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Overview

Uniprot ID	P78318
Protein Name	Immunoglobulin-binding protein 1
Gene Name	IGBP1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
276	DWYEQHRKYGALPDQ
287	LPDQGIAKAAPEEFR
295	AAPEEFRKAAQQQEE

Function

Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits

Protein Sequence

10 MAAEDELQLP 20 RLPELFETGR 30 QLLDEVEVAT 40 EPAGSRIVQE 50 KVFKGLDLLE 60 KAAEMLSQLD 70 LFSRNEDLEE 80 IASTDLKYLL 90 VPAFQGALTM 100 KQVNPSKRLD 110 HLQRAREHFI 120 NYLTQCHCYH 130 VAEFELPKTM 140 NNSAENHTAN 150 SSMAYPSLVA 160 MASQRQAKIQ 170 RYKQKKELEH 180 RLSAMKSAVE 190 SGQADDERVR 200 EYYLLHLQRW 210 IDISLEEIES 220 IDQEIKILRE 230 RDSSREASTS 240 NSSRQERPPV 250 KPFILTRNMA 260 QAKVFGAGYP 270 SLPTMTVSDW 280 YEQHRKYGAL 290 PDQGIAKAAP 300 EEFRKAAQQQ 310 EEQEEKEEED 320 DEQTLHRARE 330 WDDWKDTHPR GYGNRQNMG

Gene Ontology

Classification	GO ID	Description
Biological Process	GO:0034612	response to tumor necrosis factor
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Molecular Function	GO:0051721	protein phosphatase 2A binding
Molecular Function	GO:0019888	protein phosphatase regulator activity
Biological Process	GO:0042113	B cell activation
Biological Process	GO:0035556	intracellular signal transduction
Biological Process	GO:0032873	negative regulation of stress-activated MAPK cascade
Biological Process	GO:0000122	negative regulation of transcription by RNA polymerase II
Biological Process	GO:0035303	regulation of dephosphorylation
Biological Process	GO:0060632	regulation of microtubule-based movement
Biological Process	GO:0070555	response to interleukin-1
Biological Process	GO:0007165	signal transduction

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[2] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[4] 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.