Q9Y4B6 (VPRBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein VPRBP

Alternative name(s):
DDB1- and CUL4-associated factor 1
HIV-1 Vpr-binding protein
Short name=VprBP
Vpr-interacting protein

Gene names

Name:	VPRBP
Synonyms:	DCAF1, KIAA0800, RIP

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	1507 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex, VprBP/DCAF1 may function as the substrate recognition module within this complex. For example, VprBP/DCAF1 targets NF2 to the E3 ubiquitin-ligase complex for ubiquitination and subsequent proteasome-dependent degradation. In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1 function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1 function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage. Associated with chromatin in a DDB1-independent and cell cycle-dependent manner, VprBP/DCAF1 is recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.27
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex that could interact with HIV-1 virus Vpr protein and HIV-2 virus Vpx protein. Interacts directly with DDB1. Also forms a ternary complex with DDA1 and DDB1. Interacts with NF2 (via FERM domain). Component of EDD/UBR5-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP complex). Interacts directly with DYRK2. Ref.4 Ref.6 Ref.8 Ref.11 Ref.12 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.26
Subcellular location	Cytoplasm. Nucleus Ref.4 Ref.26.
Tissue specificity	Ubiquitously expressed. Ref.4
Domain	The DWD boxes are required for interaction with DDB1.
Sequence similarities	Belongs to the VPRBP/DCAF1 family. Contains 1 LisH domain. Contains 5 WD repeats.
Sequence caution	The sequence BAA34520.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Host-virus interaction Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat WD repeat
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.26. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
vpr	P12520	5	EBI-1996353,EBI-6164519	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y4B6-1)

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.

Isoform 2 (identifier: Q9Y4B6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     87-87: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9Y4B6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     225-673: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1507	1507	Protein VPRBP		PRO_0000287473
Regions
	Domain	846 – 878	33	LisH
	Repeat	1091 – 1130	40	WD 1
	Repeat	1133 – 1174	42	WD 2
	Repeat	1176 – 1213	38	WD 3
	Repeat	1215 – 1247	33	WD 4
	Repeat	1248 – 1290	43	WD 5
	Region	1091 – 1174	84	WD repeat-like region
	Region	1418 – 1507	90	Interaction with NF2
	Motif	1242 – 1249	8	DWD box 1 By similarity
	Motif	1278 – 1285	8	DWD box 2 By similarity
	Compositional bias	1396 – 1500	105	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	888	1	Phosphothreonine Ref.21
	Modified residue	895	1	Phosphoserine Ref.17 Ref.21 Ref.25
	Modified residue	898	1	Phosphoserine Ref.21
	Modified residue	979	1	Phosphoserine Ref.30
	Modified residue	1000	1	Phosphoserine Ref.7 Ref.28
	Cross-link	280		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14
Natural variations
	Alternative sequence	87	1	Missing in isoform 2.		VSP_025498
	Alternative sequence	225 – 673	449	Missing in isoform 3.		VSP_025499
	Natural variant	267	1	N → D. Corresponds to variant rs3749318 [ dbSNP | Ensembl ].		VAR_051486
	Natural variant	378	1	L → F. Corresponds to variant rs17712228 [ dbSNP | Ensembl ].		VAR_051487
	Natural variant	1031	1	L → P. Corresponds to variant rs9835229 [ dbSNP | Ensembl ].		VAR_051488

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 15, 2007. Version 3. Checksum: 7E71AB2CAC4962C5	FASTA	1,507	169,007
	10 20 30 40 50 60 MTTVVVHVDS KAELTTLLEQ WEKEHGSGQD MVPILTRMSQ LIEKETEEYR KGDPDPFDDR 70 80 90 100 110 120 HPGRADPECM LGHLLRILFK NDDFMNALVN AYVMTSREPP LNTAACRLLL DIMPGLETAV 130 140 150 160 170 180 VFQEKEGIVE NLFKWAREAD QPLRTYSTGL LGGAMENQDI AANYRDENSQ LVAIVLRRLR 190 200 210 220 230 240 ELQLQEVALR QENKRPSPRK LSSEPLLPLD EEAVDMDYGD MAVDVVDGDQ EEASGDMEIS 250 260 270 280 290 300 FHLDSGHKTS SRVNSTTKPE DGGLKKNKSA KQGDRENFRK AKQKLGFSSS DPDRMFVELS 310 320 330 340 350 360 NSSWSEMSPW VIGTNYTLYP MTPAIEQRLI LQYLTPLGEY QELLPIFMQL GSRELMMFYI 370 380 390 400 410 420 DLKQTNDVLL TFEALKHLAS LLLHNKFATE FVAHGGVQKL LEIPRPSMAA TGVSMCLYYL 430 440 450 460 470 480 SYNQDAMERV CMHPHNVLSD VVNYTLWLME CSHASGCCHA TMFFSICFSF RAVLELFDRY 490 500 510 520 530 540 DGLRRLVNLI STLEILNLED QGALLSDDEI FASRQTGKHT CMALRKYFEA HLAIKLEQVK 550 560 570 580 590 600 QSLQRTEGGI LVHPQPPYKA CSYTHEQIVE MMEFLIEYGP AQLYWEPAEV FLKLSCVQLL 610 620 630 640 650 660 LQLISIACNW KTYYARNDTV RFALDVLAIL TVVPKIQLQL AESVDVLDEA GSTVSTVGIS 670 680 690 700 710 720 IILGVAEGEF FIHDAEIQKS ALQIIINCVC GPDNRISSIG KFISGTPRRK LPQNPKSSEH 730 740 750 760 770 780 TLAKMWNVVQ SNNGIKVLLS LLSIKMPITD ADQIRALACK ALVGLSRSST VRQIISKLPL 790 800 810 820 830 840 FSSCQIQQLM KEPVLQDKRS DHVKFCKYAA ELIERVSGKP LLIGTDVSLA RLQKADVVAQ 850 860 870 880 890 900 SRISFPEKEL LLLIRNHLIS KGLGETATVL TKEADLPMTA ASHSSAFTPV TAAASPVSLP 910 920 930 940 950 960 RTPRIANGIA TRLGSHAAVG ASAPSAPTAH PQPRPPQGPL ALPGPSYAGN SPLIGRISFI 970 980 990 1000 1010 1020 RERPSPCNGR KIRVLRQKSD HGAYSQSPAI KKQLDRHLPS PPTLDSIITE YLREQHARCK 1030 1040 1050 1060 1070 1080 NPVATCPPFS LFTPHQCPEP KQRRQAPINF TSRLNRRASF PKYGGVDGGC FDRHLIFSRF 1090 1100 1110 1120 1130 1140 RPISVFREAN EDESGFTCCA FSARERFLML GTCTGQLKLY NVFSGQEEAS YNCHNSAITH 1150 1160 1170 1180 1190 1200 LEPSRDGSLL LTSATWSQPL SALWGMKSVF DMKHSFTEDH YVEFSKHSQD RVIGTKGDIA 1210 1220 1230 1240 1250 1260 HIYDIQTGNK LLTLFNPDLA NNYKRNCATF NPTDDLVLND GVLWDVRSAQ AIHKFDKFNM 1270 1280 1290 1300 1310 1320 NISGVFHPNG LEVIINTEIW DLRTFHLLHT VPALDQCRVV FNHTGTVMYG AMLQADDEDD 1330 1340 1350 1360 1370 1380 LMEERMKSPF GSSFRTFNAT DYKPIATIDV KRNIFDLCTD TKDCYLAVIE NQGSMDALNM 1390 1400 1410 1420 1430 1440 DTVCRLYEVG RQRLAEDEDE EEDQEEEEQE EEDDDEDDDD TDDLDELDTD QLLEAELEED 1450 1460 1470 1480 1490 1500 DNNENAGEDG DNDFSPSDEE LANLLEEGED GEDEDSDADE EVELILGDTD SSDNSDLEDD IILSLNE
	Isoform 2 [UniParc]. Checksum: 016CF082F1239B17	FASTA	1,506	168,936
	10 20 30 40 50 60 MTTVVVHVDS KAELTTLLEQ WEKEHGSGQD MVPILTRMSQ LIEKETEEYR KGDPDPFDDR 70 80 90 100 110 120 HPGRADPECM LGHLLRILFK NDDFMNLVNA YVMTSREPPL NTAACRLLLD IMPGLETAVV 130 140 150 160 170 180 FQEKEGIVEN LFKWAREADQ PLRTYSTGLL GGAMENQDIA ANYRDENSQL VAIVLRRLRE 190 200 210 220 230 240 LQLQEVALRQ ENKRPSPRKL SSEPLLPLDE EAVDMDYGDM AVDVVDGDQE EASGDMEISF 250 260 270 280 290 300 HLDSGHKTSS RVNSTTKPED GGLKKNKSAK QGDRENFRKA KQKLGFSSSD PDRMFVELSN 310 320 330 340 350 360 SSWSEMSPWV IGTNYTLYPM TPAIEQRLIL QYLTPLGEYQ ELLPIFMQLG SRELMMFYID 370 380 390 400 410 420 LKQTNDVLLT FEALKHLASL LLHNKFATEF VAHGGVQKLL EIPRPSMAAT GVSMCLYYLS 430 440 450 460 470 480 YNQDAMERVC MHPHNVLSDV VNYTLWLMEC SHASGCCHAT MFFSICFSFR AVLELFDRYD 490 500 510 520 530 540 GLRRLVNLIS TLEILNLEDQ GALLSDDEIF ASRQTGKHTC MALRKYFEAH LAIKLEQVKQ 550 560 570 580 590 600 SLQRTEGGIL VHPQPPYKAC SYTHEQIVEM MEFLIEYGPA QLYWEPAEVF LKLSCVQLLL 610 620 630 640 650 660 QLISIACNWK TYYARNDTVR FALDVLAILT VVPKIQLQLA ESVDVLDEAG STVSTVGISI 670 680 690 700 710 720 ILGVAEGEFF IHDAEIQKSA LQIIINCVCG PDNRISSIGK FISGTPRRKL PQNPKSSEHT 730 740 750 760 770 780 LAKMWNVVQS NNGIKVLLSL LSIKMPITDA DQIRALACKA LVGLSRSSTV RQIISKLPLF 790 800 810 820 830 840 SSCQIQQLMK EPVLQDKRSD HVKFCKYAAE LIERVSGKPL LIGTDVSLAR LQKADVVAQS 850 860 870 880 890 900 RISFPEKELL LLIRNHLISK GLGETATVLT KEADLPMTAA SHSSAFTPVT AAASPVSLPR 910 920 930 940 950 960 TPRIANGIAT RLGSHAAVGA SAPSAPTAHP QPRPPQGPLA LPGPSYAGNS PLIGRISFIR 970 980 990 1000 1010 1020 ERPSPCNGRK IRVLRQKSDH GAYSQSPAIK KQLDRHLPSP PTLDSIITEY LREQHARCKN 1030 1040 1050 1060 1070 1080 PVATCPPFSL FTPHQCPEPK QRRQAPINFT SRLNRRASFP KYGGVDGGCF DRHLIFSRFR 1090 1100 1110 1120 1130 1140 PISVFREANE DESGFTCCAF SARERFLMLG TCTGQLKLYN VFSGQEEASY NCHNSAITHL 1150 1160 1170 1180 1190 1200 EPSRDGSLLL TSATWSQPLS ALWGMKSVFD MKHSFTEDHY VEFSKHSQDR VIGTKGDIAH 1210 1220 1230 1240 1250 1260 IYDIQTGNKL LTLFNPDLAN NYKRNCATFN PTDDLVLNDG VLWDVRSAQA IHKFDKFNMN 1270 1280 1290 1300 1310 1320 ISGVFHPNGL EVIINTEIWD LRTFHLLHTV PALDQCRVVF NHTGTVMYGA MLQADDEDDL 1330 1340 1350 1360 1370 1380 MEERMKSPFG SSFRTFNATD YKPIATIDVK RNIFDLCTDT KDCYLAVIEN QGSMDALNMD 1390 1400 1410 1420 1430 1440 TVCRLYEVGR QRLAEDEDEE EDQEEEEQEE EDDDEDDDDT DDLDELDTDQ LLEAELEEDD 1450 1460 1470 1480 1490 1500 NNENAGEDGD NDFSPSDEEL ANLLEEGEDG EDEDSDADEE VELILGDTDS SDNSDLEDDI ILSLNE
	Isoform 3 [UniParc]. Checksum: A5A53818C128F546	FASTA	1,058	118,235
	10 20 30 40 50 60 MTTVVVHVDS KAELTTLLEQ WEKEHGSGQD MVPILTRMSQ LIEKETEEYR KGDPDPFDDR 70 80 90 100 110 120 HPGRADPECM LGHLLRILFK NDDFMNALVN AYVMTSREPP LNTAACRLLL DIMPGLETAV 130 140 150 160 170 180 VFQEKEGIVE NLFKWAREAD QPLRTYSTGL LGGAMENQDI AANYRDENSQ LVAIVLRRLR 190 200 210 220 230 240 ELQLQEVALR QENKRPSPRK LSSEPLLPLD EEAVDMDYGD MAVDDAEIQK SALQIIINCV 250 260 270 280 290 300 CGPDNRISSI GKFISGTPRR KLPQNPKSSE HTLAKMWNVV QSNNGIKVLL SLLSIKMPIT 310 320 330 340 350 360 DADQIRALAC KALVGLSRSS TVRQIISKLP LFSSCQIQQL MKEPVLQDKR SDHVKFCKYA 370 380 390 400 410 420 AELIERVSGK PLLIGTDVSL ARLQKADVVA QSRISFPEKE LLLLIRNHLI SKGLGETATV 430 440 450 460 470 480 LTKEADLPMT AASHSSAFTP VTAAASPVSL PRTPRIANGI ATRLGSHAAV GASAPSAPTA 490 500 510 520 530 540 HPQPRPPQGP LALPGPSYAG NSPLIGRISF IRERPSPCNG RKIRVLRQKS DHGAYSQSPA 550 560 570 580 590 600 IKKQLDRHLP SPPTLDSIIT EYLREQHARC KNPVATCPPF SLFTPHQCPE PKQRRQAPIN 610 620 630 640 650 660 FTSRLNRRAS FPKYGGVDGG CFDRHLIFSR FRPISVFREA NEDESGFTCC AFSARERFLM 670 680 690 700 710 720 LGTCTGQLKL YNVFSGQEEA SYNCHNSAIT HLEPSRDGSL LLTSATWSQP LSALWGMKSV 730 740 750 760 770 780 FDMKHSFTED HYVEFSKHSQ DRVIGTKGDI AHIYDIQTGN KLLTLFNPDL ANNYKRNCAT 790 800 810 820 830 840 FNPTDDLVLN DGVLWDVRSA QAIHKFDKFN MNISGVFHPN GLEVIINTEI WDLRTFHLLH 850 860 870 880 890 900 TVPALDQCRV VFNHTGTVMY GAMLQADDED DLMEERMKSP FGSSFRTFNA TDYKPIATID 910 920 930 940 950 960 VKRNIFDLCT DTKDCYLAVI ENQGSMDALN MDTVCRLYEV GRQRLAEDED EEEDQEEEEQ 970 980 990 1000 1010 1020 EEEDDDEDDD DTDDLDELDT DQLLEAELEE DDNNENAGED GDNDFSPSDE ELANLLEEGE 1030 1040 1050 DGEDEDSDAD EEVELILGDT DSSDNSDLED DIILSLNE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"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] (ISOFORMS 2 AND 3). Tissue: B-cell and Skin.
[4]	"Cytoplasmic retention of HIV-1 regulatory protein Vpr by protein-protein interaction with a novel human cytoplasmic protein VprBP." Zhang S., Feng Y., Narayan O., Zhao L.-J. Gene 263:131-140(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 107-1507, PROTEIN SEQUENCE OF 1174-1186 AND 1328-1343, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH HIV-1 VPR.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 375-1507. Tissue: Testis.
[6]	"Biochemical mechanism of HIV-I Vpr function. Specific interaction with a cellular protein." Zhao L.-J., Mukherjee S., Narayan O. J. Biol. Chem. 269:15577-15582(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 VPR.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1." Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C. Mol. Cell 23:709-721(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDB1.
[9]	"HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase." Le Rouzic E., Belaiedouni N., Estrabaud E., Morel M., Rain J.-C., Transy C., Margottin-Goguet F. Cell Cycle 6:182-188(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"The HIV1 protein Vpr acts to promote G2 cell cycle arrest by engaging a DDB1 and Cullin4A-containing ubiquitin ligase complex using VprBP/DCAF1 as an adaptor." Wen X., Duus K.M., Friedrich T.D., de Noronha C.M. J. Biol. Chem. 282:27046-27057(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"DDB1 and Cul4A are required for human immunodeficiency virus type 1 Vpr-induced G2 arrest." Tan L., Ehrlich E., Yu X.F. J. Virol. 81:10822-10830(2007) [PubMed] [Europe PMC] [Abstract] Cited for: COMPONENT OF E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, INTERACTION WITH HIV-1 VPR, FUNCTION.
[12]	"HIV-1 Vpr-mediated G2 arrest involves the DDB1-CUL4A[VPRBP] E3 ubiquitin ligase." Belzile J.P., Duisit G., Rougeau N., Mercier J., Finzi A., Cohen E.A. PLoS Pathog. 3:E85-E85(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH HIV-1 VPR.
[13]	"Lentiviral Vpr usurps Cul4-DDB1[VprBP] E3 ubiquitin ligase to modulate cell cycle." Hrecka K., Gierszewska M., Srivastava S., Kozaczkiewicz L., Swanson S.K., Florens L., Washburn M.P., Skowronski J. Proc. Natl. Acad. Sci. U.S.A. 104:11778-11783(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COMPONENT OF DDA1-DDB1-VRPBP/DCAF1 COMPLEX.
[14]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-280, MASS SPECTROMETRY. Tissue: Mammary cancer.
[15]	"HIV-1 Vpr activates the G2 checkpoint through manipulation of the ubiquitin proteasome system." DeHart J.L., Zimmerman E.S., Ardon O., Monteiro-Filho C.M., Arganaraz E.R., Planelles V. Virol. J. 4:57-57(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE CUL4A-RBX1-DDB1-VPRBP/DCAF1 COMPLEX, FUNCTION.
[16]	"Assembly with the Cul4A-DDB1[DCAF1] ubiquitin ligase protects HIV-1 Vpr from proteasomal degradation." Le Rouzic E., Morel M., Ayinde D., Belaidouni N., Letienne J., Transy C., Margottin-Goguet F. J. Biol. Chem. 283:21686-21692(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-895, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Human immunodeficiency virus type 1 Vpr-binding protein VprBP, a WD40 protein associated with the DDB1-CUL4 E3 ubiquitin ligase, is essential for DNA replication and embryonic development." McCall C.M., Miliani de Marval P.L., Chastain P.D. II, Jackson S.C., He Y.J., Kotake Y., Cook J.G., Xiong Y. Mol. Cell. Biol. 28:5621-5633(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DDB1, COMPONENT OF THE CUL4A-RBX1-DDB1-VPRBP/DCAF1 COMPLEX, CHROMATIN ASSOCIATION.
[19]	"VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for degradation." Huang J., Chen J. Oncogene 27:4056-4064(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NF2.
[20]	"Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection." Srivastava S., Swanson S.K., Manel N., Florens L., Washburn M.P., Skowronski J. PLoS Pathog. 4:E1000059-E1000059(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIV-2 VPX.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-888; SER-895 AND SER-898, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"The human immunodeficiency virus type 2 Vpx protein usurps the CUL4A-DDB1 DCAF1 ubiquitin ligase to overcome a postentry block in macrophage infection." Bergamaschi A., Ayinde D., David A., Le Rouzic E., Morel M., Collin G., Descamps D., Damond F., Brun-Vezinet F., Nisole S., Margottin-Goguet F., Pancino G., Transy C. J. Virol. 83:4854-4860(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIV-2 VPX.
[23]	"Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase." Maddika S., Chen J. Nat. Cell Biol. 11:409-419(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EDVP COMPLEX.
[24]	"Characterization of the molecular determinants of primary HIV-1 Vpr proteins: impact of the Q65R and R77Q substitutions on Vpr functions." Jacquot G., Le Rouzic E., Maidou-Peindara P., Maizy M., Lefrere J.J., Daneluzzi V., Monteiro-Filho C.M., Hong D., Planelles V., Morand-Joubert L., Benichou S. PLoS ONE 4:E7514-E7514(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 VPR.
[25]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-895, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Merlin/NF2 suppresses tumorigenesis by inhibiting the E3 ubiquitin ligase CRL4(DCAF1) in the nucleus." Li W., You L., Cooper J., Schiavon G., Pepe-Caprio A., Zhou L., Ishii R., Giovannini M., Hanemann C.O., Long S.B., Erdjument-Bromage H., Zhou P., Tempst P., Giancotti F.G. Cell 140:477-490(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH NF2.
[27]	"Evidence for an activation domain at the amino terminus of simian immunodeficiency virus Vpx." Gramberg T., Sunseri N., Landau N.R. J. Virol. 84:1387-1396(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, 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]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB018343 mRNA. Translation: BAA34520.2. Different initiation. BC022792 mRNA. Translation: AAH22792.1. BC110371 mRNA. Translation: AAI10372.1. AL080145 mRNA. Translation: CAB45738.1. AF061935 mRNA. Translation: AAG27134.1.
IPI	IPI00181396. IPI00329528. IPI00794498.
PIR	T12529.
RefSeq	NP_001165375.1. NM_001171904.1. NP_055518.1. NM_014703.2.
UniGene	Hs.716623.
3D structure databases
ProteinModelPortal	Q9Y4B6.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47048N.
IntAct	Q9Y4B6. 9 interactions.
STRING	9606.ENSP00000273612.
PTM databases
PhosphoSite	Q9Y4B6.
Polymorphism databases
DMDM	147742890.
Proteomic databases
PaxDb	Q9Y4B6.
PRIDE	Q9Y4B6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000335891; ENSP00000338857; ENSG00000145041. ENST00000563997; ENSP00000454540; ENSG00000260623. ENST00000566027; ENSP00000456445; ENSG00000260623.
GeneID	9730.
KEGG	hsa:9730.
UCSC	uc003dbe.2. human. uc021wys.1. human.
Organism-specific databases
CTD	9730.
GeneCards	GC03M051433.
HGNC	HGNC:30911. VPRBP.
HPA	HPA036142.
neXtProt	NX_Q9Y4B6.
PharmGKB	PA142670621.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG237621.
HOGENOM	HOG000007026.
HOVERGEN	HBG108659.
InParanoid	Q9Y4B6.
KO	K11789.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q9Y4B6.
Bgee	Q9Y4B6.
CleanEx	HS_VPRBP.
Genevestigator	Q9Y4B6.
Family and domain databases
Gene3D	1.25.10.10. 2 hits. 2.130.10.10. 2 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR006594. LisH_dimerisation. IPR015943. WD40/YVTN_repeat-like_dom. IPR017986. WD40_repeat_dom. [Graphical view]
SMART	SM00667. LisH. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF50978. WD40_like. 1 hit.
PROSITE	PS50896. LISH. 1 hit. PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. False negative. PS50294. WD_REPEATS_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9730.
NextBio	36604.

Entry information

Entry name

VPRBP_HUMAN

Accession

Primary (citable) accession number: Q9Y4B6
Secondary accession number(s): Q2YD74 , Q8TBD9, Q9HCA1, Q9UG37

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	May 15, 2007
Last modified:	May 1, 2013
This is version 94 of the entry and version 3 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.