Search Results
Overview
| Uniprot ID | Q6KC79 |
|---|---|
| Protein Name | Nipped-B-like protein |
| Gene Name | NIPBL |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1032 | RSSLKPIKNKPSKSN |
| 1040 | NKPSKSNKGSIDQSV |
| 1369 | GGGLLSSKAKRAKCS |
| 1599 | LVHQFSNKSTEMALR |
| 222 | LRNIHDNKVSGPLSG |
| 2574 | YSPSESAKVYDKAIN |
| 289 | AGSEGTPKGSRPPLI |
| 333 | QKKMKLGKDEKEQSE |
| 353 | DIISSPSKDSTKLTL |
| 357 | SPSKDSTKLTLRLSR |
| 493 | IERERFSKEVQDKDK |
| 504 | DKDKPLKKRKQDSYP |
| 506 | DKPLKKRKQDSYPQE |
| 603 | HPETPKKKSDPELSK |
| 610 | KSDPELSKSEMKQSE |
| 634 | ENRLVETKSSENKLE |
| 639 | ETKSSENKLETKVET |
| 697 | NGRSETTKSRPETPK |
| 726 | DGHPETPKQKGDGRP |
| 759 | EGRPETPKHRHDNRR |
| 787 | SKHKQDTKSDSPRLK |
| 802 | SERAEALKQRPDGRS |
| 857 | SRNEHGIKSDSSKTD |
| 862 | GIKSDSSKTDKLERK |
| 865 | SDSSKTDKLERKHRH |
| 907 | SNKSRSDKLGFKSPT |
| 911 | RSDKLGFKSPTSKDD |
| 916 | GFKSPTSKDDKRTEG |
| 932 | KSKVDTNKAHPDNKA |
| 954 | GGRSGALKNFVIPKI |
| 960 | LKNFVIPKIKRDKDG |
| 962 | NFVIPKIKRDKDGNV |
| 965 | IPKIKRDKDGNVTQE |
Function
Plays an important role in the loading of the cohesin complex on to DNA. Forms a heterodimeric complex (also known as cohesin loading complex) with MAU2/SCC4 which mediates the loading of the cohesin complex onto chromatin (PubMed:22628566, PubMed:28914604). Plays a role in cohesin loading at sites of DNA damage. Its recruitment to double-strand breaks (DSBs) sites occurs in a CBX3-, RNF8- and RNF168-dependent manner whereas its recruitment to UV irradiation-induced DNA damage sites occurs in a ATM-, ATR-, RNF8- and RNF168-dependent manner (PubMed:28167679). Along with ZNF609, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0032116 | SMC loading complex |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0070087 | chromo shadow domain binding |
| Molecular Function | GO:0061775 | cohesin loader activity |
| Molecular Function | GO:0042826 | histone deacetylase binding |
| Molecular Function | GO:0036033 | mediator complex binding |
| Molecular Function | GO:1990841 | promoter-specific chromatin binding |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Biological Process | GO:0007420 | brain development |
| Biological Process | GO:0071481 | cellular response to X-ray |
| Biological Process | GO:0140588 | chromatin looping |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0050890 | cognition |
| Biological Process | GO:0048589 | developmental growth |
| Biological Process | GO:0048565 | digestive tract development |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0042471 | ear morphogenesis |
| Biological Process | GO:0048557 | embryonic digestive tract morphogenesis |
| Biological Process | GO:0035115 | embryonic forelimb morphogenesis |
| Biological Process | GO:0048703 | embryonic viscerocranium morphogenesis |
| Biological Process | GO:0034087 | establishment of mitotic sister chromatid cohesion |
| Biological Process | GO:0071169 | establishment of protein localization to chromatin |
| Biological Process | GO:0035261 | external genitalia morphogenesis |
| Biological Process | GO:0048592 | eye morphogenesis |
| Biological Process | GO:0060325 | face morphogenesis |
| Biological Process | GO:0035136 | forelimb morphogenesis |
| Biological Process | GO:0061010 | gallbladder development |
| Biological Process | GO:0003007 | heart morphogenesis |
| Biological Process | GO:0008104 | intracellular protein localization |
| Biological Process | GO:0034088 | maintenance of mitotic sister chromatid cohesion |
| Biological Process | GO:0001656 | metanephros development |
| Biological Process | GO:0007064 | mitotic sister chromatid cohesion |
| Biological Process | GO:0000070 | mitotic sister chromatid segregation |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0003151 | outflow tract morphogenesis |
| Biological Process | GO:2001224 | positive regulation of neuron migration |
| Biological Process | GO:0048638 | regulation of developmental growth |
| Biological Process | GO:0045995 | regulation of embryonic development |
| Biological Process | GO:0042634 | regulation of hair cycle |
| Biological Process | GO:1990414 | replication-born double-strand break repair via sister chromatid exchange |
| Biological Process | GO:0007605 | sensory perception of sound |
| Biological Process | GO:0061038 | uterus morphogenesis |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0032039 | integrator complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0090694 | Scc2-Scc4 cohesin loading complex |
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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] 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.
[5] 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.
[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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[8] 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.