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O95163 (ELP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1332 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Neuropathy, hereditary sensory and autonomic, 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 processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DiseaseDisease mutation
Neuropathy
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

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 protein kinase activity

Inferred from direct assay Ref.8. Source: GOC

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.8. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: GOC

transcription elongation from RNA polymerase II promoter

Inferred from direct assay Ref.7. Source: HGNC

   Cellular_componentDNA-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_functionphosphorylase kinase regulator activity

Inferred from direct assay Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7PubMed 15383276PubMed 19185337PubMed 21903422Ref.12. Source: IntAct

signal transducer activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13321332Elongator complex protein 1
PRO_0000084177

Amino acid modifications

Modified residue8671Phosphoserine Ref.9 Ref.10
Modified residue11711Phosphoserine Ref.9
Modified residue11741Phosphoserine Ref.9

Natural variations

Natural variant701R → C.
Corresponds to variant rs3737311 [ dbSNP | Ensembl ].
VAR_047476
Natural variant1821M → K.
Corresponds to variant rs10521092 [ dbSNP | Ensembl ].
VAR_047477
Natural variant3121E → K. Ref.1
Corresponds to variant rs1140064 [ dbSNP | Ensembl ].
VAR_047478
Natural variant5251R → Q.
Corresponds to variant rs838827 [ dbSNP | Ensembl ].
VAR_047479
Natural variant6961R → P in HSAN3; mild phenotype; phosphorylation is reduced. Ref.2 Ref.13
VAR_011327
Natural variant7651G → E.
Corresponds to variant rs2230792 [ dbSNP | Ensembl ].
VAR_047480
Natural variant8161I → L.
Corresponds to variant rs2230793 [ dbSNP | Ensembl ].
VAR_047481
Natural variant8301I → M.
Corresponds to variant rs2230794 [ dbSNP | Ensembl ].
VAR_047482
Natural variant8481T → N.
Corresponds to variant rs10979599 [ dbSNP | Ensembl ].
VAR_047483
Natural variant9521K → I.
Corresponds to variant rs2230798 [ dbSNP | Ensembl ].
VAR_047484
Natural variant10131G → S.
Corresponds to variant rs2230795 [ dbSNP | Ensembl ].
VAR_047485
Natural variant10721C → S. Ref.2 Ref.6
Corresponds to variant rs3204145 [ dbSNP | Ensembl ].
VAR_047486
Natural variant11581P → L. Ref.6
Corresponds to variant rs1538660 [ dbSNP | Ensembl ].
VAR_047487

Experimental info

Sequence conflict3041W → R in AAC64258. Ref.1
Sequence conflict7541L → P in AAC64258. Ref.1
Sequence conflict9611C → G in CAB43219. Ref.6
Sequence conflict13201I → V in CAB43219. Ref.6

Sequences

Sequence LengthMass (Da)Tools
O95163 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 5BAC580433CC8641

FASTA1,332150,254
        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 

« Hide

References

« Hide '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. 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].
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. expand/collapse author list , 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. 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 (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, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[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, INTERACTION WITH ELP3, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.

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.
CCDSCCDS6773.1.
RefSeqNP_003631.2. NM_003640.3.
UniGeneHs.494738.

3D structure databases

ProteinModelPortalO95163.
SMRO95163. Positions 83-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114090. 52 interactions.
DIPDIP-27579N.
IntActO95163. 27 interactions.
MINTMINT-1034584.
STRING9606.ENSP00000363779.

PTM databases

PhosphoSiteO95163.

Proteomic databases

MaxQBO95163.
PaxDbO95163.
PRIDEO95163.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374647; ENSP00000363779; ENSG00000070061.
GeneID8518.
KEGGhsa:8518.
UCSCuc004bdl.3. human.

Organism-specific databases

CTD8518.
GeneCardsGC09M111629.
GeneReviewsIKBKAP.
HGNCHGNC:5959. IKBKAP.
HPACAB021340.
HPA049677.
MIM223900. phenotype.
603722. gene.
neXtProtNX_O95163.
Orphanet1764. Familial dysautonomia.
PharmGKBPA29775.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5290.
HOVERGENHBG019038.
InParanoidO95163.
KOK11373.
OMATREVKNE.
OrthoDBEOG7BCN9X.
PhylomeDBO95163.
TreeFamTF300402.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
SignaLinkO95163.

Gene expression databases

ArrayExpressO95163.
BgeeO95163.
CleanExHS_IKBKAP.
GenevestigatorO95163.

Family and domain databases

Gene3D2.120.10.30. 2 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR006849. IKI3.
[Graphical view]
PANTHERPTHR12747. PTHR12747. 1 hit.
PfamPF04762. IKI3. 1 hit.
[Graphical view]
PIRSFPIRSF017233. IKAP. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi8518.
NextBio31890.
PROO95163.
SOURCESearch...

Entry information

Entry nameELP1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 132 of the entry and version 3 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 9

Human chromosome 9: entries, gene names and cross-references to MIM