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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Proliferation marker protein Ki-67

UniprotKB/SwissProt ID: P46013 (P46013)

Gene Name: MKI67

Organism: Homo sapiens (Human)

Function: Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Chromosome. Nucleus. Nucleus, nucleolus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR000253 FHA_dom
IPR012568 KI67R
IPR029334 PP1-bd
IPR008984 SMAD_FHA_dom_sf

The S-nitrosylation sites of P46013

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1007 SEKGKITKMP C QSLQPEPINT   
2 1251 VAAGKTTKIP C DSPQSDPVDT   
3 1285 KADVEGELLA C RNLMPSAGKA   
4 1373 VAAGKTTKMP C ESSPPESADT   
5 1479 GLKELFQTPV C TDKPTTHEKT   
6 1843 TGFRELFQTP C TDNPTTDEKT   
7 1981 MTDDKITEVS C KSPQPDPVKT   
8 2206 GLKELFQTPI C TDKPTTHEKT   
9 226 GELKSVPTTQ C LDNSKKNESP   
10 2464 MTDDKITEVS C KSPQPESFKT   
11 2706 LTAGKATKIP C ESPPLEVVDT   
12 3014 GSVTGTKRLR C MPAPEEIVEE   
13 3199 KGEAGNSDSM C LRSRKTKSQP   
14 3229 VQRVTRSVKR C AENPKKAEDN   
15 824 QNAAKQPSDK C SASPPLRRQC   
16 903 SEETNTEIVE C ILKRGQKATL   
17 958 MKRSRTWGQK C APMSDLTDLK