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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.7 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.7
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. Ref.5 Ref.6 Ref.7
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
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. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular function	protein binding Inferred from physical interaction Ref.7. 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

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.4 Ref.8

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

Turn

57 – 61

5

Turn

64 – 66

3

Beta strand

73 – 79

7

Beta strand

82 – 84

3

Helix

101 – 103

3

Sequences

	Sequence		Length	Mass (Da)
	Q15370 [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

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: 7638163] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"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: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas and Placenta.
[4]	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.
[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: 11006129] [Abstract] Cited for: INTERACTION WITH VHL.
[6]	"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: 15574592] [Abstract] Cited for: INTERACTION WITH HIV VIF.
[7]	"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: 15590694] [Abstract] Cited for: FUNCTION IN EGFR DEGRADATION, INTERACTION WITH SOCS5.
[8]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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: 10205047] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH TCEB1 AND VHL.
[11]	"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: 12050673] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) COMPLEX WITH TCEB1; VHL AND HIF1A.
[12]	"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: 12004076] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH TCEB1; VHL AND HIF1A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42856 mRNA. Translation: AAA75522.1.
AC004493 Genomic DNA. Translation: AAC08452.1. Sequence problems.
BC013306 mRNA. Translation: AAH13306.1.
BC065000 mRNA. Translation: AAH65000.1.

IPI

IPI00026670.

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	[»]
2XAI	X-ray	2.58	C/F	1-118	[»]
3DCG	X-ray	2.40	A/C	1-118	[»]

ProteinModelPortal

Q15370.

SMR

Q15370. Positions 1-118.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29570N.

IntAct

Q15370. 22 interactions.

MINT

MINT-1323839.

STRING

Q15370.

PTM databases

PhosphoSite

Q15370.

Polymorphism databases

DMDM

32699512.

Proteomic databases

PeptideAtlas

Q15370.

PRIDE

Q15370.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000409906; ENSP00000386652; ENSG00000103363.

GeneID

6923.

KEGG

hsa:6923.

UCSC

uc002crm.1. human.

Organism-specific databases

CTD

6923.

GeneCards

GC16M002824.

H-InvDB

HIX0038597.

HGNC

HGNC:11619. TCEB2.

MIM

600787. gene.

neXtProt

NX_Q15370.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20176.

GeneTree

ENSGT00390000018316.

HOVERGEN

HBG008581.

OrthoDB

EOG4BG8X6.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_6185. HIV Infection.
REACT_6900. Immune System.
REACT_71. Gene Expression.
REACT_769. Pausing and recovery of elongation.

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]

KO

K03873.

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

NextBio

27083.

SOURCE

Search...

Entry information

Entry name

ELOB_HUMAN

Accession

Primary (citable) accession number: Q15370

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2003
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 119 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.