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Q14241

- ELOA1_HUMAN

UniProt

Q14241 - ELOA1_HUMAN

Protein

Transcription elongation factor B polypeptide 3

Gene

TCEB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).

    GO - Molecular functioni

    1. DNA binding Source: InterPro

    GO - Biological processi

    1. gene expression Source: Reactome
    2. positive regulation of viral transcription Source: Reactome
    3. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    4. transcription elongation from RNA polymerase II promoter Source: Reactome
    5. transcription from RNA polymerase II promoter Source: Reactome
    6. viral process Source: Reactome

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription elongation factor B polypeptide 3
    Alternative name(s):
    Elongin 110 kDa subunit
    Elongin-A
    Short name:
    EloA
    RNA polymerase II transcription factor SIII subunit A1
    SIII p110
    Gene namesi
    Name:TCEB3
    ORF Names:MSTP059
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11620. TCEB3.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. integral component of membrane Source: InterPro
    3. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36379.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 798798Transcription elongation factor B polypeptide 3PRO_0000086960Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei410 – 4101Phosphoserine2 Publications
    Modified residuei413 – 4131Phosphoserine1 Publication
    Modified residuei420 – 4201Phosphothreonine1 Publication
    Modified residuei460 – 4601N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14241.
    PaxDbiQ14241.
    PeptideAtlasiQ14241.
    PRIDEiQ14241.

    PTM databases

    PhosphoSiteiQ14241.

    Expressioni

    Gene expression databases

    BgeeiQ14241.
    GenevestigatoriQ14241.

    Organism-specific databases

    HPAiHPA005910.
    HPA052418.

    Interactioni

    Subunit structurei

    Heterotrimer of an A (A1, A2 or A3), B and C subunit. The C subunit mediates the binding of the elongin BC complex to subunit A By similarity.By similarity

    Protein-protein interaction databases

    BioGridi112786. 17 interactions.
    IntActiQ14241. 4 interactions.
    MINTiMINT-1462212.
    STRINGi9606.ENSP00000395574.

    Structurei

    Secondary structure

    1
    798
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi607 – 6093
    Helixi612 – 6198
    Helixi630 – 6367
    Beta strandi648 – 6503
    Helixi652 – 67120

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HFXX-ray2.54A/B/C/D597-682[»]
    ProteinModelPortaliQ14241.
    SMRiQ14241. Positions 600-673.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 10576TFIIS N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini592 – 63645F-boxPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni548 – 707160Activation domainBy similarityAdd
    BLAST
    Regioni576 – 58510Interacting with Elongin BC complex

    Domaini

    The elongin BC complex binding domain is also known as BC-box with the consensus [APST]-L-x(3)-C-x(3)-[AILV].

    Sequence similaritiesi

    Contains 1 F-box domain.PROSITE-ProRule annotation
    Contains 1 TFIIS N-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG114994.
    HOGENOMiHOG000059565.
    HOVERGENiHBG051467.
    InParanoidiQ14241.
    KOiK15076.
    OMAiWKVHCHR.
    OrthoDBiEOG7P2XSR.
    PhylomeDBiQ14241.
    TreeFamiTF317259.

    Family and domain databases

    Gene3Di1.20.930.10. 1 hit.
    InterProiIPR001810. F-box_dom.
    IPR010684. RNA_pol_II_trans_fac_SIII_A.
    IPR003617. TFIIS/CRSP70_N_sub.
    IPR017923. TFIIS_N.
    [Graphical view]
    PfamiPF06881. Elongin_A. 1 hit.
    PF08711. Med26. 1 hit.
    [Graphical view]
    SMARTiSM00509. TFS2N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47676. SSF47676. 1 hit.
    PROSITEiPS50181. FBOX. 1 hit.
    PS51319. TFIIS_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q14241-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHGGRSCGPR TRREPSSGEE AAPVTAMAAE SALQVVEKLQ ARLAANPDPK    50
    KLLKYLKKLS TLPITVDILA ETGVGKTVNS LRKHEHVGSF ARDLVAQWKK 100
    LVPVERNAEP DEQDFEKSNS RKRPRDALQK EEEMEGDYQE TWKATGSRSY 150
    SPDHRQKKHR KLSELERPHK VSHGHERRDE RKRCHRMSPT YSSDPESSDY 200
    GHVQSPPSCT SPHQMYVDHY RSLEEDQEPI VSHQKPGKGH SNAFQDRLGA 250
    SQERHLGEPH GKGVVSQNKE HKSSHKDKRP VDAKSDEKAS VVSREKSHKA 300
    LSKEENRRPP SGDNAREKPP SSGVKKEKDR EGSSLKKKCL PPSEAASDNH 350
    LKKPKHRDPE KAKLDKSKQG LDSFDTGKGA GDLLPKVKEK GSNNLKTPEG 400
    KVKTNLDRKS LGSLPKVEET DMEDEFEQPT MSFESYLSYD QPRKKKKKIV 450
    KTSATALGDK GLKKNDSKST GKNLDSVQKL PKVNKTKSEK PAGADLAKLR 500
    KVPDVLPVLP DLPLPAIQAN YRPLPSLELI SSFQPKRKAF SSPQEEEEAG 550
    FTGRRMNSKM QVYSGSKCAY LPKMMTLHQQ CIRVLKNNID SIFEVGGVPY 600
    SVLEPVLERC TPDQLYRIEE YNHVLIEETD QLWKVHCHRD FKEERPEEYE 650
    SWREMYLRLQ DAREQRLRVL TKNIQFAHAN KPKGRQAKMA FVNSVAKPPR 700
    DVRRRQEKFG TGGAAVPEKI KIKPAPYPMG SSHASASSIS FNPSPEEPAY 750
    DGPSTSSAHL APVVSSTVSY DPRKPTVKKI APMMAKTIKA FKNRFSRR 798
    Length:798
    Mass (Da):89,909
    Last modified:April 20, 2010 - v2
    Checksum:i2C8FD8710E27EE46
    GO

    Sequence cautioni

    The sequence AAA75492.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH02883.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAO15305.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG35905.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB40157.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence EAW95070.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti145 – 1451T → M.
    Corresponds to variant rs2235541 [ dbSNP | Ensembl ].
    VAR_020104
    Natural varianti324 – 3241V → I.
    Corresponds to variant rs520713 [ dbSNP | Ensembl ].
    VAR_033850
    Natural varianti516 – 5161A → V.
    Corresponds to variant rs550252 [ dbSNP | Ensembl ].
    VAR_033851

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK313079 mRNA. Translation: BAG35905.1. Different initiation.
    DA333869 mRNA. No translation available.
    AL031295 Genomic DNA. Translation: CAB40157.1. Different initiation.
    CH471134 Genomic DNA. Translation: EAW95070.1. Different initiation.
    L47345 mRNA. Translation: AAA75492.1. Different initiation.
    BC002883 mRNA. Translation: AAH02883.1. Different initiation.
    AF116729 mRNA. Translation: AAO15305.1. Different initiation.
    CCDSiCCDS239.2.
    PIRiJC4636.
    RefSeqiNP_003189.2. NM_003198.2.
    UniGeneiHs.15535.

    Genome annotation databases

    EnsembliENST00000418390; ENSP00000395574; ENSG00000011007.
    GeneIDi6924.
    KEGGihsa:6924.
    UCSCiuc001bho.3. human.

    Polymorphism databases

    DMDMi294862430.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK313079 mRNA. Translation: BAG35905.1 . Different initiation.
    DA333869 mRNA. No translation available.
    AL031295 Genomic DNA. Translation: CAB40157.1 . Different initiation.
    CH471134 Genomic DNA. Translation: EAW95070.1 . Different initiation.
    L47345 mRNA. Translation: AAA75492.1 . Different initiation.
    BC002883 mRNA. Translation: AAH02883.1 . Different initiation.
    AF116729 mRNA. Translation: AAO15305.1 . Different initiation.
    CCDSi CCDS239.2.
    PIRi JC4636.
    RefSeqi NP_003189.2. NM_003198.2.
    UniGenei Hs.15535.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HFX X-ray 2.54 A/B/C/D 597-682 [» ]
    ProteinModelPortali Q14241.
    SMRi Q14241. Positions 600-673.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112786. 17 interactions.
    IntActi Q14241. 4 interactions.
    MINTi MINT-1462212.
    STRINGi 9606.ENSP00000395574.

    PTM databases

    PhosphoSitei Q14241.

    Polymorphism databases

    DMDMi 294862430.

    Proteomic databases

    MaxQBi Q14241.
    PaxDbi Q14241.
    PeptideAtlasi Q14241.
    PRIDEi Q14241.

    Protocols and materials databases

    DNASUi 6924.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000418390 ; ENSP00000395574 ; ENSG00000011007 .
    GeneIDi 6924.
    KEGGi hsa:6924.
    UCSCi uc001bho.3. human.

    Organism-specific databases

    CTDi 6924.
    GeneCardsi GC01P024069.
    H-InvDB HIX0000251.
    HGNCi HGNC:11620. TCEB3.
    HPAi HPA005910.
    HPA052418.
    MIMi 600786. gene.
    neXtProti NX_Q14241.
    PharmGKBi PA36379.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG114994.
    HOGENOMi HOG000059565.
    HOVERGENi HBG051467.
    InParanoidi Q14241.
    KOi K15076.
    OMAi WKVHCHR.
    OrthoDBi EOG7P2XSR.
    PhylomeDBi Q14241.
    TreeFami TF317259.

    Enzyme and pathway databases

    Reactomei REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.

    Miscellaneous databases

    GeneWikii TCEB3.
    GenomeRNAii 6924.
    NextBioi 27089.
    PROi Q14241.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q14241.
    Genevestigatori Q14241.

    Family and domain databases

    Gene3Di 1.20.930.10. 1 hit.
    InterProi IPR001810. F-box_dom.
    IPR010684. RNA_pol_II_trans_fac_SIII_A.
    IPR003617. TFIIS/CRSP70_N_sub.
    IPR017923. TFIIS_N.
    [Graphical view ]
    Pfami PF06881. Elongin_A. 1 hit.
    PF08711. Med26. 1 hit.
    [Graphical view ]
    SMARTi SM00509. TFS2N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47676. SSF47676. 1 hit.
    PROSITEi PS50181. FBOX. 1 hit.
    PS51319. TFIIS_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "A human cDNA encoding the 110-kDa A subunit of RNA polymerase II transcription factor elongin."
      Aso T., Haque D., Fukudome K., Brower C.S., Conaway J.W., Conaway R.C.
      Gene 168:277-278(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-798.
      Tissue: Umbilical vein.
    5. "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] OF 20-798.
      Tissue: Lung.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-798.
      Tissue: Heart.
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND THR-420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "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-410 AND SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiELOA1_HUMAN
    AccessioniPrimary (citable) accession number: Q14241
    Secondary accession number(s): B2R7Q8, Q8IXH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2003
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 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

    Caution

    It is uncertain whether Met-1 or Met-27 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3