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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: Nuclear mitotic apparatus protein 1

UniprotKB/SwissProt ID: Q14980 (Q14980)

Gene Name: NUMA1

Organism: Homo sapiens (Human)

Function: Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Nucleus, nucleoplasm. Nucleus matrix. Chromosome. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cell cortex. Cell membrane. Lateral cell membrane. Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR051841 MT-Golgi_org_protein
IPR048726 NuMA_LGNBD
IPR048724 NuMA_N_HOOK

The S-nitrosylation sites of Q14980

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1367 VSELLPAKHL C QQLQAEQAAA  CCCCCHHHHH H HHHHHHCCCC  2.13%
2 160 FLQKAPVPST C SSTFPEELSP  CCCCCHHHHH H HHHHHHCCCC  3.38%
3 1907 PGRNSFYMGT C QDEPEQLDDW  CCCCCHHHHH H HHHHHHCCCC  3.88%
4 375 ELSAALQDKK C LEEKNEILQG  CCCCCHHHHH H HHHHHHCCCC  7.72%
5 65 QPVSERLDFV C SFLQKNRKHP  CCCCCHHHHH H HHHHHHCCCC  2.1%
6 80 KNRKHPSSPE C LVSAQKVLEG  CCCCCHHHHH H HHHHHHCCCC  5.3% 22178444
7 961 WLEEQQGRQF C STQAALQAME  CCCCCHHHHH H HHHHHHCCCC  3.05%