Search Results

Overview

Uniprot ID	Q6FI81
Protein Name	Anamorsin
Gene Name	CIAPIN1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
175	VGSSRQLKLSITKKS
181	LKLSITKKSSPSVKP
244	CGEGKKRKACKNCTC
247	GKKRKACKNCTCGLA

Function

Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1 (PubMed:23596212). NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity)

Protein Sequence

10 MADFGISAGQ 20 FVAVVWDKSS 30 PVEALKGLVD 40 KLQALTGNEG 50 RVSVENIKQL 60 LQSAHKESSF 70 DIILSGLVPG 80 STTLHSAEIL 90 AEIARILRPG 100 GCLFLKEPVE 110 TAVDNNSKVK 120 TASKLCSALT 130 LSGLVEVKEL 140 QREPLTPEEV 150 QSVREHLGHE 160 SDNLLFVQIT 170 GKKPNFEVGS 180 SRQLKLSITK 190 KSSPSVKPAV 200 DPAAAKLWTL 210 SANDMEDDSM 220 DLIDSDELLD 230 PEDLKKPDPA 240 SLRAASCGEG 250 KKRKACKNCT 260 CGLAEELEKE 270 KSREQMSSQP 280 KSACGNCYLG 290 DAFRCASCPY 300 LGMPAFKPGE 310 KVLLSDSNLH DA

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005758	mitochondrial intermembrane space
Cellular Component	GO:0005739	mitochondrion
Cellular Component	GO:0005654	nucleoplasm
Molecular Function	GO:0051537	2 iron, 2 sulfur cluster binding
Molecular Function	GO:0051539	4 iron, 4 sulfur cluster binding
Molecular Function	GO:0009055	electron transfer activity
Molecular Function	GO:0005506	iron ion binding
Biological Process	GO:0006915	apoptotic process
Biological Process	GO:0034599	cellular response to oxidative stress
Biological Process	GO:0030097	hemopoiesis
Biological Process	GO:0016226	iron-sulfur cluster assembly
Biological Process	GO:0043066	negative regulation of apoptotic process

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] 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.

[4] 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.

[5] 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.

[6] 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.

[7] 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.