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O95163

- ELP1_HUMAN

UniProt

O95163 - ELP1_HUMAN

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Protein
Elongator complex protein 1
Gene
IKBKAP, ELP1, IKAP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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).2 Publications
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.2 Publications

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
Complete GO annotation...

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

Cytoplasm. Nucleus 3 Publications

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 1
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the ELP1/IKA1 family.

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti304 – 3041W → R in AAC64258. 1 Publication
Sequence conflicti754 – 7541L → P in AAC64258. 1 Publication
Sequence conflicti961 – 9611C → G in CAB43219. 1 Publication
Sequence conflicti1320 – 13201I → V in CAB43219. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 133 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

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