Q15369 (ELOC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription elongation factor B polypeptide 1

Alternative name(s):
Elongin 15 kDa subunit
Elongin-C
Short name=EloC
RNA polymerase II transcription factor SIII subunit C
SIII p15

Gene names

Name:

TCEB1

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	112 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). Ref.9 The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. Ref.9
Subunit structure	Heterotrimer of an A (A1, A2 or A3), B and C subunit. Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and a substrate adapter protein that can be either SOCS1, SOCS5, TCEB3, VHL or WSB1. The elongin BC complex is part of a complex with hydroxylated HIF1A. Substrate adapter protein can be a viral protein such as HIV Vif. Interacts with VHL. Interacts with TMF1. Interacts with human respiratory syncytial virus (HRSV) protein NS1. Interacts with SPSB1. posed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.17
Subcellular location	Nucleus Probable.
Tissue specificity	Overexpressed in prostate cancer cell line PC-3 and breast cancer cell line SK-BR-3. Ref.6
Sequence similarities	Belongs to the SKP1 family.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to hypoxia Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome positive regulation of transcription elongation from RNA polymerase II promoter Inferred from electronic annotation. Source: Ensembl positive regulation of viral transcription Traceable author statement. Source: Reactome regulation of transcription from RNA polymerase II promoter Traceable author statement PubMed 7660129. Source: ProtInc regulation of transcription from RNA polymerase II promoter in response to hypoxia Traceable author statement. Source: Reactome transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro viral process Traceable author statement. Source: Reactome
Cellular_component	VCB complex Inferred from electronic annotation. Source: Ensembl cytosol Traceable author statement. Source: Reactome elongin complex Inferred from electronic annotation. Source: Ensembl nucleoplasm Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CUL2	Q13617	5	EBI-301231,EBI-456179
GAMMAHV.ORF73	O41974	2	EBI-301231,EBI-6933128	From a different organism.
MED8	Q96G25	3	EBI-301231,EBI-394405
SOCS1	O15524	2	EBI-301231,EBI-968198
SOCS2	O14508	2	EBI-301231,EBI-617737
SPSB2	Q99619	3	EBI-301231,EBI-2323209
SPSB4	Q96A44	2	EBI-301231,EBI-2323233
TCEB2	Q15370	8	EBI-301231,EBI-301238
vif	P12504	5	EBI-301231,EBI-779991	From a different organism.

Alternative products

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

Isoform 1 (identifier: Q15369-1)

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: Q15369-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 112

112

Transcription elongation factor B polypeptide 1

PRO_0000187258

Natural variations

Alternative sequence

1 – 16

16

Missing in isoform 2.

VSP_045955

Secondary structure

1

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112

Helix Strand Turn

Details...

Beta strand

18 – 22

5

Beta strand

24 – 26

3

Beta strand

28 – 32

5

Helix

33 – 36

4

Helix

40 – 46

7

Beta strand

47 – 50

4

Helix

54 – 58

5

Beta strand

59 – 61

3

Helix

67 – 83

17

Turn

84 – 86

3

Helix

97 – 99

3

Helix

100 – 110

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 98D88696E883538B	FASTA	112	12,473
	10 20 30 40 50 60 MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV 70 80 90 100 110 NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA LELLMAANFL DC
	Isoform 2 [UniParc]. Checksum: 749EC1F8EC3DB62E	FASTA	96	10,832
	10 20 30 40 50 60 MYVKLISSDG HEFIVKREHA LTSGTIKAML SGPGQFAENE TNEVNFREIP SHVLSKVCMY 70 80 90 FTYKVRYTNS STEIPEFPIA PEIALELLMA ANFLDC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human cDNA encoding the small subunit of RNA polymerase II transcription factor SIII." Garrett K.P., Haque D., Conaway R.C., Conaway J.W. Gene 150:413-414(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Peripheral blood.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Colon.
[3]	"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].
[4]	"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: Skin.
[5]	"Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 ubiquitin ligase activity." Aso T., Yamazaki K., Aigaki T., Kitajima S. Biochem. Biophys. Res. Commun. 276:355-361(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VHL.
[6]	"Amplification and overexpression of Elongin C gene discovered in prostate cancer by cDNA microarrays." Porkka K., Saramaeki O., Tanner M., Visakorpi T. Lab. Invest. 82:629-637(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation." Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D. Genes Dev. 18:2861-2866(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV VIF.
[8]	"TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3." Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U. Oncogene 23:8908-8919(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TMF1.
[9]	"Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling." Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N., Rechavi G., Yarden Y. J. Biol. Chem. 280:7038-7048(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EGFR DEGRADATION, INTERACTION WITH SOCS5.
[10]	"Structural basis for protein recognition by B30.2/SPRY domains." Woo J.S., Suh H.Y., Park S.Y., Oh B.H. Mol. Cell 24:967-976(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPSB1.
[11]	"Respiratory syncytial virus NS1 protein degrades STAT2 by using the Elongin-Cullin E3 ligase." Elliott J., Lynch O.T., Suessmuth Y., Qian P., Boyd C.R., Burrows J.F., Buick R., Stevenson N.J., Touzelet O., Gadina M., Power U.F., Johnston J.A. J. Virol. 81:3428-3436(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HRSV PROTEIN NS1.
[12]	"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].
[13]	"The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 activation by suppressing PP5." Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., Kuranaga E., Miura M., Takeda K., Ichijo H. Mol. Cell 48:692-704(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KLHDC10.
[14]	"Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function." Stebbins C.E., Kaelin W.G. Jr., Pavletich N.P. Science 284:455-461(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 17-112 IN COMPLEX WITH 1-120 OF TCEB2 AND 54-213 OF VHL.
[15]	"Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL." Hon W.-C., Wilson M.I., Harlos K., Claridge T.D.W., Schofield C.J., Pugh C.W., Maxwell P.H., Ratcliffe P.J., Stuart D.I., Jones E.Y. Nature 417:975-978(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2; 52-113 OF VHL AND 549-582 OF HIF1A.
[16]	"Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling." Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr., Pavletich N.P. Science 296:1886-1889(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH TCEB2; 54-113 OF VHL AND 556-575 OF HIF1A.
[17]	"Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation." Bullock A.N., Rodriguez M.C., Debreczeni J.E., Songyang Z., Knapp S. Structure 15:1493-1504(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2 ANS SOX4, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L34587 mRNA. Translation: AAA67650.1.
BX649138 mRNA. No translation available.
AC022868 Genomic DNA. No translation available.
BC013809 mRNA. Translation: AAH13809.1.
BC093065 mRNA. Translation: AAH93065.1.
BC100028 mRNA. Translation: AAI00029.1.
BC100283 mRNA. Translation: AAI00284.1.

RefSeq

NP_001191786.1. NM_001204857.1.
NP_001191787.1. NM_001204858.1.
NP_001191788.1. NM_001204859.1.
NP_001191789.1. NM_001204860.1.
NP_001191790.1. NM_001204861.1.
NP_001191791.1. NM_001204862.1.
NP_001191792.1. NM_001204863.1.
NP_001191793.1. NM_001204864.1.
NP_005639.1. NM_005648.3.
XP_005251347.1. XM_005251290.2.

UniGene

Hs.533437.
Hs.554594.
Hs.731928.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LM8	X-ray	1.85	C	17-112	[»]
1LQB	X-ray	2.00	B	17-112	[»]
1VCB	X-ray	2.70	B/E/H/K	1-112	[»]
2C9W	X-ray	1.90	C	17-112	[»]
2IZV	X-ray	2.55	C	17-112	[»]
2MA9	NMR	-	C	19-109	[»]
3DCG	X-ray	2.40	B/D	17-112	[»]
3ZKJ	X-ray	2.58	B/E	17-112	[»]
3ZNG	X-ray	2.85	B/E	17-112	[»]
3ZRC	X-ray	2.90	B/E/H/K	17-112	[»]
3ZRF	X-ray	2.80	B/E/H/K	17-112	[»]
3ZTC	X-ray	2.65	B/E/H/K	17-112	[»]
3ZTD	X-ray	2.79	B/E/H/K	17-112	[»]
3ZUN	X-ray	2.50	B/E/H/K	17-112	[»]
4AJY	X-ray	1.73	C	17-112	[»]
4AWJ	X-ray	2.50	B/E/H/K	17-112	[»]
4B95	X-ray	2.80	B/E/H/K	17-112	[»]
4B9K	X-ray	2.00	B/E/H/K	17-112	[»]
4BKS	X-ray	2.20	B/E/H/K	17-112	[»]
4BKT	X-ray	2.35	B/E/H/K	17-112	[»]
4N9F	X-ray	3.30	5/B/E/K/Q/T/Y/Z/h/n/t/z	17-112	[»]

ProteinModelPortal

Q15369.

SMR

Q15369. Positions 17-112.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

112783. 103 interactions.

DIP

DIP-29571N.

IntAct

Q15369. 51 interactions.

MINT

MINT-1323870.

STRING

9606.ENSP00000284811.

PTM databases

PhosphoSite

Q15369.

Polymorphism databases

DMDM

32699511.

Proteomic databases

PaxDb

Q15369.

PRIDE

Q15369.

Protocols and materials databases

DNASU

6921.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000284811; ENSP00000284811; ENSG00000154582. [Q15369-1]
ENST00000518127; ENSP00000428334; ENSG00000154582. [Q15369-1]
ENST00000519487; ENSP00000429596; ENSG00000154582. [Q15369-1]
ENST00000520210; ENSP00000430224; ENSG00000154582. [Q15369-2]
ENST00000520242; ENSP00000428171; ENSG00000154582. [Q15369-1]
ENST00000522337; ENSP00000429906; ENSG00000154582. [Q15369-1]
ENST00000523815; ENSP00000428074; ENSG00000154582. [Q15369-1]

GeneID

6921.

KEGG

hsa:6921.

UCSC

uc003xzx.2. human. [Q15369-1]

Organism-specific databases

CTD

6921.

GeneCards

GC08M074858.

HGNC

HGNC:11617. TCEB1.

MIM

600788. gene.

neXtProt

NX_Q15369.

PharmGKB

PA36376.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG298860.

HOGENOM

HOG000216525.

HOVERGEN

HBG007440.

InParanoid

Q15369.

KO

K03872.

OMA

YFHYWYR.

OrthoDB

EOG77M8QN.

PhylomeDB

Q15369.

TreeFam

TF300233.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q15369.

Bgee

Q15369.

CleanEx

HS_TCEB1.

Genevestigator

Q15369.

Family and domain databases

Gene3D

3.30.710.10. 1 hit.

InterPro

IPR011333. BTB/POZ_fold.
IPR001232. Skp1_comp.
IPR016073. Skp1_comp_POZ.
[Graphical view]

Pfam

PF03931. Skp1_POZ. 1 hit.
[Graphical view]

SMART

SM00512. Skp1. 1 hit.
[Graphical view]

SUPFAM

SSF54695. SSF54695. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

TCEB1. human.

EvolutionaryTrace

Q15369.

GeneWiki

TCEB1.

GenomeRNAi

6921.

NextBio

27077.

PRO

Q15369.

SOURCE

Search...

Entry information

Entry name

ELOC_HUMAN

Accession

Primary (citable) accession number: Q15369
Secondary accession number(s): E5RGD9, Q567Q6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2003
Last sequence update:	November 1, 1996
Last modified:	April 16, 2014
This is version 137 of the entry and version 1 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.