P62877 (RBX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	RBX1
Synonyms:	RNF75, ROC1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	108 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.11 Ref.12 Ref.19 Ref.20 Ref.21 Ref.24 Ref.26
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.23 Ref.24 Ref.25 Ref.26 Ref.27
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 process	DNA damage DNA repair Host-virus interaction Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 protein monoubiquitination Inferred from direct assay PubMed 22358839. Source: UniProtKB protein neddylation Inferred from direct assay Ref.25. Source: UniProtKB regulation of transcription from RNA polymerase II promoter in response to hypoxia Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Cul2-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: Compara cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	NEDD8 ligase activity Inferred from direct assay Ref.25. 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CUL1	Q13616	12	EBI-398523,EBI-359390
CUL4B	Q13620	4	EBI-398523,EBI-456067
CUL5	Q93034	3	EBI-398523,EBI-1057139

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 108

107

E3 ubiquitin-protein ligase RBX1

PRO_0000056013

Regions

Zinc finger

53 – 98

46

RING-type

Sites

Metal binding

42

1

Zinc 1

Metal binding

45

1

Zinc 1

Metal binding

53

1

Zinc 3

Metal binding

56

1

Zinc 3

Metal binding

68

1

Zinc 3

Metal binding

75

1

Zinc 2

Metal binding

77

1

Zinc 2

Metal binding

80

1

Zinc 1

Metal binding

82

1

Zinc 3

Metal binding

83

1

Zinc 1

Metal binding

94

1

Zinc 2

Metal binding

97

1

Zinc 2

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8 Ref.28

Modified residue

9

1

Phosphothreonine Ref.28

Experimental info

Mutagenesis

53

1

C → A: Strong reduction in ligase activity; when associated with A-56. Ref.1

Mutagenesis

56

1

C → A: Strong reduction in ligase activity; when associated with A-53. Ref.1

Mutagenesis

75

1

C → A: Strong reduction in ligase activity; when associated with A-77. Ref.1

Mutagenesis

77

1

H → A: Strong reduction in ligase activity; when associated with A-75. Ref.1

Sequence conflict

18

1

G → S in AAM21718. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

108

Helix Strand Turn

Details...

Beta strand

21 – 37

17

Beta strand

39 – 41

3

Beta strand

43 – 45

3

Turn

49 – 54

6

Helix

56 – 59

4

Turn

63 – 67

5

Beta strand

70 – 73

4

Beta strand

74 – 76

3

Beta strand

78 – 80

3

Helix

81 – 88

8

Beta strand

90 – 93

4

Beta strand

95 – 97

3

Beta strand

103 – 105

3

Sequences

	Sequence		Length	Mass (Da)
	P62877 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 30FC5ADF66096C0E	FASTA	108	12,274
	10 20 30 40 50 60 MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ 70 80 90 100 ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, 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 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 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, MASS SPECTROMETRY, FUNCTION.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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 ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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].
[30]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00003386.

PIR

T51146.

RefSeq

NP_055063.1. NM_014248.3.

UniGene

Hs.474949.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P62877.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17014N.

IntAct

P62877. 27 interactions.

MINT

MINT-235894.

STRING

9606.ENSP00000216225.

PTM databases

PhosphoSite

P62877.

Polymorphism databases

DMDM

51338609.

Proteomic databases

PaxDb

P62877.

PRIDE

P62877.

Protocols and materials databases

DNASU

9978.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216225; ENSP00000216225; ENSG00000100387.

GeneID

9978.

KEGG

hsa:9978.

UCSC

uc003azk.3. human.

Organism-specific databases

CTD

9978.

GeneCards

GC22P041347.

H-InvDB

HIX0016509.

HGNC

HGNC:9928. RBX1.

HPA

HPA003038.

MIM

603814. gene.

neXtProt

NX_P62877.

PharmGKB

PA34299.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5194.

HOGENOM

HOG000171951.

HOVERGEN

HBG001507.

InParanoid

P62877.

KO

K03868.

OMA

NRDWEFQ.

OrthoDB

EOG4QRH5F.

PhylomeDB

P62877.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1apathway. Hypoxic and oxygen homeostasis regulation of HIF-1-alpha.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

Bgee

P62877.

CleanEx

HS_RBX1.

Genevestigator

P62877.

GermOnline

ENSG00000100387. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]

Pfam

PF12678. zf-rbx1. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P62877.

GenomeRNAi

9978.

NextBio

37682.

SOURCE

Search...

Entry information

Entry name

RBX1_HUMAN

Accession

Primary (citable) accession number: P62877
Secondary accession number(s): B2RDY1 , Q8N6Z8, Q9D1S2, Q9WUK9, Q9Y254

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.