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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

Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority if the nuclear volume (PubMed:10075938). Required for maintenance and establishment of the mitotic spindle poles during symmetric cell divisions, functioning as a tether linking bulk microtubules of the spindle to centrosomes (PubMed:7769006, PubMed:11956313, PubMed:26195665). Also required for proper alignment of the mitotic spindle during asymmetric cell divisions (PubMed:21816348).2 Publications5 Publications

GO - Molecular functioni

  • structural molecule activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

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
Short name:
NuMA protein1 Publication
Alternative name(s):
Nuclear matrix protein-22
Short name:
NMP-22
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 Numa-m :
  • 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 Numa-s :
  • 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
  • centrosome Source: UniProtKB
  • chromosome Source: UniProtKB-SubCell
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • dendrite Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • Golgi membrane Source: InterPro
  • mitotic spindle Source: UniProtKB
  • mitotic spindle astral microtubule Source: UniProtKB
  • mitotic spindle pole Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • spindle Source: ProtInc
  • spindle microtubule Source: UniProtKB
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, 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. 1 Publication1
Mutagenesisi2055T → A: Reduces association with the mitotic spindle and induces plasma membrane localization. 1 Publication1
Mutagenesisi2087S → A: Abolishes association with the mitotic spindle. 1 Publication1
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 residuei1187PhosphoserineCombined sources1
Modified residuei1225PhosphoserineCombined sources1
Modified residuei1511N6-acetyllysineCombined sources1
Modified residuei1601PhosphoserineCombined sources1
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 residuei1769PhosphoserineCombined sources1
Modified residuei1772PhosphoserineCombined sources1
Modified residuei1774PhosphotyrosineCombined sources1
Modified residuei1776PhosphothreonineCombined sources1
Modified residuei1788PhosphoserineCombined sources1
Modified residuei1789PhosphoserineCombined sources1
Modified residuei1792PhosphoserineCombined sources1
Modified residuei1800PhosphoserineCombined sources1
Modified residuei1804PhosphothreonineCombined sources1
Modified residuei1830PhosphoserineCombined sources1
Modified residuei1833PhosphoserineCombined sources1
Modified residuei1834PhosphoserineCombined sources1
Modified residuei1836PhosphotyrosineCombined sources1
Modified residuei1840PhosphoserineCombined sources1
Modified residuei1844Phosphoserine; alternateCombined sources1
Glycosylationi1844O-linked (GlcNAc); alternate1 Publication1
Modified residuei1862PhosphoserineCombined sources1
Modified residuei1887PhosphoserineCombined sources1
Modified residuei1969PhosphoserineCombined sources1
Modified residuei1991PhosphoserineCombined sources1
Modified residuei2000PhosphothreonineCombined sources1
Modified residuei2003PhosphoserineCombined sources1
Modified residuei2015Phosphothreonine; by CDK11 Publication1
Modified residuei2047PhosphoserineCombined sources1
Modified residuei2055Phosphothreonine; by CDK1Combined sources1 Publication1
Modified residuei2062PhosphoserineCombined sources1
Modified residuei2077PhosphoserineCombined sources1
Modified residuei2087Phosphoserine; by CDK11 Publication1
Modified residuei2106Phosphothreonine; by CDK1Combined sources1 Publication1

Post-translational modificationi

ADP-ribosylated by TNKS during mitosis.1 Publication
Phosphorylated in the C-terminal tail during mitosis, probably by CDK1. Phosphorylation increases solubility and promotes association with dynein and subsequent translocation to the spindle poles.1 Publication
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.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 and importin-beta.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Glycoprotein, Isopeptide bond, 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. 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). Interacts with tubulin and microtubules (PubMed:11956313). Interacts with TNKS (PubMed:16076287). Interacts with GPSM2 (via TPR repeats) (PubMed:21816348). Interacts with FAM175B and the BRISC complex (PubMed:26195665).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC57Q2TAC23EBI-521611,EBI-2808286
FLJ13057Q53SE73EBI-521611,EBI-10172181
GNAI1P630964EBI-521611,EBI-618639
GPSM2P812746EBI-521611,EBI-618655
TERF2IPQ9NYB02EBI-521611,EBI-750109

Protein-protein interaction databases

BioGridi110980. 104 interactors.
DIPiDIP-32937N.
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
Regioni1700 – 2115Tail (Globular)Add BLAST416
Regioni1866 – 1936Interaction with microtubules1 PublicationAdd BLAST71
Regioni1902 – 1920Interaction with GPSM21 PublicationAdd BLAST19

Coiled coil

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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1984 – 1989Nuclear localization signal1 Publication6

Domaini

The C-terminal tubulin-binding domain mediates direct binding to microtubules, independently of dynein and dynactin, and induces their bundling and stabilization.

Keywords - Domaini

Coiled coil

Phylogenomic databases

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

Family and domain databases

InterProiIPR026650. NUMA1.
[Graphical view]
PANTHERiPTHR18902:SF24. PTHR18902:SF24. 7 hits.

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 Numa-m (identifier: Q14980-3) [UniParc]FASTAAdd to basket
Also known as: 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 Numa-s (identifier: Q14980-4) [UniParc]FASTAAdd to basket
Also known as: 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 rs34239655dbSNPEnsembl.1
Natural variantiVAR_031680794A → G.Corresponds to variant rs3750913dbSNPEnsembl.1
Natural variantiVAR_0316811153E → D.Corresponds to variant rs34311364dbSNPEnsembl.1
Natural variantiVAR_0316821825V → M.Corresponds to variant rs7949430dbSNPEnsembl.1
Natural variantiVAR_0316831836Y → H.Corresponds to variant rs35586429dbSNPEnsembl.1
Natural variantiVAR_0512482049A → T.Corresponds to variant rs5743685dbSNPEnsembl.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 Numa-m. 1 PublicationAdd BLAST391
Alternative sequenceiVSP_0443791739 – 2115SKLPR…GKAKH → RSGGSLPPYVCLWSACCLSG CILVR in isoform Numa-s. 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

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

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...

Protein-protein interaction databases

BioGridi110980. 104 interactors.
DIPiDIP-32937N.
IntActiQ14980. 36 interactors.
MINTiMINT-1489811.
STRINGi9606.ENSP00000377298.

PTM databases

iPTMnetiQ14980.
PhosphoSitePlusiQ14980.
SwissPalmiQ14980.

Polymorphism and mutation databases

BioMutaiNUMA1.
DMDMi145559510.

Proteomic databases

EPDiQ14980.
MaxQBiQ14980.
PaxDbiQ14980.
PeptideAtlasiQ14980.
PRIDEiQ14980.

Protocols and materials databases

DNASUi4926.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi4926.
DisGeNETi4926.
GeneCardsiNUMA1.
H-InvDBHIX0026234.
HGNCiHGNC:8059. NUMA1.
HPAiHPA019841.
HPA019859.
HPA029912.
MalaCardsiNUMA1.
MIMi164009. gene.
neXtProtiNX_Q14980.
OpenTargetsiENSG00000137497.
Orphaneti520. Acute promyelocytic leukemia.
PharmGKBiPA31844.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiNUMA1. human.
GeneWikiiNuclear_mitotic_apparatus_protein_1.
GenomeRNAii4926.
PROiQ14980.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

InterProiIPR026650. NUMA1.
[Graphical view]
PANTHERiPTHR18902:SF24. PTHR18902:SF24. 7 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiNUMA1_HUMAN
AccessioniPrimary (citable) accession number: Q14980
Secondary accession number(s): H0YH75, Q14981, Q9BTE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: April 17, 2007
Last modified: November 2, 2016
This is version 152 of the entry and version 2 of the sequence. [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

Miscellaneous

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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.