transported to the liver where it is selectively absorbed by hepatocytes.
GO:0140272 exogenous protein binding	IDA PMID:16394536 Human serum albumin enhances the hemolytic activity of Vibri...	UNDECIDED	Summary: Albumin stabilizes a bacterial hemolysin, but direct exogenous-protein binding is unresolved. Reason: The full original paper tests human/bovine albumin addition to Vibrio culture supernatants, hemolysis of human erythrocytes, and VvhA monomer/oligomer immunoblots. It establishes stabilization and delayed oligomerization, but the inspected assays do not directly resolve an albumin-VvhA bound pair. Retain the positive functional effect while leaving this binding assertion uncertain; neither a holdase activity nor a host-defense role is invented. Supporting Evidence: PMID:16394536 both HSA and BSA stabilize VvhA
GO:1903981 enterobactin binding	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: The mammalian ancestral enterobactin-binding assertion has direct human and bovine support. Reason: PAINT places the IBD at PTN008319942. The same primary paper experimentally tests purified human and bovine albumin and measures enterobactin association, providing direct target grounding. This is a contextual microbial-ligand interaction of the carrier; human self-evidence in the descendant list is not circular. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN008319942 SUPPORTS TRANSFER Cached PAINT IBD has mammalian taxon scope. The original human/bovine purified-albumin study directly supports the inherited binding property; target self-evidence is valid. Supporting Evidence: PMID:6234017 stoichiometry of binding to human and bovine serum albumins was established as 1:1
GO:1903981 enterobactin binding	IDA PMID:6234017 Effect of serum albumin on siderophore-mediated utilization ...	KEEP AS NON CORE	Summary: Human albumin directly binds enterobactin and ferric enterobactin. Reason: The study measures spectral changes, 1:1 binding and effects on siderophore-mediated iron utilization. Retain this specific binding property as contextual rather than an albumin iron-transmembrane-transport or antibacterial enzyme activity. Supporting Evidence: PMID:6234017 Binding of serum albumin to enterobactin increased the intensity

Gene Description

Existing Annotations Review

Core Functions

Reversibly binds and carries circulating ligands, including bilirubin, fatty acids and heme. The soluble protein supplies binding and exchange capacity; membrane translocation is performed by other proteins.

Buffers oxidant toxicity in extracellular fluid, including metal-associated oxidant stress. Human albumin and its N-terminal DAHK peptide protect cultured neurons; this does not imply albumin has every catalytic antioxidant mechanism of heme enzymes.

References

Suggested Questions for Experts

📚 Additional Documentation

Notes

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