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Protein

Nuclear mitotic apparatus protein 1

Gene

NUMA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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:7769006, PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074). 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:12445386, PubMed:11956313). 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:23027904, PubMed:22327364, 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:24996901, PubMed:24371089). Binds also to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24996901, PubMed:24371089). 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).By similarity2 Publications19 Publications

Miscellaneous

Also known as nuclear matrix protein-22/NMP-22/NMP22, an antigen used in diagnostic tests of bladder cancer.1 Publication

GO - Molecular functioni

  • disordered domain specific binding Source: CAFA
  • dynein complex binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule minus-end binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB
  • phosphatidylinositol binding Source: UniProtKB
  • protein C-terminus binding Source: CAFA
  • structural molecule activity Source: ProtInc
  • tubulin binding Source: UniProtKB

GO - Biological processi

  • anastral spindle assembly Source: UniProtKB
  • astral microtubule organization Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB-KW
  • establishment of mitotic spindle orientation Source: UniProtKB
  • lung epithelial cell differentiation Source: Ensembl
  • meiotic cell cycle Source: Ensembl
  • microtubule bundle formation Source: UniProtKB
  • nucleus organization Source: ProtInc
  • positive regulation of BMP signaling pathway Source: UniProtKB
  • positive regulation of chromosome segregation Source: UniProtKB
  • positive regulation of chromosome separation Source: UniProtKB
  • positive regulation of hair follicle development Source: UniProtKB
  • positive regulation of intracellular transport Source: UniProtKB
  • positive regulation of keratinocyte differentiation Source: UniProtKB
  • positive regulation of microtubule polymerization Source: UniProtKB
  • positive regulation of mitotic spindle elongation Source: UniProtKB
  • positive regulation of protein localization to cell cortex Source: UniProtKB
  • positive regulation of protein localization to spindle pole body Source: UniProtKB
  • positive regulation of spindle assembly Source: UniProtKB
  • regulation of metaphase plate congression Source: UniProtKB
  • regulation of mitotic spindle organization Source: UniProtKB

Keywordsi

Biological processCell cycle, Cell division, Chromosome partition, Mitosis
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
SIGNORiQ14980.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear mitotic apparatus protein 1Imported
Alternative name(s):
Nuclear matrix protein-221 Publication
Short name:
NMP-221 Publication
Nuclear mitotic apparatus protein2 Publications
Short name:
NuMA protein2 Publications
SP-H antigen1 Publication
Gene namesi
Name:NUMA1Imported
Synonyms:NMP221 Publication, NUMA1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8059. NUMA1.

Subcellular locationi

Isoform 3 :
  • Cytoplasmcytosol 1 Publication
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
  • Cytoplasmcytoskeletonspindle pole 1 Publication

  • Note: During interphase, mainly clustered at the centrosomal region in the cytosol. After entry into mitosis, detected at mitotic spindle poles.1 Publication
Isoform 4 :
  • Cytoplasmcytosol 1 Publication
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
  • Cytoplasmcytoskeletonspindle pole 1 Publication

  • Note: During interphase, mainly clustered at the centrosomal region in the cytosol. After entry into mitosis, detected at mitotic spindle poles.1 Publication

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • cell cortex Source: UniProtKB
  • cell cortex region Source: UniProtKB
  • centrosome Source: UniProtKB
  • chromosome Source: UniProtKB-SubCell
  • cortical microtubule Source: UniProtKB
  • cytoplasmic microtubule bundle Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extrinsic component of plasma membrane Source: UniProtKB
  • Golgi membrane Source: InterPro
  • microtubule bundle Source: UniProtKB
  • microtubule minus-end Source: UniProtKB
  • microtubule plus-end Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • mitotic spindle astral microtubule Source: UniProtKB
  • mitotic spindle midzone Source: UniProtKB
  • mitotic spindle pole Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nuclear matrix Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: CAFA
  • spindle Source: ProtInc
  • spindle microtubule Source: UniProtKB
  • spindle pole Source: UniProtKB
  • spindle pole centrosome Source: UniProtKB

Keywords - Cellular componenti

Cell membrane, Chromosome, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1910E → A: Abolishes interaction with GPSM2. 1 Publication1
Mutagenesisi1984R → G: No effect on nuclear localization. 1 Publication1
Mutagenesisi1988K → E: Abolishes nuclear localization. 1 Publication1
Mutagenesisi2015T → A: Abolishes association with the mitotic spindle. Increases premature accumulation at the cell cortex during metaphase; when associated with A-2055 and A-2087. 2 Publications1
Mutagenesisi2055T → A: Increases premature accumulation at the cell membrane of the polar cortical region in prophase and metaphase. Reduces association with the mitotic spindle. Increased randomization of spindle orientation. Increases premature accumulation at the cell cortex during metaphase; when associated with A-2015 and A-2087. 6 Publications1
Mutagenesisi2055T → D: Increases localization at the spindle poles. Decreases localization at the cell cortex. 1 Publication1
Mutagenesisi2055T → E: Absence of cell membrane association even in anaphase. Increased localization at spindle poles and chromosome congression defects. Does not localize to the cortex in either metaphase or anaphase. Increased randomization of spindle orientation. 2 Publications1
Mutagenesisi2087S → A: Abolishes association with the mitotic spindle. Increases premature accumulation at the cell cortex during metaphase; when associated with A-2015 and A-2055. 2 Publications1
Mutagenesisi2106T → A: Abolishes association with the mitotic spindle. 1 Publication1

Organism-specific databases

DisGeNETi4926.
MalaCardsiNUMA1.
OpenTargetsiENSG00000137497.
Orphaneti520. Acute promyelocytic leukemia.
PharmGKBiPA31844.

Polymorphism and mutation databases

BioMutaiNUMA1.
DMDMi145559510.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000579981 – 2115Nuclear mitotic apparatus protein 1Add BLAST2115

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei162PhosphoserineCombined sources1
Modified residuei163PhosphothreonineCombined sources1
Modified residuei169PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei211PhosphothreonineCombined sources1
Modified residuei271PhosphoserineCombined sources1
Modified residuei379N6-acetyllysineCombined sources1
Modified residuei388PhosphoserineCombined sources1
Modified residuei395PhosphoserineCombined sources1
Modified residuei820PhosphoserineCombined sources1
Modified residuei891N6-acetyllysineCombined sources1
Modified residuei1047Phosphothreonine; by PLK11 Publication1
Modified residuei1187PhosphoserineCombined sources1
Modified residuei1225PhosphoserineCombined sources1
Modified residuei1511N6-acetyllysineCombined sources1
Modified residuei1601PhosphoserineCombined sources1
Cross-linki1699Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1721PhosphoserineCombined sources1
Modified residuei1724PhosphoserineCombined sources1
Modified residuei1728PhosphoserineCombined sources1
Modified residuei1757PhosphoserineCombined sources1
Modified residuei1760PhosphoserineCombined sources1
Cross-linki1766Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1766Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1769Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei1772Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei1774PhosphotyrosineCombined sources1
Modified residuei1776PhosphothreonineCombined sources1
Modified residuei1788PhosphoserineCombined sources1
Modified residuei1789Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei1792PhosphoserineCombined sources1
Modified residuei1800PhosphoserineCombined sources1
Modified residuei1804PhosphothreonineCombined sources1
Cross-linki1822Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1830PhosphoserineCombined sources1
Modified residuei1833PhosphoserineCombined sources1
Modified residuei1834Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei1836PhosphotyrosineCombined sources1
Modified residuei1840PhosphoserineCombined sources1
Modified residuei1844Phosphoserine; alternateCombined sources1
Glycosylationi1844O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei1862PhosphoserineCombined sources1
Modified residuei1887PhosphoserineCombined sources1
Modified residuei1969PhosphoserineCombined sources1
Modified residuei1991PhosphoserineCombined sources1
Modified residuei2000PhosphothreonineCombined sources1
Modified residuei2003PhosphoserineCombined sources1
Modified residuei2015Phosphothreonine; by CDK12 Publications1
Modified residuei2047PhosphoserineCombined sources1
Modified residuei2055Phosphothreonine; by CDK1Combined sources2 Publications1
Modified residuei2062PhosphoserineCombined sources1
Modified residuei2077PhosphoserineCombined sources1
Modified residuei2087Phosphoserine; by CDK12 Publications1
Modified residuei2106Phosphothreonine; by CDK1Combined sources2 Publications1

Post-translational modificationi

Phosphorylation and dephosphorylation on Thr-2055 regulates the extent of cortical NUMA1 and the dynein-dynactin complex localization during mitotic metaphase and anaphase (PubMed:23921553). In metaphase, phosphorylation on Thr-2055 occurs in a kinase CDK1-dependent manner; this phosphorylation maintains low levels of cortical dynein-dynactin complex at metaphase, and hence proper spindle positioning (PubMed:7769006, PubMed:23921553, PubMed:24371089). In anaphase, dephosphorylated on Thr-2055 by phosphatase PPP2CA; this dephosphorylation stimulates its membrane association and with the dynein-dynactin complex its enrichment at the cell cortex, and hence robust spindle elongation (PubMed:23921553, PubMed:24371089). Probably also phosphorylated on Thr-2015 and Ser-2087 by CDK1; these phosphorylations may regulate its cell cortex recruitment during metaphase and anaphase (PubMed:23870127). Phosphorylated on Thr-1047, Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization (PubMed:22327364).5 Publications
ADP-ribosylated by TNKS at the onset of mitosis; ADP-ribosylation is not required for its localization to spindle poles (PubMed:16076287).1 Publication
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status (PubMed:20068230).1 Publication
Ubiquitinated with 'Lys-63'-linked polyubiquitin chains. Deubiquitination by the BRISC complex is important for the incorporation of NUMA1 into mitotic spindle poles and normal spindle pole function, probably by modulating interactions between NUMA1, dynein-dynactin complex and importin-beta.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Glycoprotein, Isopeptide bond, Lipoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14980.
MaxQBiQ14980.
PaxDbiQ14980.
PeptideAtlasiQ14980.
PRIDEiQ14980.

PTM databases

iPTMnetiQ14980.
PhosphoSitePlusiQ14980.
SwissPalmiQ14980.

Expressioni

Gene expression databases

BgeeiENSG00000137497.
CleanExiHS_NUMA1.
ExpressionAtlasiQ14980. baseline and differential.
GenevisibleiQ14980. HS.

Organism-specific databases

HPAiHPA019841.
HPA019859.
HPA029912.

Interactioni

Subunit structurei

Homodimer (PubMed:10075938). Also forms multiarm oligomers by association of C-terminal tail domains, oligomers may further assemble to form a hexagonal nuclear lattice-like network (PubMed:10075938). Associates with the dynein-dynactin complex; this association promotes the transport and accumulation of NUMA1 at the mitotic spindle poles that is inhibited by the BRISC complex in a PLK1-dependent manner (PubMed:10811826, PubMed:17172455, PubMed:23027904, PubMed:22327364, PubMed:26195665). Interacts (via C-terminus) with microtubules (MTs); this interaction is direct and promotes both MT bundle formation and stability in a dynein-dynactin complex- and CDK1-independent manner (PubMed:12445386, PubMed:11956313, PubMed:26765568). Interacts with EPB41 and EPB41L2; these interactions are negatively regulated by CDK1 during metaphase and are important for anaphase-specific localization of NUMA1 in symmetrically dividing cells (PubMed:23870127, PubMed:24996901). Interacts (via C-terminus) with GPSM2 (via TPR repeats); this interaction is direct, prevented by competitive binding of INSC, is inhibited in a PLK1-dependent manner, blocks the association of NUMA1 with MTs and inhibits NUMA1-induced MT bundle formation, prevents the association of NUMA1 with SPAG5, induces mitotic spindle pole localization of GPSM2, both metaphase cell cortex localization of NUMA1 and mitotic spindle organization (PubMed:11781568, PubMed:12445386, PubMed:22327364, PubMed:24109598, PubMed:27462074, PubMed:21816348). Does not interact with GPSM2 during anaphase (PubMed:23870127). Interacts (via C-terminus) with the nuclear importin alpha/importin beta receptor; this interaction is inhibited by RanGTP (PubMed:11163243). Interacts (via C-terminus) with KPNB1; this interaction is inhibited by RanGTP and the BRISC complex (PubMed:11229403, PubMed:26195665). Interacts with ABRAXAS2 and the BRISC complex; these interactions regulate mitotic spindle assembly (PubMed:26195665). Interacts (via N-terminal end of the coiled-coil domain) with RAE1; this interaction promotes mitotic spindle formation (PubMed:17172455). Interacts (via C-terminus) with SPAG5 (via C-terminus); this interaction promotes the recruitment of SPAG5 to the MTs at spindle poles in a dynein-dynactin-dependent manner and regulates mitotic spindle organization and proper chromosome alignment during mitosis (PubMed:27462074). Interacts with TNKS; this interaction occurs at the onset of mitosis (PubMed:12080061, PubMed:16076287). Interacts with TNKS2 (PubMed:12080061). Interacts with tubulin (PubMed:11956313).19 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • disordered domain specific binding Source: CAFA
  • dynein complex binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule minus-end binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB
  • protein C-terminus binding Source: CAFA
  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110980. 105 interactors.
DIPiDIP-32937N.
ELMiQ14980.
IntActiQ14980. 36 interactors.
MINTiMINT-1489811.
STRINGi9606.ENSP00000377298.

Structurei

Secondary structure

12115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni1917 – 1919Combined sources3
Helixi1920 – 1922Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RO2X-ray2.30B1899-1926[»]
ProteinModelPortaliQ14980.
SMRiQ14980.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 212Head (Globular)Add BLAST212
Regioni1699 – 1876Membrane-binding domain 11 PublicationAdd BLAST178
Regioni1700 – 2115Tail (Globular)Add BLAST416
Regioni1788 – 18104.1-binding domain2 PublicationsAdd BLAST23
Regioni1882 – 1985Tubulin-binding domain2 PublicationsAdd BLAST104
Regioni1892 – 1926GPSM2-binding domain4 PublicationsAdd BLAST35
Regioni1981 – 2060Membrane-binding domain 21 PublicationAdd BLAST80

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili213 – 1699Sequence analysisAdd BLAST1487

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1742 – 1748Tankyrase-binding domain1 Publication7
Motifi1984 – 1989Nuclear localization signal2 Publications6

Domaini

The C-terminal tubulin-binding domain mediates direct binding to microtubules, independently of dynein-dynactin complex, and induces their bundling and stabilization (PubMed:11956313). The 4.1-binding domain is necessary for its cortical stability and spindle orientation (PubMed:24109598).2 Publications

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFJ8. Eukaryota.
ENOG41125FF. LUCA.
GeneTreeiENSGT00730000111158.
HOGENOMiHOG000113889.
HOVERGENiHBG052694.
InParanoidiQ14980.
KOiK16808.
OMAiHLTAQVR.
OrthoDBiEOG091G00XV.
PhylomeDBiQ14980.
TreeFamiTF334442.

Family and domain databases

InterProiView protein in InterPro
IPR026650. NUMA1.
PANTHERiPTHR18902:SF28. PTHR18902:SF28. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14980-1) [UniParc]FASTAAdd to basket
Also known as: Numa-1, p230

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTLHATRGAA LLSWVNSLHV ADPVEAVLQL QDCSIFIKII DRIHGTEEGQ
60 70 80 90 100
QILKQPVSER LDFVCSFLQK NRKHPSSPEC LVSAQKVLEG SELELAKMTM
110 120 130 140 150
LLLYHSTMSS KSPRDWEQFE YKIQAELAVI LKFVLDHEDG LNLNEDLENF
160 170 180 190 200
LQKAPVPSTC SSTFPEELSP PSHQAKREIR FLELQKVASS SSGNNFLSGS
210 220 230 240 250
PASPMGDILQ TPQFQMRRLK KQLADERSNR DELELELAEN RKLLTEKDAQ
260 270 280 290 300
IAMMQQRIDR LALLNEKQAA SPLEPKELEE LRDKNESLTM RLHETLKQCQ
310 320 330 340 350
DLKTEKSQMD RKINQLSEEN GDLSFKLREF ASHLQQLQDA LNELTEEHSK
360 370 380 390 400
ATQEWLEKQA QLEKELSAAL QDKKCLEEKN EILQGKLSQL EEHLSQLQDN
410 420 430 440 450
PPQEKGEVLG DVLQLETLKQ EAATLAANNT QLQARVEMLE TERGQQEAKL
460 470 480 490 500
LAERGHFEEE KQQLSSLITD LQSSISNLSQ AKEELEQASQ AHGARLTAQV
510 520 530 540 550
ASLTSELTTL NATIQQQDQE LAGLKQQAKE KQAQLAQTLQ QQEQASQGLR
560 570 580 590 600
HQVEQLSSSL KQKEQQLKEV AEKQEATRQD HAQQLATAAE EREASLRERD
610 620 630 640 650
AALKQLEALE KEKAAKLEIL QQQLQVANEA RDSAQTSVTQ AQREKAELSR
660 670 680 690 700
KVEELQACVE TARQEQHEAQ AQVAELELQL RSEQQKATEK ERVAQEKDQL
710 720 730 740 750
QEQLQALKES LKVTKGSLEE EKRRAADALE EQQRCISELK AETRSLVEQH
760 770 780 790 800
KRERKELEEE RAGRKGLEAR LQQLGEAHQA ETEVLRRELA EAMAAQHTAE
810 820 830 840 850
SECEQLVKEV AAWRERYEDS QQEEAQYGAM FQEQLMTLKE ECEKARQELQ
860 870 880 890 900
EAKEKVAGIE SHSELQISRQ QNELAELHAN LARALQQVQE KEVRAQKLAD
910 920 930 940 950
DLSTLQEKMA ATSKEVARLE TLVRKAGEQQ ETASRELVKE PARAGDRQPE
960 970 980 990 1000
WLEEQQGRQF CSTQAALQAM EREAEQMGNE LERLRAALME SQGQQQEERG
1010 1020 1030 1040 1050
QQEREVARLT QERGRAQADL ALEKAARAEL EMRLQNALNE QRVEFATLQE
1060 1070 1080 1090 1100
ALAHALTEKE GKDQELAKLR GLEAAQIKEL EELRQTVKQL KEQLAKKEKE
1110 1120 1130 1140 1150
HASGSGAQSE AAGRTEPTGP KLEALRAEVS KLEQQCQKQQ EQADSLERSL
1160 1170 1180 1190 1200
EAERASRAER DSALETLQGQ LEEKAQELGH SQSALASAQR ELAAFRTKVQ
1210 1220 1230 1240 1250
DHSKAEDEWK AQVARGRQEA ERKNSLISSL EEEVSILNRQ VLEKEGESKE
1260 1270 1280 1290 1300
LKRLVMAESE KSQKLEERLR LLQAETASNS ARAAERSSAL REEVQSLREE
1310 1320 1330 1340 1350
AEKQRVASEN LRQELTSQAE RAEELGQELK AWQEKFFQKE QALSTLQLEH
1360 1370 1380 1390 1400
TSTQALVSEL LPAKHLCQQL QAEQAAAEKR HREELEQSKQ AAGGLRAELL
1410 1420 1430 1440 1450
RAQRELGELI PLRQKVAEQE RTAQQLRAEK ASYAEQLSML KKAHGLLAEE
1460 1470 1480 1490 1500
NRGLGERANL GRQFLEVELD QAREKYVQEL AAVRADAETR LAEVQREAQS
1510 1520 1530 1540 1550
TARELEVMTA KYEGAKVKVL EERQRFQEER QKLTAQVEQL EVFQREQTKQ
1560 1570 1580 1590 1600
VEELSKKLAD SDQASKVQQQ KLKAVQAQGG ESQQEAQRLQ AQLNELQAQL
1610 1620 1630 1640 1650
SQKEQAAEHY KLQMEKAKTH YDAKKQQNQE LQEQLRSLEQ LQKENKELRA
1660 1670 1680 1690 1700
EAERLGHELQ QAGLKTKEAE QTCRHLTAQV RSLEAQVAHA DQQLRDLGKF
1710 1720 1730 1740 1750
QVATDALKSR EPQAKPQLDL SIDSLDLSCE EGTPLSITSK LPRTQPDGTS
1760 1770 1780 1790 1800
VPGEPASPIS QRLPPKVESL ESLYFTPIPA RSQAPLESSL DSLGDVFLDS
1810 1820 1830 1840 1850
GRKTRSARRR TTQIINITMT KKLDVEEPDS ANSSFYSTRS APASQASLRA
1860 1870 1880 1890 1900
TSSTQSLARL GSPDYGNSAL LSLPGYRPTT RSSARRSQAG VSSGAPPGRN
1910 1920 1930 1940 1950
SFYMGTCQDE PEQLDDWNRI AELQQRNRVC PPHLKTCYPL ESRPSLSLGT
1960 1970 1980 1990 2000
ITDEEMKTGD PQETLRRASM QPIQIAEGTG ITTRQQRKRV SLEPHQGPGT
2010 2020 2030 2040 2050
PESKKATSCF PRPMTPRDRH EGRKQSTTEA QKKAAPASTK QADRRQSMAF
2060 2070 2080 2090 2100
SILNTPKKLG NSLLRRGASK KALSKASPNT RSGTRRSPRI ATTTASAATA
2110
AAIGATPRAK GKAKH
Length:2,115
Mass (Da):238,260
Last modified:April 17, 2007 - v2
Checksum:iDE734EC85B812CC7
GO
Isoform 2 (identifier: Q14980-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1536-1549: Missing.

Note: No experimental confirmation available.
Show »
Length:2,101
Mass (Da):236,516
Checksum:i18D8C4A34409ADE9
GO
Isoform 3 (identifier: Q14980-3) [UniParc]FASTAAdd to basket
Also known as: Numa-m1 Publication, p195

The sequence of this isoform differs from the canonical sequence as follows:
     1725-2115: LDLSCEEGTP...TPRAKGKAKH → SQANSSQTPR...ALSLPCLLFS

Show »
Length:1,776
Mass (Da):201,453
Checksum:i4CCE2F79A2228DCD
GO
Isoform 4 (identifier: Q14980-4) [UniParc]FASTAAdd to basket
Also known as: Numa-s1 Publication, p194

The sequence of this isoform differs from the canonical sequence as follows:
     1739-2115: SKLPRTQPDG...TPRAKGKAKH → RSGGSLPPYVCLWSACCLSGCILVR

Show »
Length:1,763
Mass (Da):200,097
Checksum:iB288C63D156E3E18
GO
Isoform 5 (identifier: Q14980-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     414-1549: Missing.

Note: No experimental confirmation available.
Show »
Length:979
Mass (Da):109,279
Checksum:iA1371283C8D14140
GO

Sequence cautioni

The sequence CAA77670 differs from that shown. Reason: Frameshift at positions 1270 and 1299.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti772Q → L in CAA77670 (PubMed:1541636).Curated1
Sequence conflicti815 – 816ER → DG in CAA77670 (PubMed:1541636).Curated2
Sequence conflicti873E → K in CAA77670 (PubMed:1541636).Curated1
Sequence conflicti1589L → F in CAA77670 (PubMed:1541636).Curated1
Sequence conflicti1637S → T in Z14227 (PubMed:8408288).Curated1
Sequence conflicti1637S → T in Z14228 (PubMed:8408288).Curated1
Sequence conflicti1682S → T in Z14227 (PubMed:8408288).Curated1
Sequence conflicti1682S → T in Z14228 (PubMed:8408288).Curated1
Sequence conflicti1798L → Q in CAA77669 (PubMed:8408288).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031679242K → R. Corresponds to variant dbSNP:rs34239655Ensembl.1
Natural variantiVAR_031680794A → G. Corresponds to variant dbSNP:rs3750913Ensembl.1
Natural variantiVAR_0316811153E → D. Corresponds to variant dbSNP:rs34311364Ensembl.1
Natural variantiVAR_0316821825V → M. Corresponds to variant dbSNP:rs7949430Ensembl.1
Natural variantiVAR_0316831836Y → H. Corresponds to variant dbSNP:rs35586429Ensembl.1
Natural variantiVAR_0512482049A → T. Corresponds to variant dbSNP:rs5743685Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054146414 – 1549Missing in isoform 5. 1 PublicationAdd BLAST1136
Alternative sequenceiVSP_0129101536 – 1549Missing in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_0443781725 – 2115LDLSC…GKAKH → SQANSSQTPRDSDACPHPGL VPGPSLAPSRSWPRGPGAWT VWALSLPCLLFS in isoform 3. 1 PublicationAdd BLAST391
Alternative sequenceiVSP_0443791739 – 2115SKLPR…GKAKH → RSGGSLPPYVCLWSACCLSG CILVR in isoform 4. 1 PublicationAdd BLAST377

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14227 mRNA. No translation available.
Z14228 mRNA. No translation available.
Z14229 mRNA. No translation available.
Z11583 mRNA. Translation: CAA77669.1.
Z11584 mRNA. Translation: CAA77670.1. Frameshift.
AP002490 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74826.1.
BC004165 mRNA. Translation: AAH04165.1.
CCDSiCCDS31633.1. [Q14980-1]
CCDS66156.1. [Q14980-2]
PIRiA42184.
RefSeqiNP_001273490.1. NM_001286561.1. [Q14980-2]
NP_006176.2. NM_006185.3. [Q14980-1]
XP_006718627.1. XM_006718564.1. [Q14980-1]
UniGeneiHs.325978.
Hs.591967.

Genome annotation databases

EnsembliENST00000351960; ENSP00000260051; ENSG00000137497. [Q14980-5]
ENST00000358965; ENSP00000351851; ENSG00000137497. [Q14980-2]
ENST00000393695; ENSP00000377298; ENSG00000137497. [Q14980-1]
ENST00000613205; ENSP00000480172; ENSG00000137497. [Q14980-5]
ENST00000620566; ENSP00000478624; ENSG00000137497. [Q14980-2]
GeneIDi4926.
KEGGihsa:4926.
UCSCiuc001ork.3. human. [Q14980-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiNUMA1_HUMAN
AccessioniPrimary (citable) accession number: Q14980
Secondary accession number(s): H0YH75, Q14981, Q9BTE9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: April 17, 2007
Last modified: August 30, 2017
This is version 160 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references