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O75410 (TACC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transforming acidic coiled-coil-containing protein 1
Alternative name(s):
Gastric cancer antigen Ga55
Taxin-1
Gene names
Name:TACC1
Synonyms:KIAA1103
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length805 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Likely involved in the processes that promote cell division prior to the formation of differentiated tissues.

Subunit structure

Interacts with KIAA0097/CH-TOG and with the oncogenic transcription factor YEATS4. Interacts with AURKA, AURKB and AURKC. Interacts with LSM7, TDRD7 and SNRPG. Interacts with GCN5L2 and PCAF. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.23

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Nucleus during interphase. Weakly concentrated at centrosomes during mitosis and colocalizes with AURKC at the midbody during cytokinesis. Ref.14 Ref.23

Tissue specificity

Isoform 1, isoform 3 and isoform 5 are ubiquitous. Isoform 2 is strongly expressed in the brain, weakly detectable in lung and colon, and overexpressed in gastric cancer. Isoform 4 is not detected in normal tissues, but strong expression was found in gastric cancer tissues. Down-regulated in a subset of cases of breast cancer. Ref.9 Ref.12

Developmental stage

Expressed at high level during early embryogenesis.

Post-translational modification

Isoform 1 is heavily phosphorylated; isoform 6 is not. Ref.12 Ref.23

Sequence similarities

Belongs to the TACC family.

Contains 2 SPAZ (Ser/Pro-rich AZU-1) domains.

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O75410-1)

Also known as: A; Long;

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: O75410-2)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     464-464: T → TTTEQVKFLCFLL
Isoform 3 (identifier: O75410-3)

Also known as: E;

The sequence of this isoform differs from the canonical sequence as follows:
     1-195: Missing.
Isoform 4 (identifier: O75410-4)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     1-426: Missing.
     427-464: DPFKPTTTLT...PKKAKSRLIT → MGGSHSQTPR...EQVKFLCFLL
Isoform 5 (identifier: O75410-5)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-438: Missing.
     439-464: DFCSPTGNHVNEILESPKKAKSRLIT → MGGSHSQTPRGREPAGERHPRPTETA
Isoform 6 (identifier: O75410-6)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     54-54: S → R
     55-464: Missing.
Isoform 7 (identifier: O75410-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.
     42-53: EDSQAETKSLSF → MNNILKLK
     525-553: Missing.
Isoform 8 (identifier: O75410-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-651: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21
Chain2 – 805804Transforming acidic coiled-coil-containing protein 1
PRO_0000179986

Regions

Domain215 – 29783SPAZ 1
Domain359 – 507149SPAZ 2
Region2 – 5554Interaction with LSM7 and SNRPG
Region152 – 259108Interaction with TDRD7
Region206 – 427222Interaction with YEATS4
Region701 – 805105Interaction with CH-TOG
Coiled coil610 – 805196
Motif226 – 24116Bipartite nuclear localization signal 1 Potential
Motif455 – 47117Bipartite nuclear localization signal 2 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.21
Modified residue41Phosphoserine Ref.21
Modified residue101Phosphoserine Ref.21
Modified residue2281Phosphoserine; by AURKC Ref.23
Modified residue2761Phosphoserine Ref.20
Modified residue3811Phosphoserine By similarity
Modified residue5331Phosphotyrosine Ref.16

Natural variations

Alternative sequence1 – 651651Missing in isoform 8.
VSP_012640
Alternative sequence1 – 438438Missing in isoform 5.
VSP_012639
Alternative sequence1 – 426426Missing in isoform 4.
VSP_012641
Alternative sequence1 – 195195Missing in isoform 3.
VSP_012638
Alternative sequence1 – 4141Missing in isoform 7.
VSP_012637
Alternative sequence42 – 5312EDSQA…KSLSF → MNNILKLK in isoform 7.
VSP_012643
Alternative sequence541S → R in isoform 6.
VSP_012644
Alternative sequence55 – 464410Missing in isoform 6.
VSP_012645
Alternative sequence427 – 46438DPFKP…SRLIT → MGGSHSQTPRGREPAGERHP RPTETATTEQVKFLCFLL in isoform 4.
VSP_012642
Alternative sequence439 – 46426DFCSP…SRLIT → MGGSHSQTPRGREPAGERHP RPTETA in isoform 5.
VSP_012646
Alternative sequence4641T → TTTEQVKFLCFLL in isoform 2.
VSP_012647
Alternative sequence525 – 55329Missing in isoform 7.
VSP_012648
Natural variant1871P → L.
Corresponds to variant rs34235313 [ dbSNP | Ensembl ].
VAR_053703
Natural variant2431I → T.
Corresponds to variant rs6980553 [ dbSNP | Ensembl ].
VAR_053704
Natural variant2551E → G.
Corresponds to variant rs10107016 [ dbSNP | Ensembl ].
VAR_053705

Experimental info

Mutagenesis2281S → A: Impairs phosphorylation by AURKC. Ref.23
Sequence conflict2911L → I in AAC32327. Ref.1
Sequence conflict4281P → H in AAH41391. Ref.6
Sequence conflict5881G → V in BAA83055. Ref.7
Sequence conflict6541Missing in BAA83055. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) (Long) [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 3A261EF58C165107

FASTA80587,794
        10         20         30         40         50         60 
MAFSPWQILS PVQWAKWTWS AVRGGAAGED EAGGPEGDPE EEDSQAETKS LSFSSDSEGN 

        70         80         90        100        110        120 
FETPEAETPI RSPFKESCDP SLGLAGPGAK SQESQEADEQ LVAEVVEKCS SKTCSKPSEN 

       130        140        150        160        170        180 
EVPQQAIDSH SVKNFREEPE HDFSKISIVR PFSIETKDST DISAVLGTKA AHGCVTAVSG 

       190        200        210        220        230        240 
KALPSSPPDA LQDEAMTEGS MGVTLEASAE ADLKAGNSCP ELVPSRRSKL RKPKPVPLRK 

       250        260        270        280        290        300 
KAIGGEFSDT NAAVEGTPLP KASYHFSPEE LDENTSPLLG DARFQKSPPD LKETPGTLSS 

       310        320        330        340        350        360 
DTNDSGVELG EESRSSPLKL EFDFTEDTGN IEARKALPRK LGRKLGSTLT PKIQKDGISK 

       370        380        390        400        410        420 
SAGLEQPTDP VARDGPLSQT SSKPDPSQWE SPSFNPFGSH SVLQNSPPLS SEGSYHFDPD 

       430        440        450        460        470        480 
NFDESMDPFK PTTTLTSSDF CSPTGNHVNE ILESPKKAKS RLITSGCKVK KHETQSLALD 

       490        500        510        520        530        540 
ACSRDEGAVI SQISDISNRD GHATDEEKLA STSCGQKSAG AEVKGEPEED LEYFECSNVP 

       550        560        570        580        590        600 
VSTINHAFSS SEAGIEKETC QKMEEDGSTV LGLLESSAEK APVSVSCGGE SPLDGICLSE 

       610        620        630        640        650        660 
SDKTAVLTLI REEIITKEIE ANEWKKKYEE TRQEVLEMRK IVAEYEKTIA QMIEDEQRTS 

       670        680        690        700        710        720 
MTSQKSFQQL TMEKEQALAD LNSVERSLSD LFRRYENLKG VLEGFKKNEE ALKKCAQDYL 

       730        740        750        760        770        780 
ARVKQEEQRY QALKIHAEEK LDKANEEIAQ VRTKAKAESA ALHAGLRKEQ MKVESLERAL 

       790        800 
QQKNQEIEEL TKICDELIAK LGKTD 

« Hide

Isoform 2 (F) [UniParc].

Checksum: B9D4BDE7B742E813
Show »

FASTA81789,218
Isoform 3 (E) [UniParc].

Checksum: 802527D4B613A881
Show »

FASTA61067,073
Isoform 4 (D) [UniParc].

Checksum: A3CF1029DF65E860
Show »

FASTA37942,326
Isoform 5 (C) [UniParc].

Checksum: F1761EA28D5AB9A8
Show »

FASTA36740,903
Isoform 6 (Short) [UniParc].

Checksum: B29F0EA1DCAAF8E1
Show »

FASTA39543,984
Isoform 7 [UniParc].

Checksum: 385263AECC0C7060
Show »

FASTA73179,872
Isoform 8 [UniParc].

Checksum: F7CF945C5A3E277D
Show »

FASTA15417,815

References

« Hide 'large scale' references
[1]"Cloning of TACC1, an embryonically expressed, potentially transforming coiled coil containing gene, from the 8p11 breast cancer amplicon."
Still I.H., Hamilton M., Vince P., Wolfman A., Cowell J.K.
Oncogene 18:4032-4038(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Structure-function evolution of the transforming acidic coiled coil genes revealed by analysis of phylogenetically diverse organisms."
Still I.H., Vettaikkorumakankauv A.K., DiMatteo A., Liang P.
BMC Evol. Biol. 4:16-16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
[3]"Cloning of a novel human gene similar to TACC1."
Li F., Yao K.T.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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 7).
Tissue: Brain.
[7]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 364-805 (ISOFORM 2).
Tissue: Brain.
[8]"Serological identification and expression analysis of gastric cancer-associated genes."
Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.
Br. J. Cancer 86:1824-1830(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 450-805 (ISOFORM 2).
Tissue: Gastric adenocarcinoma.
[9]"Altered splicing pattern of TACC1 mRNA in gastric cancer."
Line A., Slucka Z., Stengrevics A., Li G., Rees R.C.
Cancer Genet. Cytogenet. 139:78-83(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-543 (ISOFORM 3), NUCLEOTIDE SEQUENCE OF 1-571 (ISOFORMS 4 AND 5), TISSUE SPECIFICITY.
Tissue: Stomach cancer.
[10]"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: CHARACTERIZATION.
Tissue: Brain, Fetal brain and Skeletal muscle.
[11]"Interaction of the transforming acidic coiled-coil 1 (TACC1) protein with ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein complexes in human cells."
Lauffart B., Howell S.J., Tasch J.E., Cowell J.K., Still I.H.
Biochem. J. 363:195-200(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIAA0097 AND YEATS4.
[12]"Carcinogenesis and translational controls: TACC1 is down-regulated in human cancers and associates with mRNA regulators."
Conte N., Charafe-Jauffret E., Delaval B., Adelaide J., Ginestier C., Geneix J., Isnardon D., Jacquemier J., Birnbaum D.
Oncogene 21:5619-5630(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LSM7 AND SNRPG, TISSUE SPECIFICITY, PHOSPHORYLATION.
[13]"TACC1-chTOG-Aurora A protein complex in breast cancer."
Conte N., Delaval B., Ginestier C., Ferrand A., Isnardon D., Larroque C., Prigent C., Seraphin B., Jacquemier J., Birnbaum D.
Oncogene 22:8102-8116(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIAA0097; LSM7; TDRD7 AND AURKA.
[14]"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.
[15]"Aurora B -TACC1 protein complex in cytokinesis."
Delaval B., Ferrand A., Conte N., Larroque C., Hernandez-Verdun D., Prigent C., Birnbaum D.
Oncogene 23:4516-4522(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AURKB.
[16]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[19]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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-276, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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].
[23]"Aurora-C interacts with and phosphorylates the transforming acidic coiled-coil 1 protein."
Gabillard J.C., Ulisse S., Baldini E., Sorrenti S., Cremet J.Y., Coccaro C., Prigent C., D'Armiento M., Arlot-Bonnemains Y.
Biochem. Biophys. Res. Commun. 408:647-653(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AURKC, PHOSPHORYLATION AT SER-228 BY AURKC, MUTAGENESIS OF SER-228.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF049910 mRNA. Translation: AAC32327.1.
AY177411 mRNA. Translation: AAO53446.1.
AY139007 mRNA. Translation: AAN28955.1.
AK314620 mRNA. Translation: BAG37186.1.
CH471080 Genomic DNA. Translation: EAW63293.1.
CH471080 Genomic DNA. Translation: EAW63296.1.
CH471080 Genomic DNA. Translation: EAW63298.1.
BC041391 mRNA. Translation: AAH41391.1.
AB029026 mRNA. Translation: BAA83055.1.
AY039239 mRNA. Translation: AAK68658.1.
AY072874 mRNA. Translation: AAL62461.1.
AY072875 mRNA. Translation: AAL62462.1.
AY072876 mRNA. Translation: AAL62463.2.
CCDSCCDS47845.1. [O75410-6]
CCDS55224.1. [O75410-3]
CCDS6109.1. [O75410-1]
RefSeqNP_001116296.1. NM_001122824.1. [O75410-6]
NP_001139688.1. NM_001146216.2. [O75410-3]
NP_006274.2. NM_006283.2. [O75410-1]
XP_005273682.1. XM_005273625.2. [O75410-2]
UniGeneHs.279245.

3D structure databases

ProteinModelPortalO75410.
SMRO75410. Positions 605-651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112730. 18 interactions.
IntActO75410. 13 interactions.
MINTMINT-8417725.

PTM databases

PhosphoSiteO75410.

Proteomic databases

MaxQBO75410.
PaxDbO75410.
PRIDEO75410.

Protocols and materials databases

DNASU6867.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276520; ENSP00000276520; ENSG00000147526. [O75410-6]
ENST00000317827; ENSP00000321703; ENSG00000147526. [O75410-1]
ENST00000330691; ENSP00000332794; ENSG00000147526. [O75410-4]
ENST00000348567; ENSP00000327818; ENSG00000147526. [O75410-5]
ENST00000379931; ENSP00000369263; ENSG00000147526. [O75410-2]
ENST00000518415; ENSP00000428706; ENSG00000147526. [O75410-7]
ENST00000520615; ENSP00000428450; ENSG00000147526. [O75410-3]
ENST00000521050; ENSP00000428949; ENSG00000147526.
ENST00000521642; ENSP00000428466; ENSG00000147526.
GeneID6867.
KEGGhsa:6867.
UCSCuc003xlz.3. human. [O75410-1]
uc003xma.3. human. [O75410-5]
uc003xmb.4. human. [O75410-7]
uc003xmf.4. human. [O75410-6]
uc003xmh.4. human. [O75410-2]

Organism-specific databases

CTD6867.
GeneCardsGC08P038586.
H-InvDBHIX0007462.
HGNCHGNC:11522. TACC1.
HPACAB017041.
HPA024702.
MIM605301. gene.
neXtProtNX_O75410.
Orphanet251579. Giant cell glioblastoma.
251576. Gliosarcoma.
PharmGKBPA36299.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83363.
HOVERGENHBG105967.
KOK14281.
OMASFQQLTM.
PhylomeDBO75410.
TreeFamTF333149.

Gene expression databases

ArrayExpressO75410.
BgeeO75410.
GenevestigatorO75410.

Family and domain databases

InterProIPR007707. TACC.
[Graphical view]
PANTHERPTHR13924. PTHR13924. 1 hit.
PfamPF05010. TACC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTACC1. human.
GeneWikiTACC1.
GenomeRNAi6867.
NextBio26803.
PMAP-CutDBO75410.
PROO75410.
SOURCESearch...

Entry information

Entry nameTACC1_HUMAN
AccessionPrimary (citable) accession number: O75410
Secondary accession number(s): B2RBD9 expand/collapse secondary AC list , D3DSX6, Q6Y687, Q86YG7, Q8IUJ2, Q8IUJ3, Q8IUJ4, Q8IZG2, Q8NEY7, Q9UPP9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 2005
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM