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P23193

- TCEA1_HUMAN

UniProt

P23193 - TCEA1_HUMAN

Protein

Transcription elongation factor A protein 1

Gene

TCEA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri259 – 29941TFIIS-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. DNA repair Source: Reactome
    2. erythrocyte differentiation Source: Ensembl
    3. gene expression Source: Reactome
    4. nucleotide-excision repair Source: Reactome
    5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. positive regulation of viral transcription Source: Reactome
    7. regulation of DNA-templated transcription, elongation Source: InterPro
    8. transcription-coupled nucleotide-excision repair Source: Reactome
    9. transcription elongation from RNA polymerase II promoter Source: Reactome
    10. transcription from RNA polymerase II promoter Source: Reactome
    11. viral process Source: Reactome

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    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 A protein 1
    Alternative name(s):
    Transcription elongation factor S-II protein 1
    Transcription elongation factor TFIIS.o
    Gene namesi
    Name:TCEA1
    Synonyms:GTF2S, TFIIS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:11612. TCEA1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleolus Source: HPA
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving TCEA1 may be a cause of salivary gland pleiomorphic adenomas (PA) [181030]. Pleiomorphic adenomas are the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.

    Organism-specific databases

    PharmGKBiPA36371.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 301301Transcription elongation factor A protein 1PRO_0000121446Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei97 – 971Phosphoserine2 Publications
    Modified residuei100 – 1001Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP23193.
    PaxDbiP23193.
    PRIDEiP23193.

    PTM databases

    PhosphoSiteiP23193.

    Miscellaneous databases

    PMAP-CutDBP23193.

    Expressioni

    Gene expression databases

    ArrayExpressiP23193.
    BgeeiP23193.
    CleanExiHS_TCEA1.
    GenevestigatoriP23193.

    Organism-specific databases

    HPAiHPA043786.

    Interactioni

    Subunit structurei

    Interacts with EAF2 By similarity. Associates with UBR5 and forms a transcription regulatory complex made of CDK9, RNAP II, UBR5 and TFIIS/TCEA1 that can stimulate target gene transcription (e.g. gamma fibrinogen/FGG) by recruiting their promoters.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LEO1Q8WVC04EBI-2608271,EBI-932432
    PAF1Q8N7H54EBI-2608271,EBI-2607770

    Protein-protein interaction databases

    BioGridi112779. 45 interactions.
    DIPiDIP-48480N.
    IntActiP23193. 9 interactions.
    MINTiMINT-3009864.
    STRINGi9606.ENSP00000382541.

    Structurei

    Secondary structure

    1
    301
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi139 – 15113
    Helixi152 – 1565
    Helixi157 – 1615
    Helixi165 – 18016
    Beta strandi182 – 1843
    Helixi185 – 19814
    Helixi204 – 2118
    Helixi217 – 2226
    Turni225 – 2273
    Beta strandi264 – 2663
    Beta strandi271 – 2766
    Beta strandi278 – 2836
    Beta strandi286 – 2949
    Beta strandi297 – 2993

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TFINMR-A252-301[»]
    3NDQX-ray1.93A131-232[»]
    ProteinModelPortaliP23193.
    SMRiP23193. Positions 1-84, 132-301.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23193.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8078TFIIS N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini140 – 256117TFIIS centralPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TFS-II family.Curated
    Contains 1 TFIIS central domain.PROSITE-ProRule annotation
    Contains 1 TFIIS N-terminal domain.PROSITE-ProRule annotation
    Contains 1 TFIIS-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri259 – 29941TFIIS-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1594.
    HOGENOMiHOG000195015.
    HOVERGENiHBG055022.
    InParanoidiP23193.
    KOiK03145.
    OMAiRAMISFW.
    OrthoDBiEOG7GQXWQ.
    PhylomeDBiP23193.
    TreeFamiTF314970.

    Family and domain databases

    Gene3Di1.10.472.30. 1 hit.
    1.20.930.10. 1 hit.
    InterProiIPR016492. TF_IIS-rel.
    IPR003617. TFIIS/CRSP70_N_sub.
    IPR003618. TFIIS_cen_dom.
    IPR017923. TFIIS_N.
    IPR017890. TFS2M.
    IPR006289. TFSII.
    IPR001222. Znf_TFIIS.
    [Graphical view]
    PfamiPF08711. Med26. 1 hit.
    PF01096. TFIIS_C. 1 hit.
    PF07500. TFIIS_M. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006704. TF_IIS. 1 hit.
    SMARTiSM00510. TFS2M. 1 hit.
    SM00509. TFS2N. 1 hit.
    SM00440. ZnF_C2C2. 1 hit.
    [Graphical view]
    SUPFAMiSSF46942. SSF46942. 1 hit.
    SSF47676. SSF47676. 1 hit.
    TIGRFAMsiTIGR01385. TFSII. 1 hit.
    PROSITEiPS51321. TFIIS_CENTRAL. 1 hit.
    PS51319. TFIIS_N. 1 hit.
    PS00466. ZF_TFIIS_1. 1 hit.
    PS51133. ZF_TFIIS_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P23193-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEDEVVRFAK KMDKMVQKKN AAGALDLLKE LKNIPMTLEL LQSTRIGMSV    50
    NAIRKQSTDE EVTSLAKSLI KSWKKLLDGP STEKDLDEKK KEPAITSQNS 100
    PEAREESTSS GNVSNRKDET NARDTYVSSF PRAPSTSDSV RLKCREMLAA 150
    ALRTGDDYIA IGADEEELGS QIEEAIYQEI RNTDMKYKNR VRSRISNLKD 200
    AKNPNLRKNV LCGNIPPDLF ARMTAEEMAS DELKEMRKNL TKEAIREHQM 250
    AKTGGTQTDL FTCGKCKKKN CTYTQVQTRS ADEPMTTFVV CNECGNRWKF 300
    C 301
    Length:301
    Mass (Da):33,970
    Last modified:November 1, 1995 - v2
    Checksum:i8A685107A56D2DA1
    GO
    Isoform 2 (identifier: P23193-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         22-42: Missing.

    Show »
    Length:280
    Mass (Da):31,664
    Checksum:i31833641990136EF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1271V → L in AAA61138. (PubMed:1378807)Curated
    Sequence conflicti141 – 1411R → Q in CAA51940. (PubMed:8112616)Curated
    Sequence conflicti205 – 2051N → Y in CAA51940. (PubMed:8112616)Curated
    Sequence conflicti237 – 2371R → W in CAA51940. (PubMed:8112616)Curated
    Sequence conflicti285 – 2851M → V in CAA51940. (PubMed:8112616)Curated
    Sequence conflicti300 – 3001F → I in AC100821. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei22 – 4221Missing in isoform 2. 1 PublicationVSP_006409Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62585 mRNA. Translation: CAA44470.1.
    X57198 mRNA. Translation: CAA40484.1.
    M81601 mRNA. Translation: AAA61138.1.
    X73534 Genomic DNA. Translation: CAA51940.1.
    AK290454 mRNA. Translation: BAF83143.1.
    CR542221 mRNA. Translation: CAG47017.1.
    BT019995 mRNA. Translation: AAV38798.1.
    AC100821 Genomic DNA. No translation available.
    BC072460 mRNA. Translation: AAH72460.1.
    CCDSiCCDS47857.1. [P23193-2]
    CCDS47858.1. [P23193-1]
    PIRiS17361.
    S26831.
    S34159.
    RefSeqiNP_006747.1. NM_006756.3. [P23193-1]
    NP_958845.1. NM_201437.2. [P23193-2]
    UniGeneiHs.491745.

    Genome annotation databases

    EnsembliENST00000396401; ENSP00000395483; ENSG00000187735. [P23193-2]
    ENST00000521604; ENSP00000428426; ENSG00000187735. [P23193-1]
    GeneIDi6917.
    KEGGihsa:6917.
    UCSCiuc003xru.3. human. [P23193-1]
    uc003xrv.3. human. [P23193-2]

    Polymorphism databases

    DMDMi1174652.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62585 mRNA. Translation: CAA44470.1 .
    X57198 mRNA. Translation: CAA40484.1 .
    M81601 mRNA. Translation: AAA61138.1 .
    X73534 Genomic DNA. Translation: CAA51940.1 .
    AK290454 mRNA. Translation: BAF83143.1 .
    CR542221 mRNA. Translation: CAG47017.1 .
    BT019995 mRNA. Translation: AAV38798.1 .
    AC100821 Genomic DNA. No translation available.
    BC072460 mRNA. Translation: AAH72460.1 .
    CCDSi CCDS47857.1. [P23193-2 ]
    CCDS47858.1. [P23193-1 ]
    PIRi S17361.
    S26831.
    S34159.
    RefSeqi NP_006747.1. NM_006756.3. [P23193-1 ]
    NP_958845.1. NM_201437.2. [P23193-2 ]
    UniGenei Hs.491745.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TFI NMR - A 252-301 [» ]
    3NDQ X-ray 1.93 A 131-232 [» ]
    ProteinModelPortali P23193.
    SMRi P23193. Positions 1-84, 132-301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112779. 45 interactions.
    DIPi DIP-48480N.
    IntActi P23193. 9 interactions.
    MINTi MINT-3009864.
    STRINGi 9606.ENSP00000382541.

    PTM databases

    PhosphoSitei P23193.

    Polymorphism databases

    DMDMi 1174652.

    Proteomic databases

    MaxQBi P23193.
    PaxDbi P23193.
    PRIDEi P23193.

    Protocols and materials databases

    DNASUi 6917.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396401 ; ENSP00000395483 ; ENSG00000187735 . [P23193-2 ]
    ENST00000521604 ; ENSP00000428426 ; ENSG00000187735 . [P23193-1 ]
    GeneIDi 6917.
    KEGGi hsa:6917.
    UCSCi uc003xru.3. human. [P23193-1 ]
    uc003xrv.3. human. [P23193-2 ]

    Organism-specific databases

    CTDi 6917.
    GeneCardsi GC08M054929.
    H-InvDB HIX0057264.
    HGNCi HGNC:11612. TCEA1.
    HPAi HPA043786.
    MIMi 601425. gene.
    neXtProti NX_P23193.
    PharmGKBi PA36371.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1594.
    HOGENOMi HOG000195015.
    HOVERGENi HBG055022.
    InParanoidi P23193.
    KOi K03145.
    OMAi RAMISFW.
    OrthoDBi EOG7GQXWQ.
    PhylomeDBi P23193.
    TreeFami TF314970.

    Enzyme and pathway databases

    Reactomei REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    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

    EvolutionaryTracei P23193.
    GeneWikii TCEA1.
    GenomeRNAii 6917.
    NextBioi 27057.
    PMAP-CutDB P23193.
    PROi P23193.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23193.
    Bgeei P23193.
    CleanExi HS_TCEA1.
    Genevestigatori P23193.

    Family and domain databases

    Gene3Di 1.10.472.30. 1 hit.
    1.20.930.10. 1 hit.
    InterProi IPR016492. TF_IIS-rel.
    IPR003617. TFIIS/CRSP70_N_sub.
    IPR003618. TFIIS_cen_dom.
    IPR017923. TFIIS_N.
    IPR017890. TFS2M.
    IPR006289. TFSII.
    IPR001222. Znf_TFIIS.
    [Graphical view ]
    Pfami PF08711. Med26. 1 hit.
    PF01096. TFIIS_C. 1 hit.
    PF07500. TFIIS_M. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006704. TF_IIS. 1 hit.
    SMARTi SM00510. TFS2M. 1 hit.
    SM00509. TFS2N. 1 hit.
    SM00440. ZnF_C2C2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46942. SSF46942. 1 hit.
    SSF47676. SSF47676. 1 hit.
    TIGRFAMsi TIGR01385. TFSII. 1 hit.
    PROSITEi PS51321. TFIIS_CENTRAL. 1 hit.
    PS51319. TFIIS_N. 1 hit.
    PS00466. ZF_TFIIS_1. 1 hit.
    PS51133. ZF_TFIIS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression and characterization of the human transcription elongation factor, TFIIS."
      Yoo O., Yoon H., Baek K., Jeon C., Miyamoto K., Ueno A., Agarwal K.
      Nucleic Acids Res. 19:1073-1079(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Kidney.
    2. "Characterization of a HeLa cDNA clone encoding the human SII protein, an elongation factor for RNA polymerase II."
      Chen H.C., England L., Kane C.M.
      Gene 116:253-258(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Characterization of the gene encoding the human transcriptional elongation factor TFIIS."
      Park H.R., Baek K.H., Jeon C.J., Agarwal K., Yoo O.
      Gene 139:263-267(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    4. "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] (ISOFORM 1).
      Tissue: Brain.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Uterus.
    9. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-9 AND 32-44, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    10. "Conserved mechanism of PLAG1 activation in salivary gland tumors with and without chromosome 8q12 abnormalities: identification of SII as a new fusion partner gene."
      Astroem A.-K., Voz M.L., Kas K., Roeijer E., Wedell B., Mandahl N., Van de Ven W., Mark J., Stenman G.
      Cancer Res. 59:918-923(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B."
      Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K., Price D.H., Coulombe B.
      J. Biol. Chem. 286:5012-5022(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBR5 AND CDK9.
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS."
      Qian X., Jeon C., Yoon H., Agarwal K., Weiss M.A.
      Nature 365:277-279(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 256-301.

    Entry informationi

    Entry nameiTCEA1_HUMAN
    AccessioniPrimary (citable) accession number: P23193
    Secondary accession number(s): A6NF25
    , A8K339, Q15563, Q6FG87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 157 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

    Miscellaneous

    S-II binds to RNA-polymerase II in the absence of transcription.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3