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O95163

- ELP1_HUMAN

UniProt

O95163 - ELP1_HUMAN

Protein

Elongator complex protein 1

Gene

IKBKAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    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. Involved in cell migration.

    GO - Molecular functioni

    1. phosphorylase kinase regulator activity Source: UniProtKB
    2. protein binding Source: IntAct
    3. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. immune response Source: ProtInc
    3. positive regulation of cell migration Source: UniProtKB
    4. protein complex assembly Source: ProtInc
    5. protein phosphorylation Source: ProtInc
    6. regulation of protein kinase activity Source: GOC
    7. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. signal transduction Source: GOC
    9. transcription elongation from RNA polymerase II promoter Source: HGNC

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    SignaLinkiO95163.

    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
    p150
    Gene namesi
    Name:IKBKAP
    Synonyms:ELP1, IKAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:5959. IKBKAP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. DNA-directed RNA polymerase II, holoenzyme Source: HGNC
    3. Elongator holoenzyme complex Source: UniProtKB
    4. nucleolus Source: HGNC
    5. transcription elongation factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti696 – 6961R → P in HSAN3; mild phenotype; phosphorylation is reduced. 2 Publications
    VAR_011327

    Keywords - Diseasei

    Disease mutation, Neuropathy

    Organism-specific databases

    MIMi223900. phenotype.
    Orphaneti1764. Familial dysautonomia.
    PharmGKBiPA29775.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13321332Elongator complex protein 1PRO_0000084177Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei867 – 8671Phosphoserine2 Publications
    Modified residuei1171 – 11711Phosphoserine1 Publication
    Modified residuei1174 – 11741Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95163.
    PaxDbiO95163.
    PRIDEiO95163.

    PTM databases

    PhosphoSiteiO95163.

    Expressioni

    Gene expression databases

    ArrayExpressiO95163.
    BgeeiO95163.
    CleanExiHS_IKBKAP.
    GenevestigatoriO95163.

    Organism-specific databases

    HPAiCAB021340.
    HPA049677.

    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 ELP3.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ELP3Q9H9T38EBI-347559,EBI-355217
    HTTP428584EBI-347559,EBI-466029
    IRF4Q153062EBI-347559,EBI-751345

    Protein-protein interaction databases

    BioGridi114090. 54 interactions.
    DIPiDIP-27579N.
    IntActiO95163. 28 interactions.
    MINTiMINT-1034584.
    STRINGi9606.ENSP00000363779.

    Structurei

    3D structure databases

    ProteinModelPortaliO95163.
    SMRiO95163. Positions 83-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ELP1/IKA1 family.Curated

    Phylogenomic databases

    eggNOGiCOG5290.
    HOVERGENiHBG019038.
    InParanoidiO95163.
    KOiK11373.
    OMAiTREVKNE.
    OrthoDBiEOG7BCN9X.
    PhylomeDBiO95163.
    TreeFamiTF300402.

    Family and domain databases

    Gene3Di2.120.10.30. 2 hits.
    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.

    O95163-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRNLKLFRTL EFRDIQGPGN PQCFSLRTEQ GTVLIGSEHG LIEVDPVSRE     50
    VKNEVSLVAE GFLPEDGSGR IVGVQDLLDQ ESVCVATASG DVILCSLSTQ 100
    QLECVGSVAS GISVMSWSPD QELVLLATGQ QTLIMMTKDF EPILEQQIHQ 150
    DDFGESKFIT VGWGRKETQF HGSEGRQAAF QMQMHESALP WDDHRPQVTW 200
    RGDGQFFAVS VVCPETGARK VRVWNREFAL QSTSEPVAGL GPALAWKPSG 250
    SLIASTQDKP NQQDIVFFEK NGLLHGHFTL PFLKDEVKVN DLLWNADSSV 300
    LAVWLEDLQR EESSIPKTCV QLWTVGNYHW YLKQSLSFST CGKSKIVSLM 350
    WDPVTPYRLH VLCQGWHYLA YDWHWTTDRS VGDNSSDLSN VAVIDGNRVL 400
    VTVFRQTVVP PPMCTYQLLF PHPVNQVTFL AHPQKSNDLA VLDASNQISV 450
    YKCGDCPSAD PTVKLGAVGG SGFKVCLRTP HLEKRYKIQF ENNEDQDVNP 500
    LKLGLLTWIE EDVFLAVSHS EFSPRSVIHH LTAASSEMDE EHGQLNVSSS 550
    AAVDGVIISL CCNSKTKSVV LQLADGQIFK YLWESPSLAI KPWKNSGGFP 600
    VRFPYPCTQT ELAMIGEEEC VLGLTDRCRF FINDIEVASN ITSFAVYDEF 650
    LLLTTHSHTC QCFCLRDASF KTLQAGLSSN HVSHGEVLRK VERGSRIVTV 700
    VPQDTKLVLQ MPRGNLEVVH HRALVLAQIR KWLDKLMFKE AFECMRKLRI 750
    NLNLIYDHNP KVFLGNVETF IKQIDSVNHI NLFFTELKEE DVTKTMYPAP 800
    VTSSVYLSRD PDGNKIDLVC DAMRAVMESI NPHKYCLSIL TSHVKKTTPE 850
    LEIVLQKVHE LQGNAPSDPD AVSAEEALKY LLHLVDVNEL YDHSLGTYDF 900
    DLVLMVAEKS QKDPKEYLPF LNTLKKMETN YQRFTIDKYL KRYEKAIGHL 950
    SKCGPEYFPE CLNLIKDKNL YNEALKLYSP SSQQYQDISI AYGEHLMQEH 1000
    MYEPAGLMFA RCGAHEKALS AFLTCGNWKQ ALCVAAQLNF TKDQLVGLGR 1050
    TLAGKLVEQR KHIDAAMVLE ECAQDYEEAV LLLLEGAAWE EALRLVYKYN 1100
    RLDIIETNVK PSILEAQKNY MAFLDSQTAT FSRHKKRLLV VRELKEQAQQ 1150
    AGLDDEVPHG QESDLFSETS SVVSGSEMSG KYSHSNSRIS ARSSKNRRKA 1200
    ERKKHSLKEG SPLEDLALLE ALSEVVQNTE NLKDEVYHIL KVLFLFEFDE 1250
    QGRELQKAFE DTLQLMERSL PEIWTLTYQQ NSATPVLGPN STANSIMASY 1300
    QQQKTSVPVL DAELFIPPKI NRRTQWKLSL LD 1332
    Length:1,332
    Mass (Da):150,254
    Last modified:November 25, 2008 - v3
    Checksum:i5BAC580433CC8641
    GO

    Sequence cautioni

    The sequence CAB43219.1 differs from that shown. Reason: Frameshift at position 1286.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti304 – 3041W → R in AAC64258. (PubMed:9751059)Curated
    Sequence conflicti754 – 7541L → P in AAC64258. (PubMed:9751059)Curated
    Sequence conflicti961 – 9611C → G in CAB43219. (PubMed:17974005)Curated
    Sequence conflicti1320 – 13201I → V in CAB43219. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti70 – 701R → C.
    Corresponds to variant rs3737311 [ dbSNP | Ensembl ].
    VAR_047476
    Natural varianti182 – 1821M → K.
    Corresponds to variant rs10521092 [ dbSNP | Ensembl ].
    VAR_047477
    Natural varianti312 – 3121E → K.1 Publication
    Corresponds to variant rs1140064 [ dbSNP | Ensembl ].
    VAR_047478
    Natural varianti525 – 5251R → Q.
    Corresponds to variant rs838827 [ dbSNP | Ensembl ].
    VAR_047479
    Natural varianti696 – 6961R → P in HSAN3; mild phenotype; phosphorylation is reduced. 2 Publications
    VAR_011327
    Natural varianti765 – 7651G → E.
    Corresponds to variant rs2230792 [ dbSNP | Ensembl ].
    VAR_047480
    Natural varianti816 – 8161I → L.
    Corresponds to variant rs2230793 [ dbSNP | Ensembl ].
    VAR_047481
    Natural varianti830 – 8301I → M.
    Corresponds to variant rs2230794 [ dbSNP | Ensembl ].
    VAR_047482
    Natural varianti848 – 8481T → N.
    Corresponds to variant rs10979599 [ dbSNP | Ensembl ].
    VAR_047483
    Natural varianti952 – 9521K → I.
    Corresponds to variant rs2230798 [ dbSNP | Ensembl ].
    VAR_047484
    Natural varianti1013 – 10131G → S.
    Corresponds to variant rs2230795 [ dbSNP | Ensembl ].
    VAR_047485
    Natural varianti1072 – 10721C → S.2 Publications
    Corresponds to variant rs3204145 [ dbSNP | Ensembl ].
    VAR_047486
    Natural varianti1158 – 11581P → L.1 Publication
    Corresponds to variant rs1538660 [ dbSNP | Ensembl ].
    VAR_047487

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS6773.1.
    RefSeqiNP_003631.2. NM_003640.3.
    UniGeneiHs.494738.

    Genome annotation databases

    EnsembliENST00000374647; ENSP00000363779; ENSG00000070061.
    GeneIDi8518.
    KEGGihsa:8518.
    UCSCiuc004bdl.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS6773.1.
    RefSeqi NP_003631.2. NM_003640.3.
    UniGenei Hs.494738.

    3D structure databases

    ProteinModelPortali O95163.
    SMRi O95163. Positions 83-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114090. 54 interactions.
    DIPi DIP-27579N.
    IntActi O95163. 28 interactions.
    MINTi MINT-1034584.
    STRINGi 9606.ENSP00000363779.

    PTM databases

    PhosphoSitei O95163.

    Proteomic databases

    MaxQBi O95163.
    PaxDbi O95163.
    PRIDEi O95163.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374647 ; ENSP00000363779 ; ENSG00000070061 .
    GeneIDi 8518.
    KEGGi hsa:8518.
    UCSCi uc004bdl.3. human.

    Organism-specific databases

    CTDi 8518.
    GeneCardsi GC09M111629.
    GeneReviewsi IKBKAP.
    HGNCi HGNC:5959. IKBKAP.
    HPAi CAB021340.
    HPA049677.
    MIMi 223900. phenotype.
    603722. gene.
    neXtProti NX_O95163.
    Orphaneti 1764. Familial dysautonomia.
    PharmGKBi PA29775.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5290.
    HOVERGENi HBG019038.
    InParanoidi O95163.
    KOi K11373.
    OMAi TREVKNE.
    OrthoDBi EOG7BCN9X.
    PhylomeDBi O95163.
    TreeFami TF300402.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.
    SignaLinki O95163.

    Miscellaneous databases

    GenomeRNAii 8518.
    NextBioi 31890.
    PROi O95163.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95163.
    Bgeei O95163.
    CleanExi HS_IKBKAP.
    Genevestigatori O95163.

    Family and domain databases

    Gene3Di 2.120.10.30. 2 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR006849. IKI3.
    [Graphical view ]
    PANTHERi PTHR12747. PTHR12747. 1 hit.
    Pfami PF04762. IKI3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017233. IKAP. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 961-1332, VARIANTS SER-1072 AND LEU-1158.
      Tissue: Brain.
    7. 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. 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. 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. Cited for: VARIANT HSAN3 PRO-696, EFFECT ON PHOSPHORYLATION.

    Entry informationi

    Entry nameiELP1_HUMAN
    AccessioniPrimary (citable) accession number: O95163
    Secondary accession number(s): Q5JSV2, Q9H327, Q9UG87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 134 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3