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Overview

Uniprot IDP02768
Protein NameAlbumin
Gene NameALB
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
130 NECFLQHKDDNPNLP
161 NEETFLKKYLYEIAR
205 KAACLLPKLDELRDE
214 DELRDEGKASSAKQR
223 SSAKQRLKCASLQKF
300 DSISSKLKECCEKPL
341 VESKDVCKNYAEAKD
375 VLLLRLAKTYETTLE
402 AKVFDEFKPLVEEPQ
438 LLVRYTKKVPQVSTP
499 PVSDRVTKCCTESLV
65 CPFEDHVKLVNEVTE
75 NEVTEFAKTCVADES
97 LHTLFGDKLCTVATL

Function

Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (PubMed:19021548). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017)

Protein Sequence

10 MKWVTFISLL 20 FLFSSAYSRG 30 VFRRDAHKSE 40 VAHRFKDLGE 50 ENFKALVLIA 60 FAQYLQQCPF 70 EDHVKLVNEV 80 TEFAKTCVAD 90 ESAENCDKSL 100 HTLFGDKLCT 110 VATLRETYGE 120 MADCCAKQEP 130 ERNECFLQHK 140 DDNPNLPRLV 150 RPEVDVMCTA 160 FHDNEETFLK 170 KYLYEIARRH 180 PYFYAPELLF 190 FAKRYKAAFT 200 ECCQAADKAA 210 CLLPKLDELR 220 DEGKASSAKQ 230 RLKCASLQKF 240 GERAFKAWAV 250 ARLSQRFPKA 260 EFAEVSKLVT 270 DLTKVHTECC 280 HGDLLECADD 290 RADLAKYICE 300 NQDSISSKLK 310 ECCEKPLLEK 320 SHCIAEVEND 330 EMPADLPSLA 340 ADFVESKDVC 350 KNYAEAKDVF 360 LGMFLYEYAR 370 RHPDYSVVLL 380 LRLAKTYETT 390 LEKCCAAADP 400 HECYAKVFDE 410 FKPLVEEPQN 420 LIKQNCELFE 430 QLGEYKFQNA 440 LLVRYTKKVP 450 QVSTPTLVEV 460 SRNLGKVGSK 470 CCKHPEAKRM 480 PCAEDYLSVV 490 LNQLCVLHEK 500 TPVSDRVTKC 510 CTESLVNRRP 520 CFSALEVDET 530 YVPKEFNAET 540 FTFHADICTL 550 SEKERQIKKQ 560 TALVELVKHK 570 PKATKEQLKA 580 VMDDFAAFVE 590 KCCKADDKET 600 CFAEEGKKLV AASQAALGL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0072562 blood microparticle
Cellular Component GO:0005788 endoplasmic reticulum lumen
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005634 nucleus
Cellular Component GO:0031093 platelet alpha granule lumen
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0016209 antioxidant activity
Molecular Function GO:0005507 copper ion binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:1903981 enterobactin binding
Molecular Function GO:0140272 exogenous protein binding
Molecular Function GO:0005504 fatty acid binding
Molecular Function GO:0020037 heme binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0140104 molecular carrier activity
Molecular Function GO:0051087 protein-folding chaperone binding
Molecular Function GO:0030170 pyridoxal phosphate binding
Molecular Function GO:0015643 toxic substance binding
Biological Process GO:0015723 bilirubin transport
Biological Process GO:0072732 cellular response to calcium ion starvation
Biological Process GO:0034599 cellular response to oxidative stress
Biological Process GO:0009267 cellular response to starvation
Biological Process GO:0006783 heme biosynthetic process
Biological Process GO:0042167 heme catabolic process
Biological Process GO:0051902 negative regulation of mitochondrial depolarization
Biological Process GO:0031667 response to nutrient levels

Reference

[1] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.