Search Results

Overview

Uniprot IDQ13309
Protein NameS-phase kinase-associated protein 2
Gene NameSKP2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
73 PRKRLKSKGSDKDFV
77 LKSKGSDKDFVIVRR

Function

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription (PubMed:9736735, PubMed:11931757, PubMed:12435635, PubMed:12769844, PubMed:12840033, PubMed:15342634, PubMed:15668399, PubMed:15949444, PubMed:16103164, PubMed:16262255, PubMed:16581786, PubMed:16951159, PubMed:17908926, PubMed:17962192, PubMed:22464731, PubMed:22770219, PubMed:32267835). Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition (By similarity). Degradation of CDKN1B/p27kip also requires CKS1 (By similarity). Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, NBN, FOXO1, UBP43, YTHDF2, and probably MYC, TOB1 and TAL1 (PubMed:11931757, PubMed:12435635, PubMed:12769844, PubMed:12840033, PubMed:15342634, PubMed:15668399, PubMed:15949444, PubMed:16103164, PubMed:16581786, PubMed:16951159, PubMed:17908926, PubMed:17962192, PubMed:22464731, PubMed:32267835). Degradation of TAL1 also requires STUB1 (PubMed:17962192). Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2 (PubMed:9736735, PubMed:16262255). Promotes ubiquitination and destruction of CDH1 in a CK1-dependent manner, thereby regulating cell migration (PubMed:22770219). Following phosphorylation in response to DNA damage, mediates 'Lys-63'-linked ubiquitination of NBN, promoting ATM recruitment to DNA damage sites and DNA repair via homologous recombination (PubMed:22464731)

Protein Sequence

10 MHRKHLQEIP 20 DLSSNVATSF 30 TWGWDSSKTS 40 ELLSGMGVSA 50 LEKEEPDSEN 60 IPQELLSNLG 70 HPESPPRKRL 80 KSKGSDKDFV 90 IVRRPKLNRE 100 NFPGVSWDSL 110 PDELLLGIFS 120 CLCLPELLKV 130 SGVCKRWYRL 140 ASDESLWQTL 150 DLTGKNLHPD 160 VTGRLLSQGV 170 IAFRCPRSFM 180 DQPLAEHFSP 190 FRVQHMDLSN 200 SVIEVSTLHG 210 ILSQCSKLQN 220 LSLEGLRLSD 230 PIVNTLAKNS 240 NLVRLNLSGC 250 SGFSEFALQT 260 LLSSCSRLDE 270 LNLSWCFDFT 280 EKHVQVAVAH 290 VSETITQLNL 300 SGYRKNLQKS 310 DLSTLVRRCP 320 NLVHLDLSDS 330 VMLKNDCFQE 340 FFQLNYLQHL 350 SLSRCYDIIP 360 ETLLELGEIP 370 TLKTLQVFGI 380 VPDGTLQLLK 390 EALPHLQINC 400 SHFTTIARPT 410 IGNKKNQEIW 420 GIKCRLTLQK PSCL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0019005 SCF ubiquitin ligase complex
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:1990756 ubiquitin-like ligase-substrate adaptor activity
Biological Process GO:0051607 defense response to virus
Biological Process GO:0000082 G1/S transition of mitotic cell cycle
Biological Process GO:0045087 innate immune response
Biological Process GO:1905168 positive regulation of double-strand break repair via homologous recombination
Biological Process GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
Biological Process GO:0070936 protein K48-linked ubiquitination
Biological Process GO:0070534 protein K63-linked ubiquitination
Biological Process GO:0042981 regulation of apoptotic process
Biological Process GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process

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] 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.