Q15370 (ELOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription elongation factor B polypeptide 2

Alternative name(s):
Elongin 18 kDa subunit
Elongin-B
Short name=EloB
RNA polymerase II transcription factor SIII subunit B
SIII p18

Gene names

Name:

TCEB2

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	118 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.1 Ref.10 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.1 Ref.10
Pathway	Protein modification; protein ubiquitination.
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 By similarity. Substrate adapter protein can be a viral protein such as HIV Vif. Interacts with VHL. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with SPSB1. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.16
Subcellular location	Nucleus Probable.
Sequence similarities	Contains 1 ubiquitin-like domain.
Sequence caution	The sequence AAC08452.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of viral transcription Traceable author statement. Source: Reactome protein complex assembly Traceable author statement PubMed 7660129. Source: ProtInc protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway 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 viral reproduction Traceable author statement. Source: Reactome
Cellular_component	Cul2-RING ubiquitin ligase complex Inferred from direct assay PubMed 17636018. Source: UniProtKB Cul5-RING ubiquitin ligase complex Inferred from direct assay PubMed 17636018. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ubiquitin protein ligase binding Inferred from direct assay PubMed 17636018. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MED8	Q96G25	5	EBI-301238,EBI-394405
TCEB1	Q15369	3	EBI-301238,EBI-301231
vif	P12504	5	EBI-301238,EBI-779991	From a different organism.

Alternative products

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

Isoform 1 (identifier: Q15370-1)

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: Q15370-2)

The sequence of this isoform differs from the canonical sequence as follows:
     118-118: Q → HLHVHSQTMAKSRNTSWSQCPGLTACSTREPQDGPTQVHPRWGL

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 118

118

Transcription elongation factor B polypeptide 2

PRO_0000114914

Regions

Domain

1 – 66

66

Ubiquitin-like

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.6

Natural variations

Alternative sequence

118

1

Q → HLHVHSQTMAKSRNTSWSQC PGLTACSTREPQDGPTQVHP RWGL in isoform 2.

VSP_045784

Secondary structure

1

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118

Helix Strand Turn

Details...

Beta strand

2 – 10

9

Beta strand

12 – 19

8

Helix

24 – 35

12

Helix

39 – 41

3

Beta strand

42 – 46

5

Beta strand

49 – 51

3

Turn

57 – 61

5

Helix

64 – 66

3

Beta strand

73 – 79

7

Beta strand

82 – 84

3

Beta strand

96 – 98

3

Helix

101 – 103

3

Beta strand

110 – 112

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C045F58FBED0EC47	FASTA	118	13,133
	10 20 30 40 50 60 MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC 70 80 90 100 110 GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVQ
	Isoform 2 [UniParc]. Checksum: 72277A4ACF21429F	FASTA	161	17,911
	10 20 30 40 50 60 MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC 70 80 90 100 110 120 GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVHLH 130 140 150 160 VHSQTMAKSR NTSWSQCPGL TACSTREPQD GPTQVHPRWG L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog." Garrett K.P., Aso T., Bradsher J.N., Foundling S.I., Lane W.S., Conaway R.C., Conaway J.W. Proc. Natl. Acad. Sci. U.S.A. 92:7172-7176(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]	Bonaldo M.F., Lennon G., Soares M.B. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1). Tissue: Pancreas and Placenta.
[6]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-8 AND 44-80, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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].
[12]	"The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity." Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C., Feng Y., Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J., Ingvarsson S., Ratcliffe P.J., Longmore G.D., Sharp T.V. Nat. Cell Biol. 14:201-208(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH LIMD1; EGLN1/PHD2; VHL AND CUL2.
[13]	"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) IN COMPLEX WITH TCEB1 AND VHL.
[14]	"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) COMPLEX WITH TCEB1; VHL AND HIF1A.
[15]	"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 TCEB1; VHL AND HIF1A.
[16]	"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) IN COMPLEX WITH TCEB1 ANS SOX4, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42856 mRNA. Translation: AAA75522.1.
BM700019 mRNA. No translation available.
AC004493 Genomic DNA. Translation: AAC08452.1. Sequence problems.
AC092117 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85472.1.
CH471112 Genomic DNA. Translation: EAW85474.1.
BC013306 mRNA. Translation: AAH13306.1.
BC065000 mRNA. Translation: AAH65000.1.

IPI

IPI00026670.
IPI00410162.

PIR

I59405.

RefSeq

NP_009039.1. NM_007108.3.
NP_996896.1. NM_207013.2.

UniGene

Hs.172772.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LM8	X-ray	1.85	B	1-118	[»]
1LQB	X-ray	2.00	A	1-118	[»]
1VCB	X-ray	2.70	A/D/G/J	1-118	[»]
2C9W	X-ray	1.90	B	1-118	[»]
2IZV	X-ray	2.55	B	1-118	[»]
2JZ3	NMR	-	B	1-118	[»]
3DCG	X-ray	2.40	A/C	1-118	[»]
3ZKJ	X-ray	2.58	C/F	1-118	[»]
3ZRC	X-ray	2.90	A/D/G/J	1-118	[»]
3ZRF	X-ray	2.80	A/D/G/J	1-118	[»]
3ZTC	X-ray	2.65	A/D/G/J	1-118	[»]
3ZTD	X-ray	2.79	A/D/G/J	1-118	[»]
3ZUN	X-ray	2.50	A/D/G/J	1-118	[»]
4AJY	X-ray	1.73	B	1-118	[»]
4AWJ	X-ray	2.50	A/D/G/J	1-104	[»]
4B95	X-ray	2.80	A/D/G/J	1-118	[»]
4B9K	X-ray	2.00	A/D/G/J	1-104	[»]

ProteinModelPortal

Q15370.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29570N.

IntAct

Q15370. 28 interactions.

MINT

MINT-1323839.

STRING

9606.ENSP00000262306.

PTM databases

PhosphoSite

Q15370.

Polymorphism databases

DMDM

32699512.

Proteomic databases

PaxDb

Q15370.

PeptideAtlas

Q15370.

PRIDE

Q15370.

Protocols and materials databases

DNASU

6923.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262306; ENSP00000262306; ENSG00000103363.
ENST00000409906; ENSP00000386652; ENSG00000103363.

GeneID

6923.

KEGG

hsa:6923.

UCSC

uc002crn.3. human.

Organism-specific databases

CTD

6923.

GeneCards

GC16M002824.

HGNC

HGNC:11619. TCEB2.

MIM

600787. gene.

neXtProt

NX_Q15370.

PharmGKB

PA36378.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG316144.

HOGENOM

HOG000293425.

HOVERGEN

HBG008581.

KO

K03873.

OrthoDB

EOG4BG8X6.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1apathway. Hypoxic and oxygen homeostasis regulation of HIF-1-alpha.

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.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q15370.

Bgee

Q15370.

CleanEx

HS_TCEB2.

Genevestigator

Q15370.

GermOnline

ENSG00000103363. Homo sapiens.

Family and domain databases

InterPro

IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

Pfam

PF00240. ubiquitin. 1 hit.
[Graphical view]

SMART

SM00213. UBQ. 1 hit.
[Graphical view]

PROSITE

PS00299. UBIQUITIN_1. False negative.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q15370.

GenomeRNAi

6923.

NextBio

27083.

SOURCE

Search...

Entry information

Entry name

ELOB_HUMAN

Accession

Primary (citable) accession number: Q15370
Secondary accession number(s): B7WPD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2003
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 134 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.