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Reviewed, UniProtKB/Swiss-Prot Q14980 (NUMA1_HUMAN)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length2115 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

May be a structural component of the nucleus.

Subcellular location

Nucleus. Note: Dissociates from condensing chromosomes during early prophase, 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

Sequence caution

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

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Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processmitotic anaphase Ref.2

Traceable author statement. Source: ProtInc

nucleus organization Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentspindle microtubule Ref.2

Traceable author statement. Source: ProtInc

spindle pole

Inferred from direct assay. Source: UniProtKB

   Molecular functionstructural molecule activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

GNAI1P630961EBI-521611,EBI-618639
GPSM2P812742EBI-521611,EBI-618655

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14980-1)

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21152115Nuclear mitotic apparatus protein 1
PRO_0000057998

Regions

Coiled coil213 – 16991487 Potential

Amino acid modifications

Modified residue1691Phosphoserine Ref.6 Ref.8 Ref.13
Modified residue1721Phosphoserine Ref.8
Modified residue1981Phosphoserine Ref.13
Modified residue2001Phosphoserine Ref.8
Modified residue2031Phosphoserine Ref.8 Ref.13
Modified residue2111Phosphothreonine Ref.8 Ref.13
Modified residue3881Phosphoserine Ref.10
Modified residue3951Phosphoserine Ref.10
Modified residue8201Phosphoserine Ref.10
Modified residue9631Phosphothreonine Ref.10
Modified residue12621Phosphoserine Ref.8
Modified residue16011Phosphoserine Ref.10
Modified residue17211Phosphoserine Ref.6 Ref.8 Ref.13
Modified residue17241Phosphoserine Ref.6 Ref.8 Ref.13
Modified residue17281Phosphoserine Ref.6 Ref.13
Modified residue17331Phosphothreonine Ref.6 Ref.8
Modified residue17571Phosphoserine Ref.6 Ref.8 Ref.13 Ref.10 Ref.4 Ref.7 Ref.9 Ref.11 Ref.12
Modified residue17601Phosphoserine Ref.10
Modified residue17691Phosphoserine Ref.8 Ref.13 Ref.7
Modified residue17721Phosphoserine Ref.8 Ref.13
Modified residue17741Phosphotyrosine Ref.13 Ref.5
Modified residue17761Phosphothreonine Ref.8 Ref.13 Ref.7
Modified residue17881Phosphoserine Ref.13
Modified residue17891Phosphoserine Ref.13
Modified residue17921Phosphoserine Ref.13
Modified residue18001Phosphoserine Ref.13
Modified residue18041Phosphothreonine Ref.13
Modified residue18301Phosphoserine Ref.8 Ref.13
Modified residue18331Phosphoserine Ref.8 Ref.13
Modified residue18341Phosphoserine Ref.8 Ref.13
Modified residue18361Phosphotyrosine Ref.13
Modified residue18371Phosphoserine Ref.13
Modified residue18401Phosphoserine Ref.13 Ref.7
Modified residue18471Phosphoserine Ref.7
Modified residue18531Phosphoserine Ref.4
Modified residue18621Phosphoserine Ref.6 Ref.8 Ref.13
Modified residue18721Phosphoserine Ref.8 Ref.13
Modified residue18871Phosphoserine Ref.13
Modified residue19451Phosphoserine Ref.8
Modified residue19691Phosphoserine Ref.13 Ref.12
Modified residue19911Phosphoserine Ref.13
Modified residue20001Phosphothreonine Ref.6 Ref.8 Ref.13
Modified residue20551Phosphothreonine Ref.7
Modified residue20771Phosphoserine Ref.9
Modified residue21061Phosphothreonine Ref.7

Natural variations

Alternative sequence1536 – 154914Missing in isoform 2.
VSP_012910
Natural variant2421K → R: dbSNP rs34239655.
VAR_031679
Natural variant7941A → G: dbSNP rs3750913.
VAR_031680
Natural variant11531E → D: dbSNP rs34311364.
VAR_031681
Natural variant18251V → M: dbSNP rs7949430.
VAR_031682
Natural variant18361Y → H: dbSNP rs35586429.
VAR_031683
Natural variant20491A → T: dbSNP rs5743685.
VAR_051248

Experimental info

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 conflict17981L → Q in CAA77669. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [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.

Checksum: 18D8C4A34409ADE9
Show »

FASTA2,101236,516

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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: 1541630] [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: 1541636] [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: 8408288] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757 AND SER-1853, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1774, MASS SPECTROMETRY.
[6]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-1721; SER-1724; SER-1728; THR-1733; SER-1757; SER-1862 AND THR-2000, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757; SER-1769; THR-1776; SER-1840; SER-1847; THR-2055 AND THR-2106, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-172; SER-200; SER-203; THR-211; SER-1262; SER-1721; SER-1724; THR-1733; SER-1757; SER-1769; SER-1772; THR-1776; SER-1830; SER-1833; SER-1834; SER-1862; SER-1872; SER-1945 AND THR-2000, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"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: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757 AND SER-2077, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"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: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-395; SER-820; THR-963; SER-1601; SER-1757 AND SER-1760, MASS SPECTROMETRY.
[11]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, MASS SPECTROMETRY.
[12]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757 AND SER-1969, MASS SPECTROMETRY.
[13]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-198; 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-1837; SER-1840; SER-1862; SER-1872; SER-1887; SER-1969; SER-1991 AND THR-2000, MASS SPECTROMETRY.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

Z11583 mRNA. Translation: CAA77669.1.
Z11584 mRNA. Translation: CAA77670.1. Frameshift.
IPIIPI00006196.
IPI00292771.
PIRA42184.
RefSeqNP_006176.2.
UniGeneHs.325978

3D structure databases

HSSPHSSP built from PDB template 1D7M based on UniProtKB O15813.
ModBaseSearch...

Protein-protein interaction databases

IntActQ14980. 7 interactions.

PTM databases

PhosphoSiteQ14980.

Proteomic databases

PRIDEQ14980.

Genome annotation databases

EnsemblENSG00000137497. Homo sapiens. [Contig view]
GeneID4926.
KEGGhsa:4926.

Organism-specific databases

GeneCardsGC11M071391.
H-InvDBHIX0009904.
HGNCHGNC:8059. NUMA1.
MIM164009. gene.
PharmGKBPA31844.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ14980.
OMAQ14980. EGRKQST.

Enzyme and pathway databases

Pathway_Interaction_DBcaspase_pathway. Caspase cascade in apoptosis.

Gene expression databases

ArrayExpressQ14980.
BgeeQ14980.
CleanExHS_NUMA1.
GermOnlineENSG00000137497. Homo sapiens.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio18971.
SOURCESearch...

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Entry information

Entry nameNUMA1_HUMAN
AccessionPrimary (citable) accession number: Q14980
Secondary accession number(s): Q14981
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: April 17, 2007
Last modified: June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 11

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents