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Overview

Uniprot IDP07724
Protein NameAlbumin
Gene NameAlb
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
117 ELADCCTKQEPERNE
210 TPKLDGVKEKALVSS
212 KLDGVKEKALVSSVR
223 SSVRQRMKCSSMQKF
229 MKCSSMQKFGERAFK
264 KLATDLTKVNKECCH
267 TDLTKVNKECCHGDL
286 DDRAELAKYMCENQA
305 KLQTCCDKPLLKKAH
309 CCDKPLLKKAHCLSE
376 LLLRLAKKYEATLEK
413 EEPKNLVKTNCDLYE
438 ILVRYTQKAPQVSTP
460 NLGRVGTKCCTLPED
490 RVCLLHEKTPVSEHV
524 VDETYVPKEFKAETF
543 DICTLPEKEKQIKKQ
549 EKEKQIKKQTALAEL
558 TALAELVKHKPKATA
560 LAELVKHKPKATAEQ
588 TCCKAADKDTCFSTE
75 QEVTDFAKTCVADES

Function

Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). 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 (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity)

Protein Sequence

10 MKWVTFLLLL 20 FVSGSAFSRG 30 VFRREAHKSE 40 IAHRYNDLGE 50 QHFKGLVLIA 60 FSQYLQKCSY 70 DEHAKLVQEV 80 TDFAKTCVAD 90 ESAANCDKSL 100 HTLFGDKLCA 110 IPNLRENYGE 120 LADCCTKQEP 130 ERNECFLQHK 140 DDNPSLPPFE 150 RPEAEAMCTS 160 FKENPTTFMG 170 HYLHEVARRH 180 PYFYAPELLY 190 YAEQYNEILT 200 QCCAEADKES 210 CLTPKLDGVK 220 EKALVSSVRQ 230 RMKCSSMQKF 240 GERAFKAWAV 250 ARLSQTFPNA 260 DFAEITKLAT 270 DLTKVNKECC 280 HGDLLECADD 290 RAELAKYMCE 300 NQATISSKLQ 310 TCCDKPLLKK 320 AHCLSEVEHD 330 TMPADLPAIA 340 ADFVEDQEVC 350 KNYAEAKDVF 360 LGTFLYEYSR 370 RHPDYSVSLL 380 LRLAKKYEAT 390 LEKCCAEANP 400 PACYGTVLAE 410 FQPLVEEPKN 420 LVKTNCDLYE 430 KLGEYGFQNA 440 ILVRYTQKAP 450 QVSTPTLVEA 460 ARNLGRVGTK 470 CCTLPEDQRL 480 PCVEDYLSAI 490 LNRVCLLHEK 500 TPVSEHVTKC 510 CSGSLVERRP 520 CFSALTVDET 530 YVPKEFKAET 540 FTFHSDICTL 550 PEKEKQIKKQ 560 TALAELVKHK 570 PKATAEQLKT 580 VMDDFAQFLD 590 TCCKAADKDT 600 CFSTEGPNLV TRCKDALA

Gene Ontology

Classification GO ID Description
Biological Process GO:0051902 negative regulation of mitochondrial depolarization
Cellular Component GO:0005604 basement membrane
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005794 Golgi apparatus
Cellular Component GO:0043209 myelin sheath
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0003677 DNA binding
Molecular Function GO:1903981 enterobactin binding
Molecular Function GO:0019899 enzyme 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:0072341 modified amino acid binding
Molecular Function GO:0140104 molecular carrier activity
Molecular Function GO:0019825 oxygen binding
Molecular Function GO:0051087 protein-folding chaperone binding
Molecular Function GO:0030170 pyridoxal phosphate binding
Molecular Function GO:0015643 toxic substance binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0015723 bilirubin transport
Biological Process GO:0072732 cellular response to calcium ion starvation
Biological Process GO:0009267 cellular response to starvation
Biological Process GO:0046010 positive regulation of circadian sleep/wake cycle, non-REM sleep
Biological Process GO:0031667 response to nutrient levels

Reference

[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.

[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.

[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.