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Q9UBF6

- RBX2_HUMAN

UniProt

Q9UBF6 - RBX2_HUMAN

Protein

RING-box protein 2

Gene

RNF7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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 1By similarity
    Metal bindingi53 – 531Zinc 1By similarity
    Metal bindingi61 – 611Zinc 3By similarity
    Metal bindingi64 – 641Zinc 3By similarity
    Metal bindingi73 – 731Zinc 3By similarity
    Metal bindingi80 – 801Zinc 2By similarity
    Metal bindingi82 – 821Zinc 2By similarity
    Metal bindingi85 – 851Zinc 1By similarity
    Metal bindingi87 – 871Zinc 3By similarity
    Metal bindingi88 – 881Zinc 1By similarity
    Metal bindingi99 – 991Zinc 2By similarity
    Metal bindingi102 – 1021Zinc 2By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri61 – 10343RING-typePROSITE-ProRule annotationAdd
    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

    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 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

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

    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.1 Publication

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.Curated
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri61 – 10343RING-typePROSITE-ProRule annotationAdd
    BLAST

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231K → T in AAD30147. (PubMed:10230407)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei57 – 11357VMDAC…QRIGK → MPVLDVKLKTNKRTVLWSGE NVIIPSTTAACPCG in isoform 3. 1 PublicationVSP_041444Add
    BLAST
    Alternative sequencei59 – 7416Missing in isoform 4. CuratedVSP_044525Add
    BLAST
    Alternative sequencei60 – 11354ACLRC…QRIGK → EGIGVRNWSEALNLINASEM GFDCRSGSTALAVPSVSLAS HQPCLDDHR in isoform 2. 2 PublicationsVSP_008449Add
    BLAST

    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

    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: October 1, 2014
    This is version 123 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