TCAL1_HUMAN
ID TCAL1_HUMAN Reviewed; 159 AA.
AC Q15170; Q9UJQ9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Transcription elongation factor A protein-like 1 {ECO:0000305};
DE Short=TCEA-like protein 1;
DE AltName: Full=Nuclear phosphoprotein p21/SIIR;
DE AltName: Full=Transcription elongation factor S-II protein-like 1;
GN Name=TCEAL1 {ECO:0000312|HGNC:HGNC:11616}; Synonyms=SIIR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8206389; DOI=10.1016/0378-1119(94)90112-0;
RA Yeh C.-H., Shatkin A.J.;
RT "A HeLa-cell-encoded p21 is homologous to transcription elongation factor
RT SII.";
RL Gene 143:285-287(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10051408; DOI=10.1006/geno.1998.5705;
RA Pillutla R.C., Shimamoto A., Furuichi Y., Shatkin A.J.;
RT "Genomic structure and chromosomal localization of TCEAL1, a human gene
RT encoding the nuclear phosphoprotein p21/SIIR.";
RL Genomics 56:217-220(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION AT SER-33; SER-38; SER-39; SER-43 AND SER-44, AND
RP MUTAGENESIS OF 38-SER-SER-39 AND 43-SER-SER-44.
RX PubMed=7592688; DOI=10.1074/jbc.270.43.25313;
RA Yeh C.-H., Zong W.-X., Shatkin A.J.;
RT "The Ser36-Ser37 pair in HeLa nuclear protein p21/SIIR mediates Ser/Thr
RT phosphorylation and is essential for Rous sarcoma virus long terminal
RT repeat repression.";
RL J. Biol. Chem. 270:25313-25315(1995).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in transcriptional regulation. Modulates
CC various viral and cellular promoters in a promoter context-dependent
CC manner. For example, transcription from the FOS promoter is increased,
CC while Rous sarcoma virus (RSV) long terminal repeat (LTR) promoter
CC activity is repressed. Does not bind DNA directly.
CC -!- INTERACTION:
CC Q15170; O95273: CCNDBP1; NbExp=3; IntAct=EBI-2511314, EBI-748961;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highly expressed
CC in heart, ovary, prostate and skeletal muscle. Moderately expressed in
CC brain, placenta, testis and small intestine. Weakly expressed in lung,
CC liver and spleen. Expressed in several cancer cell lines.
CC {ECO:0000269|PubMed:10051408}.
CC -!- PTM: Phosphorylation of Ser-38 and Ser-39 is critical for
CC transcriptional repression. {ECO:0000269|PubMed:7592688}.
CC -!- SIMILARITY: Belongs to the TFS-II family. TFA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60149.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD17840.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M99701; AAA60149.1; ALT_FRAME; mRNA.
DR EMBL; AF095906; AAD17840.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL049610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000809; AAH00809.1; -; mRNA.
DR CCDS; CCDS35358.1; -.
DR PIR; I53785; I53785.
DR AlphaFoldDB; Q15170; -.
DR SMR; Q15170; -.
DR BioGRID; 114745; 76.
DR IntAct; Q15170; 48.
DR MINT; Q15170; -.
DR iPTMnet; Q15170; -.
DR PhosphoSitePlus; Q15170; -.
DR BioMuta; TCEAL1; -.
DR DMDM; 108935936; -.
DR EPD; Q15170; -.
DR jPOST; Q15170; -.
DR MassIVE; Q15170; -.
DR MaxQB; Q15170; -.
DR PeptideAtlas; Q15170; -.
DR PRIDE; Q15170; -.
DR Antibodypedia; 29090; 368 antibodies from 30 providers.
DR DNASU; 9338; -.
DR Ensembl; ENST00000372624.3; ENSP00000361707.3; ENSG00000172465.14.
DR Ensembl; ENST00000372625.8; ENSP00000361708.3; ENSG00000172465.14.
DR Ensembl; ENST00000372626.7; ENSP00000361709.3; ENSG00000172465.14.
DR GeneID; 9338; -.
DR MANE-Select; ENST00000372625.8; ENSP00000361708.3; NM_004780.3; NP_004771.2.
DR UCSC; uc004eks.4; human.
DR CTD; 9338; -.
DR DisGeNET; 9338; -.
DR GeneCards; TCEAL1; -.
DR HGNC; HGNC:11616; TCEAL1.
DR HPA; ENSG00000172465; Low tissue specificity.
DR MIM; 300237; gene.
DR neXtProt; NX_Q15170; -.
DR OpenTargets; ENSG00000172465; -.
DR PharmGKB; PA36375; -.
DR VEuPathDB; HostDB:ENSG00000172465; -.
DR GeneTree; ENSGT00950000183164; -.
DR HOGENOM; CLU_140430_0_0_1; -.
DR InParanoid; Q15170; -.
DR OMA; RPPQECL; -.
DR OrthoDB; 1545661at2759; -.
DR PhylomeDB; Q15170; -.
DR TreeFam; TF336871; -.
DR PathwayCommons; Q15170; -.
DR SignaLink; Q15170; -.
DR BioGRID-ORCS; 9338; 19 hits in 705 CRISPR screens.
DR ChiTaRS; TCEAL1; human.
DR GeneWiki; TCEAL1; -.
DR GenomeRNAi; 9338; -.
DR Pharos; Q15170; Tbio.
DR PRO; PR:Q15170; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q15170; protein.
DR Genevisible; Q15170; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0050699; F:WW domain binding; IBA:GO_Central.
DR InterPro; IPR010370; TCEAL1.
DR InterPro; IPR021156; TF_A-like/BEX.
DR PANTHER; PTHR14754:SF12; PTHR14754:SF12; 1.
DR Pfam; PF04538; BEX; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..159
FT /note="Transcription elongation factor A protein-like 1"
FT /id="PRO_0000239203"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7592688"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7592688"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7592688"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7592688"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7592688"
FT VARIANT 5
FT /note="R -> C (in dbSNP:rs34421776)"
FT /id="VAR_057270"
FT MUTAGEN 38..39
FT /note="SS->AA: Loss of transcriptional repression."
FT /evidence="ECO:0000269|PubMed:7592688"
FT MUTAGEN 43..44
FT /note="SS->AA: No effect on transcriptional repression."
FT /evidence="ECO:0000269|PubMed:7592688"
FT CONFLICT 67
FT /note="R -> L (in Ref. 1; AAA60149 and 2; AAD17840)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="Missing (in Ref. 1; AAA60149 and 2; AAD17840)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="G -> V (in Ref. 1; AAA60149 and 2; AAD17840)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="K -> N (in Ref. 1; AAA60149 and 2; AAD17840)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="S -> I (in Ref. 1; AAA60149 and 2; AAD17840)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="K -> R (in Ref. 1; AAA60149 and 2; AAD17840)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="SR -> GG (in Ref. 1; AAA60149 and 2; AAD17840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 18641 MW; FB45224005BA6B5A CRC64;
MDKPRKENEE EPQSAPKTDE ERPPVEHSPE KQSPEEQSSE EQSSEEEFFP EELLPELLPE
MLLSEERPPQ EGLSRKDLFE GRPPMEQPPC GVGKHKLEEG SFKERLARSR PQFRGDIHGR
NLSNEEMIQA ADELEEMKRV RNKLMIMHWK AKRSRPYPI
