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Protein

Elongator complex protein 1

Gene

Ikbkap

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May act as a scaffold protein that may assemble active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK).By similarity
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. Involved in neurogenesis (PubMed:19185337). Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (PubMed:19185337).2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Elongator complex protein 1
Short name:
ELP1
Alternative name(s):
IkappaB kinase complex-associated protein
Short name:
IKK complex-associated protein
Gene namesi
Name:Ikbkap
Synonyms:Elp1, Ikap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914544. Ikbkap.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13331333Elongator complex protein 1PRO_0000283995Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1172 – 11721PhosphoserineBy similarity
Modified residuei1175 – 11751PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7TT37.
MaxQBiQ7TT37.
PaxDbiQ7TT37.
PRIDEiQ7TT37.

PTM databases

PhosphoSiteiQ7TT37.

Expressioni

Tissue specificityi

Widely expressed with highest levels in brain.1 Publication

Developmental stagei

Expressed at embryonic days 7, 11, 15 and 17 with the highest expression at embryonic day 11.1 Publication

Gene expression databases

BgeeiQ7TT37.
GenevisibleiQ7TT37. MM.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi230947. 1 interaction.
IntActiQ7TT37. 1 interaction.
MINTiMINT-4600543.
STRINGi10090.ENSMUSP00000030140.

Structurei

3D structure databases

ProteinModelPortaliQ7TT37.
SMRiQ7TT37. Positions 87-135, 421-451, 638-664, 876-912.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ELP1/IKA1 family.Curated

Phylogenomic databases

eggNOGiKOG1920. Eukaryota.
COG5290. LUCA.
GeneTreeiENSGT00390000013344.
HOVERGENiHBG019038.
InParanoidiQ7TT37.
KOiK11373.
OMAiHTYEVSL.
OrthoDBiEOG7BCN9X.
PhylomeDBiQ7TT37.
TreeFamiTF300402.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR006849. Iki3.
[Graphical view]
PANTHERiPTHR12747. PTHR12747. 1 hit.
PfamiPF04762. IKI3. 1 hit.
[Graphical view]
PIRSFiPIRSF017233. IKAP. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7TT37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNLKLHRTL EFRDIQAPGK PQCFCLRAEQ GTVLIGSERG LTEVDPVRRE
60 70 80 90 100
VKTEISLVAE GFLPEDGSGC IVGIQDLLDQ ESVCVATASG DVIVCNLSTQ
110 120 130 140 150
QLECVGSVAS GISVMSWSPD QELLLLATAQ QTLIMMTKDF EVIAEEQIHQ
160 170 180 190 200
DDFGEGKFVT VGWGSKQTQF HGSEGRPTAF PVQLPENALP WDDRRPHITW
210 220 230 240 250
RGDGQYFAVS VVCRQTEARK IRVWNREFAL QSTSESVPGL GPALAWKPSG
260 270 280 290 300
SLIASTQDKP NQQDVVFFEK NGLLHGHFTL PFLKDEVKVN DLLWNADSSV
310 320 330 340 350
LAIWLEDLPK EDSSTLKSYV QLWTVGNYHW YLKQSLPFST TGKNQIVSLL
360 370 380 390 400
WDPVTPCRLH VLCTGWRYLC CDWHWTTDRS SGNSANDLAN VAVIDGNRVL
410 420 430 440 450
VTVFRQTVVP PPMCTYRLLI PHPVNQVIFS AHLGNDLAVL DASNQISVYK
460 470 480 490 500
CGDKPNMDST VKLGAVGGNG FKVPLTTPHL EKRYSIQFGN NEEEEEEEVN
510 520 530 540 550
ALQLSFLTWV EDDTFLAISY SHSSSQSIIH HLTVTHSEVD EEQGQLDVSS
560 570 580 590 600
SVTVDGVVIG LCCCSKTKSL AVQLADGQVL KYLWESPSLA VEPWKNSEGI
610 620 630 640 650
PVRFVHPCTQ MEVATIGGEE CVLGLTDRCR FFINDTEVAS NITSFAVCDD
660 670 680 690 700
FLLVTTHSHT CQVFSLSGAS LKMLQAALSG SHEASGEILR KVERGSRIVT
710 720 730 740 750
VVPQDTKLIL QMPRGNLEVV HHRALVLAQI RKWLDKLMFK EAFECMRKLR
760 770 780 790 800
INLNLIHDHN PKVFLENVET FVKQIDSVNH INLFFTELRE EDVTKTMYPP
810 820 830 840 850
PITKSVQVST HPDGKKLDLI CDAMRAAMEA INPRKFCLSI LTSHVKKTTP
860 870 880 890 900
ELEIVLQKVQ ELQGNLPFDP ESVSVEEALK YLLLLVDVNE LFNHSLGTYD
910 920 930 940 950
FNLVLMVAEK SQKDPKEYLP FLNTLKKMET NYQRFTIDKY LKRYEKALGH
960 970 980 990 1000
LSKCGPEYFT ECLNLIKDKN LYKEALKLYR PDSPQYQAVS MAYGEHLMQE
1010 1020 1030 1040 1050
HLYEPAGLVF ARCGAQEKAL EAFLACGSWQ QALCVAAQLQ MSKDKVAGLA
1060 1070 1080 1090 1100
RTLAGKLVEQ RKHSEAATVL EQYAQDYEEA VLLLLEGSAW EEALRLVYKY
1110 1120 1130 1140 1150
DRVDIIETSV KPSILEAQKN YMDFLDSETA TFIRHKNRLQ VVRALRRQAP
1160 1170 1180 1190 1200
QVHVDHEVAH GPESDLFSET SSIMSGSEMS GRYSHSNSRI SARSSKNRRK
1210 1220 1230 1240 1250
AERKKHSLKE GSPLEGLALL EALSEVVQSV EKLKDEVRAI LKVLFLFEFE
1260 1270 1280 1290 1300
EQAKELQRAF ESTLQLMERA VPEIWTPAGQ QSSTTPVLGP SSTANSITAS
1310 1320 1330
YQQQKTCVPA LDAGVYMPPK MDPRSQWKLS LLE
Length:1,333
Mass (Da):149,584
Last modified:March 1, 2004 - v2
Checksum:iC40E0098DD4DF63C
GO

Sequence cautioni

The sequence AAL36025.1 differs from that shown. Reason: Frameshift at position 498. Curated
The sequence AAO15309.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421T → P in AAO15309 (Ref. 3) Curated
Sequence conflicti120 – 1201D → G in BAE27720 (PubMed:16141072).Curated
Sequence conflicti215 – 2162QT → HS in AAO15309 (Ref. 3) Curated
Sequence conflicti221 – 2211I → V in AAL40925 (PubMed:11722848).Curated
Sequence conflicti346 – 3461I → V in AAL40925 (PubMed:11722848).Curated
Sequence conflicti346 – 3461I → V in AAO15309 (Ref. 3) Curated
Sequence conflicti582 – 5821Y → I in AAL36025 (PubMed:11747609).Curated
Sequence conflicti634 – 6352ND → LV in AAL36025 (PubMed:11747609).Curated
Sequence conflicti649 – 6491D → A in AAL40925 (PubMed:11722848).Curated
Sequence conflicti663 – 6631V → G in AAL36025 (PubMed:11747609).Curated
Sequence conflicti663 – 6631V → G in AAL40925 (PubMed:11722848).Curated
Sequence conflicti663 – 6631V → G in AAO15309 (Ref. 3) Curated
Sequence conflicti693 – 6942ER → VW in AAL36025 (PubMed:11747609).Curated
Sequence conflicti773 – 7731K → F in AAL36025 (PubMed:11747609).Curated
Sequence conflicti1110 – 11101V → I in AAL36025 (PubMed:11747609).Curated
Sequence conflicti1110 – 11101V → I in AAL40925 (PubMed:11722848).Curated
Sequence conflicti1110 – 11101V → I in AAO15309 (Ref. 3) Curated
Sequence conflicti1159 – 11591A → G in BAB23291 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF367244 mRNA. Translation: AAL36025.1. Frameshift.
AF387811 mRNA. Translation: AAL40925.1.
AF140786 mRNA. Translation: AAO15309.1. Frameshift.
AK004402 mRNA. Translation: BAB23291.1.
AK076152 mRNA. Translation: BAC36221.1.
AK035944 mRNA. Translation: BAC29252.1.
AK147153 mRNA. Translation: BAE27720.1.
AL807762, AL929577 Genomic DNA. Translation: CAM25708.1.
AL929577, AL807762 Genomic DNA. Translation: CAM24766.1.
BC052387 mRNA. Translation: AAH52387.2.
BC054468 mRNA. Translation: AAH54468.1.
CCDSiCCDS38765.1.
RefSeqiNP_080355.2. NM_026079.3.
UniGeneiMm.282743.

Genome annotation databases

EnsembliENSMUST00000030140; ENSMUSP00000030140; ENSMUSG00000028431.
GeneIDi230233.
KEGGimmu:230233.
UCSCiuc012del.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF367244 mRNA. Translation: AAL36025.1. Frameshift.
AF387811 mRNA. Translation: AAL40925.1.
AF140786 mRNA. Translation: AAO15309.1. Frameshift.
AK004402 mRNA. Translation: BAB23291.1.
AK076152 mRNA. Translation: BAC36221.1.
AK035944 mRNA. Translation: BAC29252.1.
AK147153 mRNA. Translation: BAE27720.1.
AL807762, AL929577 Genomic DNA. Translation: CAM25708.1.
AL929577, AL807762 Genomic DNA. Translation: CAM24766.1.
BC052387 mRNA. Translation: AAH52387.2.
BC054468 mRNA. Translation: AAH54468.1.
CCDSiCCDS38765.1.
RefSeqiNP_080355.2. NM_026079.3.
UniGeneiMm.282743.

3D structure databases

ProteinModelPortaliQ7TT37.
SMRiQ7TT37. Positions 87-135, 421-451, 638-664, 876-912.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230947. 1 interaction.
IntActiQ7TT37. 1 interaction.
MINTiMINT-4600543.
STRINGi10090.ENSMUSP00000030140.

PTM databases

PhosphoSiteiQ7TT37.

Proteomic databases

EPDiQ7TT37.
MaxQBiQ7TT37.
PaxDbiQ7TT37.
PRIDEiQ7TT37.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030140; ENSMUSP00000030140; ENSMUSG00000028431.
GeneIDi230233.
KEGGimmu:230233.
UCSCiuc012del.1. mouse.

Organism-specific databases

CTDi8518.
MGIiMGI:1914544. Ikbkap.

Phylogenomic databases

eggNOGiKOG1920. Eukaryota.
COG5290. LUCA.
GeneTreeiENSGT00390000013344.
HOVERGENiHBG019038.
InParanoidiQ7TT37.
KOiK11373.
OMAiHTYEVSL.
OrthoDBiEOG7BCN9X.
PhylomeDBiQ7TT37.
TreeFamiTF300402.

Miscellaneous databases

ChiTaRSiIkbkap. mouse.
NextBioi379841.
PROiQ7TT37.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TT37.
GenevisibleiQ7TT37. MM.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR006849. Iki3.
[Graphical view]
PANTHERiPTHR12747. PTHR12747. 1 hit.
PfamiPF04762. IKI3. 1 hit.
[Graphical view]
PIRSFiPIRSF017233. IKAP. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, characterization, and genomic structure of the mouse Ikbkap gene."
    Cuajungco M.P., Leyne M., Mull J., Gill S.P., Gusella J.F., Slaugenhaupt S.A.
    DNA Cell Biol. 20:579-586(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
  2. "Genomic organization and chromosomal localization of the mouse IKBKAP gene."
    Coli R., Anderson S.L., Volpi S.A., Rubin B.Y.
    Gene 279:81-89(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/SvJ.
    Tissue: Spleen.
  3. "Molecular cloning and biochemical analysis of murine IKAP."
    Shirane M., Hatakeyama S., Nakayama K.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum and Head.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Eye.
  7. "Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin."
    Creppe C., Malinouskaya L., Volvert M.L., Gillard M., Close P., Malaise O., Laguesse S., Cornez I., Rahmouni S., Ormenese S., Belachew S., Malgrange B., Chapelle J.P., Siebenlist U., Moonen G., Chariot A., Nguyen L.
    Cell 136:551-564(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEUROGENESIS, SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "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: FUNCTION.

Entry informationi

Entry nameiELP1_MOUSE
AccessioniPrimary (citable) accession number: Q7TT37
Secondary accession number(s): Q3UHY6
, Q7TQH1, Q8C6B3, Q8CBI3, Q8CH82, Q8VHU5, Q8VHV9, Q9CT81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: March 1, 2004
Last modified: May 11, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.