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P62877 (RBX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:RBX1
Synonyms:RNF75, ROC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.12 Ref.19 Ref.20 Ref.21 Ref.22 Ref.26 Ref.28

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.1 Ref.2 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29

Subcellular location

Cytoplasm. Nucleus Ref.12.

Tissue specificity

Widely expressed.

Domain

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

Sequence similarities

Belongs to the RING-box family.

Contains 1 RING-type zinc finger.

Sequence caution

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Host-virus interaction
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

Notch signaling pathway

Traceable author statement. Source: Reactome

SCF-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 15103331. Source: UniProtKB

cellular response to hypoxia

Traceable author statement. Source: Reactome

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 20389280. Source: UniProtKB

protein monoubiquitination

Inferred from direct assay PubMed 22358839. Source: UniProtKB

protein neddylation

Inferred from direct assay Ref.27. Source: UniProtKB

protein ubiquitination

Inferred from direct assay PubMed 15103331PubMed 17543862PubMed 20389280. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentCul2-RING ubiquitin ligase complex

Inferred from direct assay PubMed 17636018. Source: UniProtKB

Cul3-RING ubiquitin ligase complex

Inferred from direct assay Ref.19PubMed 17543862PubMed 20389280PubMed 22358839. Source: UniProtKB

Cul4A-RING ubiquitin ligase complex

Inferred from direct assay Ref.17PubMed 17085480PubMed 18794347PubMed 20129063PubMed 20223979. Source: UniProtKB

Cul4B-RING ubiquitin ligase complex

Inferred from direct assay PubMed 18794347. Source: UniProtKB

Cul5-RING ubiquitin ligase complex

Inferred from direct assay PubMed 17636018. Source: UniProtKB

SCF ubiquitin ligase complex

Inferred from direct assay PubMed 15103331PubMed 21572392PubMed 23263282. Source: UniProtKB

VCB complex

Inferred from electronic annotation. Source: Ensembl

cullin-RING ubiquitin ligase complex

Inferred from direct assay PubMed 22405651. Source: MGI

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionNEDD8 ligase activity

Inferred from direct assay Ref.27. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from direct assay PubMed 17636018. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 22405651. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 108108E3 ubiquitin-protein ligase RBX1
PRO_0000423264
Initiator methionine11Removed; alternate Ref.8
Chain2 – 108107E3 ubiquitin-protein ligase RBX1, N-terminally processed
PRO_0000056013

Regions

Zinc finger53 – 9846RING-type

Sites

Metal binding421Zinc 1
Metal binding451Zinc 1
Metal binding531Zinc 3
Metal binding561Zinc 3
Metal binding681Zinc 3
Metal binding751Zinc 2
Metal binding771Zinc 2
Metal binding801Zinc 1
Metal binding821Zinc 3
Metal binding831Zinc 1
Metal binding941Zinc 2
Metal binding971Zinc 2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.30
Modified residue21N-acetylalanine; in E3 ubiquitin-protein ligase RBX1, N-terminally processed Ref.8 Ref.25 Ref.30 Ref.32 Ref.33
Modified residue91Phosphothreonine Ref.30

Experimental info

Mutagenesis531C → A: Strong reduction in ligase activity; when associated with A-56. Ref.1
Mutagenesis561C → A: Strong reduction in ligase activity; when associated with A-53. Ref.1
Mutagenesis751C → A: Strong reduction in ligase activity; when associated with A-77. Ref.1
Mutagenesis771H → A: Strong reduction in ligase activity; when associated with A-75. Ref.1
Sequence conflict181G → S in AAM21718. Ref.9

Secondary structure

......................... 108
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62877 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 30FC5ADF66096C0E

FASTA10812,274
        10         20         30         40         50         60 
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ 

        70         80         90        100 
ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH 

« Hide

References

« Hide 'large scale' references
[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]"Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase."
Kamura T., Koepp D.M., Conrad M.N., Skowyra D., Moreland R.J., Iliopoulos O., Lane W.S., Kaelin W.G. Jr., Elledge S.J., Conaway R.C., Harper J.W., Conaway J.W.
Science 284:657-661(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN CBC(VHL) COMPLEX.
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. 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].
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. expand/collapse author list , 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]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome."
Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C., Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.
Science 292:1382-1385(2001) [PubMed] [Europe PMC] [Abstract]
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]"Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase."
Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I., Oda T., Kitagawa M.
J. Biol. Chem. 284:27766-27779(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex."
Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P., Chu C., Koepp D.M., Elledge S.J., Pagano M., Conaway R.C., Conaway J.W., Harper J.W., Pavletich N.P.
Nature 416:703-709(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT51146.
RefSeqNP_055063.1. NM_014248.3.
UniGeneHs.474949.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP62877.
SMRP62877. Positions 19-106.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115301. 143 interactions.
DIPDIP-17014N.
IntActP62877. 42 interactions.
MINTMINT-235894.
STRING9606.ENSP00000216225.

PTM databases

PhosphoSiteP62877.

Polymorphism databases

DMDM51338609.

Proteomic databases

PaxDbP62877.
PRIDEP62877.

Protocols and materials databases

DNASU9978.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216225; ENSP00000216225; ENSG00000100387.
GeneID9978.
KEGGhsa:9978.
UCSCuc003azk.3. human.

Organism-specific databases

CTD9978.
GeneCardsGC22P041347.
H-InvDBHIX0016509.
HGNCHGNC:9928. RBX1.
HPAHPA003038.
MIM603814. gene.
neXtProtNX_P62877.
PharmGKBPA34299.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5194.
HOGENOMHOG000171951.
HOVERGENHBG001507.
InParanoidP62877.
KOK03868.
OMAARSVCPL.
OrthoDBEOG7CG721.
PhylomeDBP62877.
TreeFamTF105503.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_6900. Immune System.
SignaLinkP62877.
UniPathwayUPA00143.

Gene expression databases

BgeeP62877.
CleanExHS_RBX1.
GenevestigatorP62877.

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

EvolutionaryTraceP62877.
GeneWikiRBX1.
GenomeRNAi9978.
NextBio37682.
PROP62877.
SOURCESearch...

Entry information

Entry nameRBX1_HUMAN
AccessionPrimary (citable) accession number: P62877
Secondary accession number(s): B2RDY1 expand/collapse secondary AC list , Q8N6Z8, Q9D1S2, Q9WUK9, Q9Y254
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 115 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 22

Human chromosome 22: entries, gene names and cross-references to MIM