Reviewed, UniProtKB/Swiss-Prot O95163 (ELP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Elongator complex protein 1
      Short name=ELP1
Alternative name(s):
    IkappaB kinase complex-associated protein
      Short name=IKK complex-associated protein
    p150

Gene names

Name:	IKBKAP
Synonyms:	ELP1, IKAP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May act as a scaffold protein that may assemble active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK). Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4.
Subunit structure	Interacts preferentially with MAP3K14/NIK followed by IKK-alpha and IKK-beta. Component of the RNA polymerase II elongator complex (Elongator), which consists of IKBKAP/ELP1, STIP1/ELP2, ELP3, ELP4, and two yet unidentified proteins, p30 and p38. Elongator associates with the C-terminal domain (CTD) of Pol II largest subunit. Interacts with ELP3.
Subcellular location	Cytoplasm. Nucleus.
Post-translational modification	Phosphorylated.
Involvement in disease	Defects in IKBKAP are the cause of familial dysautonomia (FD) [MIM:223900]; also known as Riley-Day syndrome or hereditary sensory and autonomic neuropathy type III. This autosomal recessive disorder is due to the poor development and survival, and progressive degeneration of the sensory, sympathetic and parasympathetic neurons. FD individuals are affected with a variety of symptoms such as decreased sensitivity to pain and temperature, cardiovascular instability, recurrent pneumonias, vomiting crises, and gastrointestinal dysfunction. It is primarily confined to individuals of Ashkenazi Jewish descent, with an incidence of 1/3600 live births.
Sequence similarities	Belongs to the ELP1/IKA1 family.
Sequence caution	The sequence CAB43219.1 differs from that shown. Reason: Frameshift at position 1286.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Disease	Disease mutation
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	immune response Ref.1 Traceable author statement. Source: ProtInc protein amino acid phosphorylation Ref.1 Traceable author statement. Source: ProtInc protein complex assembly Ref.1 Traceable author statement. Source: ProtInc regulation of transcription from RNA polymerase II promoter Ref.7 Ref.8 Inferred from direct assay. Source: UniProtKB
Cellular component	DNA-directed RNA polymerase II, holoenzyme Ref.7 Inferred from direct assay. Source: HGNC cytoplasm Ref.7 Inferred from direct assay. Source: UniProtKB nucleolus Ref.7 Inferred from direct assay. Source: HGNC transcription elongation factor complex Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	phosphorylase kinase regulator activity Ref.1 Ref.8 Inferred from direct assay. Source: UniProtKB protein binding Ref.7 Inferred from physical interaction. Source: IntAct signal transducer activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HTT	P42858	1	EBI-347559,EBI-466029
MAP3K7	O43318	1	EBI-347559,EBI-358684
PBX2	P40425	1	EBI-347559,EBI-348489

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1332	1332	Elongator complex protein 1		PRO_0000084177
Natural variations
	Natural variant	70	1	R → C: dbSNP rs3737311.		VAR_047476
	Natural variant	182	1	M → K: dbSNP rs10521092.		VAR_047477
	Natural variant	312	1	E → K: dbSNP rs1140064.		VAR_047478
	Natural variant	525	1	R → Q: dbSNP rs838827.		VAR_047479
	Natural variant	696	1	R → P in FD; mild phenotype; phosphorylation is reduced.		VAR_011327
	Natural variant	765	1	G → E: dbSNP rs2230792.		VAR_047480
	Natural variant	816	1	I → L: dbSNP rs2230793.		VAR_047481
	Natural variant	830	1	I → M: dbSNP rs2230794.		VAR_047482
	Natural variant	848	1	T → N: dbSNP rs10979599.		VAR_047483
	Natural variant	952	1	K → I: dbSNP rs2230798.		VAR_047484
	Natural variant	1013	1	G → S: dbSNP rs2230795.		VAR_047485
	Natural variant	1072	1	C → S: dbSNP rs3204145.		VAR_047486
	Natural variant	1158	1	P → L: dbSNP rs1538660.		VAR_047487
Experimental info
	Sequence conflict	304	1	W → R in AAC64258. Ref.1
	Sequence conflict	754	1	L → P in AAC64258. Ref.1
	Sequence conflict	961	1	C → G in CAB43219. Ref.6
	Sequence conflict	1320	1	I → V in CAB43219. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O95163-1 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: 5BAC580433CC8641	FASTA	1,332	150,254
	10 20 30 40 50 60 MRNLKLFRTL EFRDIQGPGN PQCFSLRTEQ GTVLIGSEHG LIEVDPVSRE VKNEVSLVAE 70 80 90 100 110 120 GFLPEDGSGR IVGVQDLLDQ ESVCVATASG DVILCSLSTQ QLECVGSVAS GISVMSWSPD 130 140 150 160 170 180 QELVLLATGQ QTLIMMTKDF EPILEQQIHQ DDFGESKFIT VGWGRKETQF HGSEGRQAAF 190 200 210 220 230 240 QMQMHESALP WDDHRPQVTW RGDGQFFAVS VVCPETGARK VRVWNREFAL QSTSEPVAGL 250 260 270 280 290 300 GPALAWKPSG SLIASTQDKP NQQDIVFFEK NGLLHGHFTL PFLKDEVKVN DLLWNADSSV 310 320 330 340 350 360 LAVWLEDLQR EESSIPKTCV QLWTVGNYHW YLKQSLSFST CGKSKIVSLM WDPVTPYRLH 370 380 390 400 410 420 VLCQGWHYLA YDWHWTTDRS VGDNSSDLSN VAVIDGNRVL VTVFRQTVVP PPMCTYQLLF 430 440 450 460 470 480 PHPVNQVTFL AHPQKSNDLA VLDASNQISV YKCGDCPSAD PTVKLGAVGG SGFKVCLRTP 490 500 510 520 530 540 HLEKRYKIQF ENNEDQDVNP LKLGLLTWIE EDVFLAVSHS EFSPRSVIHH LTAASSEMDE 550 560 570 580 590 600 EHGQLNVSSS AAVDGVIISL CCNSKTKSVV LQLADGQIFK YLWESPSLAI KPWKNSGGFP 610 620 630 640 650 660 VRFPYPCTQT ELAMIGEEEC VLGLTDRCRF FINDIEVASN ITSFAVYDEF LLLTTHSHTC 670 680 690 700 710 720 QCFCLRDASF KTLQAGLSSN HVSHGEVLRK VERGSRIVTV VPQDTKLVLQ MPRGNLEVVH 730 740 750 760 770 780 HRALVLAQIR KWLDKLMFKE AFECMRKLRI NLNLIYDHNP KVFLGNVETF IKQIDSVNHI 790 800 810 820 830 840 NLFFTELKEE DVTKTMYPAP VTSSVYLSRD PDGNKIDLVC DAMRAVMESI NPHKYCLSIL 850 860 870 880 890 900 TSHVKKTTPE LEIVLQKVHE LQGNAPSDPD AVSAEEALKY LLHLVDVNEL YDHSLGTYDF 910 920 930 940 950 960 DLVLMVAEKS QKDPKEYLPF LNTLKKMETN YQRFTIDKYL KRYEKAIGHL SKCGPEYFPE 970 980 990 1000 1010 1020 CLNLIKDKNL YNEALKLYSP SSQQYQDISI AYGEHLMQEH MYEPAGLMFA RCGAHEKALS 1030 1040 1050 1060 1070 1080 AFLTCGNWKQ ALCVAAQLNF TKDQLVGLGR TLAGKLVEQR KHIDAAMVLE ECAQDYEEAV 1090 1100 1110 1120 1130 1140 LLLLEGAAWE EALRLVYKYN RLDIIETNVK PSILEAQKNY MAFLDSQTAT FSRHKKRLLV 1150 1160 1170 1180 1190 1200 VRELKEQAQQ AGLDDEVPHG QESDLFSETS SVVSGSEMSG KYSHSNSRIS ARSSKNRRKA 1210 1220 1230 1240 1250 1260 ERKKHSLKEG SPLEDLALLE ALSEVVQNTE NLKDEVYHIL KVLFLFEFDE QGRELQKAFE 1270 1280 1290 1300 1310 1320 DTLQLMERSL PEIWTLTYQQ NSATPVLGPN STANSIMASY QQQKTSVPVL DAELFIPPKI 1330 NRRTQWKLSL LD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"IKAP is a scaffold protein of the IkappaB kinase complex." Cohen L., Henzel W.J., Baeuerle P.A. Nature 395:292-296(1998) [PubMed: 9751059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT LYS-312. Tissue: Cervix carcinoma.
[2]	"Tissue-specific expression of a splicing mutation in the IKBKAP gene causes familial dysautonomia." Slaugenhaupt S.A., Blumenfeld A., Gill S.P., Leyne M., Mull J., Cuajungco M.P., Liebert C.B., Chadwick B.P., Idelson M., Reznik L., Robbins C.M., Makalowska I., Brownstein M.J., Krappmann D., Scheidereit C., Maayan C., Axelrod F.B., Gusella J.F. Am. J. Hum. Genet. 68:598-605(2001) [PubMed: 11179008] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT FD PRO-696, VARIANT SER-1072.
[3]	"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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Hippocampus.
[4]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	The German cDNA consortium Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 961-1332, VARIANTS SER-1072 AND LEU-1158. Tissue: Brain.
[7]	"Purification and characterization of the human elongator complex." Hawkes N.A., Otero G., Winkler G.S., Marshall N., Dahmus M.E., Krappmann D., Scheidereit C., Thomas C.L., Schiavo G., Erdjument-Bromage H., Tempst P., Svejstrup J.Q. J. Biol. Chem. 277:3047-3052(2002) [PubMed: 11714725] [Abstract] Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX.
[8]	"Human Elongator facilitates RNA polymerase II transcription through chromatin." Kim J.H., Lane W.S., Reinberg D. Proc. Natl. Acad. Sci. U.S.A. 99:1241-1246(2002) [PubMed: 11818576] [Abstract] Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR CORE COMPLEX, MASS SPECTROMETRY, INTERACTION WITH ELP3, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX.
[9]	"Familial dysautonomia is caused by mutations of the IKAP gene." Anderson S.L., Coli R., Daly I.W., Kichula E.A., Rork M.J., Volpi S.A., Ekstein J., Rubin B.Y. Am. J. Hum. Genet. 68:753-758(2001) [PubMed: 11179021] [Abstract] Cited for: VARIANT FD PRO-696, EFFECT ON PHOSPHORYLATION.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF044195 mRNA. Translation: AAC64258.1. AF153419 mRNA. Translation: AAG43369.1. AK001641 mRNA. Translation: BAG50955.1. AK289962 mRNA. Translation: BAF82651.1. AL354797, AL359692 Genomic DNA. Translation: CAI39465.1. AL359692, AL354797 Genomic DNA. Translation: CAI40569.1. CH471105 Genomic DNA. Translation: EAW59027.1. AL049945 mRNA. Translation: CAB43219.1. Frameshift.
UniGene	Hs.494738
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:27579N.
IntAct	O95163.
PTM databases
PhosphoSite	O95163.
Genome annotation databases
Ensembl	ENSG00000070061. Homo sapiens. [Contig view]
Organism-specific databases
HGNC	HGNC:5959. IKBKAP.
MIM	223900. phenotype. 603722. gene.
Orphanet	1764. Familial dysautonomia.
PharmGKB	PA29775.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	O95163.
Gene expression databases
ArrayExpress	O95163.
CleanEx	HS_IKBKAP.
GermOnline	ENSG00000070061. Homo sapiens.
Family and domain databases
InterPro	IPR006849. IKI3. [Graphical view]
PANTHER	PTHR12747. IKI3. 1 hit.
Pfam	PF04762. IKI3. 1 hit. [Graphical view]
PIRSF	PIRSF017233. IKAP. 1 hit.
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

ELP1_HUMAN

Accession

Primary (citable) accession number: O95163
Secondary accession number(s): Q5JSV2, Q9H327, Q9UG87

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	November 25, 2008
Last modified:	November 25, 2008
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)