O14776 (TCRG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription elongation regulator 1

Alternative name(s):
TATA box-binding protein-associated factor 2S
Transcription factor CA150

Gene names

Name:	TCERG1
Synonyms:	CA150, TAF2S

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1098 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter. Ref.1 Ref.5
Subunit structure	Binds formin By similarity. Binds RNA polymerase II, HD and SF1.
Subcellular location	Nucleus Ref.1 Ref.4 Ref.7.
Tissue specificity	Detected in brain neurons. Ref.6
Induction	Up-regulated in brain tissue from patients with Huntington disease. Ref.6
Domain	The FF domains bind the phosphorylated C-terminus of the largest subunit of RNA polymerase II, probably mediate interaction with HTATSF1 and preferentially bind peptides with the consensus sequence [DE](2-5)-[FWY]-[DE]2-5. The WW domains bind Pro-rich domains.
Sequence similarities	Contains 6 FF domains. Contains 3 WW domains.
Sequence caution	The sequence BAD93147.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
Molecular function	Activator Repressor
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	nucleus Traceable author statement Ref.1. Source: ProtInc
Molecular_function	RNA polymerase II transcription corepressor activity Inferred from direct assay PubMed 20956529. Source: BHF-UCL transcription coactivator activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BARD1	Q99728	2	EBI-473271,EBI-473181
HTT	P42858	3	EBI-473271,EBI-466029

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14776-1)

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.

Isoform 2 (identifier: O14776-2)

The sequence of this isoform differs from the canonical sequence as follows:
     379-399: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1098

1098

Transcription elongation regulator 1

PRO_0000076063

Regions

Domain

131 – 164

34

WW 1

Domain

429 – 462

34

WW 2

Domain

528 – 561

34

WW 3

Domain

661 – 709

49

FF 1

Domain

727 – 776

50

FF 2

Domain

794 – 843

50

FF 3

Domain

898 – 949

52

FF 4

Domain

956 – 1007

52

FF 5

Domain

1014 – 1074

61

FF 6

Coiled coil

184 – 244

61

Potential

Coiled coil

606 – 655

50

Potential

Coiled coil

844 – 906

63

Potential

Motif

626 – 630

5

Nuclear localization signal Potential

Compositional bias

32 – 132

101

Pro-rich

Compositional bias

169 – 258

90

Ala/Gln-rich

Compositional bias

260 – 331

72

Thr-rich

Compositional bias

328 – 378

51

Pro-rich

Compositional bias

454 – 515

62

Glu-rich

Compositional bias

1083 – 1087

5

Poly-Pro

Natural variations

Alternative sequence

379 – 399

21

Missing in isoform 2.

VSP_026933

Experimental info

Mutagenesis

148 – 150

3

YYY → AAA: Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 446-AAA-448.

Mutagenesis

446 – 448

3

YYY → AAA: Loss of interaction with SF1. Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 148-AAA-150. Ref.5

Mutagenesis

545 – 547

3

FFY → AAA: No effect. Ref.5

Sequence conflict

324

1

P → R in AAB80727. Ref.1

Secondary structure

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1098

Helix Strand Turn

Details...

Beta strand

429 – 438

10

Beta strand

441 – 443

3

Beta strand

446 – 455

10

Beta strand

523 – 528

6

Beta strand

530 – 533

4

Beta strand

535 – 542

8

Beta strand

544 – 548

5

Turn

549 – 552

4

Turn

560 – 564

5

Helix

567 – 573

7

Turn

576 – 578

3

Beta strand

652 – 656

5

Helix

661 – 672

12

Beta strand

677 – 679

3

Helix

681 – 684

4

Helix

685 – 687

3

Turn

688 – 690

3

Helix

692 – 696

5

Helix

699 – 732

34

Turn

733 – 735

3

Helix

747 – 753

7

Turn

759 – 762

4

Turn

765 – 772

8

Helix

773 – 780

8

Turn

782 – 786

5

Helix

787 – 790

4

Helix

792 – 804

13

Helix

814 – 821

8

Beta strand

822 – 824

3

Helix

825 – 828

4

Helix

833 – 844

12

Beta strand

888 – 890

3

Helix

892 – 910

19

Helix

918 – 927

10

Helix

931 – 934

4

Helix

939 – 956

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 24, 2007. Version 2. Checksum: 5F0A0C3A07EBF00F	FASTA	1,098	123,901
	10 20 30 40 50 60 MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP PPFGMMRGPP 70 80 90 100 110 120 PPPRPPFGRP PFDPNMPPMP PPGGIPPPMG PPHLQRPPFM PPPMSSMPPP PGMMFPPGMP 130 140 150 160 170 180 PVTAPGTPAL PPTEEIWVEN KTPDGKVYYY NARTRESAWT KPDGVKVIQQ SELTPMLAAQ 190 200 210 220 230 240 AQVQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ 250 260 270 280 290 300 AQVQAQVQAQ VQAQAVGAST PTTSSPAPAV STSTSSSTPS STTSTTTTAT SVAQTVSTPT 310 320 330 340 350 360 TQDQTPSSAV SVATPTVSVS TPAPTATPVQ TVPQPHPQTL PPAVPHSVPQ PTTAIPAFPP 370 380 390 400 410 420 VMVPPFRVPL PGMPIPLPGV AMMQIVSCPY VKTVATTKTG VLPGMAPPIV PMIHPQVAIA 430 440 450 460 470 480 ASPATLAGAT AVSEWTEYKT ADGKTYYYNN RTLESTWEKP QELKEKEKLE EKIKEPIKEP 490 500 510 520 530 540 SEEPLPMETE EEDPKEEPIK EIKEEPKEEE MTEEEKAAQK AKPVATAPIP GTPWCVVWTG 550 560 570 580 590 600 DERVFFYNPT TRLSMWDRPD DLIGRADVDK IIQEPPHKKG MEELKKLRHP TPTMLSIQKW 610 620 630 640 650 660 QFSMSAIKEE QELMEEINED EPVKAKKRKR DDNKDIDSEK EAAMEAEIKA ARERAIVPLE 670 680 690 700 710 720 ARMKQFKDML LERGVSAFST WEKELHKIVF DPRYLLLNPK ERKQVFDQYV KTRAEEERRE 730 740 750 760 770 780 KKNKIMQAKE DFKKMMEEAK FNPRATFSEF AAKHAKDSRF KAIEKMKDRE ALFNEFVAAA 790 800 810 820 830 840 RKKEKEDSKT RGEKIKSDFF ELLSNHHLDS QSRWSKVKDK VESDPRYKAV DSSSMREDLF 850 860 870 880 890 900 KQYIEKIAKN LDSEKEKELE RQARIEASLR EREREVQKAR SEQTKEIDRE REQHKREEAI 910 920 930 940 950 960 QNFKALLSDM VRSSDVSWSD TRRTLRKDHR WESGSLLERE EKEKLFNEHI EALTKKKREH 970 980 990 1000 1010 1020 FRQLLDETSA ITLTSTWKEV KKIIKEDPRC IKFSSSDRKK QREFEEYIRD KYITAKADFR 1030 1040 1050 1060 1070 1080 TLLKETKFIT YRSKKLIQES DQHLKDVEKI LQNDKRYLVL DCVPEERRKL IVAYVDDLDR 1090 RGPPPPPTAS EPTRRSTK
	Isoform 2 [UniParc]. Checksum: D02B6E70E31F1551	FASTA	1,077	121,690
	10 20 30 40 50 60 MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP PPFGMMRGPP 70 80 90 100 110 120 PPPRPPFGRP PFDPNMPPMP PPGGIPPPMG PPHLQRPPFM PPPMSSMPPP PGMMFPPGMP 130 140 150 160 170 180 PVTAPGTPAL PPTEEIWVEN KTPDGKVYYY NARTRESAWT KPDGVKVIQQ SELTPMLAAQ 190 200 210 220 230 240 AQVQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ 250 260 270 280 290 300 AQVQAQVQAQ VQAQAVGAST PTTSSPAPAV STSTSSSTPS STTSTTTTAT SVAQTVSTPT 310 320 330 340 350 360 TQDQTPSSAV SVATPTVSVS TPAPTATPVQ TVPQPHPQTL PPAVPHSVPQ PTTAIPAFPP 370 380 390 400 410 420 VMVPPFRVPL PGMPIPLPGV LPGMAPPIVP MIHPQVAIAA SPATLAGATA VSEWTEYKTA 430 440 450 460 470 480 DGKTYYYNNR TLESTWEKPQ ELKEKEKLEE KIKEPIKEPS EEPLPMETEE EDPKEEPIKE 490 500 510 520 530 540 IKEEPKEEEM TEEEKAAQKA KPVATAPIPG TPWCVVWTGD ERVFFYNPTT RLSMWDRPDD 550 560 570 580 590 600 LIGRADVDKI IQEPPHKKGM EELKKLRHPT PTMLSIQKWQ FSMSAIKEEQ ELMEEINEDE 610 620 630 640 650 660 PVKAKKRKRD DNKDIDSEKE AAMEAEIKAA RERAIVPLEA RMKQFKDMLL ERGVSAFSTW 670 680 690 700 710 720 EKELHKIVFD PRYLLLNPKE RKQVFDQYVK TRAEEERREK KNKIMQAKED FKKMMEEAKF 730 740 750 760 770 780 NPRATFSEFA AKHAKDSRFK AIEKMKDREA LFNEFVAAAR KKEKEDSKTR GEKIKSDFFE 790 800 810 820 830 840 LLSNHHLDSQ SRWSKVKDKV ESDPRYKAVD SSSMREDLFK QYIEKIAKNL DSEKEKELER 850 860 870 880 890 900 QARIEASLRE REREVQKARS EQTKEIDRER EQHKREEAIQ NFKALLSDMV RSSDVSWSDT 910 920 930 940 950 960 RRTLRKDHRW ESGSLLEREE KEKLFNEHIE ALTKKKREHF RQLLDETSAI TLTSTWKEVK 970 980 990 1000 1010 1020 KIIKEDPRCI KFSSSDRKKQ REFEEYIRDK YITAKADFRT LLKETKFITY RSKKLIQESD 1030 1040 1050 1060 1070 QHLKDVEKIL QNDKRYLVLD CVPEERRKLI VAYVDDLDRR GPPPPPTASE PTRRSTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription." Sune C., Hayashi T., Liu Y., Lane W.S., Young R.A., Garcia-Blanco M.A. Mol. Cell. Biol. 17:6029-6039(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 610-620; 745-753; 928-939 AND 945-955, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNA POLYMERASE II. Tissue: Cervix carcinoma.
[2]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Aortic endothelium.
[3]	"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 2).
[4]	"Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II." Carty S.M., Goldstrohm A.C., Sune C., Garcia-Blanco M.A., Greenleaf A.L. Proc. Natl. Acad. Sci. U.S.A. 97:9015-9020(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY, INTERACTION WITH RNA POLYMERASE II.
[5]	"The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1." Goldstrohm A.C., Albrecht T.R., Sune C., Bedford M.T., Garcia-Blanco M.A. Mol. Cell. Biol. 21:7617-7628(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 148-TYR--TYR-150; 446-TYR--TYR-448 AND 545-PHE--TYR-547, INTERACTION WITH RNA POLYMERASE II AND SF1.
[6]	"The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis." Holbert S., Denghien I., Kiechle T., Rosenblatt A., Wellington C., Hayden M.R., Margolis R.L., Ross C.A., Dausset J., Ferrante R.J., Neri C. Proc. Natl. Acad. Sci. U.S.A. 98:1811-1816(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HD, INDUCTION, TISSUE SPECIFICITY.
[7]	"FF domains of CA150 bind transcription and splicing factors through multiple weak interactions." Smith M.J., Kulkarni S., Pawson T. Mol. Cell. Biol. 24:9274-9285(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTATSF1, SUBCELLULAR LOCATION.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"General structural motifs of amyloid protofilaments." Ferguson N., Becker J., Tidow H., Tremmel S., Sharpe T.D., Krause G., Flinders J., Petrovich M., Berriman J., Oschkinat H., Fersht A.R. Proc. Natl. Acad. Sci. U.S.A. 103:16248-16253(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 428-464.
[10]	"Solution structure of WW domain and FF domains in transcription elongation regulator 1." RIKEN structural genomics initiative (RSGI) Submitted (APR-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 520-959.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF017789 mRNA. Translation: AAB80727.1.
AB209910 mRNA. Translation: BAD93147.1. Different initiation.
BC111727 mRNA. Translation: AAI11728.1.

IPI

IPI00247871.
IPI00744062.

PIR

T08599.

RefSeq

NP_001035095.1. NM_001040006.1.
NP_006697.2. NM_006706.3.

UniGene

Hs.735127.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DK7	NMR	-	A	520-579	[»]
2DOD	NMR	-	A	651-719	[»]
2DOE	NMR	-	A	784-853	[»]
2DOF	NMR	-	A	888-959	[»]
2E71	NMR	-	A	717-786	[»]
2KIQ	NMR	-	A	724-782	[»]
2KIS	NMR	-	A	659-724	[»]
2NNT	NMR	-	A/B/C/D	428-464	[»]
3HFH	X-ray	2.70	A/B	661-845	[»]
4FQG	X-ray	2.00	A/B	895-1081	[»]

ProteinModelPortal

O14776.

ModBase

Search...

Protein-protein interaction databases

IntAct

O14776. 11 interactions.

MINT

MINT-158391.

STRING

9606.ENSP00000296702.

PTM databases

PhosphoSite

O14776.

Proteomic databases

PaxDb

O14776.

PRIDE

O14776.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296702; ENSP00000296702; ENSG00000113649.
ENST00000394421; ENSP00000377943; ENSG00000113649.

GeneID

10915.

KEGG

hsa:10915.

UCSC

uc003lob.3. human.
uc003loc.3. human.

Organism-specific databases

CTD

10915.

GeneCards

GC05P145807.

HGNC

HGNC:15630. TCERG1.

MIM

605409. gene.

neXtProt

NX_O14776.

PharmGKB

PA38007.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5104.

HOGENOM

HOG000008544.

HOVERGEN

HBG062908.

InParanoid

O14776.

KO

K12824.

OMA

MEEMNED.

OrthoDB

EOG40CHGM.

PhylomeDB

O14776.

Gene expression databases

ArrayExpress

O14776.

Bgee

O14776.

CleanEx

HS_TCERG1.

Genevestigator

O14776.

GermOnline

ENSG00000113649. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.440. 5 hits.

InterPro

IPR002713. FF_domain.
IPR001202. WW_dom.
[Graphical view]

Pfam

PF01846. FF. 6 hits.
PF00397. WW. 2 hits.
[Graphical view]

SMART

SM00441. FF. 6 hits.
SM00456. WW. 3 hits.
[Graphical view]

SUPFAM

SSF81698. FF. 5 hits.
SSF51045. WW_Rsp5_WWP. 3 hits.

PROSITE

PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O14776.

GenomeRNAi

10915.

NextBio

41457.

SOURCE

Search...

Entry information

Entry name

TCRG1_HUMAN

Accession

Primary (citable) accession number: O14776
Secondary accession number(s): Q2NKN2, Q59EA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	July 24, 2007
Last modified:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.