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Q14980

- NUMA1_HUMAN

UniProt

Q14980 - NUMA1_HUMAN

Protein

Nuclear mitotic apparatus protein 1

Gene

NUMA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. establishment of mitotic spindle orientation Source: Ensembl
    2. G2/M transition of mitotic cell cycle Source: Reactome
    3. lung epithelial cell differentiation Source: Ensembl
    4. meiotic cell cycle Source: Ensembl
    5. mitotic anaphase Source: ProtInc
    6. mitotic cell cycle Source: Reactome
    7. mitotic nuclear division Source: UniProtKB-KW
    8. nucleus organization Source: ProtInc

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_15510. Recruitment of NuMA to mitotic centrosomes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear mitotic apparatus protein 1
    Short name:
    NuMA protein
    Alternative name(s):
    SP-H antigen
    Gene namesi
    Name:NUMA1
    Synonyms:NUMA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:8059. NUMA1.

    Subcellular locationi

    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.
    Isoform Numa-m : Cytoplasm
    Note: Mainly clustered at the centrosomal region.
    Isoform Numa-s : Cytoplasm
    Note: Mainly clustered at the centrosomal region.

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. chromosome Source: UniProtKB-SubCell
    3. cytoplasm Source: HPA
    4. cytosol Source: Reactome
    5. dendrite Source: Ensembl
    6. Golgi membrane Source: InterPro
    7. neuronal cell body Source: Ensembl
    8. nuclear matrix Source: UniProtKB-SubCell
    9. nucleoplasm Source: Reactome
    10. nucleus Source: HPA
    11. spindle Source: ProtInc
    12. spindle microtubule Source: ProtInc
    13. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Cytoskeleton, Microtubule, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1984 – 19841R → G: No effect on nuclear localization. 1 Publication
    Mutagenesisi1988 – 19881K → E: Abolishes nuclear localization. 1 Publication
    Mutagenesisi2015 – 20151T → A: Abolishes association with the mitotic spindle. 1 Publication
    Mutagenesisi2055 – 20551T → A: Reduces association with the mitotic spindle and induces plasma membrane localization. 1 Publication
    Mutagenesisi2087 – 20871S → A: Abolishes association with the mitotic spindle. 1 Publication
    Mutagenesisi2106 – 21061T → A: Abolishes association with the mitotic spindle. 1 Publication

    Organism-specific databases

    Orphaneti520. Acute promyelocytic leukemia.
    PharmGKBiPA31844.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21152115Nuclear mitotic apparatus protein 1PRO_0000057998Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei169 – 1691Phosphoserine2 Publications
    Modified residuei203 – 2031Phosphoserine3 Publications
    Modified residuei211 – 2111Phosphothreonine2 Publications
    Modified residuei271 – 2711Phosphoserine1 Publication
    Modified residuei379 – 3791N6-acetyllysine1 Publication
    Modified residuei388 – 3881Phosphoserine1 Publication
    Modified residuei395 – 3951Phosphoserine1 Publication
    Modified residuei820 – 8201Phosphoserine1 Publication
    Modified residuei891 – 8911N6-acetyllysine1 Publication
    Modified residuei1187 – 11871Phosphoserine1 Publication
    Modified residuei1225 – 12251Phosphoserine2 Publications
    Modified residuei1511 – 15111N6-acetyllysine1 Publication
    Modified residuei1601 – 16011Phosphoserine1 Publication
    Modified residuei1721 – 17211Phosphoserine1 Publication
    Modified residuei1724 – 17241Phosphoserine1 Publication
    Modified residuei1728 – 17281Phosphoserine1 Publication
    Modified residuei1757 – 17571Phosphoserine9 Publications
    Modified residuei1760 – 17601Phosphoserine1 Publication
    Modified residuei1769 – 17691Phosphoserine4 Publications
    Modified residuei1772 – 17721Phosphoserine1 Publication
    Modified residuei1774 – 17741Phosphotyrosine1 Publication
    Modified residuei1776 – 17761Phosphothreonine3 Publications
    Modified residuei1788 – 17881Phosphoserine2 Publications
    Modified residuei1789 – 17891Phosphoserine1 Publication
    Modified residuei1792 – 17921Phosphoserine1 Publication
    Modified residuei1800 – 18001Phosphoserine2 Publications
    Modified residuei1804 – 18041Phosphothreonine1 Publication
    Modified residuei1830 – 18301Phosphoserine2 Publications
    Modified residuei1833 – 18331Phosphoserine1 Publication
    Modified residuei1834 – 18341Phosphoserine1 Publication
    Modified residuei1836 – 18361Phosphotyrosine1 Publication
    Modified residuei1840 – 18401Phosphoserine2 Publications
    Glycosylationi1844 – 18441O-linked (GlcNAc)1 Publication
    Modified residuei1862 – 18621Phosphoserine2 Publications
    Modified residuei1887 – 18871Phosphoserine1 Publication
    Modified residuei1969 – 19691Phosphoserine2 Publications
    Modified residuei1991 – 19911Phosphoserine2 Publications
    Modified residuei2000 – 20001Phosphothreonine2 Publications
    Modified residuei2003 – 20031Phosphoserine1 Publication
    Modified residuei2015 – 20151Phosphothreonine; by CDK11 Publication
    Modified residuei2055 – 20551Phosphothreonine; by CDK11 Publication
    Modified residuei2077 – 20771Phosphoserine1 Publication
    Modified residuei2087 – 20871Phosphoserine; by CDK11 Publication
    Modified residuei2106 – 21061Phosphothreonine; by CDK12 Publications

    Post-translational modificationi

    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.
    O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.1 Publication

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ14980.
    PaxDbiQ14980.
    PRIDEiQ14980.

    PTM databases

    PhosphoSiteiQ14980.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14980.
    BgeeiQ14980.
    CleanExiHS_NUMA1.
    GenevestigatoriQ14980.

    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. Interacts with TNKS.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GNAI1P630964EBI-521611,EBI-618639
    GPSM2P812746EBI-521611,EBI-618655

    Protein-protein interaction databases

    BioGridi110980. 59 interactions.
    DIPiDIP-32937N.
    IntActiQ14980. 15 interactions.
    MINTiMINT-1489811.
    STRINGi9606.ENSP00000352675.

    Structurei

    Secondary structure

    1
    2115
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni1917 – 19193
    Helixi1920 – 19223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RO2X-ray2.30B1899-1926[»]
    ProteinModelPortaliQ14980.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 212212Head (Globular)Add
    BLAST
    Regioni1700 – 2115416Tail (Globular)Add
    BLAST
    Regioni1866 – 193671Interaction with microtubulesAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili213 – 16991487Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1984 – 19896Nuclear localization signal1 Publication

    Domaini

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000113889.
    HOVERGENiHBG052694.
    KOiK16808.
    OMAiHEAQAQV.
    PhylomeDBiQ14980.
    TreeFamiTF334442.

    Family and domain databases

    InterProiIPR026650. NUMA1.
    [Graphical view]
    PANTHERiPTHR18902:SF24. PTHR18902:SF24. 1 hit.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    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

    MTLHATRGAA LLSWVNSLHV ADPVEAVLQL QDCSIFIKII DRIHGTEEGQ     50
    QILKQPVSER LDFVCSFLQK NRKHPSSPEC LVSAQKVLEG SELELAKMTM 100
    LLLYHSTMSS KSPRDWEQFE YKIQAELAVI LKFVLDHEDG LNLNEDLENF 150
    LQKAPVPSTC SSTFPEELSP PSHQAKREIR FLELQKVASS SSGNNFLSGS 200
    PASPMGDILQ TPQFQMRRLK KQLADERSNR DELELELAEN RKLLTEKDAQ 250
    IAMMQQRIDR LALLNEKQAA SPLEPKELEE LRDKNESLTM RLHETLKQCQ 300
    DLKTEKSQMD RKINQLSEEN GDLSFKLREF ASHLQQLQDA LNELTEEHSK 350
    ATQEWLEKQA QLEKELSAAL QDKKCLEEKN EILQGKLSQL EEHLSQLQDN 400
    PPQEKGEVLG DVLQLETLKQ EAATLAANNT QLQARVEMLE TERGQQEAKL 450
    LAERGHFEEE KQQLSSLITD LQSSISNLSQ AKEELEQASQ AHGARLTAQV 500
    ASLTSELTTL NATIQQQDQE LAGLKQQAKE KQAQLAQTLQ QQEQASQGLR 550
    HQVEQLSSSL KQKEQQLKEV AEKQEATRQD HAQQLATAAE EREASLRERD 600
    AALKQLEALE KEKAAKLEIL QQQLQVANEA RDSAQTSVTQ AQREKAELSR 650
    KVEELQACVE TARQEQHEAQ AQVAELELQL RSEQQKATEK ERVAQEKDQL 700
    QEQLQALKES LKVTKGSLEE EKRRAADALE EQQRCISELK AETRSLVEQH 750
    KRERKELEEE RAGRKGLEAR LQQLGEAHQA ETEVLRRELA EAMAAQHTAE 800
    SECEQLVKEV AAWRERYEDS QQEEAQYGAM FQEQLMTLKE ECEKARQELQ 850
    EAKEKVAGIE SHSELQISRQ QNELAELHAN LARALQQVQE KEVRAQKLAD 900
    DLSTLQEKMA ATSKEVARLE TLVRKAGEQQ ETASRELVKE PARAGDRQPE 950
    WLEEQQGRQF CSTQAALQAM EREAEQMGNE LERLRAALME SQGQQQEERG 1000
    QQEREVARLT QERGRAQADL ALEKAARAEL EMRLQNALNE QRVEFATLQE 1050
    ALAHALTEKE GKDQELAKLR GLEAAQIKEL EELRQTVKQL KEQLAKKEKE 1100
    HASGSGAQSE AAGRTEPTGP KLEALRAEVS KLEQQCQKQQ EQADSLERSL 1150
    EAERASRAER DSALETLQGQ LEEKAQELGH SQSALASAQR ELAAFRTKVQ 1200
    DHSKAEDEWK AQVARGRQEA ERKNSLISSL EEEVSILNRQ VLEKEGESKE 1250
    LKRLVMAESE KSQKLEERLR LLQAETASNS ARAAERSSAL REEVQSLREE 1300
    AEKQRVASEN LRQELTSQAE RAEELGQELK AWQEKFFQKE QALSTLQLEH 1350
    TSTQALVSEL LPAKHLCQQL QAEQAAAEKR HREELEQSKQ AAGGLRAELL 1400
    RAQRELGELI PLRQKVAEQE RTAQQLRAEK ASYAEQLSML KKAHGLLAEE 1450
    NRGLGERANL GRQFLEVELD QAREKYVQEL AAVRADAETR LAEVQREAQS 1500
    TARELEVMTA KYEGAKVKVL EERQRFQEER QKLTAQVEQL EVFQREQTKQ 1550
    VEELSKKLAD SDQASKVQQQ KLKAVQAQGG ESQQEAQRLQ AQLNELQAQL 1600
    SQKEQAAEHY KLQMEKAKTH YDAKKQQNQE LQEQLRSLEQ LQKENKELRA 1650
    EAERLGHELQ QAGLKTKEAE QTCRHLTAQV RSLEAQVAHA DQQLRDLGKF 1700
    QVATDALKSR EPQAKPQLDL SIDSLDLSCE EGTPLSITSK LPRTQPDGTS 1750
    VPGEPASPIS QRLPPKVESL ESLYFTPIPA RSQAPLESSL DSLGDVFLDS 1800
    GRKTRSARRR TTQIINITMT KKLDVEEPDS ANSSFYSTRS APASQASLRA 1850
    TSSTQSLARL GSPDYGNSAL LSLPGYRPTT RSSARRSQAG VSSGAPPGRN 1900
    SFYMGTCQDE PEQLDDWNRI AELQQRNRVC PPHLKTCYPL ESRPSLSLGT 1950
    ITDEEMKTGD PQETLRRASM QPIQIAEGTG ITTRQQRKRV SLEPHQGPGT 2000
    PESKKATSCF PRPMTPRDRH EGRKQSTTEA QKKAAPASTK QADRRQSMAF 2050
    SILNTPKKLG NSLLRRGASK KALSKASPNT RSGTRRSPRI ATTTASAATA 2100
    AAIGATPRAK GKAKH 2115
    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 CAA77670.1 differs from that shown. Reason: Frameshift at positions 1270 and 1299.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti772 – 7721Q → L in CAA77670. (PubMed:1541636)Curated
    Sequence conflicti815 – 8162ER → DG in CAA77670. (PubMed:1541636)Curated
    Sequence conflicti873 – 8731E → K in CAA77670. (PubMed:1541636)Curated
    Sequence conflicti1589 – 15891L → F in CAA77670. (PubMed:1541636)Curated
    Sequence conflicti1637 – 16371S → T in Z14227. (PubMed:8408288)Curated
    Sequence conflicti1637 – 16371S → T in Z14228. (PubMed:8408288)Curated
    Sequence conflicti1682 – 16821S → T in Z14227. (PubMed:8408288)Curated
    Sequence conflicti1682 – 16821S → T in Z14228. (PubMed:8408288)Curated
    Sequence conflicti1798 – 17981L → Q in CAA77669. (PubMed:8408288)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti242 – 2421K → R.
    Corresponds to variant rs34239655 [ dbSNP | Ensembl ].
    VAR_031679
    Natural varianti794 – 7941A → G.
    Corresponds to variant rs3750913 [ dbSNP | Ensembl ].
    VAR_031680
    Natural varianti1153 – 11531E → D.
    Corresponds to variant rs34311364 [ dbSNP | Ensembl ].
    VAR_031681
    Natural varianti1825 – 18251V → M.
    Corresponds to variant rs7949430 [ dbSNP | Ensembl ].
    VAR_031682
    Natural varianti1836 – 18361Y → H.
    Corresponds to variant rs35586429 [ dbSNP | Ensembl ].
    VAR_031683
    Natural varianti2049 – 20491A → T.
    Corresponds to variant rs5743685 [ dbSNP | Ensembl ].
    VAR_051248

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei414 – 15491136Missing in isoform 5. 1 PublicationVSP_054146Add
    BLAST
    Alternative sequencei1536 – 154914Missing in isoform 2. 1 PublicationVSP_012910Add
    BLAST
    Alternative sequencei1725 – 2115391LDLSC…GKAKH → SQANSSQTPRDSDACPHPGL VPGPSLAPSRSWPRGPGAWT VWALSLPCLLFS in isoform Numa-m. 1 PublicationVSP_044378Add
    BLAST
    Alternative sequencei1739 – 2115377SKLPR…GKAKH → RSGGSLPPYVCLWSACCLSG CILVR in isoform Numa-s. 1 PublicationVSP_044379Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_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]
    UniGeneiHs.325978.
    Hs.591967.

    Genome annotation databases

    EnsembliENST00000351960; ENSP00000260051; ENSG00000137497. [Q14980-5]
    ENST00000358965; ENSP00000351851; ENSG00000137497. [Q14980-2]
    ENST00000393695; ENSP00000377298; ENSG00000137497. [Q14980-1]
    GeneIDi4926.
    KEGGihsa:4926.
    UCSCiuc001ork.1. human.
    uc001orl.1. human. [Q14980-1]
    uc001orm.1. human. [Q14980-2]
    uc001orn.2. human. [Q14980-4]

    Polymorphism databases

    DMDMi145559510.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS31633.1. [Q14980-1 ]
    CCDS66156.1. [Q14980-2 ]
    PIRi A42184.
    RefSeqi NP_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 ]
    UniGenei Hs.325978.
    Hs.591967.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RO2 X-ray 2.30 B 1899-1926 [» ]
    ProteinModelPortali Q14980.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110980. 59 interactions.
    DIPi DIP-32937N.
    IntActi Q14980. 15 interactions.
    MINTi MINT-1489811.
    STRINGi 9606.ENSP00000352675.

    PTM databases

    PhosphoSitei Q14980.

    Polymorphism databases

    DMDMi 145559510.

    Proteomic databases

    MaxQBi Q14980.
    PaxDbi Q14980.
    PRIDEi Q14980.

    Protocols and materials databases

    DNASUi 4926.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351960 ; ENSP00000260051 ; ENSG00000137497 . [Q14980-5 ]
    ENST00000358965 ; ENSP00000351851 ; ENSG00000137497 . [Q14980-2 ]
    ENST00000393695 ; ENSP00000377298 ; ENSG00000137497 . [Q14980-1 ]
    GeneIDi 4926.
    KEGGi hsa:4926.
    UCSCi uc001ork.1. human.
    uc001orl.1. human. [Q14980-1 ]
    uc001orm.1. human. [Q14980-2 ]
    uc001orn.2. human. [Q14980-4 ]

    Organism-specific databases

    CTDi 4926.
    GeneCardsi GC11M071713.
    H-InvDB HIX0026234.
    HGNCi HGNC:8059. NUMA1.
    HPAi HPA019841.
    HPA019859.
    HPA029912.
    MIMi 164009. gene.
    neXtProti NX_Q14980.
    Orphaneti 520. Acute promyelocytic leukemia.
    PharmGKBi PA31844.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000113889.
    HOVERGENi HBG052694.
    KOi K16808.
    OMAi HEAQAQV.
    PhylomeDBi Q14980.
    TreeFami TF334442.

    Enzyme and pathway databases

    Reactomei REACT_15510. Recruitment of NuMA to mitotic centrosomes.

    Miscellaneous databases

    ChiTaRSi NUMA1. human.
    GeneWikii Nuclear_mitotic_apparatus_protein_1.
    GenomeRNAii 4926.
    NextBioi 18971.
    PROi Q14980.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14980.
    Bgeei Q14980.
    CleanExi HS_NUMA1.
    Genevestigatori Q14980.

    Family and domain databases

    InterProi IPR026650. NUMA1.
    [Graphical view ]
    PANTHERi PTHR18902:SF24. PTHR18902:SF24. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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. 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. 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. Cited for: REVIEW.
    27. 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. 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.

    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: October 1, 2014
    This is version 128 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

    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

    External Data

    Dasty 3