IKI3/YLR384C Protein Information

Standard Name	Iki3p 1
Systematic Name	Ylr384cp
Alias	Elp1p 2 , Tot1p 3 , Kti7p 4
ORF Classification	Verified
Description	Subunit of Elongator complex, which is required for modification of wobble nucleosides in tRNA; maintains structural integrity of Elongator; homolog of human IKAP, mutations in which cause familial dysautonomia (FD) (5, 6, 7, 8)
Name Description	Insensitive to KIller toxin 1

Experimental Data
Molecules/cell	10500 9

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,349
Molecular Weight (Da)	152,989
Isoelectric Point (pI)	4.79

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Iki3p (InterPro)
Physical Interactions	There are 99 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000005324A \| Q06706 MIPS: YLR384C NCBI: 2116970 \| 2498477 \| 398366061 \| 609430 \| NP_013488.3 GenBank/EMBL/DDBJ: DAA09685.1 \| D87841 \| U19104

Amino Acid Sequence (or in FASTA format)
1 MVEHDKSGSK RQELRSNMRN LITLNKGKFK PTASTAEGDE DDLSFTLLDS 51 VFDTLSDSIT CVLGSTDIGA IEVQQFMKDG SRNVLASFNI QTFDDKLLSF 101 VHFADINQLV FVFEQGDIIT ATYDPVSLDP AETLIEIMGT IDNGIAAAQW 151 SYDEETLAMV TKDRNVVVLS KLFEPISEYH LEVDDLKISK HVTVGWGKKE 201 TQFRGKGARA MEREALASLK ASGLVGNQLR DPTMPYMVDT GDVTALDSHE 251 ITISWRGDCD YFAVSSVEEV PDEDDETKSI KRRAFRVFSR EGQLDSASEP 301 VTGMEHQLSW KPQGSLIASI QRKTDLGEED SVDVIFFERN GLRHGEFDTR 351 LPLDEKVESV CWNSNSEALA VVLANRIQLW TSKNYHWYLK QELYASDISY 401 VKWHPEKDFT LMFSDAGFIN IVDFAYKMAQ GPTLEPFDNG TSLVVDGRTV 451 NITPLALANV PPPMYYRDFE TPGNVLDVAC SFSNEIYAAI NKDVLIFAAV 501 PSIEEMKKGK HPSIVCEFPK SEFTSEVDSL RQVAFINDSI VGVLLDTDNL 551 SRIALLDIQD ITQPTLITIV EVYDKIVLLR SDFDYNHLVY ETRDGTVCQL 601 DAEGQLMEIT KFPQLVRDFR VKRVHNTSAE DDDNWSAESS ELVAFGITNN 651 GKLFANQVLL ASAVTSLEIT DSFLLFTTAQ HNLQFVHLNS TDFKPLPLVE 701 EGVEDERVRA IERGSILVSV IPSKSSVVLQ ATRGNLETIY PRIMVLAEVR 751 KNIMAKRYKE AFIVCRTHRI NLDILHDYAP ELFIENLEVF INQIGRVDYL 801 NLFISCLSED DVTKTKYKET LYSGISKSFG MEPAPLTEMQ IYMKKKMFDP 851 KTSKVNKICD AVLNVLLSNP EYKKKYLQTI ITAYASQNPQ NLSAALKLIS 901 ELENSEEKDS CVTYLCFLQD VNVVYKSALS LYDVSLALLV AQKSQMDPRE 951 YLPFLQELQD NEPLRRKFLI DDYLGNYEKA LEHLSEIDKD GNVSEEVIDY 1001 VESHDLYKHG LALYRYDSEK QNVIYNIYAK HLSSNQMYTD AAVAYEMLGK 1051 LKEAMGAYQS AKRWREAMSI AVQKFPEEVE SVAEELISSL TFEHRYVDAA 1101 DIQLEYLDNV KEAVALYCKA YRYDIASLVA IKAKKDELLE EVVDPGLGEG 1151 FGIIAELLAD CKGQINSQLR RLRELRAKKE ENPYAFYGQE TEQADDVSVA 1201 PSETSTQESF FTRYTGKTGG TAKTGASRRT AKNKRREERK RARGKKGTIY 1251 EEEYLVQSVG RLIERLNQTK PDAVRVVEGL CRRNMREQAH QIQKNFVEVL 1301 DLLKANVKEI YSISEKDRER VNENGEVYYI PEIPVPEIHD FPKSHIVDF*

Amino Acid Sequence (or in FASTA format)

       1  MVEHDKSGSK RQELRSNMRN LITLNKGKFK PTASTAEGDE DDLSFTLLDS
      51  VFDTLSDSIT CVLGSTDIGA IEVQQFMKDG SRNVLASFNI QTFDDKLLSF
     101  VHFADINQLV FVFEQGDIIT ATYDPVSLDP AETLIEIMGT IDNGIAAAQW
     151  SYDEETLAMV TKDRNVVVLS KLFEPISEYH LEVDDLKISK HVTVGWGKKE
     201  TQFRGKGARA MEREALASLK ASGLVGNQLR DPTMPYMVDT GDVTALDSHE
     251  ITISWRGDCD YFAVSSVEEV PDEDDETKSI KRRAFRVFSR EGQLDSASEP
     301  VTGMEHQLSW KPQGSLIASI QRKTDLGEED SVDVIFFERN GLRHGEFDTR
     351  LPLDEKVESV CWNSNSEALA VVLANRIQLW TSKNYHWYLK QELYASDISY
     401  VKWHPEKDFT LMFSDAGFIN IVDFAYKMAQ GPTLEPFDNG TSLVVDGRTV
     451  NITPLALANV PPPMYYRDFE TPGNVLDVAC SFSNEIYAAI NKDVLIFAAV
     501  PSIEEMKKGK HPSIVCEFPK SEFTSEVDSL RQVAFINDSI VGVLLDTDNL
     551  SRIALLDIQD ITQPTLITIV EVYDKIVLLR SDFDYNHLVY ETRDGTVCQL
     601  DAEGQLMEIT KFPQLVRDFR VKRVHNTSAE DDDNWSAESS ELVAFGITNN
     651  GKLFANQVLL ASAVTSLEIT DSFLLFTTAQ HNLQFVHLNS TDFKPLPLVE
     701  EGVEDERVRA IERGSILVSV IPSKSSVVLQ ATRGNLETIY PRIMVLAEVR
     751  KNIMAKRYKE AFIVCRTHRI NLDILHDYAP ELFIENLEVF INQIGRVDYL
     801  NLFISCLSED DVTKTKYKET LYSGISKSFG MEPAPLTEMQ IYMKKKMFDP
     851  KTSKVNKICD AVLNVLLSNP EYKKKYLQTI ITAYASQNPQ NLSAALKLIS
     901  ELENSEEKDS CVTYLCFLQD VNVVYKSALS LYDVSLALLV AQKSQMDPRE
     951  YLPFLQELQD NEPLRRKFLI DDYLGNYEKA LEHLSEIDKD GNVSEEVIDY
    1001  VESHDLYKHG LALYRYDSEK QNVIYNIYAK HLSSNQMYTD AAVAYEMLGK
    1051  LKEAMGAYQS AKRWREAMSI AVQKFPEEVE SVAEELISSL TFEHRYVDAA
    1101  DIQLEYLDNV KEAVALYCKA YRYDIASLVA IKAKKDELLE EVVDPGLGEG
    1151  FGIIAELLAD CKGQINSQLR RLRELRAKKE ENPYAFYGQE TEQADDVSVA
    1201  PSETSTQESF FTRYTGKTGG TAKTGASRRT AKNKRREERK RARGKKGTIY
    1251  EEEYLVQSVG RLIERLNQTK PDAVRVVEGL CRRNMREQAH QIQKNFVEVL
    1301  DLLKANVKEI YSISEKDRER VNENGEVYYI PEIPVPEIHD FPKSHIVDF*

external links for Iki3p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
YGOB	CYC2008 (complexes)	Pfam domains
YOGY	Complexome	YeastRC Structure Prediction (Seattle)
	DIP
	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Iki3p

1)	Yajima H, et al. (1997) Characterization of IKI1 and IKI3 genes conferring pGKL killer sensitivity on Saccharomyces cerevisiae. Biosci Biotechnol Biochem 61(4):704-9
2)	Otero G, et al. (1999) Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Mol Cell 3(1):109-18
3)	Frohloff F, et al. (2001) Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin. EMBO J 20(8):1993-2003
4)	Butler AR, et al. (1994) Two Saccharomyces cerevisiae genes which control sensitivity to G1 arrest induced by Kluyveromyces lactis toxin. Mol Cell Biol 14(9):6306-16
5)	Kishida M, et al. (1996) Isolation and genetic characterization of pGKL killer-insensitive mutants (iki) from Saccharomyces cerevisiae. Biosci Biotechnol Biochem 60(5):798-801
6)	Frohloff F, et al. (2003) Subunit communications crucial for the functional integrity of the yeast RNA polymerase II elongator (gamma-toxin target (TOT)) complex. J Biol Chem 278(2):956-61
7)	Rahl PB, et al. (2005) Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation. Mol Cell 17(6):841-53
8)	Esberg A, et al. (2006) Elevated levels of two tRNA species bypass the requirement for elongator complex in transcription and exocytosis. Mol Cell 24(1):139-48
9)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41