O95163 (ELP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1332 AA.
Sequence status	Complete.
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). Ref.7 Ref.8 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. Involved in cell migration. Ref.7 Ref.8
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, ELP5 and ELP6. Elongator associates with the C-terminal domain (CTD) of Pol II largest subunit. Interacts with ELP3. Ref.7 Ref.8 Ref.12
Subcellular location	Cytoplasm. Nucleus Ref.7 Ref.8 Ref.12.
Involvement in disease	Hereditary sensory and autonomic neuropathy 3 (HSAN3) [MIM:223900]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN3 patients manifest a variety of symptoms such as alacrima, decreased taste, decreased sensitivity to pain and temperature, vasomotor instability, hypoactive or absent deep tendon reflexes, vomiting crises, and gastrointestinal dysfunction. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.13
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 Neuropathy
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	immune response Traceable author statement Ref.1. Source: ProtInc positive regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB protein complex assembly Traceable author statement Ref.1. Source: ProtInc protein phosphorylation Traceable author statement Ref.1. Source: ProtInc regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.8. Source: UniProtKB transcription elongation from RNA polymerase II promoter Inferred from direct assay Ref.7. Source: HGNC
Cellular_component	DNA-directed RNA polymerase II, holoenzyme Inferred from direct assay Ref.7. Source: HGNC Elongator holoenzyme complex Inferred from direct assay Ref.12. Source: UniProtKB cytoplasm Inferred from direct assay Ref.7Ref.12. Source: UniProtKB nucleolus Inferred from direct assay Ref.7. Source: HGNC transcription elongation factor complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	phosphorylase kinase regulator activity Inferred from direct assay Ref.8. Source: UniProtKB signal transducer activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ELP3	Q9H9T3	4	EBI-347559,EBI-355217
HTT	P42858	4	EBI-347559,EBI-466029
IRF4	Q15306	2	EBI-347559,EBI-751345

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
Amino acid modifications
	Modified residue	867	1	Phosphoserine Ref.9 Ref.10
	Modified residue	1171	1	Phosphoserine Ref.9
	Modified residue	1174	1	Phosphoserine Ref.9
Natural variations
	Natural variant	70	1	R → C. Corresponds to variant rs3737311 [ dbSNP | Ensembl ].		VAR_047476
	Natural variant	182	1	M → K. Corresponds to variant rs10521092 [ dbSNP | Ensembl ].		VAR_047477
	Natural variant	312	1	E → K. Ref.1 Corresponds to variant rs1140064 [ dbSNP | Ensembl ].		VAR_047478
	Natural variant	525	1	R → Q. Corresponds to variant rs838827 [ dbSNP | Ensembl ].		VAR_047479
	Natural variant	696	1	R → P in HSAN3; mild phenotype; phosphorylation is reduced. Ref.2 Ref.13		VAR_011327
	Natural variant	765	1	G → E. Corresponds to variant rs2230792 [ dbSNP | Ensembl ].		VAR_047480
	Natural variant	816	1	I → L. Corresponds to variant rs2230793 [ dbSNP | Ensembl ].		VAR_047481
	Natural variant	830	1	I → M. Corresponds to variant rs2230794 [ dbSNP | Ensembl ].		VAR_047482
	Natural variant	848	1	T → N. Corresponds to variant rs10979599 [ dbSNP | Ensembl ].		VAR_047483
	Natural variant	952	1	K → I. Corresponds to variant rs2230798 [ dbSNP | Ensembl ].		VAR_047484
	Natural variant	1013	1	G → S. Corresponds to variant rs2230795 [ dbSNP | Ensembl ].		VAR_047485
	Natural variant	1072	1	C → S. Ref.2 Ref.6 Corresponds to variant rs3204145 [ dbSNP | Ensembl ].		VAR_047486
	Natural variant	1158	1	P → L. Ref.6 Corresponds to variant rs1538660 [ dbSNP | Ensembl ].		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 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HSAN3 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] [Europe PMC] [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] [Europe PMC] [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 full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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] [Europe PMC] [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] [Europe PMC] [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]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-867; SER-1171 AND SER-1174, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-867, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"DERP6 (ELP5) and C3ORF75 (ELP6) regulate tumorigenicity and migration of melanoma cells as subunits of Elongator." Close P., Gillard M., Ladang A., Jiang Z., Papuga J., Hawkes N., Nguyen L., Chapelle J.P., Bouillenne F., Svejstrup J., Fillet M., Chariot A. J. Biol. Chem. 287:32535-32545(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, SUBCELLULAR LOCATION.
[13]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HSAN3 PRO-696, EFFECT ON PHOSPHORYLATION.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00293735.
RefSeq	NP_003631.2. NM_003640.3.
UniGene	Hs.494738.
3D structure databases
ProteinModelPortal	O95163.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27579N.
IntAct	O95163. 22 interactions.
MINT	MINT-1034584.
STRING	9606.ENSP00000363779.
PTM databases
PhosphoSite	O95163.
Proteomic databases
PaxDb	O95163.
PRIDE	O95163.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374647; ENSP00000363779; ENSG00000070061.
GeneID	8518.
KEGG	hsa:8518.
UCSC	uc004bdl.3. human.
Organism-specific databases
CTD	8518.
GeneCards	GC09M111629.
HGNC	HGNC:5959. IKBKAP.
HPA	CAB021340.
MIM	223900. phenotype. 603722. gene.
neXtProt	NX_O95163.
Orphanet	1764. Familial dysautonomia.
PharmGKB	PA29775.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5290.
HOVERGEN	HBG019038.
InParanoid	O95163.
KO	K11373.
OMA	HPVNQVT.
OrthoDB	EOG4KPT90.
PhylomeDB	O95163.
Gene expression databases
ArrayExpress	O95163.
Bgee	O95163.
CleanEx	HS_IKBKAP.
Genevestigator	O95163.
GermOnline	ENSG00000070061. Homo sapiens.
Family and domain databases
Gene3D	2.120.10.30. 2 hits.
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR006849. IKI3. [Graphical view]
PANTHER	PTHR12747. PTHR12747. 1 hit.
Pfam	PF04762. IKI3. 1 hit. [Graphical view]
PIRSF	PIRSF017233. IKAP. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL1818.
GenomeRNAi	8518.
NextBio	31890.
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:	May 1, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.