SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P62877

- RBX1_HUMAN

UniProt

P62877 - RBX1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
E3 ubiquitin-protein ligase RBX1
Gene
RBX1, RNF75, ROC1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM.8 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Zinc 1
Metal bindingi45 – 451Zinc 1
Metal bindingi53 – 531Zinc 3
Metal bindingi56 – 561Zinc 3
Metal bindingi68 – 681Zinc 3
Metal bindingi75 – 751Zinc 2
Metal bindingi77 – 771Zinc 2
Metal bindingi80 – 801Zinc 1
Metal bindingi82 – 821Zinc 3
Metal bindingi83 – 831Zinc 1
Metal bindingi94 – 941Zinc 2
Metal bindingi97 – 971Zinc 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri53 – 9846RING-type
Add
BLAST

GO - Molecular functioni

  1. NEDD8 ligase activity Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. ubiquitin protein ligase binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: MGI
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. Notch signaling pathway Source: Reactome
  3. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. cellular response to hypoxia Source: Reactome
  5. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  6. protein monoubiquitination Source: UniProtKB
  7. protein neddylation Source: UniProtKB
  8. protein ubiquitination Source: UniProtKB
  9. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  10. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_115697. Prolactin receptor signaling.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_200841. degradation of DVL.
REACT_22442. Interleukin-1 signaling.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9453. Vif-mediated degradation of APOBEC3G.
SignaLinkiP62877.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RBX1 (EC:6.3.2.-)
Alternative name(s):
Protein ZYP
RING finger protein 75
RING-box protein 1
Short name:
Rbx1
Regulator of cullins 1
Cleaved into the following chain:
Gene namesi
Name:RBX1
Synonyms:RNF75, ROC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:9928. RBX1.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. Cul2-RING ubiquitin ligase complex Source: UniProtKB
  2. Cul3-RING ubiquitin ligase complex Source: UniProtKB
  3. Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
  4. Cul4B-RING E3 ubiquitin ligase complex Source: UniProtKB
  5. Cul5-RING ubiquitin ligase complex Source: UniProtKB
  6. SCF ubiquitin ligase complex Source: UniProtKB
  7. VCB complex Source: Ensembl
  8. cullin-RING ubiquitin ligase complex Source: MGI
  9. cytosol Source: UniProtKB
  10. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531C → A: Strong reduction in ligase activity; when associated with A-56. 1 Publication
Mutagenesisi56 – 561C → A: Strong reduction in ligase activity; when associated with A-53. 1 Publication
Mutagenesisi75 – 751C → A: Strong reduction in ligase activity; when associated with A-77. 1 Publication
Mutagenesisi77 – 771H → A: Strong reduction in ligase activity; when associated with A-75. 1 Publication

Organism-specific databases

PharmGKBiPA34299.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 108108E3 ubiquitin-protein ligase RBX1
PRO_0000423264Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 108107E3 ubiquitin-protein ligase RBX1, N-terminally processed
PRO_0000056013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylalanine; in E3 ubiquitin-protein ligase RBX1, N-terminally processed5 Publications
Modified residuei9 – 91Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62877.
PaxDbiP62877.
PRIDEiP62877.

PTM databases

PhosphoSiteiP62877.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiP62877.
CleanExiHS_RBX1.
GenevestigatoriP62877.

Organism-specific databases

HPAiHPA003038.

Interactioni

Subunit structurei

Part of a SCF complex consisting of CUL1, RBX1, SKP1 and SKP2. Part of a SCF-like complex consisting of CUL7, RBX1, SKP1 and FBXW8. Part of CBC(VHL) complexes with elongin BC complex (TCEB1 and TCEB2), CUL2 or CUL5 and VHL. Part of the CSA complex (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II. Part of multisubunit E3 ubiquitin ligase complexes with elongin BC complex (TCEB1 and TCEB2), CUL2 and MED8; elongin BC complex (TCEB1 and TCEB2), CUL5 and MUF1. Part of multisubunit complexes with elongin BC complex (TCEB1 and TCEB2), elongin A/TCEB3 or SOCS1 or WSB1 and CUL5. Interacts directly with CUL1 and probably also with CUL2, CUL3, CUL4A, CUL4B, CUL5 and CUL7. Probably interacts with CDC34. Interacts with COPS6. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and CUL4A or CUL4B. Interacts with UBE2M. Part of a SCF complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts with PML via FBXO3. Interacts with human adenovirus early E1A protein; this interaction inhibits RBX1-CUL1-dependent elongation reaction of ubiquitin chains by the SCF(FBW7) complex. Component of the SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and CCNF. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and CDC34. Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein. Part of the BCR(ENC1) complex containing ENC1. Part of the BCR(GAN) complex containing GAN. Part of the BCR(KLHL41) complex containing KLHL41. Part of the BCR(KEAP1) complex containing KEAP1.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL1Q1361612EBI-398523,EBI-359390
CUL2Q136175EBI-398523,EBI-456179
CUL4BQ136204EBI-398523,EBI-456067
CUL5Q930343EBI-398523,EBI-1057139
SKP2Q133093EBI-398523,EBI-456291

Protein-protein interaction databases

BioGridi115301. 147 interactions.
DIPiDIP-17014N.
IntActiP62877. 42 interactions.
MINTiMINT-235894.
STRINGi9606.ENSP00000216225.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 3717
Beta strandi39 – 413
Beta strandi43 – 453
Turni49 – 546
Helixi56 – 594
Turni63 – 675
Beta strandi70 – 734
Beta strandi74 – 763
Beta strandi78 – 803
Helixi81 – 888
Beta strandi90 – 934
Beta strandi95 – 973
Beta strandi103 – 1053

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LDJX-ray3.00B19-108[»]
1LDKX-ray3.10C19-108[»]
1U6GX-ray3.10B1-108[»]
2HYEX-ray3.10D1-108[»]
2LGVNMR-A12-108[»]
3DPLX-ray2.60R5-108[»]
3DQVX-ray3.00R/Y5-108[»]
3RTRX-ray3.21B/D/F/H5-108[»]
4F52X-ray3.00B/D5-108[»]
ProteinModelPortaliP62877.
SMRiP62877. Positions 19-106.

Miscellaneous databases

EvolutionaryTraceiP62877.

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.
HOGENOMiHOG000171951.
HOVERGENiHBG001507.
InParanoidiP62877.
KOiK03868.
OMAiARSVCPL.
OrthoDBiEOG7CG721.
PhylomeDBiP62877.
TreeFamiTF105503.

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]

Sequencei

Sequence statusi: Complete.

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

P62877-1 [UniParc]FASTAAdd to Basket

« Hide

MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM    50
DLCIECQANQ ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE 100
WEFQKYGH 108
Length:108
Mass (Da):12,274
Last modified:August 16, 2004 - v1
Checksum:i30FC5ADF66096C0E
GO

Sequence cautioni

The sequence AAH17370.2 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181G → S in AAM21718. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF142059 mRNA. Translation: AAD30146.1.
AF140598 mRNA. Translation: AAD29715.1.
CR456560 mRNA. Translation: CAG30446.1.
AK315722 mRNA. Translation: BAG38078.1.
AL080242 Genomic DNA. Translation: CAB62925.1.
CH471095 Genomic DNA. Translation: EAW60403.1.
BC001466 mRNA. Translation: AAH01466.1.
BC017370 mRNA. Translation: AAH17370.2. Different initiation.
AY099360 mRNA. Translation: AAM21718.1.
CCDSiCCDS14009.1.
PIRiT51146.
RefSeqiNP_055063.1. NM_014248.3.
UniGeneiHs.474949.

Genome annotation databases

EnsembliENST00000216225; ENSP00000216225; ENSG00000100387.
GeneIDi9978.
KEGGihsa:9978.
UCSCiuc003azk.3. human.

Polymorphism databases

DMDMi51338609.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF142059 mRNA. Translation: AAD30146.1 .
AF140598 mRNA. Translation: AAD29715.1 .
CR456560 mRNA. Translation: CAG30446.1 .
AK315722 mRNA. Translation: BAG38078.1 .
AL080242 Genomic DNA. Translation: CAB62925.1 .
CH471095 Genomic DNA. Translation: EAW60403.1 .
BC001466 mRNA. Translation: AAH01466.1 .
BC017370 mRNA. Translation: AAH17370.2 . Different initiation.
AY099360 mRNA. Translation: AAM21718.1 .
CCDSi CCDS14009.1.
PIRi T51146.
RefSeqi NP_055063.1. NM_014248.3.
UniGenei Hs.474949.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LDJ X-ray 3.00 B 19-108 [» ]
1LDK X-ray 3.10 C 19-108 [» ]
1U6G X-ray 3.10 B 1-108 [» ]
2HYE X-ray 3.10 D 1-108 [» ]
2LGV NMR - A 12-108 [» ]
3DPL X-ray 2.60 R 5-108 [» ]
3DQV X-ray 3.00 R/Y 5-108 [» ]
3RTR X-ray 3.21 B/D/F/H 5-108 [» ]
4F52 X-ray 3.00 B/D 5-108 [» ]
ProteinModelPortali P62877.
SMRi P62877. Positions 19-106.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115301. 147 interactions.
DIPi DIP-17014N.
IntActi P62877. 42 interactions.
MINTi MINT-235894.
STRINGi 9606.ENSP00000216225.

PTM databases

PhosphoSitei P62877.

Polymorphism databases

DMDMi 51338609.

Proteomic databases

MaxQBi P62877.
PaxDbi P62877.
PRIDEi P62877.

Protocols and materials databases

DNASUi 9978.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216225 ; ENSP00000216225 ; ENSG00000100387 .
GeneIDi 9978.
KEGGi hsa:9978.
UCSCi uc003azk.3. human.

Organism-specific databases

CTDi 9978.
GeneCardsi GC22P041347.
H-InvDB HIX0016509.
HGNCi HGNC:9928. RBX1.
HPAi HPA003038.
MIMi 603814. gene.
neXtProti NX_P62877.
PharmGKBi PA34299.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5194.
HOGENOMi HOG000171951.
HOVERGENi HBG001507.
InParanoidi P62877.
KOi K03868.
OMAi ARSVCPL.
OrthoDBi EOG7CG721.
PhylomeDBi P62877.
TreeFami TF105503.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_115697. Prolactin receptor signaling.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_200841. degradation of DVL.
REACT_22442. Interleukin-1 signaling.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9453. Vif-mediated degradation of APOBEC3G.
SignaLinki P62877.

Miscellaneous databases

EvolutionaryTracei P62877.
GeneWikii RBX1.
GenomeRNAii 9978.
NextBioi 37682.
PROi P62877.
SOURCEi Search...

Gene expression databases

Bgeei P62877.
CleanExi HS_RBX1.
Genevestigatori P62877.

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. "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], INTERACTION WITH CULLINS, MUTAGENESIS OF CYS-53; CYS-56; CYS-75 AND HIS-77.
    Tissue: Cervix carcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN CBC(VHL) COMPLEX.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Tissue: Testis.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Brain and Placenta.
  8. Bienvenut W.V., Vousden K.H., Lukashchuk N.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-20, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung carcinoma.
  9. "Genomic organization and expression of the ubiquitin-proteasome complex-associated protein Rbx1/ROC1/Hrt1."
    Perin J.-P., Seddiqi N., Charbonnier F., Goudou D., Belkadi L., Rieger F., Alliel P.M.
    Cell. Mol. Biol. 45:1131-1137(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-108.
    Tissue: Brain.
  10. "Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha."
    Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.
    Mol. Cell 3:527-533(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 92-105, INTERACTION WITH CUL1, IDENTIFICATION IN A COMPLEX WITH CUL1; SKP1 AND SKP2.
    Tissue: Cervix carcinoma.
  11. "The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2."
    Kamura T., Conrad M.N., Yan Q., Conaway R.C., Conaway J.W.
    Genes Dev. 13:2928-2933(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1."
    Furukawa M., Zhang Y., McCarville J., Ohta T., Xiong Y.
    Mol. Cell. Biol. 20:8185-8197(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase."
    Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E., Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 276:29748-29753(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MUF1, IDENTIFICATION IN COMPLEXES WITH CUL5.
  14. Cited for: INTERACTION WITH COPS6.
  15. "Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase."
    Brower C.S., Sato S., Tomomori-Sato C., Kamura T., Pause A., Stearman R., Klausner R.D., Malik S., Lane W.S., Sorokina I., Roeder R.G., Conaway J.W., Conaway R.C.
    Proc. Natl. Acad. Sci. U.S.A. 99:10353-10358(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MED8.
  16. "CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex."
    Dias D.C., Dolios G., Wang R., Pan Z.Q.
    Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SCF-LIKE COMPLEX, INTERACTION WITH CUL7.
  17. "The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage."
    Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.
    Cell 113:357-367(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CSA COMPLEX WITH ERCC8; DDB1 AND CUL4A, INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II AND THE COP9 SIGNALOSOME.
  18. "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase."
    Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D., Deshaies R.J., Dixit V.M.
    Science 303:1371-1374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE DCX DET1-COP1 COMPLEX WITH DDB1; CUL4A; COP1 AND DET1.
  19. "Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway."
    Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.
    J. Biol. Chem. 280:30091-30099(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE BCR(KLHL41) COMPLEX, IDENTIFICATION IN THE BCR(ENC1) COMPLEX, IDENTIFICATION IN THE BCR(KEAP1) COMPLEX, IDENTIFICATION IN THE BCR(GAN) COMPLEX.
  20. "CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome."
    Groisman R., Kuraoka I., Chevallier O., Gaye N., Magnaldo T., Tanaka K., Kisselev A.F., Harel-Bellan A., Nakatani Y.
    Genes Dev. 20:1429-1434(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage."
    Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y.
    Mol. Cell 22:383-394(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH DDB1; DDB2; CUL4A AND CUL4B, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  22. "Regulation of TIP60 by ATF2 modulates ATM activation."
    Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.
    J. Biol. Chem. 283:17605-17614(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation."
    Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P., Kitabayashi I.
    Mol. Cell. Biol. 28:7126-7138(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CUL1; FBXO3; SKP1 AND PML.
  25. "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].
  26. "Histidine triad nucleotide-binding protein 1 up-regulates cellular levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src."
    Cen B., Li H., Weinstein I.B.
    J. Biol. Chem. 284:5265-5276(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A UBIQUITIN LIGASE COMPLEX WITH HINT1 AND CDC34, FUNCTION.
  27. "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 UBE2M.
  28. Cited for: FUNCTION, INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
  29. "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation."
    D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L., Washburn M.P., Dynlacht B., Pagano M.
    Nature 466:138-142(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SCF(CYCLIN F) COMPLEX.
  30. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-108 IN COMPLEX WITH 17-776 OF CUL1, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH CUL1; SKP1 AND SKP2.

Entry informationi

Entry nameiRBX1_HUMAN
AccessioniPrimary (citable) accession number: P62877
Secondary accession number(s): B2RDY1
, Q8N6Z8, Q9D1S2, Q9WUK9, Q9Y254
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: September 3, 2014
This is version 119 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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

Similar proteinsi