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Q9UBF6 (RBX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RING-box protein 2

Short name=Rbx2
Alternative name(s):
CKII beta-binding protein 1
Short name=CKBBP1
RING finger protein 7
Regulator of cullins 2
Sensitive to apoptosis gene protein
Gene names
Name:RNF7
Synonyms:RBX2, ROC2, SAG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length113 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.10

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.2 Ref.10 Ref.13

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ASB2Q96Q272EBI-398632,EBI-2880677
IKBKGQ9Y6K93EBI-398632,EBI-81279
vifP125044EBI-398632,EBI-779991From a different organism.

Alternative products

This entry describes 4 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.
Isoform 3 (identifier: Q9UBF6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     57-113: VMDACLRCQA...QDWVVQRIGK → MPVLDVKLKTNKRTVLWSGENVIIPSTTAACPCG
Isoform 4 (identifier: Q9UBF6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     59-74: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 113112RING-box protein 2
PRO_0000056023

Regions

Zinc finger61 – 10343RING-type

Sites

Metal binding501Zinc 1 By similarity
Metal binding531Zinc 1 By similarity
Metal binding611Zinc 3 By similarity
Metal binding641Zinc 3 By similarity
Metal binding731Zinc 3 By similarity
Metal binding801Zinc 2 By similarity
Metal binding821Zinc 2 By similarity
Metal binding851Zinc 1 By similarity
Metal binding871Zinc 3 By similarity
Metal binding881Zinc 1 By similarity
Metal binding991Zinc 2 By similarity
Metal binding1021Zinc 2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.12
Modified residue101Phosphothreonine; by CK2 Ref.11

Natural variations

Alternative sequence57 – 11357VMDAC…QRIGK → MPVLDVKLKTNKRTVLWSGE NVIIPSTTAACPCG in isoform 3.
VSP_041444
Alternative sequence59 – 7416Missing in isoform 4.
VSP_044525
Alternative sequence60 – 11354ACLRC…QRIGK → EGIGVRNWSEALNLINASEM GFDCRSGSTALAVPSVSLAS HQPCLDDHR in isoform 2.
VSP_008449

Experimental info

Sequence conflict231K → T in AAD30147. Ref.2

Secondary structure

................. 113
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CE1E6CAC940C8257

FASTA11312,683
        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) [UniParc].

Checksum: 77A887E012AEE520
Show »

FASTA10811,557
Isoform 3 [UniParc].

Checksum: E26F96D19B016540
Show »

FASTA909,642
Isoform 4 [UniParc].

Checksum: 5277FEE26DCEB81F
Show »

FASTA9710,876

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Corpus callosum and Uterus.
[7]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.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. expand/collapse author list , 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].
[9]"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: Brain and Kidney.
[10]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CUL1, FUNCTION.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-10 BY CK2.
[12]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBE2F.
[14]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AK289894 mRNA. Translation: BAF82583.1.
DB272382 mRNA. No translation available.
AC112771 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78991.1.
CH471052 Genomic DNA. Translation: EAW78992.1.
CH471052 Genomic DNA. Translation: EAW78994.1.
CH471052 Genomic DNA. Translation: EAW78995.1.
CH471052 Genomic DNA. Translation: EAW78996.1.
BC005966 mRNA. Translation: AAH05966.1.
BC008627 mRNA. Translation: AAH08627.1.
CCDSCCDS3118.1. [Q9UBF6-1]
CCDS43158.1. [Q9UBF6-3]
CCDS56283.1. [Q9UBF6-4]
RefSeqNP_001188299.1. NM_001201370.1. [Q9UBF6-4]
NP_055060.1. NM_014245.4. [Q9UBF6-1]
NP_899060.1. NM_183237.2. [Q9UBF6-3]
UniGeneHs.134623.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ECLNMR-A40-113[»]
ProteinModelPortalQ9UBF6.
SMRQ9UBF6. Positions 40-113.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114977. 52 interactions.
IntActQ9UBF6. 28 interactions.
MINTMINT-1470812.
STRING9606.ENSP00000273480.

PTM databases

PhosphoSiteQ9UBF6.

Polymorphism databases

DMDM37538003.

Proteomic databases

MaxQBQ9UBF6.
PaxDbQ9UBF6.
PRIDEQ9UBF6.

Protocols and materials databases

DNASU9616.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273480; ENSP00000273480; ENSG00000114125. [Q9UBF6-1]
ENST00000393000; ENSP00000376725; ENSG00000114125. [Q9UBF6-3]
ENST00000477012; ENSP00000419339; ENSG00000114125. [Q9UBF6-2]
ENST00000480908; ENSP00000419084; ENSG00000114125. [Q9UBF6-4]
GeneID9616.
KEGGhsa:9616.
UCSCuc003euc.3. human. [Q9UBF6-3]
uc003eud.3. human. [Q9UBF6-1]
uc021xeu.1. human. [Q9UBF6-4]

Organism-specific databases

CTD9616.
GeneCardsGC03P141457.
HGNCHGNC:10070. RNF7.
HPAHPA036995.
MIM603863. gene.
neXtProtNX_Q9UBF6.
PharmGKBPA34444.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5194.
HOVERGENHBG001507.
InParanoidQ9UBF6.
KOK10611.
OMADICAICR.
OrthoDBEOG7CG721.
PhylomeDBQ9UBF6.
TreeFamTF351049.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UBF6.
BgeeQ9UBF6.
CleanExHS_RNF7.
HS_SAG.
GenevestigatorQ9UBF6.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamPF12678. zf-rbx1. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UBF6.
GeneWikiRNF7.
GenomeRNAi9616.
NextBio36073.
PROQ9UBF6.
SOURCESearch...

Entry information

Entry nameRBX2_HUMAN
AccessionPrimary (citable) accession number: Q9UBF6
Secondary accession number(s): A8K1H9 expand/collapse secondary AC list , A8MTB5, C9JYL3, D3DNF7, D3DNF8, Q9BXN8, Q9Y5M7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM