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Q14980

- NUMA1_HUMAN

UniProt

Q14980 - NUMA1_HUMAN

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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

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. 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 cell cycle Source: Reactome
  6. mitotic nuclear division Source: UniProtKB-KW
  7. nucleus organization Source: ProtInc
Complete GO annotation...

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 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
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-KW
  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: Ensembl
  9. nucleoplasm Source: Reactome
  10. nucleus Source: UniProtKB
  11. spindle Source: ProtInc
  12. spindle microtubule Source: UniProtKB
  13. spindle pole Source: UniProtKB
Complete GO annotation...

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

BgeeiQ14980.
CleanExiHS_NUMA1.
ExpressionAtlasiQ14980. baseline and differential.
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. 65 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 – 19193Combined sources
Helixi1920 – 19223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00730000111158.
HOGENOMiHOG000113889.
HOVERGENiHBG052694.
InParanoidiQ14980.
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

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

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:
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_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]
ENST00000613205; ENSP00000480172; ENSG00000137497. [Q14980-5]
ENST00000620566; ENSP00000478624; ENSG00000137497. [Q14980-2]
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:
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 .
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:
PDBei
RCSB PDBi
PDBji
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. 65 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 ]
ENST00000613205 ; ENSP00000480172 ; ENSG00000137497 . [Q14980-5 ]
ENST00000620566 ; ENSP00000478624 ; ENSG00000137497 . [Q14980-2 ]
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.
GeneTreei ENSGT00730000111158.
HOGENOMi HOG000113889.
HOVERGENi HBG052694.
InParanoidi Q14980.
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

Bgeei Q14980.
CleanExi HS_NUMA1.
ExpressionAtlasi Q14980. baseline and differential.
Genevestigatori Q14980.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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. "Sensitivity and specificity of NMP-22, telomerase, and BTA in the detection of human bladder cancer."
    Landman J., Chang Y., Kavaler E., Droller M.J., Liu B.C.
    Urology 52:398-402(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: USED IN DIAGNOSTIC TESTS.
  11. "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.
  12. "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.
  13. "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].
  14. "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.
  15. "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.
  16. "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.
  17. 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.
  18. "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.
  19. "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.
  20. 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.
  21. "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].
  22. "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.
  23. "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.
  24. "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].
  25. "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.
  26. "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.
  27. Cited for: REVIEW.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "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].
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "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: November 26, 2014
This is version 130 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

External Data

Dasty 3