P42282 (TTKA_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein tramtrack, alpha isoform

Alternative name(s):
Repressor protein fushi tarazu
Tramtrack p88

Gene names

Name:	ttk
Synonyms:	FTZ-F2
ORF Names:	CG1856

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	813 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to a number of sites in the transcriptional regulatory region of ftz. Isoform alpha is required to repress genes that promote the R7 cell fate. Probable repressor of the transcription of the segmentation genes ftz, eve, h, odd, run, and en. May bind to the region 5'-AGGG[CT]GG-3'. Degradation of ttk is directed by binding of sinah or sina, via the adapter molecule phyl which binds to the BTB domain of ttk. Ref.1 Ref.7
Subunit structure	Interacts with CoRest/CG33525, suggesting that it acts by recruiting a CoRest-containing corepressor complex. Interacts with phyl. Ref.6 Ref.7
Subcellular location	Nucleus Probable.
Developmental stage	Expressed both maternally and zygotically. Expressed in preblastoderm embryos, followed by complete decay upon formation of the cellular blastoderm when ftz striped expression is at its peak.
Sequence similarities	Contains 1 BTB (POZ) domain. Contains 2 C2H2-type zinc fingers.
Caution	It is uncertain whether Met-1 or Met-3 is the initiator.
Sequence caution	The sequence CAA77786.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	R1/R6 development Inferred from mutant phenotype. Source: FlyBase R7 cell development Inferred from mutant phenotype. Source: FlyBase brain morphogenesis Inferred from mutant phenotype. Source: FlyBase branch fusion, open tracheal system Inferred from mutant phenotype. Source: FlyBase cell fate determination Traceable author statement. Source: FlyBase chitin-based cuticle development Inferred from mutant phenotype. Source: FlyBase compound eye cone cell differentiation Inferred from mutant phenotype. Source: FlyBase compound eye corneal lens morphogenesis Inferred from mutant phenotype. Source: FlyBase dendrite morphogenesis Inferred from mutant phenotype. Source: FlyBase dorsal appendage formation Inferred from mutant phenotype. Source: FlyBase dorsal trunk growth, open tracheal system Inferred from mutant phenotype. Source: FlyBase inter-male aggressive behavior Inferred from mutant phenotype. Source: FlyBase locomotion involved in locomotory behavior Inferred from mutant phenotype. Source: FlyBase negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.6. Source: FlyBase peripheral nervous system development Traceable author statement. Source: FlyBase regulation of embryonic cell shape Inferred from mutant phenotype. Source: FlyBase regulation of tube size, open tracheal system Inferred from mutant phenotype. Source: FlyBase startle response Inferred from mutant phenotype. Source: FlyBase tracheal outgrowth, open tracheal system Inferred from mutant phenotype. Source: FlyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay Ref.2. Source: FlyBase polytene chromosome Inferred from direct assay. Source: FlyBase
Molecular function	RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay Ref.2. Source: FlyBase chromatin binding Inferred from direct assay Ref.6. Source: FlyBase protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ebi	Q95RJ9	2	EBI-77008,EBI-421390
phyl	Q27934	10	EBI-77008,EBI-77033
sina	P21461	4	EBI-77008,EBI-77019

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha (identifier: P42282-1)

Also known as: p88; A; E;

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 Beta (identifier: P17789-1)

Also known as: p69; C; D; F;

The sequence of this isoform can be found in the external entry P17789.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 813	813	Protein tramtrack, alpha isoform		PRO_0000047078
Regions
	Domain	33 – 98	66	BTB
	Zinc finger	610 – 638	29	C2H2-type 1
	Zinc finger	646 – 669	24	C2H2-type 2
Amino acid modifications
	Modified residue	203	1	Phosphoserine Ref.8
	Modified residue	205	1	Phosphoserine Ref.8
	Modified residue	206	1	Phosphoserine Ref.8
	Modified residue	209	1	Phosphothreonine Ref.8
	Modified residue	682	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	186	1	L → V in CAA77785. Ref.2
	Sequence conflict	186	1	L → V in CAA77786. Ref.2
	Sequence conflict	358	1	P → R in CAA50633. Ref.1
	Sequence conflict	524	1	E → Q in CAA50633. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha (p88) (A) (E) [UniParc]. Last modified May 10, 2004. Version 3. Checksum: CF3EE14069C79AA2	FASTA	813	88,383
	10 20 30 40 50 60 MKMASQRFCL RWNNHQSNLL SVFDQLLHAE TFTDVTLAVE GQHLKAHKMV LSACSPYFNT 70 80 90 100 110 120 LFVSHPEKHP IVILKDVPYS DMKSLLDFMY RGEVSVDQER LTAFLRVAES LRIKGLTEVN 130 140 150 160 170 180 DDKPSPAAAA AGAGATGSES TATTPQLQRI QPYLVPQRNR SQAGGLLASA ANAGNTPTLP 190 200 210 220 230 240 VQPSLLSSAL MPKRKRGRPR KLSGSSNGTG NDYDDFDREN MMNDSSDLGN GKMCNESYSG 250 260 270 280 290 300 NDDGSDDNQP NAGHTDDLNE SRDSLPSKRS KNSKDHRVVS HHEDNSTSVT PTKATPELSQ 310 320 330 340 350 360 RLFGSSSTTI SATAPGGSST GPSETISLLE ISDERESAPV HLPTILGLKI RAINTTTPAQ 370 380 390 400 410 420 QGSPQTPTKS KPKIRQATGS NNSNSLLKQQ LRGGAKDPEV PPATRITGAV TPNAALNAEE 430 440 450 460 470 480 QSKEMPKKNQ DEVNACIGLH SLANAAEQQA AQVASTGNLH HQLLLHMAAN NSMLNTTDYY 490 500 510 520 530 540 QQQQQESPSS AGQFMDDDLE LLSLNDQQDK SDEPDHEMVT LADENAGLPG YQGNEAEATP 550 560 570 580 590 600 AQEDSPAAET ATAPPPAPRS GKKGAKRPIQ RRRVRRKAQS TLDDQAEHLT EMSVRGLDLF 610 620 630 640 650 660 RYASVVEGVY RCTECAKENM QKTFKNKYSF QRHAFLYHEG KHRKVFPCPV CSKEFSRPDK 670 680 690 700 710 720 MKNHLKMTHE NFTPPKDIGA FSPLKYLISA AAAGDMHATI YQQQQDHYHR QLAEQLEQQN 730 740 750 760 770 780 ASFDSRDSSL ILPDVKMEHA EDQDAEQEAE LSDGGYDASN PAAAAAAMLS LQQDVIIKDE 790 800 810 IQISPSPSPT PPASCAVAEG KSLALASTAQ TAT
	Isoform Beta (p69) (C) (D) (F) [UniParc]. See P17789.		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tramtrack is a transcriptional repressor required for cell fate determination in the Drosophila eye." Xiong W.C., Montell C. Genes Dev. 7:1085-1096(1993) [PubMed: 8504931] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"Alternatively spliced transcripts of the Drosophila tramtrack gene encode zinc finger proteins with distinct DNA binding specificities." Read D., Manley J.L. EMBO J. 11:1035-1044(1992) [PubMed: 1372245] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DNA-BINDING. Tissue: Embryo.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[5]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-487. Strain: Berkeley.
[6]	"A conserved role but different partners for the transcriptional corepressor CoREST in fly and mammalian nervous system formation." Dallman J.E., Allopenna J., Bassett A., Travers A., Mandel G. J. Neurosci. 24:7186-7193(2004) [PubMed: 15306652] [Abstract] Cited for: INTERACTION WITH CG33525.
[7]	"Two modes of degradation of the tramtrack transcription factors by Siah homologues." Cooper S.E., Murawsky C.M., Lowe N., Travers A.A. J. Biol. Chem. 283:1076-1083(2008) [PubMed: 17962185] [Abstract] Cited for: FUNCTION, INTERACTION WITH PHYL.
[8]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-205; SER-206; THR-209 AND SER-682, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X71626 mRNA. Translation: CAA50633.1. Z11723 mRNA. Translation: CAA77785.1. Z11723 mRNA. Translation: CAA77786.1. Different initiation. AE014297 Genomic DNA. Translation: AAF57179.1. AE014297 Genomic DNA. Translation: AAF57180.1. AE014297 Genomic DNA. Translation: AAN14282.1. BT025183 mRNA. Translation: ABF00108.1.
PIR	S36018.
RefSeq	NP_001189329.1. NM_001202400.1. NP_733443.1. NM_170564.2. NP_733444.1. NM_170565.1. NP_733445.1. NM_170566.2.
UniGene	Dm.1526.
3D structure databases
ProteinModelPortal	P42282.
SMR	P42282. Positions 9-125, 558-676.
ModBase	Search...
Protein-protein interaction databases
IntAct	P42282. 11 interactions.
MINT	MINT-282844.
STRING	P42282.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0085825; FBpp0085186; FBgn0003870. FBtr0085827; FBpp0085188; FBgn0003870. FBtr0085829; FBpp0085190; FBgn0003870. FBtr0303227; FBpp0292319; FBgn0003870.
GeneID	48317.
KEGG	dme:Dmel_CG1856.
Organism-specific databases
CTD	7272.
FlyBase	FBgn0003870. ttk.
Phylogenomic databases
eggNOG	inNOG08918.
GeneTree	EMGT00050000002223.
InParanoid	P42282.
OrthoDB	EOG4ZCRMW.
PhylomeDB	P42282.
Gene expression databases
ArrayExpress	P42282.
Bgee	P42282.
GermOnline	CG1856. Drosophila melanogaster.
Family and domain databases
InterPro	IPR017956. AT_hook_DNA-bd_motif. IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. IPR013069. BTB_POZ. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.30.710.10. BTB/POZ_fold. 1 hit. G3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 1 hit.
KO	K09237.
Pfam	PF00651. BTB. 1 hit. PF00096. zf-C2H2. 1 hit. [Graphical view]
SMART	SM00384. AT_hook. 1 hit. SM00225. BTB. 1 hit. SM00355. ZnF_C2H2. 2 hits. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
PROSITE	PS50097. BTB. 1 hit. PS00028. ZINC_FINGER_C2H2_1. 1 hit. PS50157. ZINC_FINGER_C2H2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	839310.

Entry information

Entry name

TTKA_DROME

Accession

Primary (citable) accession number: P42282
Secondary accession number(s): A4V3Q3 , Q0KHY0, Q1LZ43, Q24313, Q9V9V2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	May 10, 2004
Last modified:	January 25, 2012
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project