RING-box protein 2 - Homo sapiens (Human)

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General annotation (Comments)

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Reviewed, UniProtKB/Swiss-Prot Q9UBF6 (RBX2_HUMAN)

Last modified June 16, 2009. Version 70. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Protein names

Recommended name:
    RING-box protein 2
      Short name=Rbx2
Alternative name(s):
    RING finger protein 7
    Regulator of cullins 2
    CKII beta-binding protein 1
      Short name=CKBBP1
    Sensitive to apoptosis gene protein

Gene names

Name:	RNF7
Synonyms:	RBX2, ROC2, SAG

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Sequence length	113 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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Function	Probable component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL5 via its interaction with UBE2F. May play a role in protecting cells from apoptosis induced by redox agents. Ref.7
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Probable part of SCF complexes, which consist of SKP1, CUL1, RNF7/RBX2 and a F-box protein. Interacts (preferentially) with CUL5. Also interacts (with lower preference) with CUL1, CUL2, CUL3, CUL4A and CUL4B. Interacts with UBE2F. Interacts with CSNK2B, the interaction is not affected by phosphorylation by CK2. Ref.7 Ref.2
Subcellular location	Cytoplasm. Nucleus. Ref.3
Tissue specificity	Expressed in heart, liver, skeletal muscle and pancreas. At very low levels expressed in brain, placenta and lung. Ref.1
Induction	By 1,10-phenanthroline. Ref.3
Domain	The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion.
Post-translational modification	Phosphorylation by CK2 is required for efficient degradation of NFKBIA and CDKN1B.
Sequence similarities	Belongs to the RING-box family. Contains 1 RING-type zinc finger.

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Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	anti-apoptosis Ref.3 Traceable author statement. Source: ProtInc induction of apoptosis by oxidative stress Ref.3 Traceable author statement. Source: ProtInc modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein neddylation Ref.9 Inferred from direct assay. Source: UniProtKB redox signal response Ref.3 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Ref.3 Non-traceable author statement. Source: UniProtKB nucleus Ref.3 Non-traceable author statement. Source: UniProtKB
Molecular function	NEDD8 ligase activity Ref.9 Inferred from direct assay. Source: UniProtKB copper ion binding Ref.3 Traceable author statement. Source: ProtInc protein binding Ref.9 Inferred from physical interaction. Source: UniProtKB zinc ion binding Ref.3 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 113

113

RING-box protein 2

PRO_0000056023

Zinc finger

61 – 103

RING-type

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 3 By similarity

Metal binding

Zinc 3 By similarity

Metal binding

Zinc 3 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 3 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

102

Zinc 2 By similarity

Modified residue

Phosphothreonine; by CK2

Alternative sequence

60 – 113

ACLRC…QRIGK → EGIGVRNWSEALNLINASEM GFDCRSGSTALAVPSVSLAS HQPCLDDHR in isoform 2.

VSP_008449

Sequence conflict

K → T in AAD30147. Ref.2

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Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: CE1E6CAC940C8257 Show »	FASTA	113	12,683
10 20 30 40 50 60 MADVEDGEET CALASHSGSS GSKSGGDKMF SLKKWNAVAM WSWDVECDTC AICRVQVMDA 70 80 90 100 110 CLRCQAENKQ EDCVVVWGEC NHSFHNCCMS LWVKQNNRCP LCQQDWVVQR IGK « Hide
Isoform 2 (SAG-v). Checksum: 77A887E012AEE520 Show »	FASTA	108	11,557
10 20 30 40 50 60 MADVEDGEET CALASHSGSS GSKSGGDKMF SLKKWNAVAM WSWDVECDTC AICRVQVMDE 70 80 90 100 GIGVRNWSEA LNLINASEMG FDCRSGSTAL AVPSVSLASH QPCLDDHR « Hide

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	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein kinase CKII interacts with and phosphorylates the SAG protein containing ring-H2 finger motif." Son M.-Y., Park J.-W., Kim Y.-S., Kang S.-W., Marshak D.R., Park W., Bae Y.-S. Biochem. Biophys. Res. Commun. 263:743-748(1999) [PubMed: 10512750] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]	"ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity." Ohta T., Michel J.J., Schottelius A.J., Xiong Y. Mol. Cell 3:535-541(1999) [PubMed: 10230407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CULLINS.
[3]	"SAG, a novel zinc RING finger protein that protects cells from apoptosis induced by redox agents." Duan H., Wang Y., Aviram M., Swaroop M., Loo J.A., Bian J., Tian Y., Mueller T., Bisgaier C.L., Sun Y. Mol. Cell. Biol. 19:3145-3155(1999) [PubMed: 10082581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION.
[4]	"SAG/ROC2/Rbx2/Hrt2, a component of SCF E3 ubiquitin ligase: genomic structure, a splicing variant, and two family pseudogenes." Swaroop M., Gosink M., Sun Y. DNA Cell Biol. 20:425-434(2001) [PubMed: 11506706] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"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] (ISOFORM 1). Tissue: Brain and Kidney.
[7]	"Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth, but not for germination: chip profiling implicates its role in cell cycle regulation." Swaroop M., Wang Y., Miller P., Duan H., Jatkoe T., Madore S.J., Sun Y. Oncogene 19:2855-2866(2000) [PubMed: 10851089] [Abstract] Cited for: INTERACTION WITH CUL1, FUNCTION.
[8]	"Phosphorylation of threonine 10 on CKBBP1/SAG/ROC2/Rbx2 by protein kinase CKII promotes the degradation of IkappaBalpha and p27Kip1." Kim Y.-S., Lee J.-Y., Son M.-Y., Park W., Bae Y.-S. J. Biol. Chem. 278:28462-28469(2003) [PubMed: 12748192] [Abstract] Cited for: PHOSPHORYLATION BY CK2.
[9]	"E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification." Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A. Mol. Cell 33:483-495(2009) [PubMed: 19250909] [Abstract] Cited for: INTERACTION WITH UBE2F.
[10]	"Solution structure of the RING domain of the human RING-box protein 2." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 40-113.
+	Additional computationally mapped references.

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Atlas of Genetics and Cytogenetics in Oncology and Haematology

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AF164679 mRNA. Translation: AAD55984.1.
AF142060 mRNA. Translation: AAD30147.1.
AF092878 mRNA. Translation: AAD25962.1.
AF312226 mRNA. Translation: AAK37450.1.
BT007348 mRNA. Translation: AAP36012.1.
BC005966 mRNA. Translation: AAH05966.1.
BC008627 mRNA. Translation: AAH08627.1.

IPI

IPI00030891.
IPI00033132.

RefSeq

NP_055060.1.
NP_899060.1.

UniGene

Hs.134623

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ECL	NMR	-	A	40-113	[»]

ModBase

Search...

IntAct

Q9UBF6. 3 interactions.

PhosphoSite

Q9UBF6.

PRIDE

Q9UBF6.

Ensembl

ENSG00000114125. Homo sapiens. [Contig view]

GeneID

9616.

KEGG

hsa:9616.

GeneCards

GC03P142939.

H-InvDB

HIX0003730.

HGNC

HGNC:10070. RNF7.

MIM

603863. gene.

PharmGKB

PA34444.

GenAtlas

Search...

HOGENOM

Q9UBF6.

HOVERGEN

Q9UBF6.

OMA

Q9UBF6. LRCQADN.

ArrayExpress

Q9UBF6.

Bgee

Q9UBF6.

CleanEx

HS_RNF7.
HS_SAG.

GermOnline

ENSG00000114125. Homo sapiens.

InterPro

IPR001841. Znf_RING.
[Graphical view]

SMART

SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

NextBio

36073.

SOURCE

Search...

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

Isoform 1 (identifier: Q9UBF6-1)

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: Q9UBF6-2)

Also known as: SAG-v;

The sequence of this isoform differs from the canonical sequence as follows:
60-113: ACLRCQAENK...QDWVVQRIGK → EGIGVRNWSE...SHQPCLDDHR

Note: Inactive.

Entry name

RBX2_HUMAN

Accession

Primary (citable) accession number: Q9UBF6
Secondary accession number(s): Q9BXN8, Q9Y5M7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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