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Q14980 (NUMA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear mitotic apparatus protein 1

Short name=NuMA protein
Alternative name(s):
SP-H antigen
Gene names
Name:NUMA1
Synonyms:NUMA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2115 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority if the nuclear volume. Required for maintenance and establishment of the mitotic spindle poles, functionning as a tether linking bulk microtubules of the spindle to centrosomes. May be involved in coordination of the alignment of the mitotic spindle to the cellular polarity axis, which is a prerequisite for asymmetric cell divisions. Ref.21

Subunit structure

Homodimer. Also forms multiarm oligomers by association of C-terminal tail domains, oligomers may further assemble to form a hexagonal nuclear lattice-like network. Interacts with TNKS. Ref.10 Ref.11 Ref.30

Subcellular location

Nucleus matrix. Chromosome. Cytoplasmcytoskeletonspindle pole. Note: Resides in the nuclear matrix during interphases. Dissociates from condensing chromosomes during early prophase, and relocates to the spindle poles via dynein/dynamin association, it remain there until the anaphase onset. Before the complete disintegration of the nuclear lamina. As mitosis progresses it reassociates with telophase chromosomes very early during nuclear reformation, before substantial accumulation of lamins on chromosomal surfaces is evident. Ref.1 Ref.8 Ref.11

Isoform Numa-m: Cytoplasm. Note: Mainly clustered at the centrosomal region. Ref.1 Ref.8 Ref.11

Isoform Numa-s: Cytoplasm. Note: Mainly clustered at the centrosomal region. Ref.1 Ref.8 Ref.11

Domain

The C-terminal tubulin-binding domain mediates direct binding to microtubules, independantly of dynein and dynactin, and induces their bundling and stabilization. Ref.10

Post-translational modification

ADP-ribosylated by TNKS during mitosis.

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. Ref.9

O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status. Ref.24

Sequence caution

The sequence CAA77670.1 differs from that shown. Reason: Frameshift at positions 1270 and 1299.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentChromosome
Cytoplasm
Cytoskeleton
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMAcetylation
ADP-ribosylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

establishment of mitotic spindle orientation

Inferred from electronic annotation. Source: Ensembl

lung epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

meiotic cell cycle

Inferred from electronic annotation. Source: Ensembl

mitotic anaphase

Traceable author statement Ref.2. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus organization

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

chromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

dendrite

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

spindle

Traceable author statement PubMed 7004645. Source: ProtInc

spindle microtubule

Traceable author statement Ref.2. Source: ProtInc

spindle pole

Inferred from direct assay PubMed 14718566. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 15537540. Source: IntAct

structural molecule activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GNAI1P630964EBI-521611,EBI-618639
GPSM2P812746EBI-521611,EBI-618655

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14980-1)

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.
Isoform 2 (identifier: Q14980-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1536-1549: Missing.
Note: No experimental confirmation available.
Isoform Numa-m (identifier: Q14980-3)

Also known as: p195;

The sequence of this isoform differs from the canonical sequence as follows:
     1725-2115: LDLSCEEGTP...TPRAKGKAKH → SQANSSQTPR...ALSLPCLLFS
Isoform Numa-s (identifier: Q14980-4)

Also known as: p194;

The sequence of this isoform differs from the canonical sequence as follows:
     1739-2115: SKLPRTQPDG...TPRAKGKAKH → RSGGSLPPYVCLWSACCLSGCILVR
Isoform 5 (identifier: Q14980-5)

The sequence of this isoform differs from the canonical sequence as follows:
     414-1549: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21152115Nuclear mitotic apparatus protein 1
PRO_0000057998

Regions

Region1 – 212212Head (Globular)
Region1700 – 2115416Tail (Globular)
Region1866 – 193671Interaction with microtubules
Coiled coil213 – 16991487 Potential
Motif1984 – 19896Nuclear localization signal Ref.8

Amino acid modifications

Modified residue1691Phosphoserine Ref.19 Ref.25
Modified residue2031Phosphoserine Ref.19 Ref.22 Ref.25
Modified residue2111Phosphothreonine Ref.19 Ref.25
Modified residue2711Phosphoserine Ref.25
Modified residue3791N6-acetyllysine Ref.23
Modified residue3881Phosphoserine Ref.16
Modified residue3951Phosphoserine Ref.16
Modified residue8201Phosphoserine Ref.16
Modified residue8911N6-acetyllysine Ref.23
Modified residue11871Phosphoserine Ref.25
Modified residue12251Phosphoserine Ref.22 Ref.25
Modified residue15111N6-acetyllysine Ref.23
Modified residue16011Phosphoserine Ref.16
Modified residue17211Phosphoserine Ref.19
Modified residue17241Phosphoserine Ref.19
Modified residue17281Phosphoserine Ref.19
Modified residue17571Phosphoserine Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.25 Ref.28
Modified residue17601Phosphoserine Ref.16
Modified residue17691Phosphoserine Ref.14 Ref.19 Ref.22 Ref.25
Modified residue17721Phosphoserine Ref.19
Modified residue17741Phosphotyrosine Ref.19
Modified residue17761Phosphothreonine Ref.14 Ref.19 Ref.22
Modified residue17881Phosphoserine Ref.19 Ref.22
Modified residue17891Phosphoserine Ref.19
Modified residue17921Phosphoserine Ref.19
Modified residue18001Phosphoserine Ref.19 Ref.22
Modified residue18041Phosphothreonine Ref.19
Modified residue18301Phosphoserine Ref.19 Ref.25
Modified residue18331Phosphoserine Ref.19
Modified residue18341Phosphoserine Ref.19
Modified residue18361Phosphotyrosine Ref.19
Modified residue18401Phosphoserine Ref.14 Ref.19
Modified residue18621Phosphoserine Ref.19 Ref.25
Modified residue18871Phosphoserine Ref.19
Modified residue19691Phosphoserine Ref.19 Ref.25
Modified residue19911Phosphoserine Ref.19 Ref.25
Modified residue20001Phosphothreonine Ref.19 Ref.25
Modified residue20031Phosphoserine Ref.25
Modified residue20151Phosphothreonine; by CDK1 Ref.9
Modified residue20551Phosphothreonine; by CDK1 Ref.9
Modified residue20771Phosphoserine Ref.15
Modified residue20871Phosphoserine; by CDK1 Ref.9
Modified residue21061Phosphothreonine; by CDK1 Ref.9 Ref.14
Glycosylation18441O-linked (GlcNAc) Ref.24

Natural variations

Alternative sequence414 – 15491136Missing in isoform 5.
VSP_054146
Alternative sequence1536 – 154914Missing in isoform 2.
VSP_012910
Alternative sequence1725 – 2115391LDLSC…GKAKH → SQANSSQTPRDSDACPHPGL VPGPSLAPSRSWPRGPGAWT VWALSLPCLLFS in isoform Numa-m.
VSP_044378
Alternative sequence1739 – 2115377SKLPR…GKAKH → RSGGSLPPYVCLWSACCLSG CILVR in isoform Numa-s.
VSP_044379
Natural variant2421K → R.
Corresponds to variant rs34239655 [ dbSNP | Ensembl ].
VAR_031679
Natural variant7941A → G.
Corresponds to variant rs3750913 [ dbSNP | Ensembl ].
VAR_031680
Natural variant11531E → D.
Corresponds to variant rs34311364 [ dbSNP | Ensembl ].
VAR_031681
Natural variant18251V → M.
Corresponds to variant rs7949430 [ dbSNP | Ensembl ].
VAR_031682
Natural variant18361Y → H.
Corresponds to variant rs35586429 [ dbSNP | Ensembl ].
VAR_031683
Natural variant20491A → T.
Corresponds to variant rs5743685 [ dbSNP | Ensembl ].
VAR_051248

Experimental info

Mutagenesis19841R → G: No effect on nuclear localization. Ref.8
Mutagenesis19881K → E: Abolishes nuclear localization. Ref.8
Mutagenesis20151T → A: Abolishes association with the mitotic spindle. Ref.9
Mutagenesis20551T → A: Reduces association with the mitotic spindle and induces plasma membrane localization. Ref.9
Mutagenesis20871S → A: Abolishes association with the mitotic spindle. Ref.9
Mutagenesis21061T → A: Abolishes association with the mitotic spindle. Ref.9
Sequence conflict7721Q → L in CAA77670. Ref.2
Sequence conflict815 – 8162ER → DG in CAA77670. Ref.2
Sequence conflict8731E → K in CAA77670. Ref.2
Sequence conflict15891L → F in CAA77670. Ref.2
Sequence conflict16371S → T in Z14227. Ref.3
Sequence conflict16371S → T in Z14228. Ref.3
Sequence conflict16821S → T in Z14227. Ref.3
Sequence conflict16821S → T in Z14228. Ref.3
Sequence conflict17981L → Q in CAA77669. Ref.3

Secondary structure

.... 2115
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Numa-1) (p230) [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: DE734EC85B812CC7

FASTA2,115238,260
        10         20         30         40         50         60 
MTLHATRGAA LLSWVNSLHV ADPVEAVLQL QDCSIFIKII DRIHGTEEGQ QILKQPVSER 

        70         80         90        100        110        120 
LDFVCSFLQK NRKHPSSPEC LVSAQKVLEG SELELAKMTM LLLYHSTMSS KSPRDWEQFE 

       130        140        150        160        170        180 
YKIQAELAVI LKFVLDHEDG LNLNEDLENF LQKAPVPSTC SSTFPEELSP PSHQAKREIR 

       190        200        210        220        230        240 
FLELQKVASS SSGNNFLSGS PASPMGDILQ TPQFQMRRLK KQLADERSNR DELELELAEN 

       250        260        270        280        290        300 
RKLLTEKDAQ IAMMQQRIDR LALLNEKQAA SPLEPKELEE LRDKNESLTM RLHETLKQCQ 

       310        320        330        340        350        360 
DLKTEKSQMD RKINQLSEEN GDLSFKLREF ASHLQQLQDA LNELTEEHSK ATQEWLEKQA 

       370        380        390        400        410        420 
QLEKELSAAL QDKKCLEEKN EILQGKLSQL EEHLSQLQDN PPQEKGEVLG DVLQLETLKQ 

       430        440        450        460        470        480 
EAATLAANNT QLQARVEMLE TERGQQEAKL LAERGHFEEE KQQLSSLITD LQSSISNLSQ 

       490        500        510        520        530        540 
AKEELEQASQ AHGARLTAQV ASLTSELTTL NATIQQQDQE LAGLKQQAKE KQAQLAQTLQ 

       550        560        570        580        590        600 
QQEQASQGLR HQVEQLSSSL KQKEQQLKEV AEKQEATRQD HAQQLATAAE EREASLRERD 

       610        620        630        640        650        660 
AALKQLEALE KEKAAKLEIL QQQLQVANEA RDSAQTSVTQ AQREKAELSR KVEELQACVE 

       670        680        690        700        710        720 
TARQEQHEAQ AQVAELELQL RSEQQKATEK ERVAQEKDQL QEQLQALKES LKVTKGSLEE 

       730        740        750        760        770        780 
EKRRAADALE EQQRCISELK AETRSLVEQH KRERKELEEE RAGRKGLEAR LQQLGEAHQA 

       790        800        810        820        830        840 
ETEVLRRELA EAMAAQHTAE SECEQLVKEV AAWRERYEDS QQEEAQYGAM FQEQLMTLKE 

       850        860        870        880        890        900 
ECEKARQELQ EAKEKVAGIE SHSELQISRQ QNELAELHAN LARALQQVQE KEVRAQKLAD 

       910        920        930        940        950        960 
DLSTLQEKMA ATSKEVARLE TLVRKAGEQQ ETASRELVKE PARAGDRQPE WLEEQQGRQF 

       970        980        990       1000       1010       1020 
CSTQAALQAM EREAEQMGNE LERLRAALME SQGQQQEERG QQEREVARLT QERGRAQADL 

      1030       1040       1050       1060       1070       1080 
ALEKAARAEL EMRLQNALNE QRVEFATLQE ALAHALTEKE GKDQELAKLR GLEAAQIKEL 

      1090       1100       1110       1120       1130       1140 
EELRQTVKQL KEQLAKKEKE HASGSGAQSE AAGRTEPTGP KLEALRAEVS KLEQQCQKQQ 

      1150       1160       1170       1180       1190       1200 
EQADSLERSL EAERASRAER DSALETLQGQ LEEKAQELGH SQSALASAQR ELAAFRTKVQ 

      1210       1220       1230       1240       1250       1260 
DHSKAEDEWK AQVARGRQEA ERKNSLISSL EEEVSILNRQ VLEKEGESKE LKRLVMAESE 

      1270       1280       1290       1300       1310       1320 
KSQKLEERLR LLQAETASNS ARAAERSSAL REEVQSLREE AEKQRVASEN LRQELTSQAE 

      1330       1340       1350       1360       1370       1380 
RAEELGQELK AWQEKFFQKE QALSTLQLEH TSTQALVSEL LPAKHLCQQL QAEQAAAEKR 

      1390       1400       1410       1420       1430       1440 
HREELEQSKQ AAGGLRAELL RAQRELGELI PLRQKVAEQE RTAQQLRAEK ASYAEQLSML 

      1450       1460       1470       1480       1490       1500 
KKAHGLLAEE NRGLGERANL GRQFLEVELD QAREKYVQEL AAVRADAETR LAEVQREAQS 

      1510       1520       1530       1540       1550       1560 
TARELEVMTA KYEGAKVKVL EERQRFQEER QKLTAQVEQL EVFQREQTKQ VEELSKKLAD 

      1570       1580       1590       1600       1610       1620 
SDQASKVQQQ KLKAVQAQGG ESQQEAQRLQ AQLNELQAQL SQKEQAAEHY KLQMEKAKTH 

      1630       1640       1650       1660       1670       1680 
YDAKKQQNQE LQEQLRSLEQ LQKENKELRA EAERLGHELQ QAGLKTKEAE QTCRHLTAQV 

      1690       1700       1710       1720       1730       1740 
RSLEAQVAHA DQQLRDLGKF QVATDALKSR EPQAKPQLDL SIDSLDLSCE EGTPLSITSK 

      1750       1760       1770       1780       1790       1800 
LPRTQPDGTS VPGEPASPIS QRLPPKVESL ESLYFTPIPA RSQAPLESSL DSLGDVFLDS 

      1810       1820       1830       1840       1850       1860 
GRKTRSARRR TTQIINITMT KKLDVEEPDS ANSSFYSTRS APASQASLRA TSSTQSLARL 

      1870       1880       1890       1900       1910       1920 
GSPDYGNSAL LSLPGYRPTT RSSARRSQAG VSSGAPPGRN SFYMGTCQDE PEQLDDWNRI 

      1930       1940       1950       1960       1970       1980 
AELQQRNRVC PPHLKTCYPL ESRPSLSLGT ITDEEMKTGD PQETLRRASM QPIQIAEGTG 

      1990       2000       2010       2020       2030       2040 
ITTRQQRKRV SLEPHQGPGT PESKKATSCF PRPMTPRDRH EGRKQSTTEA QKKAAPASTK 

      2050       2060       2070       2080       2090       2100 
QADRRQSMAF SILNTPKKLG NSLLRRGASK KALSKASPNT RSGTRRSPRI ATTTASAATA 

      2110 
AAIGATPRAK GKAKH 

« Hide

Isoform 2 [UniParc].

Checksum: 18D8C4A34409ADE9
Show »

FASTA2,101236,516
Isoform Numa-m (p195) [UniParc].

Checksum: 4CCE2F79A2228DCD
Show »

FASTA1,776201,453
Isoform Numa-s (p194) [UniParc].

Checksum: B288C63D156E3E18
Show »

FASTA1,763200,097
Isoform 5 [UniParc].

Checksum: A1371283C8D14140
Show »

FASTA979109,279

References

« Hide 'large scale' references
[1]"NuMA: an unusually long coiled-coil related protein in the mammalian nucleus."
Yang C.H., Lambie E.J., Snyder M.
J. Cell Biol. 116:1303-1317(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
[2]"Primary structure of NuMA, an intranuclear protein that defines a novel pathway for segregation of proteins at mitosis."
Compton D.A., Szilak I., Cleveland D.W.
J. Cell Biol. 116:1395-1408(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Primary structure and microtubule-interacting domain of the SP-H antigen: a mitotic map located at the spindle pole characterized as a homologous protein to NuMA."
Maekawa T., Kuriyama R.
J. Cell Sci. 105:589-600(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Lung.
[7]"Nuclear proteins of the bovine esophageal epithelium. II. The NuMA gene gives rise to multiple mRNAs and gene products reactive with monoclonal antibody W1."
Tang T.K., Tang C.J., Chen Y.L., Wu C.W.
J. Cell Sci. 104:249-260(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1576-2115 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 975-1776 (ISOFORM NUMA-M), NUCLEOTIDE SEQUENCE [MRNA] OF 610-1763 (ISOFORM NUMA-S), ALTERNATIVE SPLICING.
[8]"Nuclear mitotic apparatus protein (NuMA): spindle association, nuclear targeting and differential subcellular localization of various NuMA isoforms."
Tang T.K., Tang C.J., Chao Y.J., Wu C.W.
J. Cell Sci. 107:1389-1402(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, MUTAGENESIS OF ARG-1984 AND LYS-1988, NUCLEAR LOCALIZATION SIGNAL.
[9]"Mutation of the predicted p34cdc2 phosphorylation sites in NuMA impair the assembly of the mitotic spindle and block mitosis."
Compton D.A., Luo C.
J. Cell Sci. 108:621-633(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-2015; THR-2055; SER-2087 AND THR-2106, MUTAGENESIS OF THR-2015; THR-2055; SER-2087 AND THR-2106.
[10]"Direct binding of NuMA to tubulin is mediated by a novel sequence motif in the tail domain that bundles and stabilizes microtubules."
Haren L., Merdes A.
J. Cell Sci. 115:1815-1824(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICROTUBULES, TUBULIN-BINDING DOMAIN.
[11]"NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis."
Chang W., Dynek J.N., Smith S.
Biochem. J. 391:177-184(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ADP-RIBOSYLATION, INTERACTION WITH TNKS, SUBCELLULAR LOCATION.
[12]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757; SER-1769; THR-1776; SER-1840 AND THR-2106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2077, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-395; SER-820; SER-1601; SER-1757 AND SER-1760, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-203; THR-211; SER-1721; SER-1724; SER-1728; SER-1757; SER-1769; SER-1772; TYR-1774; THR-1776; SER-1788; SER-1789; SER-1792; SER-1800; THR-1804; SER-1830; SER-1833; SER-1834; TYR-1836; SER-1840; SER-1862; SER-1887; SER-1969; SER-1991 AND THR-2000, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Requirements for NuMA in maintenance and establishment of mammalian spindle poles."
Silk A.D., Holland A.J., Cleveland D.W.
J. Cell Biol. 184:677-690(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-1225; SER-1757; SER-1769; THR-1776; SER-1788 AND SER-1800, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-379; LYS-891 AND LYS-1511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis."
Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.
Sci. Signal. 3:RA2-RA2(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-1844.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-203; THR-211; SER-271; SER-1187; SER-1225; SER-1757; SER-1769; SER-1830; SER-1862; SER-1969; SER-1991; THR-2000 AND SER-2003, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"NuMA after 30 years: the matrix revisited."
Radulescu A.E., Cleveland D.W.
Trends Cell Biol. 20:214-222(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Self assembly of NuMA: multiarm oligomers as structural units of a nuclear lattice."
Harborth J., Wang J., Gueth-Hallonet C., Weber K., Osborn M.
EMBO J. 18:1689-1700(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31633.1. [Q14980-1]
CCDS66156.1. [Q14980-2]
PIRA42184.
RefSeqNP_001273490.1. NM_001286561.1. [Q14980-2]
NP_006176.2. NM_006185.3. [Q14980-1]
XP_006718625.1. XM_006718562.1. [Q14980-1]
XP_006718626.1. XM_006718563.1. [Q14980-1]
XP_006718627.1. XM_006718564.1. [Q14980-1]
XP_006718628.1. XM_006718565.1. [Q14980-1]
XP_006718629.1. XM_006718566.1. [Q14980-1]
XP_006718630.1. XM_006718567.1. [Q14980-1]
XP_006718631.1. XM_006718568.1. [Q14980-1]
XP_006718632.1. XM_006718569.1. [Q14980-1]
XP_006718633.1. XM_006718570.1. [Q14980-2]
UniGeneHs.325978.
Hs.591967.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RO2X-ray2.30B1899-1926[»]
ProteinModelPortalQ14980.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110980. 58 interactions.
DIPDIP-32937N.
IntActQ14980. 14 interactions.
MINTMINT-1489811.
STRING9606.ENSP00000352675.

PTM databases

PhosphoSiteQ14980.

Polymorphism databases

DMDM145559510.

Proteomic databases

MaxQBQ14980.
PaxDbQ14980.
PRIDEQ14980.

Protocols and materials databases

DNASU4926.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351960; ENSP00000260051; ENSG00000137497.
ENST00000358965; ENSP00000351851; ENSG00000137497. [Q14980-2]
ENST00000393695; ENSP00000377298; ENSG00000137497. [Q14980-1]
GeneID4926.
KEGGhsa:4926.
UCSCuc001orl.1. human. [Q14980-1]
uc001orm.1. human. [Q14980-2]
uc001orn.2. human. [Q14980-4]

Organism-specific databases

CTD4926.
GeneCardsGC11M071713.
H-InvDBHIX0026234.
HGNCHGNC:8059. NUMA1.
HPAHPA019841.
HPA019859.
HPA029912.
MIM164009. gene.
neXtProtNX_Q14980.
Orphanet520. Acute promyelocytic leukemia.
PharmGKBPA31844.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000113889.
HOVERGENHBG052694.
KOK16808.
OMAHEAQAQV.
PhylomeDBQ14980.
TreeFamTF334442.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ14980.
BgeeQ14980.
CleanExHS_NUMA1.
GenevestigatorQ14980.

Family and domain databases

InterProIPR026650. NUMA1.
[Graphical view]
PANTHERPTHR18902:SF24. PTHR18902:SF24. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNUMA1. human.
GeneWikiNuclear_mitotic_apparatus_protein_1.
GenomeRNAi4926.
NextBio18971.
PROQ14980.
SOURCESearch...

Entry information

Entry nameNUMA1_HUMAN
AccessionPrimary (citable) accession number: Q14980
Secondary accession number(s): H0YH75, Q14981, Q9BTE9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM