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Q9UBF6

- RBX2_HUMAN

UniProt

Q9UBF6 - RBX2_HUMAN

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Protein

RING-box protein 2

Gene
RNF7, RBX2, ROC2, SAG
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Zinc 1 By similarity
Metal bindingi53 – 531Zinc 1 By similarity
Metal bindingi61 – 611Zinc 3 By similarity
Metal bindingi64 – 641Zinc 3 By similarity
Metal bindingi73 – 731Zinc 3 By similarity
Metal bindingi80 – 801Zinc 2 By similarity
Metal bindingi82 – 821Zinc 2 By similarity
Metal bindingi85 – 851Zinc 1 By similarity
Metal bindingi87 – 871Zinc 3 By similarity
Metal bindingi88 – 881Zinc 1 By similarity
Metal bindingi99 – 991Zinc 2 By similarity
Metal bindingi102 – 1021Zinc 2 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri61 – 10343RING-typeAdd
BLAST

GO - Molecular functioni

  1. copper ion binding Source: ProtInc
  2. NEDD8 ligase activity Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. zinc ion binding Source: ProtInc

GO - Biological processi

  1. intrinsic apoptotic signaling pathway in response to oxidative stress Source: ProtInc
  2. negative regulation of apoptotic process Source: ProtInc
  3. protein neddylation Source: UniProtKB
  4. protein ubiquitination Source: UniProtKB-UniPathway
  5. response to redox state Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RNF7
Synonyms:RBX2, ROC2, SAG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:10070. RNF7.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. Cul5-RING ubiquitin ligase complex Source: MGI
  2. cytoplasm Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 113112RING-box protein 2PRO_0000056023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei10 – 101Phosphothreonine; by CK21 Publication

Post-translational modificationi

Phosphorylation by CK2 is required for efficient degradation of NFKBIA and CDKN1B.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UBF6.
PaxDbiQ9UBF6.
PRIDEiQ9UBF6.

PTM databases

PhosphoSiteiQ9UBF6.

Expressioni

Tissue specificityi

Expressed in heart, liver, skeletal muscle and pancreas. At very low levels expressed in brain, placenta and lung.1 Publication

Inductioni

By 1,10-phenanthroline.1 Publication

Gene expression databases

ArrayExpressiQ9UBF6.
BgeeiQ9UBF6.
CleanExiHS_RNF7.
HS_SAG.
GenevestigatoriQ9UBF6.

Organism-specific databases

HPAiHPA036995.

Interactioni

Subunit structurei

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 CK2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASB2Q96Q272EBI-398632,EBI-2880677
IKBKGQ9Y6K93EBI-398632,EBI-81279
vifP125044EBI-398632,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi114977. 52 interactions.
IntActiQ9UBF6. 28 interactions.
MINTiMINT-1470812.
STRINGi9606.ENSP00000273480.

Structurei

Secondary structure

1
113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni51 – 544
Helixi64 – 674
Turni70 – 723
Beta strandi75 – 784
Beta strandi83 – 853
Helixi86 – 927
Turni93 – 953
Turni100 – 1023
Beta strandi108 – 1125

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ECLNMR-A40-113[»]
ProteinModelPortaliQ9UBF6.
SMRiQ9UBF6. Positions 40-113.

Miscellaneous databases

EvolutionaryTraceiQ9UBF6.

Family & Domainsi

Domaini

The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion.

Sequence similaritiesi

Belongs to the RING-box family.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5194.
HOVERGENiHBG001507.
InParanoidiQ9UBF6.
KOiK10611.
OMAiDICAICR.
OrthoDBiEOG7CG721.
PhylomeDBiQ9UBF6.
TreeFamiTF351049.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamiPF12678. zf-rbx1. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UBF6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MADVEDGEET CALASHSGSS GSKSGGDKMF SLKKWNAVAM WSWDVECDTC    50
AICRVQVMDA CLRCQAENKQ EDCVVVWGEC NHSFHNCCMS LWVKQNNRCP 100
LCQQDWVVQR IGK 113
Length:113
Mass (Da):12,683
Last modified:May 1, 2000 - v1
Checksum:iCE1E6CAC940C8257
GO
Isoform 2 (identifier: Q9UBF6-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:108
Mass (Da):11,557
Checksum:i77A887E012AEE520
GO
Isoform 3 (identifier: Q9UBF6-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-113: VMDACLRCQA...QDWVVQRIGK → MPVLDVKLKTNKRTVLWSGENVIIPSTTAACPCG

Show »
Length:90
Mass (Da):9,642
Checksum:iE26F96D19B016540
GO
Isoform 4 (identifier: Q9UBF6-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-74: Missing.

Note: No experimental confirmation available.

Show »
Length:97
Mass (Da):10,876
Checksum:i5277FEE26DCEB81F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei57 – 11357VMDAC…QRIGK → MPVLDVKLKTNKRTVLWSGE NVIIPSTTAACPCG in isoform 3. VSP_041444Add
BLAST
Alternative sequencei59 – 7416Missing in isoform 4. VSP_044525Add
BLAST
Alternative sequencei60 – 11354ACLRC…QRIGK → EGIGVRNWSEALNLINASEM GFDCRSGSTALAVPSVSLAS HQPCLDDHR in isoform 2. VSP_008449Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231K → T in AAD30147. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3118.1. [Q9UBF6-1]
CCDS43158.1. [Q9UBF6-3]
CCDS56283.1. [Q9UBF6-4]
RefSeqiNP_001188299.1. NM_001201370.1. [Q9UBF6-4]
NP_055060.1. NM_014245.4. [Q9UBF6-1]
NP_899060.1. NM_183237.2. [Q9UBF6-3]
UniGeneiHs.134623.

Genome annotation databases

EnsembliENST00000273480; ENSP00000273480; ENSG00000114125. [Q9UBF6-1]
ENST00000393000; ENSP00000376725; ENSG00000114125. [Q9UBF6-3]
ENST00000477012; ENSP00000419339; ENSG00000114125. [Q9UBF6-2]
ENST00000480908; ENSP00000419084; ENSG00000114125. [Q9UBF6-4]
GeneIDi9616.
KEGGihsa:9616.
UCSCiuc003euc.3. human. [Q9UBF6-3]
uc003eud.3. human. [Q9UBF6-1]
uc021xeu.1. human. [Q9UBF6-4]

Polymorphism databases

DMDMi37538003.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3118.1. [Q9UBF6-1 ]
CCDS43158.1. [Q9UBF6-3 ]
CCDS56283.1. [Q9UBF6-4 ]
RefSeqi NP_001188299.1. NM_001201370.1. [Q9UBF6-4 ]
NP_055060.1. NM_014245.4. [Q9UBF6-1 ]
NP_899060.1. NM_183237.2. [Q9UBF6-3 ]
UniGenei Hs.134623.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ECL NMR - A 40-113 [» ]
ProteinModelPortali Q9UBF6.
SMRi Q9UBF6. Positions 40-113.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114977. 52 interactions.
IntActi Q9UBF6. 28 interactions.
MINTi MINT-1470812.
STRINGi 9606.ENSP00000273480.

PTM databases

PhosphoSitei Q9UBF6.

Polymorphism databases

DMDMi 37538003.

Proteomic databases

MaxQBi Q9UBF6.
PaxDbi Q9UBF6.
PRIDEi Q9UBF6.

Protocols and materials databases

DNASUi 9616.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000273480 ; ENSP00000273480 ; ENSG00000114125 . [Q9UBF6-1 ]
ENST00000393000 ; ENSP00000376725 ; ENSG00000114125 . [Q9UBF6-3 ]
ENST00000477012 ; ENSP00000419339 ; ENSG00000114125 . [Q9UBF6-2 ]
ENST00000480908 ; ENSP00000419084 ; ENSG00000114125 . [Q9UBF6-4 ]
GeneIDi 9616.
KEGGi hsa:9616.
UCSCi uc003euc.3. human. [Q9UBF6-3 ]
uc003eud.3. human. [Q9UBF6-1 ]
uc021xeu.1. human. [Q9UBF6-4 ]

Organism-specific databases

CTDi 9616.
GeneCardsi GC03P141457.
HGNCi HGNC:10070. RNF7.
HPAi HPA036995.
MIMi 603863. gene.
neXtProti NX_Q9UBF6.
PharmGKBi PA34444.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5194.
HOVERGENi HBG001507.
InParanoidi Q9UBF6.
KOi K10611.
OMAi DICAICR.
OrthoDBi EOG7CG721.
PhylomeDBi Q9UBF6.
TreeFami TF351049.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

EvolutionaryTracei Q9UBF6.
GeneWikii RNF7.
GenomeRNAii 9616.
NextBioi 36073.
PROi Q9UBF6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UBF6.
Bgeei Q9UBF6.
CleanExi HS_RNF7.
HS_SAG.
Genevestigatori Q9UBF6.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view ]
Pfami PF12678. zf-rbx1. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiRBX2_HUMAN
AccessioniPrimary (citable) accession number: Q9UBF6
Secondary accession number(s): A8K1H9
, A8MTB5, C9JYL3, D3DNF7, D3DNF8, Q9BXN8, Q9Y5M7
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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