Search Results

Overview

Uniprot IDQ14980
Protein NameNuclear mitotic apparatus protein 1
Gene NameNUMA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1442 EQLSMLKKAHGLLAE
1511 ELEVMTAKYEGAKVK
1571 ASKVQQQKLKAVQAQ
1573 KVQQQKLKAVQAQGG
1699 QQLRDLGKFQVATDA
1708 QVATDALKSREPQAK
1935 RVCPPHLKTCYPLES
2004 GPGTPESKKATSCFP
2005 PGTPESKKATSCFPR
2058 SILNTPKKLGNSLLR
2075 ASKKALSKASPNTRS
267 RLALLNEKQAASPLE
939 TASRELVKEPARAGD

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)

Protein Sequence

10 MTLHATRGAA 20 LLSWVNSLHV 30 ADPVEAVLQL 40 QDCSIFIKII 50 DRIHGTEEGQ 60 QILKQPVSER 70 LDFVCSFLQK 80 NRKHPSSPEC 90 LVSAQKVLEG 100 SELELAKMTM 110 LLLYHSTMSS 120 KSPRDWEQFE 130 YKIQAELAVI 140 LKFVLDHEDG 150 LNLNEDLENF 160 LQKAPVPSTC 170 SSTFPEELSP 180 PSHQAKREIR 190 FLELQKVASS 200 SSGNNFLSGS 210 PASPMGDILQ 220 TPQFQMRRLK 230 KQLADERSNR 240 DELELELAEN 250 RKLLTEKDAQ 260 IAMMQQRIDR 270 LALLNEKQAA 280 SPLEPKELEE 290 LRDKNESLTM 300 RLHETLKQCQ 310 DLKTEKSQMD 320 RKINQLSEEN 330 GDLSFKLREF 340 ASHLQQLQDA 350 LNELTEEHSK 360 ATQEWLEKQA 370 QLEKELSAAL 380 QDKKCLEEKN 390 EILQGKLSQL 400 EEHLSQLQDN 410 PPQEKGEVLG 420 DVLQLETLKQ 430 EAATLAANNT 440 QLQARVEMLE 450 TERGQQEAKL 460 LAERGHFEEE 470 KQQLSSLITD 480 LQSSISNLSQ 490 AKEELEQASQ 500 AHGARLTAQV 510 ASLTSELTTL 520 NATIQQQDQE 530 LAGLKQQAKE 540 KQAQLAQTLQ 550 QQEQASQGLR 560 HQVEQLSSSL 570 KQKEQQLKEV 580 AEKQEATRQD 590 HAQQLATAAE 600 EREASLRERD 610 AALKQLEALE 620 KEKAAKLEIL 630 QQQLQVANEA 640 RDSAQTSVTQ 650 AQREKAELSR 660 KVEELQACVE 670 TARQEQHEAQ 680 AQVAELELQL 690 RSEQQKATEK 700 ERVAQEKDQL 710 QEQLQALKES 720 LKVTKGSLEE 730 EKRRAADALE 740 EQQRCISELK 750 AETRSLVEQH 760 KRERKELEEE 770 RAGRKGLEAR 780 LQQLGEAHQA 790 ETEVLRRELA 800 EAMAAQHTAE 810 SECEQLVKEV 820 AAWRERYEDS 830 QQEEAQYGAM 840 FQEQLMTLKE 850 ECEKARQELQ 860 EAKEKVAGIE 870 SHSELQISRQ 880 QNELAELHAN 890 LARALQQVQE 900 KEVRAQKLAD 910 DLSTLQEKMA 920 ATSKEVARLE 930 TLVRKAGEQQ 940 ETASRELVKE 950 PARAGDRQPE 960 WLEEQQGRQF 970 CSTQAALQAM 980 EREAEQMGNE 990 LERLRAALME 1000 SQGQQQEERG 1010 QQEREVARLT 1020 QERGRAQADL 1030 ALEKAARAEL 1040 EMRLQNALNE 1050 QRVEFATLQE 1060 ALAHALTEKE 1070 GKDQELAKLR 1080 GLEAAQIKEL 1090 EELRQTVKQL 1100 KEQLAKKEKE 1110 HASGSGAQSE 1120 AAGRTEPTGP 1130 KLEALRAEVS 1140 KLEQQCQKQQ 1150 EQADSLERSL 1160 EAERASRAER 1170 DSALETLQGQ 1180 LEEKAQELGH 1190 SQSALASAQR 1200 ELAAFRTKVQ 1210 DHSKAEDEWK 1220 AQVARGRQEA 1230 ERKNSLISSL 1240 EEEVSILNRQ 1250 VLEKEGESKE 1260 LKRLVMAESE 1270 KSQKLEERLR 1280 LLQAETASNS 1290 ARAAERSSAL 1300 REEVQSLREE 1310 AEKQRVASEN 1320 LRQELTSQAE 1330 RAEELGQELK 1340 AWQEKFFQKE 1350 QALSTLQLEH 1360 TSTQALVSEL 1370 LPAKHLCQQL 1380 QAEQAAAEKR 1390 HREELEQSKQ 1400 AAGGLRAELL 1410 RAQRELGELI 1420 PLRQKVAEQE 1430 RTAQQLRAEK 1440 ASYAEQLSML 1450 KKAHGLLAEE 1460 NRGLGERANL 1470 GRQFLEVELD 1480 QAREKYVQEL 1490 AAVRADAETR 1500 LAEVQREAQS 1510 TARELEVMTA 1520 KYEGAKVKVL 1530 EERQRFQEER 1540 QKLTAQVEQL 1550 EVFQREQTKQ 1560 VEELSKKLAD 1570 SDQASKVQQQ 1580 KLKAVQAQGG 1590 ESQQEAQRLQ 1600 AQLNELQAQL 1610 SQKEQAAEHY 1620 KLQMEKAKTH 1630 YDAKKQQNQE 1640 LQEQLRSLEQ 1650 LQKENKELRA 1660 EAERLGHELQ 1670 QAGLKTKEAE 1680 QTCRHLTAQV 1690 RSLEAQVAHA 1700 DQQLRDLGKF 1710 QVATDALKSR 1720 EPQAKPQLDL 1730 SIDSLDLSCE 1740 EGTPLSITSK 1750 LPRTQPDGTS 1760 VPGEPASPIS 1770 QRLPPKVESL 1780 ESLYFTPIPA 1790 RSQAPLESSL 1800 DSLGDVFLDS 1810 GRKTRSARRR 1820 TTQIINITMT 1830 KKLDVEEPDS 1840 ANSSFYSTRS 1850 APASQASLRA 1860 TSSTQSLARL 1870 GSPDYGNSAL 1880 LSLPGYRPTT 1890 RSSARRSQAG 1900 VSSGAPPGRN 1910 SFYMGTCQDE 1920 PEQLDDWNRI 1930 AELQQRNRVC 1940 PPHLKTCYPL 1950 ESRPSLSLGT 1960 ITDEEMKTGD 1970 PQETLRRASM 1980 QPIQIAEGTG 1990 ITTRQQRKRV 2000 SLEPHQGPGT 2010 PESKKATSCF 2020 PRPMTPRDRH 2030 EGRKQSTTEA 2040 QKKAAPASTK 2050 QADRRQSMAF 2060 SILNTPKKLG 2070 NSLLRRGASK 2080 KALSKASPNT 2090 RSGTRRSPRI 2100 ATTTASAATA 2110 AAIGATPRAK GKAKH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005938 cell cortex
Molecular Function GO:0070840 dynein complex binding
Molecular Function GO:0008017 microtubule binding
Molecular Function GO:0051011 microtubule minus-end binding
Molecular Function GO:0051010 microtubule plus-end binding
Molecular Function GO:0035091 phosphatidylinositol binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0005198 structural molecule activity
Molecular Function GO:0015631 tubulin binding
Biological Process GO:0055048 anastral spindle assembly
Biological Process GO:0030953 astral microtubule organization
Biological Process GO:0051301 cell division
Biological Process GO:0000132 establishment of mitotic spindle orientation
Biological Process GO:0051321 meiotic cell cycle
Biological Process GO:0001578 microtubule bundle formation
Biological Process GO:0006997 nucleus organization
Biological Process GO:0030513 positive regulation of BMP signaling pathway
Biological Process GO:0051984 positive regulation of chromosome segregation
Biological Process GO:1905820 positive regulation of chromosome separation
Biological Process GO:0051798 positive regulation of hair follicle development
Biological Process GO:0032388 positive regulation of intracellular transport
Biological Process GO:0045618 positive regulation of keratinocyte differentiation
Biological Process GO:0031116 positive regulation of microtubule polymerization
Biological Process GO:1902846 positive regulation of mitotic spindle elongation
Biological Process GO:1904778 positive regulation of protein localization to cell cortex
Biological Process GO:1902365 positive regulation of protein localization to spindle pole body
Biological Process GO:1905832 positive regulation of spindle assembly
Biological Process GO:0090235 regulation of metaphase plate congression
Biological Process GO:0060236 regulation of mitotic spindle organization
Cellular Component GO:0099738 cell cortex region
Cellular Component GO:0005813 centrosome
Cellular Component GO:0005694 chromosome
Cellular Component GO:0055028 cortical microtubule
Cellular Component GO:1905720 cytoplasmic microtubule bundle
Cellular Component GO:0005829 cytosol
Cellular Component GO:0030425 dendrite
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0097575 lateral cell cortex
Cellular Component GO:0016328 lateral plasma membrane
Cellular Component GO:0097427 microtubule bundle
Cellular Component GO:0036449 microtubule minus-end
Cellular Component GO:0035371 microtubule plus-end
Cellular Component GO:0072686 mitotic spindle
Cellular Component GO:0061673 mitotic spindle astral microtubule
Cellular Component GO:1990023 mitotic spindle midzone
Cellular Component GO:0097431 mitotic spindle pole
Cellular Component GO:0043025 neuronal cell body
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0005819 spindle
Cellular Component GO:0005876 spindle microtubule
Cellular Component GO:0000922 spindle pole
Cellular Component GO:0031616 spindle pole centrosome
Molecular Function GO:0097718 disordered domain specific binding

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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.