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Protein

Transforming acidic coiled-coil-containing protein 2

Gene

TACC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity). May play a role in organizing centrosomal microtubules. May act as a tumor suppressor protein. May represent a tumor progression marker.By similarity1 Publication

GO - Molecular functioni

  • nuclear hormone receptor binding Source: MGI

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming acidic coiled-coil-containing protein 2
Alternative name(s):
Anti-Zuai-1
Short name:
AZU-1
Gene namesi
Name:TACC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:11523. TACC2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36300.

Polymorphism and mutation databases

BioMutaiTACC2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 29482948Transforming acidic coiled-coil-containing protein 2PRO_0000179988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971PhosphoserineCombined sources
Modified residuei201 – 2011PhosphoserineCombined sources
Modified residuei269 – 2691PhosphoserineCombined sources
Modified residuei493 – 4931PhosphoserineCombined sources
Modified residuei561 – 5611PhosphoserineCombined sources
Modified residuei571 – 5711PhosphoserineCombined sources
Modified residuei575 – 5751PhosphoserineCombined sources
Modified residuei758 – 7581PhosphoserineCombined sources
Modified residuei962 – 9621PhosphoserineCombined sources
Modified residuei1025 – 10251PhosphoserineCombined sources
Modified residuei1267 – 12671PhosphoserineCombined sources
Modified residuei1313 – 13131PhosphoserineCombined sources
Modified residuei1562 – 15621PhosphoserineCombined sources
Modified residuei2072 – 20721PhosphoserineCombined sources
Modified residuei2161 – 21611PhosphoserineBy similarity
Modified residuei2226 – 22261PhosphoserineCombined sources
Modified residuei2246 – 22461PhosphothreonineCombined sources
Modified residuei2256 – 22561PhosphoserineCombined sources
Modified residuei2317 – 23171PhosphoserineCombined sources
Modified residuei2321 – 23211PhosphoserineCombined sources
Modified residuei2359 – 23591PhosphoserineCombined sources
Modified residuei2389 – 23891PhosphoserineCombined sources
Modified residuei2392 – 23921PhosphoserineBy similarity
Modified residuei2394 – 23941PhosphoserineCombined sources
Modified residuei2403 – 24031PhosphoserineCombined sources
Modified residuei2430 – 24301PhosphothreonineCombined sources
Modified residuei2451 – 24511PhosphothreonineCombined sources
Modified residuei2455 – 24551PhosphothreonineCombined sources
Modified residuei2458 – 24581PhosphothreonineCombined sources
Modified residuei2512 – 25121PhosphoserineCombined sources
Modified residuei2534 – 25341PhosphoserineCombined sources
Modified residuei2553 – 25531PhosphothreonineBy similarity
Modified residuei2557 – 25571PhosphoserineCombined sources
Modified residuei2569 – 25691PhosphoserineCombined sources
Isoform 2 (identifier: O95359-2)
Modified residuei325 – 3251PhosphothreonineCombined sources
Isoform 3 (identifier: O95359-3)
Modified residuei2625 – 26251PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylated by TTK; which is required for localization in centrosome.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO95359.
MaxQBiO95359.
PaxDbiO95359.
PeptideAtlasiO95359.
PRIDEiO95359.

PTM databases

iPTMnetiO95359.
PhosphoSiteiO95359.

Expressioni

Tissue specificityi

Strongly expressed in heart, skeletal muscle, brain, prostate, thyroid and trachea.2 Publications

Developmental stagei

Expressed in fetal brain, lung, liver and kidney.1 Publication

Gene expression databases

BgeeiO95359.
ExpressionAtlasiO95359. baseline and differential.
GenevisibleiO95359. HS.

Organism-specific databases

HPAiHPA031020.
HPA031021.

Interactioni

Subunit structurei

Interacts with CCDC100/CEP120 (By similarity). Interacts with microtubules. Interacts with YEATS4, GCN5L2 and PCAF.By similarity2 Publications

GO - Molecular functioni

  • nuclear hormone receptor binding Source: MGI

Protein-protein interaction databases

BioGridi115830. 22 interactions.
IntActiO95359. 3 interactions.
MINTiMINT-1203853.
STRINGi9606.ENSP00000334280.

Structurei

3D structure databases

ProteinModelPortaliO95359.
SMRiO95359. Positions 2902-2945.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2315 – 240389SPAZAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2675 – 270329Sequence analysisAdd
BLAST
Coiled coili2746 – 2947202Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi482 – 54968Pro-richAdd
BLAST
Compositional biasi1956 – 201661Pro-richAdd
BLAST
Compositional biasi2420 – 24234Poly-Lys

Sequence similaritiesi

Belongs to the TACC family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IIVK. Eukaryota.
ENOG410YMFS. LUCA.
GeneTreeiENSGT00530000063855.
HOVERGENiHBG093142.
InParanoidiO95359.
KOiK14282.
OMAiFQTSEPR.
OrthoDBiEOG7FNC6K.
PhylomeDBiO95359.
TreeFamiTF333149.

Family and domain databases

InterProiIPR007707. TACC.
[Graphical view]
PfamiPF05010. TACC. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 4 (identifier: O95359-4) [UniParc]FASTAAdd to basket

Also known as: Long, TACC2s

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
MGNENSTSDN QRTLSAQTPR SAQPPGNSQN IKRKQQDTPG SPDHRDASSI
60 70 80 90 100
GSVGLGGFCT ASESSASLDP CLVSPEVTEP RKDPQGARGP EGSLLPSPPP
110 120 130 140 150
SQEREHPSSS MPFAECPPEG CLASPAAAPE DGPQTQSPRR EPAPNAPGDI
160 170 180 190 200
AAAFPAERDS STPYQEIAAV PSAGRERQPK EEGQKSSFSF SSGIDQSPGM
210 220 230 240 250
SPVPLREPMK APLCGEGDQP GGFESQEKEA AGGFPPAESR QGVASVQVTP
260 270 280 290 300
EAPAAAQQGT ESSAVLEKSP LKPMAPIPQD PAPRASDRER GQGEAPPQYL
310 320 330 340 350
TDDLEFLRAC HLPRSNSGAA PEAEVNAASQ ESCQQPVGAY LPHAELPWGL
360 370 380 390 400
PSPALVPEAG GSGKEALDTI DVQGHPQTGM RGTKPNQVVC VAAGGQPEGG
410 420 430 440 450
LPVSPEPSLL TPTEEAHPAS SLASFPAAQI PIAVEEPGSS SRESVSKAGM
460 470 480 490 500
PVSADAAKEV VDAGLVGLER QVSDLGSKGE HPEGDPGEVP APSPQERGEH
510 520 530 540 550
LNTEQSHEVQ PGVPPPPLPK EQSHEVQPGA PPPPLPKAPS ESARGPPGPT
560 570 580 590 600
DGAKVHEDST SPAVAKEGSR SPGDSPGGKE EAPEPPDGGD PGNLQGEDSQ
610 620 630 640 650
AFSSKRDPEV GKDELSKPSS DAESRDHPSS HSAQPPRKGG AGHTDGPHSQ
660 670 680 690 700
TAEADASGLP HKLGEEDPVL PPVPDGAGEP TVPEGAIWEG SGLQPKCPDT
710 720 730 740 750
LQSREGLGRM ESFLTLESEK SDFPPTPVAE VAPKAQEGES TLEIRKMGSC
760 770 780 790 800
DGEGLLTSPD QPRGPACDAS RQEFHAGVPH PPQGENLAAD LGLTALILDQ
810 820 830 840 850
DQQGIPSCPG EGWIRGAASE WPLLSSEKHL QPSQAQPETS IFDVLKEQAQ
860 870 880 890 900
PPENGKETSP SHPGFKDQGA DSSQIHVPVE PQEDNNLPTH GGQEQALGSE
910 920 930 940 950
LQSQLPKGTL SDTPTSSPTD MVWESSLTEE SELSAPTRQK LPALGEKRPE
960 970 980 990 1000
GACGDGQSSR VSPPAADVLK DFSLAGNFSR KETCCTGQGP NKSQQALADA
1010 1020 1030 1040 1050
LEEGSQHEEA CQRHPGASEA ADGCSPLWGL SKREMASGNT GEAPPCQPDS
1060 1070 1080 1090 1100
VALLDAVPCL PALAPASPGV TPTQDAPETE ACDETQEGRQ QPVPAPQQKM
1110 1120 1130 1140 1150
ECWATSDAES PKLLASFPSA GEQGGEAGAA ETGGSAGAGD PGKQQAPEKP
1160 1170 1180 1190 1200
GEATLSCGLL QTEHCLTSGE EASTSALRES CQAEHPMASC QDALLPAREL
1210 1220 1230 1240 1250
GGIPRSTMDF STHQAVPDPK ELLLSGPPEV AAPDTPYLHV DSAAQRGAED
1260 1270 1280 1290 1300
SGVKAVSSAD PRAPGESPCP VGEPPLALEN AASLKLFAGS LAPLLQPGAA
1310 1320 1330 1340 1350
GGEIPAVQAS SGSPKARTTE GPVDSMPCLD RMPLLAKGKQ ATGEEKAATA
1360 1370 1380 1390 1400
PGAGAKASGE GMAGDAAGET EGSMERMGEP SQDPKQGTSG GVDTSSEQIA
1410 1420 1430 1440 1450
TLTGFPDFRE HIAKIFEKPV LGALATPGEK AGAGRSAVGK DLTRPLGPEK
1460 1470 1480 1490 1500
LLDGPPGVDV TLLPAPPARL QVEKKQQLAG EAEISHLALQ DPASDKLLGP
1510 1520 1530 1540 1550
AGLTWERNLP GAGVGKEMAG VPPTLREDER PEGPGAAWPG LEGQAYSQLE
1560 1570 1580 1590 1600
RSRQELASGL PSPAATQELP VERAAAFQVA PHSHGEEAVA QDRIPSGKQH
1610 1620 1630 1640 1650
QETSACDSPH GEDGPGDFAH TGVPGHVPRS TCAPSPQREV LTVPEANSEP
1660 1670 1680 1690 1700
WTLDTLGGER RPGVTAGILE MRNALGNQST PAPPTGEVAD TPLEPGKVAG
1710 1720 1730 1740 1750
AAGEAEGDIT LSTAETQACA SGDLPEAGTT RTFSVVAGDL VLPGSCQDPA
1760 1770 1780 1790 1800
CSDKAPGMEG TAALHGDSPA RPQQAKEQPG PERPIPAGDG KVCVSSPPEP
1810 1820 1830 1840 1850
DETHDPKLQH LAPEELHTDR ESPRPGPSML PSVPKKDAPR VMDKVTSDET
1860 1870 1880 1890 1900
RGAEGTESSP VADDIIQPAA PADLESPTLA ASSYHGDVVG QVSTDLIAQS
1910 1920 1930 1940 1950
ISPAAAHAGL PPSAAEHIVS PSAPAGDRVE ASTPSCPDPA KDLSRSSDSE
1960 1970 1980 1990 2000
EAFETPESTT PVKAPPAPPP PPPEVIPEPE VSTQPPPEEP GCGSETVPVP
2010 2020 2030 2040 2050
DGPRSDSVEG SPFRPPSHSF SAVFDEDKPI ASSGTYNLDF DNIELVDTFQ
2060 2070 2080 2090 2100
TLEPRASDAK NQEGKVNTRR KSTDSVPISK STLSRSLSLQ ASDFDGASSS
2110 2120 2130 2140 2150
GNPEAVALAP DAYSTGSSSA SSTLKRTKKP RPPSLKKKQT TKKPTETPPV
2160 2170 2180 2190 2200
KETQQEPDEE SLVPSGENLA SETKTESAKT EGPSPALLEE TPLEPAVGPK
2210 2220 2230 2240 2250
AACPLDSESA EGVVPPASGG GRVQNSPPVG RKTLPLTTAP EAGEVTPSDS
2260 2270 2280 2290 2300
GGQEDSPAKG LSVRLEFDYS EDKSSWDNQQ ENPPPTKKIG KKPVAKMPLR
2310 2320 2330 2340 2350
RPKMKKTPEK LDNTPASPPR SPAEPNDIPI AKGTYTFDID KWDDPNFNPF
2360 2370 2380 2390 2400
SSTSKMQESP KLPQQSYNFD PDTCDESVDP FKTSSKTPSS PSKSPASFEI
2410 2420 2430 2440 2450
PASAMEANGV DGDGLNKPAK KKKTPLKTDT FRVKKSPKRS PLSDPPSQDP
2460 2470 2480 2490 2500
TPAATPETPP VISAVVHATD EEKLAVTNQK WTCMTVDLEA DKQDYPQPSD
2510 2520 2530 2540 2550
LSTFVNETKF SSPTEELDYR NSYEIEYMEK IGSSLPQDDD APKKQALYLM
2560 2570 2580 2590 2600
FDTSQESPVK SSPVRMSESP TPCSGSSFEE TEALVNTAAK NQHPVPRGLA
2610 2620 2630 2640 2650
PNQESHLQVP EKSSQKELEA MGLGTPSEAI EITAPEGSFA SADALLSRLA
2660 2670 2680 2690 2700
HPVSLCGALD YLEPDLAEKN PPLFAQKLQE ELEFAIMRIE ALKLARQIAL
2710 2720 2730 2740 2750
ASRSHQDAKR EAAHPTDVSI SKTALYSRIG TAEVEKPAGL LFQQPDLDSA
2760 2770 2780 2790 2800
LQIARAEIIT KEREVSEWKD KYEESRREVM EMRKIVAEYE KTIAQMIEDE
2810 2820 2830 2840 2850
QREKSVSHQT VQQLVLEKEQ ALADLNSVEK SLADLFRRYE KMKEVLEGFR
2860 2870 2880 2890 2900
KNEEVLKRCA QEYLSRVKKE EQRYQALKVH AEEKLDRANA EIAQVRGKAQ
2910 2920 2930 2940
QEQAAHQASL RKEQLRVDAL ERTLEQKNKE IEELTKICDE LIAKMGKS
Length:2,948
Mass (Da):309,427
Last modified:January 9, 2007 - v3
Checksum:i9DC4CC5231A5ADBD
GO
Isoform 1 (identifier: O95359-1) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-1922: Missing.
     1923-1945: APAGDRVEASTPSCPDPAKDLSR → MGGSQSLQPAPASDLNLEASEAM

Show »
Length:1,026
Mass (Da):112,111
Checksum:iE2575FCB446E9CF8
GO
Isoform 2 (identifier: O95359-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2296: Missing.
     2429-2432: Missing.
     2633-2709: Missing.

Show »
Length:571
Mass (Da):64,156
Checksum:i0C89A2D8C537269B
GO
Isoform 3 (identifier: O95359-3) [UniParc]FASTAAdd to basket

Also known as: ECTACC

The sequence of this isoform differs from the canonical sequence as follows:
     2633-2709: Missing.

Show »
Length:2,871
Mass (Da):301,058
Checksum:iFC2C1DE101824B9D
GO
Isoform 5 (identifier: O95359-5) [UniParc]FASTAAdd to basket

Also known as: TACC21

The sequence of this isoform differs from the canonical sequence as follows:
     49-1857: Missing.
     1900-1944: Missing.

Show »
Length:1,094
Mass (Da):119,359
Checksum:i99E9A4FC30C86B52
GO
Isoform 6 (identifier: O95359-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1922: Missing.
     1923-1945: APAGDRVEASTPSCPDPAKDLSR → MGGSQSLQPAPASDLNLEASEAM
     2680-2709: Missing.

Show »
Length:996
Mass (Da):108,690
Checksum:iE1DCE1E83FB72A71
GO

Sequence cautioni

The sequence AAF29537.2 differs from that shown.Intron retention.Curated
The sequence AAF63433.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2896 – 28961R → Q in AAO62629 (PubMed:12620397).Curated
Sequence conflicti2896 – 28961R → Q in AAO62630 (PubMed:12620397).Curated
Sequence conflicti2909 – 29091S → T in AAH39311 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701V → I.
Corresponds to variant rs11200385 [ dbSNP | Ensembl ].
VAR_053706
Natural varianti798 – 7981L → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_036381
Natural varianti830 – 8301L → F.1 Publication
Corresponds to variant rs10887063 [ dbSNP | Ensembl ].
VAR_053707
Natural varianti1103 – 11031W → R.1 Publication
Corresponds to variant rs7073433 [ dbSNP | Ensembl ].
VAR_053708
Natural varianti1347 – 13471A → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_036382
Natural varianti1425 – 14251A → T.
Corresponds to variant rs4752642 [ dbSNP | Ensembl ].
VAR_053709
Natural varianti1492 – 14921P → L.
Corresponds to variant rs7920896 [ dbSNP | Ensembl ].
VAR_053710
Natural varianti1916 – 19161E → K.
Corresponds to variant rs12765679 [ dbSNP | Ensembl ].
VAR_053711
Natural varianti2078 – 20781I → T.
Corresponds to variant rs7083331 [ dbSNP | Ensembl ].
VAR_029803
Natural varianti2102 – 21021N → S.
Corresponds to variant rs3750843 [ dbSNP | Ensembl ].
VAR_020478
Natural varianti2197 – 21971V → A.
Corresponds to variant rs2295873 [ dbSNP | Ensembl ].
VAR_020479
Natural varianti2210 – 22101A → V.
Corresponds to variant rs2295874 [ dbSNP | Ensembl ].
VAR_029804
Natural varianti2216 – 22161P → L.
Corresponds to variant rs2295875 [ dbSNP | Ensembl ].
VAR_053712
Natural varianti2261 – 22611L → H.
Corresponds to variant rs2295876 [ dbSNP | Ensembl ].
VAR_020480
Natural varianti2271 – 22711E → D.
Corresponds to variant rs11200483 [ dbSNP | Ensembl ].
VAR_053713
Natural varianti2718 – 27181V → I.
Corresponds to variant rs2295878 [ dbSNP | Ensembl ].
VAR_020481
Natural varianti2732 – 27321A → T.1 Publication
Corresponds to variant rs2295879 [ dbSNP | Ensembl ].
VAR_020482
Natural varianti2900 – 29001Q → K.1 Publication
Corresponds to variant rs1063627 [ dbSNP | Ensembl ].
VAR_029805

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 22962296Missing in isoform 2. 1 PublicationVSP_022151Add
BLAST
Alternative sequencei1 – 19221922Missing in isoform 1 and isoform 6. 2 PublicationsVSP_022153Add
BLAST
Alternative sequencei49 – 18571809Missing in isoform 5. 1 PublicationVSP_022154Add
BLAST
Alternative sequencei1900 – 194445Missing in isoform 5. 1 PublicationVSP_022155Add
BLAST
Alternative sequencei1923 – 194523APAGD…KDLSR → MGGSQSLQPAPASDLNLEAS EAM in isoform 1 and isoform 6. 2 PublicationsVSP_022156Add
BLAST
Alternative sequencei2429 – 24324Missing in isoform 2. 1 PublicationVSP_006368
Alternative sequencei2633 – 270977Missing in isoform 2 and isoform 3. 3 PublicationsVSP_006369Add
BLAST
Alternative sequencei2680 – 270930Missing in isoform 6. 1 PublicationVSP_022158Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176646 mRNA. Translation: AAF63433.1. Different initiation.
AF095791 mRNA. Translation: AAC64968.2.
AF528098 mRNA. Translation: AAO62629.1.
AF528099 mRNA. Translation: AAO62630.1.
AL135793, AC063960 Genomic DNA. Translation: CAI95127.1.
AL135793 Genomic DNA. Translation: CAI95128.1.
AL135793 Genomic DNA. Translation: CAI95131.1.
AL135793, AC063960 Genomic DNA. Translation: CAI95134.1.
BC000999 mRNA. Translation: AAH00999.1.
BC039311 mRNA. Translation: AAH39311.1.
AF220152 mRNA. Translation: AAF29537.2. Sequence problems.
AL713712 mRNA. Translation: CAD28509.1.
CCDSiCCDS7625.1. [O95359-5]
CCDS7626.1. [O95359-4]
CCDS7627.1. [O95359-1]
CCDS7628.1. [O95359-6]
RefSeqiNP_001278807.1. NM_001291878.1.
NP_008928.1. NM_006997.3. [O95359-1]
NP_996742.1. NM_206860.2. [O95359-6]
NP_996743.1. NM_206861.2. [O95359-5]
NP_996744.3. NM_206862.3.
UniGeneiHs.501252.
Hs.713875.

Genome annotation databases

EnsembliENST00000260733; ENSP00000260733; ENSG00000138162. [O95359-1]
ENST00000334433; ENSP00000334280; ENSG00000138162. [O95359-4]
ENST00000358010; ENSP00000350701; ENSG00000138162. [O95359-5]
ENST00000360561; ENSP00000353763; ENSG00000138162. [O95359-6]
ENST00000369000; ENSP00000357996; ENSG00000138162. [O95359-2]
ENST00000369005; ENSP00000358001; ENSG00000138162. [O95359-4]
ENST00000513429; ENSP00000425062; ENSG00000138162. [O95359-5]
GeneIDi10579.
KEGGihsa:10579.
UCSCiuc001lfv.4. human. [O95359-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176646 mRNA. Translation: AAF63433.1. Different initiation.
AF095791 mRNA. Translation: AAC64968.2.
AF528098 mRNA. Translation: AAO62629.1.
AF528099 mRNA. Translation: AAO62630.1.
AL135793, AC063960 Genomic DNA. Translation: CAI95127.1.
AL135793 Genomic DNA. Translation: CAI95128.1.
AL135793 Genomic DNA. Translation: CAI95131.1.
AL135793, AC063960 Genomic DNA. Translation: CAI95134.1.
BC000999 mRNA. Translation: AAH00999.1.
BC039311 mRNA. Translation: AAH39311.1.
AF220152 mRNA. Translation: AAF29537.2. Sequence problems.
AL713712 mRNA. Translation: CAD28509.1.
CCDSiCCDS7625.1. [O95359-5]
CCDS7626.1. [O95359-4]
CCDS7627.1. [O95359-1]
CCDS7628.1. [O95359-6]
RefSeqiNP_001278807.1. NM_001291878.1.
NP_008928.1. NM_006997.3. [O95359-1]
NP_996742.1. NM_206860.2. [O95359-6]
NP_996743.1. NM_206861.2. [O95359-5]
NP_996744.3. NM_206862.3.
UniGeneiHs.501252.
Hs.713875.

3D structure databases

ProteinModelPortaliO95359.
SMRiO95359. Positions 2902-2945.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115830. 22 interactions.
IntActiO95359. 3 interactions.
MINTiMINT-1203853.
STRINGi9606.ENSP00000334280.

PTM databases

iPTMnetiO95359.
PhosphoSiteiO95359.

Polymorphism and mutation databases

BioMutaiTACC2.

Proteomic databases

EPDiO95359.
MaxQBiO95359.
PaxDbiO95359.
PeptideAtlasiO95359.
PRIDEiO95359.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260733; ENSP00000260733; ENSG00000138162. [O95359-1]
ENST00000334433; ENSP00000334280; ENSG00000138162. [O95359-4]
ENST00000358010; ENSP00000350701; ENSG00000138162. [O95359-5]
ENST00000360561; ENSP00000353763; ENSG00000138162. [O95359-6]
ENST00000369000; ENSP00000357996; ENSG00000138162. [O95359-2]
ENST00000369005; ENSP00000358001; ENSG00000138162. [O95359-4]
ENST00000513429; ENSP00000425062; ENSG00000138162. [O95359-5]
GeneIDi10579.
KEGGihsa:10579.
UCSCiuc001lfv.4. human. [O95359-4]

Organism-specific databases

CTDi10579.
GeneCardsiTACC2.
HGNCiHGNC:11523. TACC2.
HPAiHPA031020.
HPA031021.
MIMi605302. gene.
neXtProtiNX_O95359.
PharmGKBiPA36300.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIVK. Eukaryota.
ENOG410YMFS. LUCA.
GeneTreeiENSGT00530000063855.
HOVERGENiHBG093142.
InParanoidiO95359.
KOiK14282.
OMAiFQTSEPR.
OrthoDBiEOG7FNC6K.
PhylomeDBiO95359.
TreeFamiTF333149.

Miscellaneous databases

ChiTaRSiTACC2. human.
GeneWikiiTACC2.
GenomeRNAii10579.
PROiO95359.
SOURCEiSearch...

Gene expression databases

BgeeiO95359.
ExpressionAtlasiO95359. baseline and differential.
GenevisibleiO95359. HS.

Family and domain databases

InterProiIPR007707. TACC.
[Graphical view]
PfamiPF05010. TACC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "AZU-1: a candidate breast tumor suppressor and biomarker for tumor progression."
    Chen H.-M., Schmeichel K.L., Mian I.S., Lelievre S., Petersen O.W., Bissell M.J.
    Mol. Biol. Cell 11:1357-1367(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION.
  2. "The TACC domain identifies a family of centrosomal proteins that can interact with microtubules."
    Gergely F., Karlsson C., Still I.H., Cowell J.K., Kilmartin J., Raff J.W.
    Proc. Natl. Acad. Sci. U.S.A. 97:14352-14357(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain, Fetal brain and Skeletal muscle.
  3. "Molecular cloning, genomic structure and interactions of the putative breast tumor suppressor TACC2."
    Lauffart B., Gangisetty O., Still I.H.
    Genomics 81:192-201(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH YEATS4, VARIANTS PHE-830; ARG-1103 AND LYS-2900.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 6).
    Tissue: Placenta and Testis.
  6. "Cloning and structural characterization of ECTACC, a new member of the transforming acidic coiled coil (TACC) gene family: cDNA sequence and expression analysis in human microvascular endothelial cells."
    Pu J.J., Li C., Rodriguez M., Banerjee D.
    Cytokine 13:129-137(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1990-2948 (ISOFORM 3), TISSUE SPECIFICITY.
    Tissue: Endothelial cell.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2065-2948 (ISOFORM 3), VARIANT THR-2732.
    Tissue: Brain.
  8. "TTK kinase is essential for the centrosomal localization of TACC2."
    Dou Z., Ding X., Zereshki A., Zhang Y., Zhang J., Wang F., Sun J., Huang H., Yao X.
    FEBS Lett. 572:51-56(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
  9. "The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases."
    Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.
    Oncogene 23:2559-2563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCN5L2 AND PCAF, SUBCELLULAR LOCATION.
  10. "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-2317 AND SER-2321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-2256 AND SER-2512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-201; SER-571; SER-575; SER-758; SER-962; SER-1025; SER-1267; SER-1313; SER-1562; SER-2072; THR-2246; SER-2256; SER-2317; SER-2321; SER-2359; SER-2389; SER-2394; SER-2403 AND SER-2512, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-325 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2625 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-197; SER-201; SER-269; SER-493; SER-561; SER-2226; THR-2246; SER-2256; SER-2317; SER-2321; THR-2451; THR-2455; THR-2458; SER-2512 AND SER-2557, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-2072; SER-2256; SER-2317 AND SER-2321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2256; SER-2317; THR-2430; SER-2512; SER-2534 AND SER-2569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2072; SER-2226 AND SER-2317, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-798 AND SER-1347.

Entry informationi

Entry nameiTACC2_HUMAN
AccessioniPrimary (citable) accession number: O95359
Secondary accession number(s): Q4VXL0
, Q4VXL3, Q4VXL6, Q4VXL7, Q5U5T7, Q86WG6, Q86WG7, Q8TCK9, Q9BVQ1, Q9NZ41, Q9NZR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 9, 2007
Last modified: July 6, 2016
This is version 143 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.