Q14980 (NUMA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear mitotic apparatus protein 1
Short name=NuMA protein

Alternative name(s):
SP-H antigen

Gene names

Name:	NUMA1
Synonyms:	NUMA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2115 AA.
Sequence status	Complete.
Protein existence	Evidence 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.18
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.8 Ref.9 Ref.25
Subcellular location	Nucleus matrix. Chromosome. Cytoplasm › cytoskeleton › spindle 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.6 Ref.9 Isoform Numa-m: Cytoplasm. Note: Mainly clustered at the centrosomal region. Ref.1 Ref.6 Ref.9 Isoform Numa-s: Cytoplasm. Note: Mainly clustered at the centrosomal region. Ref.1 Ref.6 Ref.9
Domain	The C-terminal tubulin-binding domain mediates direct binding to microtubules, independantly of dynein and dynactin, and induces their bundling and stabilization. Ref.8
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.7
Sequence caution	The sequence CAA77670.1 differs from that shown. Reason: Frameshift at positions 1270 and 1299.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Chromosome Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	ADP-ribosylation Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW establishment of mitotic spindle orientation Inferred from electronic annotation. Source: Compara lung epithelial cell differentiation Inferred from electronic annotation. Source: Compara mitotic anaphase Traceable author statement Ref.2. Source: ProtInc nucleus organization Traceable author statement Ref.1. Source: ProtInc
Cellular_component	apical part of cell Inferred from electronic annotation. Source: Compara chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome spindle microtubule Traceable author statement Ref.2. Source: ProtInc spindle pole Inferred from direct assay PubMed 14718566. Source: UniProtKB
Molecular_function	structural molecule activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GNAI1	P63096	4	EBI-521611,EBI-618639
GPSM2	P81274	6	EBI-521611,EBI-618655

Alternative products

This entry describes 4 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2115

2115

Nuclear mitotic apparatus protein 1

PRO_0000057998

Regions

Region

1 – 212

212

Head (Globular)

Region

1700 – 2115

416

Tail (Globular)

Region

1866 – 1936

71

Interaction with microtubules

Coiled coil

213 – 1699

1487

Potential

Motif

1984 – 1989

6

Nuclear localization signal Ref.6

Amino acid modifications

Modified residue

169

1

Phosphoserine Ref.17 Ref.21

Modified residue

203

1

Phosphoserine Ref.17 Ref.19 Ref.21

Modified residue

211

1

Phosphothreonine Ref.17 Ref.21

Modified residue

271

1

Phosphoserine Ref.21

Modified residue

379

1

N6-acetyllysine Ref.20

Modified residue

388

1

Phosphoserine Ref.14

Modified residue

395

1

Phosphoserine Ref.14

Modified residue

820

1

Phosphoserine Ref.14

Modified residue

891

1

N6-acetyllysine Ref.20

Modified residue

1187

1

Phosphoserine Ref.21

Modified residue

1225

1

Phosphoserine Ref.19 Ref.21

Modified residue

1511

1

N6-acetyllysine Ref.20

Modified residue

1601

1

Phosphoserine Ref.14

Modified residue

1721

1

Phosphoserine Ref.17

Modified residue

1724

1

Phosphoserine Ref.17

Modified residue

1728

1

Phosphoserine Ref.17

Modified residue

1757

1

Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.24

Modified residue

1760

1

Phosphoserine Ref.14

Modified residue

1769

1

Phosphoserine Ref.12 Ref.17 Ref.19 Ref.21

Modified residue

1772

1

Phosphoserine Ref.17

Modified residue

1774

1

Phosphotyrosine Ref.17

Modified residue

1776

1

Phosphothreonine Ref.12 Ref.17 Ref.19

Modified residue

1788

1

Phosphoserine Ref.17 Ref.19

Modified residue

1789

1

Phosphoserine Ref.17

Modified residue

1792

1

Phosphoserine Ref.17

Modified residue

1800

1

Phosphoserine Ref.17 Ref.19

Modified residue

1804

1

Phosphothreonine Ref.17

Modified residue

1830

1

Phosphoserine Ref.17 Ref.21

Modified residue

1833

1

Phosphoserine Ref.17

Modified residue

1834

1

Phosphoserine Ref.17

Modified residue

1836

1

Phosphotyrosine Ref.17

Modified residue

1840

1

Phosphoserine Ref.12 Ref.17

Modified residue

1862

1

Phosphoserine Ref.17 Ref.21

Modified residue

1887

1

Phosphoserine Ref.17

Modified residue

1969

1

Phosphoserine Ref.17 Ref.21

Modified residue

1991

1

Phosphoserine Ref.17 Ref.21

Modified residue

2000

1

Phosphothreonine Ref.17 Ref.21

Modified residue

2003

1

Phosphoserine Ref.21

Modified residue

2015

1

Phosphothreonine; by CDK1 Ref.7

Modified residue

2055

1

Phosphothreonine; by CDK1 Ref.7

Modified residue

2077

1

Phosphoserine Ref.13

Modified residue

2087

1

Phosphoserine; by CDK1 Ref.7

Modified residue

2106

1

Phosphothreonine; by CDK1 Ref.7 Ref.12

Natural variations

Alternative sequence

1536 – 1549

14

Missing in isoform 2.

VSP_012910

Alternative sequence

1725 – 2115

391

LDLSC…GKAKH → SQANSSQTPRDSDACPHPGL VPGPSLAPSRSWPRGPGAWT VWALSLPCLLFS in isoform Numa-m.

VSP_044378

Alternative sequence

1739 – 2115

377

SKLPR…GKAKH → RSGGSLPPYVCLWSACCLSG CILVR in isoform Numa-s.

VSP_044379

Natural variant

242

1

K → R.
Corresponds to variant rs34239655 [ dbSNP | Ensembl ].

VAR_031679

Natural variant

794

1

A → G.
Corresponds to variant rs3750913 [ dbSNP | Ensembl ].

VAR_031680

Natural variant

1153

1

E → D.
Corresponds to variant rs34311364 [ dbSNP | Ensembl ].

VAR_031681

Natural variant

1825

1

V → M.
Corresponds to variant rs7949430 [ dbSNP | Ensembl ].

VAR_031682

Natural variant

1836

1

Y → H.
Corresponds to variant rs35586429 [ dbSNP | Ensembl ].

VAR_031683

Natural variant

2049

1

A → T.
Corresponds to variant rs5743685 [ dbSNP | Ensembl ].

VAR_051248

Experimental info

Mutagenesis

1984

1

R → G: No effect on nuclear localization. Ref.6

Mutagenesis

1988

1

K → E: Abolishes nuclear localization. Ref.6

Mutagenesis

2015

1

T → A: Abolishes association with the mitotic spindle. Ref.7

Mutagenesis

2055

1

T → A: Reduces association with the mitotic spindle and induces plasma membrane localization. Ref.7

Mutagenesis

2087

1

S → A: Abolishes association with the mitotic spindle. Ref.7

Mutagenesis

2106

1

T → A: Abolishes association with the mitotic spindle. Ref.7

Sequence conflict

772

1

Q → L in CAA77670. Ref.2

Sequence conflict

815 – 816

2

ER → DG in CAA77670. Ref.2

Sequence conflict

873

1

E → K in CAA77670. Ref.2

Sequence conflict

1589

1

L → F in CAA77670. Ref.2

Sequence conflict

1637

1

S → T in Z14227. Ref.3

Sequence conflict

1637

1

S → T in Z14228. Ref.3

Sequence conflict

1682

1

S → T in Z14227. Ref.3

Sequence conflict

1682

1

S → T in Z14228. Ref.3

Sequence conflict

1798

1

L → Q in CAA77669. Ref.3

Secondary structure

1

.

.

.

.

2115

Helix Strand Turn

Details...

Turn

1917 – 1919

3

Helix

1920 – 1922

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Numa-1) (p230) [UniParc]. Last modified April 17, 2007. Version 2. Checksum: DE734EC85B812CC7	FASTA	2,115	238,260
	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
	Isoform 2 [UniParc]. Checksum: 18D8C4A34409ADE9	FASTA	2,101	236,516
	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 QKLTAQVEEL SKKLADSDQA SKVQQQKLKA 1570 1580 1590 1600 1610 1620 VQAQGGESQQ EAQRLQAQLN ELQAQLSQKE QAAEHYKLQM EKAKTHYDAK KQQNQELQEQ 1630 1640 1650 1660 1670 1680 LRSLEQLQKE NKELRAEAER LGHELQQAGL KTKEAEQTCR HLTAQVRSLE AQVAHADQQL 1690 1700 1710 1720 1730 1740 RDLGKFQVAT DALKSREPQA KPQLDLSIDS LDLSCEEGTP LSITSKLPRT QPDGTSVPGE 1750 1760 1770 1780 1790 1800 PASPISQRLP PKVESLESLY FTPIPARSQA PLESSLDSLG DVFLDSGRKT RSARRRTTQI 1810 1820 1830 1840 1850 1860 INITMTKKLD VEEPDSANSS FYSTRSAPAS QASLRATSST QSLARLGSPD YGNSALLSLP 1870 1880 1890 1900 1910 1920 GYRPTTRSSA RRSQAGVSSG APPGRNSFYM GTCQDEPEQL DDWNRIAELQ QRNRVCPPHL 1930 1940 1950 1960 1970 1980 KTCYPLESRP SLSLGTITDE EMKTGDPQET LRRASMQPIQ IAEGTGITTR QQRKRVSLEP 1990 2000 2010 2020 2030 2040 HQGPGTPESK KATSCFPRPM TPRDRHEGRK QSTTEAQKKA APASTKQADR RQSMAFSILN 2050 2060 2070 2080 2090 2100 TPKKLGNSLL RRGASKKALS KASPNTRSGT RRSPRIATTT ASAATAAAIG ATPRAKGKAK H
	Isoform Numa-m (p195) [UniParc]. Checksum: 4CCE2F79A2228DCD	FASTA	1,776	201,453
	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 SIDSSQANSS QTPRDSDACP 1750 1760 1770 HPGLVPGPSL APSRSWPRGP GAWTVWALSL PCLLFS
	Isoform Numa-s (p194) [UniParc]. Checksum: B288C63D156E3E18	FASTA	1,763	200,097
	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 EGTPLSITRS 1750 1760 GGSLPPYVCL WSACCLSGCI LVR

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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].
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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, MASS SPECTROMETRY. Tissue: T-cell.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"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, MASS SPECTROMETRY.
[21]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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.
[23]	"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].
[24]	"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, MASS SPECTROMETRY.
[25]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00006196.
IPI00292771.

PIR

A42184.

RefSeq

NP_006176.2. NM_006185.2.

UniGene

Hs.325978.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3RO2	X-ray	2.30	B	1899-1926	[»]

ProteinModelPortal

Q14980.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32937N.

IntAct

Q14980. 10 interactions.

MINT

MINT-1489811.

STRING

9606.ENSP00000352675.

PTM databases

PhosphoSite

Q14980.

Polymorphism databases

DMDM

145559510.

Proteomic databases

PaxDb

Q14980.

PRIDE

Q14980.

Protocols and materials databases

DNASU

4926.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358965; ENSP00000351851; ENSG00000137497.
ENST00000393695; ENSP00000377298; ENSG00000137497.

GeneID

4926.

KEGG

hsa:4926.

UCSC

uc001orl.1. human.
uc001orm.1. human.

Organism-specific databases

CTD

4926.

GeneCards

GC11M071713.

H-InvDB

HIX0026234.

HGNC

HGNC:8059. NUMA1.

HPA

HPA019841.
HPA019859.
HPA029912.

MIM

164009. gene.

neXtProt

NX_Q14980.

PharmGKB

PA31844.

GenAtlas

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Phylogenomic databases

eggNOG

NOG12793.

HOGENOM

HOG000113889.

HOVERGEN

HBG052694.

KO

K16808.

OMA

RENPPRE.

OrthoDB

EOG4J9MZ0.

PhylomeDB

Q14980.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

Q14980.

Bgee

Q14980.

CleanEx

HS_NUMA1.

Genevestigator

Q14980.

GermOnline

ENSG00000137497. Homo sapiens.

Family and domain databases

ProtoNet

Search...

Other

ChiTaRS

NUMA1. human.

GenomeRNAi

4926.

NextBio

18971.

SOURCE

Search...

Entry information

Entry name

NUMA1_HUMAN

Accession

Primary (citable) accession number: Q14980
Secondary accession number(s): H0YH75, Q14981

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	April 17, 2007
Last modified:	April 3, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.