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Q9Y4B6

- VPRBP_HUMAN

UniProt

Q9Y4B6 - VPRBP_HUMAN

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Protein

Protein VPRBP

Gene

VPRBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: VPRBP is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:23362280). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714). In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP 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. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT. In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage.21 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. histone kinase activity (H2A-T120 specific) Source: UniProtKB

GO - Biological processi

  1. B cell differentiation Source: UniProtKB
  2. cell competition in a multicellular organism Source: UniProtKB
  3. histone H2A-T120 phosphorylation Source: UniProtKB
  4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  5. protein ubiquitination Source: UniProtKB-UniPathway
  6. transcription, DNA-templated Source: UniProtKB-KW
  7. V(D)J recombination Source: UniProtKB
  8. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein VPRBP
Alternative name(s):
DDB1- and CUL4-associated factor 1
HIV-1 Vpr-binding protein
Short name:
VprBP
Serine/threonine-protein kinase VPRBP (EC:2.7.11.1)
Vpr-interacting protein
Gene namesi
Name:VPRBP
Synonyms:DCAF1, KIAA0800, RIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:30911. VPRBP.

Subcellular locationi

Cytoplasm. Nucleus
Note: Associated with chromatin in a DDB1-independent and cell cycle-dependent manner: recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi194 – 1941K → R: Abolishes serine/threonine-protein kinase kinase activity. 1 Publication
Mutagenesisi361 – 3611D → A: Abolishes serine/threonine-protein kinase kinase activity. 1 Publication
Mutagenesisi363 – 3631K → A: Abolishes serine/threonine-protein kinase kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA142670621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15071507Protein VPRBPPRO_0000287473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki280 – 280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei701 – 7011N6-acetyllysineBy similarity
Modified residuei888 – 8881Phosphothreonine1 Publication
Modified residuei895 – 8951Phosphoserine3 Publications
Modified residuei898 – 8981Phosphoserine1 Publication
Modified residuei979 – 9791Phosphoserine1 Publication
Modified residuei1000 – 10001Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y4B6.
PaxDbiQ9Y4B6.
PRIDEiQ9Y4B6.

PTM databases

PhosphoSiteiQ9Y4B6.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Inductioni

Up-regulated in a number of cancer cell lines (at protein level).1 Publication

Gene expression databases

BgeeiQ9Y4B6.
CleanExiHS_VPRBP.
ExpressionAtlasiQ9Y4B6. baseline and differential.
GenevestigatoriQ9Y4B6.

Organism-specific databases

HPAiHPA036142.

Interactioni

Subunit structurei

Component of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex. Interacts with DDB1; the interaction is direct. Also forms a ternary complex with DDA1 and DDB1. Interacts with NF2 (via FERM domain). Component of the EDVP complex, a E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP. Interacts with DYRK2; the interaction is direct. Interacts with RAG1; the interaction is direct. Interacts with LLGL1 and LLGL2. Interacts with histone H3. Interact with HIV-1 virus Vpr protein and HIV-2 virus Vpx protein; the interaction is direct.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDB1Q165313EBI-1996353,EBI-350322
LATS1O958354EBI-1996353,EBI-444209
LATS2Q9NRM72EBI-1996353,EBI-3506895
vprP125205EBI-1996353,EBI-6164519From a different organism.
vpxP180452EBI-1996353,EBI-6558105From a different organism.
vpxP195082EBI-1996353,EBI-6558117From a different organism.

Protein-protein interaction databases

BioGridi115079. 69 interactions.
DIPiDIP-47048N.
IntActiQ9Y4B6. 21 interactions.
MINTiMINT-4947153.
STRINGi9606.ENSP00000273612.

Structurei

Secondary structure

1
1507
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1076 – 10783
Beta strandi1081 – 10877
Beta strandi1096 – 11016
Beta strandi1107 – 11126
Beta strandi1115 – 11217
Turni1122 – 11243
Beta strandi1127 – 11326
Beta strandi1140 – 11434
Beta strandi1147 – 11537
Beta strandi1158 – 11658
Beta strandi1167 – 11693
Beta strandi1171 – 11766
Beta strandi1180 – 11845
Beta strandi1186 – 11883
Beta strandi1191 – 11966
Beta strandi1199 – 12046
Turni1205 – 12073
Beta strandi1210 – 12145
Turni1217 – 12193
Beta strandi1234 – 12396
Beta strandi1242 – 12454
Turni1246 – 12494
Beta strandi1250 – 12545
Beta strandi1259 – 12624
Beta strandi1270 – 12756
Beta strandi1278 – 12814
Turni1282 – 12843
Beta strandi1287 – 12904
Helixi1292 – 12943
Beta strandi1297 – 13015
Beta strandi1305 – 13139
Beta strandi1329 – 133810
Turni1339 – 13413
Beta strandi1344 – 13496
Beta strandi1351 – 13599
Beta strandi1361 – 13633
Beta strandi1365 – 13717
Turni1375 – 13784
Beta strandi1382 – 13887
Beta strandi1482 – 14865
Beta strandi1501 – 15055

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WA0X-ray2.31G/H1418-1507[»]
4CC9X-ray2.47A1058-1396[»]
4P7IX-ray2.60C/D1447-1507[»]
4PXWX-ray1.72A/B1039-1401[»]
ProteinModelPortaliQ9Y4B6.
SMRiQ9Y4B6. Positions 1073-1392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini562 – 59332ChromoAdd
BLAST
Domaini846 – 87833LisHPROSITE-ProRule annotationAdd
BLAST
Repeati1091 – 113040WD 1Add
BLAST
Repeati1133 – 117442WD 2Add
BLAST
Repeati1176 – 121338WD 3Add
BLAST
Repeati1215 – 124733WD 4Add
BLAST
Repeati1248 – 129043WD 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni141 – 500360Protein kinase-likeAdd
BLAST
Regioni1091 – 1290200WD repeat-like regionAdd
BLAST
Regioni1418 – 150790Interaction with NF2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1242 – 12498DWD box 1
Motifi1278 – 12858DWD box 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1396 – 1500105Asp/Glu-rich (acidic)Add
BLAST

Domaini

The protein kinase-like region mediates the threonine-protein kinase activity.1 Publication
The DWD boxes are required for interaction with DDB1.
The chromo domain with a restricted pocket directly recognizes monomethylated substrates.1 Publication

Sequence similaritiesi

Belongs to the VPRBP/DCAF1 family.Curated
Contains 1 chromo domain.Curated
Contains 1 LisH domain.PROSITE-ProRule annotation
Contains 5 WD repeats.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiNOG237621.
GeneTreeiENSGT00390000005874.
HOGENOMiHOG000007026.
HOVERGENiHBG108659.
InParanoidiQ9Y4B6.
KOiK11789.
OMAiDERIRSP.
PhylomeDBiQ9Y4B6.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
2.130.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR006594. LisH_dimerisation.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
SMARTiSM00667. LisH. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF50978. SSF50978. 2 hits.
PROSITEiPS50896. LISH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y4B6-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTTVVVHVDS KAELTTLLEQ WEKEHGSGQD MVPILTRMSQ LIEKETEEYR
60 70 80 90 100
KGDPDPFDDR HPGRADPECM LGHLLRILFK NDDFMNALVN AYVMTSREPP
110 120 130 140 150
LNTAACRLLL DIMPGLETAV VFQEKEGIVE NLFKWAREAD QPLRTYSTGL
160 170 180 190 200
LGGAMENQDI AANYRDENSQ LVAIVLRRLR ELQLQEVALR QENKRPSPRK
210 220 230 240 250
LSSEPLLPLD EEAVDMDYGD MAVDVVDGDQ EEASGDMEIS FHLDSGHKTS
260 270 280 290 300
SRVNSTTKPE DGGLKKNKSA KQGDRENFRK AKQKLGFSSS DPDRMFVELS
310 320 330 340 350
NSSWSEMSPW VIGTNYTLYP MTPAIEQRLI LQYLTPLGEY QELLPIFMQL
360 370 380 390 400
GSRELMMFYI DLKQTNDVLL TFEALKHLAS LLLHNKFATE FVAHGGVQKL
410 420 430 440 450
LEIPRPSMAA TGVSMCLYYL SYNQDAMERV CMHPHNVLSD VVNYTLWLME
460 470 480 490 500
CSHASGCCHA TMFFSICFSF RAVLELFDRY DGLRRLVNLI STLEILNLED
510 520 530 540 550
QGALLSDDEI FASRQTGKHT CMALRKYFEA HLAIKLEQVK QSLQRTEGGI
560 570 580 590 600
LVHPQPPYKA CSYTHEQIVE MMEFLIEYGP AQLYWEPAEV FLKLSCVQLL
610 620 630 640 650
LQLISIACNW KTYYARNDTV RFALDVLAIL TVVPKIQLQL AESVDVLDEA
660 670 680 690 700
GSTVSTVGIS IILGVAEGEF FIHDAEIQKS ALQIIINCVC GPDNRISSIG
710 720 730 740 750
KFISGTPRRK LPQNPKSSEH TLAKMWNVVQ SNNGIKVLLS LLSIKMPITD
760 770 780 790 800
ADQIRALACK ALVGLSRSST VRQIISKLPL FSSCQIQQLM KEPVLQDKRS
810 820 830 840 850
DHVKFCKYAA ELIERVSGKP LLIGTDVSLA RLQKADVVAQ SRISFPEKEL
860 870 880 890 900
LLLIRNHLIS KGLGETATVL TKEADLPMTA ASHSSAFTPV TAAASPVSLP
910 920 930 940 950
RTPRIANGIA TRLGSHAAVG ASAPSAPTAH PQPRPPQGPL ALPGPSYAGN
960 970 980 990 1000
SPLIGRISFI RERPSPCNGR KIRVLRQKSD HGAYSQSPAI KKQLDRHLPS
1010 1020 1030 1040 1050
PPTLDSIITE YLREQHARCK NPVATCPPFS LFTPHQCPEP KQRRQAPINF
1060 1070 1080 1090 1100
TSRLNRRASF PKYGGVDGGC FDRHLIFSRF RPISVFREAN EDESGFTCCA
1110 1120 1130 1140 1150
FSARERFLML GTCTGQLKLY NVFSGQEEAS YNCHNSAITH LEPSRDGSLL
1160 1170 1180 1190 1200
LTSATWSQPL SALWGMKSVF DMKHSFTEDH YVEFSKHSQD RVIGTKGDIA
1210 1220 1230 1240 1250
HIYDIQTGNK LLTLFNPDLA NNYKRNCATF NPTDDLVLND GVLWDVRSAQ
1260 1270 1280 1290 1300
AIHKFDKFNM NISGVFHPNG LEVIINTEIW DLRTFHLLHT VPALDQCRVV
1310 1320 1330 1340 1350
FNHTGTVMYG AMLQADDEDD LMEERMKSPF GSSFRTFNAT DYKPIATIDV
1360 1370 1380 1390 1400
KRNIFDLCTD TKDCYLAVIE NQGSMDALNM DTVCRLYEVG RQRLAEDEDE
1410 1420 1430 1440 1450
EEDQEEEEQE EEDDDEDDDD TDDLDELDTD QLLEAELEED DNNENAGEDG
1460 1470 1480 1490 1500
DNDFSPSDEE LANLLEEGED GEDEDSDADE EVELILGDTD SSDNSDLEDD

IILSLNE
Length:1,507
Mass (Da):169,007
Last modified:May 15, 2007 - v3
Checksum:i7E71AB2CAC4962C5
GO
Isoform 2 (identifier: Q9Y4B6-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:1,506
Mass (Da):168,936
Checksum:i016CF082F1239B17
GO
Isoform 3 (identifier: Q9Y4B6-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:1,058
Mass (Da):118,235
Checksum:iA5A53818C128F546
GO

Sequence cautioni

The sequence BAA34520.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti267 – 2671N → D.
Corresponds to variant rs3749318 [ dbSNP | Ensembl ].
VAR_051486
Natural varianti378 – 3781L → F Does not affect serine/threonine-protein kinase kinase activity.
Corresponds to variant rs17712228 [ dbSNP | Ensembl ].
VAR_051487
Natural varianti1031 – 10311L → P.
Corresponds to variant rs9835229 [ dbSNP | Ensembl ].
VAR_051488

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei87 – 871Missing in isoform 2. 1 PublicationVSP_025498
Alternative sequencei225 – 673449Missing in isoform 3. 1 PublicationVSP_025499Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB018343 mRNA. Translation: BAA34520.2. Different initiation.
AC092037 Genomic DNA. No translation available.
BC022792 mRNA. Translation: AAH22792.1.
BC110371 mRNA. Translation: AAI10372.1.
AL080145 mRNA. Translation: CAB45738.1.
AF061935 mRNA. Translation: AAG27134.1.
CCDSiCCDS74943.1. [Q9Y4B6-1]
CCDS74944.1. [Q9Y4B6-2]
PIRiT12529.
RefSeqiNP_001165375.1. NM_001171904.1. [Q9Y4B6-2]
NP_055518.1. NM_014703.2. [Q9Y4B6-1]
XP_005276808.1. XM_005276751.2. [Q9Y4B6-1]
XP_005276809.1. XM_005276752.2. [Q9Y4B6-1]
XP_005276810.1. XM_005276753.2. [Q9Y4B6-1]
XP_005276811.1. XM_005276754.2. [Q9Y4B6-1]
XP_005276812.1. XM_005276755.2. [Q9Y4B6-1]
XP_006713489.1. XM_006713426.1. [Q9Y4B6-1]
XP_006713490.1. XM_006713427.1. [Q9Y4B6-1]
UniGeneiHs.716623.

Genome annotation databases

EnsembliENST00000335891; ENSP00000338857; ENSG00000145041. [Q9Y4B6-3]
ENST00000423656; ENSP00000393183; ENSG00000145041. [Q9Y4B6-1]
ENST00000504652; ENSP00000421724; ENSG00000145041. [Q9Y4B6-2]
GeneIDi9730.
KEGGihsa:9730.
UCSCiuc003dbe.2. human. [Q9Y4B6-1]
uc021wys.1. human. [Q9Y4B6-2]

Polymorphism databases

DMDMi147742890.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB018343 mRNA. Translation: BAA34520.2 . Different initiation.
AC092037 Genomic DNA. No translation available.
BC022792 mRNA. Translation: AAH22792.1 .
BC110371 mRNA. Translation: AAI10372.1 .
AL080145 mRNA. Translation: CAB45738.1 .
AF061935 mRNA. Translation: AAG27134.1 .
CCDSi CCDS74943.1. [Q9Y4B6-1 ]
CCDS74944.1. [Q9Y4B6-2 ]
PIRi T12529.
RefSeqi NP_001165375.1. NM_001171904.1. [Q9Y4B6-2 ]
NP_055518.1. NM_014703.2. [Q9Y4B6-1 ]
XP_005276808.1. XM_005276751.2. [Q9Y4B6-1 ]
XP_005276809.1. XM_005276752.2. [Q9Y4B6-1 ]
XP_005276810.1. XM_005276753.2. [Q9Y4B6-1 ]
XP_005276811.1. XM_005276754.2. [Q9Y4B6-1 ]
XP_005276812.1. XM_005276755.2. [Q9Y4B6-1 ]
XP_006713489.1. XM_006713426.1. [Q9Y4B6-1 ]
XP_006713490.1. XM_006713427.1. [Q9Y4B6-1 ]
UniGenei Hs.716623.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3WA0 X-ray 2.31 G/H 1418-1507 [» ]
4CC9 X-ray 2.47 A 1058-1396 [» ]
4P7I X-ray 2.60 C/D 1447-1507 [» ]
4PXW X-ray 1.72 A/B 1039-1401 [» ]
ProteinModelPortali Q9Y4B6.
SMRi Q9Y4B6. Positions 1073-1392.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115079. 69 interactions.
DIPi DIP-47048N.
IntActi Q9Y4B6. 21 interactions.
MINTi MINT-4947153.
STRINGi 9606.ENSP00000273612.

PTM databases

PhosphoSitei Q9Y4B6.

Polymorphism databases

DMDMi 147742890.

Proteomic databases

MaxQBi Q9Y4B6.
PaxDbi Q9Y4B6.
PRIDEi Q9Y4B6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335891 ; ENSP00000338857 ; ENSG00000145041 . [Q9Y4B6-3 ]
ENST00000423656 ; ENSP00000393183 ; ENSG00000145041 . [Q9Y4B6-1 ]
ENST00000504652 ; ENSP00000421724 ; ENSG00000145041 . [Q9Y4B6-2 ]
GeneIDi 9730.
KEGGi hsa:9730.
UCSCi uc003dbe.2. human. [Q9Y4B6-1 ]
uc021wys.1. human. [Q9Y4B6-2 ]

Organism-specific databases

CTDi 9730.
GeneCardsi GC03M051433.
HGNCi HGNC:30911. VPRBP.
HPAi HPA036142.
neXtProti NX_Q9Y4B6.
PharmGKBi PA142670621.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG237621.
GeneTreei ENSGT00390000005874.
HOGENOMi HOG000007026.
HOVERGENi HBG108659.
InParanoidi Q9Y4B6.
KOi K11789.
OMAi DERIRSP.
PhylomeDBi Q9Y4B6.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GeneWikii VPRBP.
GenomeRNAii 9730.
NextBioi 36604.
PROi Q9Y4B6.

Gene expression databases

Bgeei Q9Y4B6.
CleanExi HS_VPRBP.
ExpressionAtlasi Q9Y4B6. baseline and differential.
Genevestigatori Q9Y4B6.

Family and domain databases

Gene3Di 1.25.10.10. 2 hits.
2.130.10.10. 2 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR006594. LisH_dimerisation.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view ]
SMARTi SM00667. LisH. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
SSF50978. SSF50978. 2 hits.
PROSITEi PS50896. LISH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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.
  5. "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.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 375-1507.
    Tissue: Testis.
  7. "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.
  8. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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.
  10. "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery."
    Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.
    Nature 443:590-593(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. Cited for: FUNCTION, COMPONENT OF DDA1-DDB1-VRPBP/DCAF1 COMPLEX.
  16. "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.
    Tissue: Mammary cancer.
  17. "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.
  18. "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.
  19. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "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.
  21. "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.
  22. "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.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-888; SER-895 AND SER-898, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "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.
  25. "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: IDENTIFICATION IN THE EDVP COMPLEX, FUNCTION.
  26. "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.
  27. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  28. "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.
  29. Cited for: FUNCTION, INTERACTION WITH LLGL1 AND LLGL2.
  30. "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.
  31. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Dyrk2-associated EDD-DDB1-VprBP E3 ligase inhibits telomerase by TERT degradation."
    Jung H.Y., Wang X., Jun S., Park J.I.
    J. Biol. Chem. 288:7252-7262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TERT.
  35. "EZH2 generates a methyl degron that is recognized by the DCAF1/DDB1/CUL4 E3 ubiquitin ligase complex."
    Lee J.M., Lee J.S., Kim H., Kim K., Park H., Kim J.Y., Lee S.H., Kim I.S., Kim J., Lee M., Chung C.H., Seo S.B., Yoon J.B., Ko E., Noh D.Y., Kim K.I., Kim K.K., Baek S.H.
    Mol. Cell 48:572-586(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  36. "Vpr-binding protein antagonizes p53-mediated transcription via direct interaction with H3 tail."
    Kim K., Heo K., Choi J., Jackson S., Kim H., Xiong Y., An W.
    Mol. Cell. Biol. 32:783-796(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONE H3.
  37. "VprBP has intrinsic kinase activity targeting histone H2A and represses gene transcription."
    Kim K., Kim J.M., Kim J.S., Choi J., Lee Y.S., Neamati N., Song J.S., Heo K., An W.
    Mol. Cell 52:459-467(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION, MUTAGENESIS OF LYS-194; ASP-361 AND LYS-363, CHARACTERIZATION OF VARIANT PHE-378.
  38. "HIV-1 Vpr Induces the Degradation of ZIP and sZIP, Adaptors of the NuRD Chromatin Remodeling Complex, by Hijacking DCAF1/VprBP."
    Maudet C., Sourisce A., Dragin L., Lahouassa H., Rain J.C., Bouaziz S., Ramirez B.C., Margottin-Goguet F.
    PLoS ONE 8:E77320-E77320(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIV-1 VPR.
  39. "Structural basis of lentiviral subversion of a cellular protein degradation pathway."
    Schwefel D., Groom H.C., Boucherit V.C., Christodoulou E., Walker P.A., Stoye J.P., Bishop K.N., Taylor I.A.
    Nature 505:234-238(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 1058-1396 IN COMPLEX WITH SAMHD1 AND IMMUNODEFICIENCY VIRUS PROTEIN VPX, FUNCTION, INTERACTION WITH SAMHD1 AND VIRAL VPX.

Entry informationi

Entry nameiVPRBP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4B6
Secondary accession number(s): Q2YD74
, Q8TBD9, Q9HCA1, Q9UG37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: October 29, 2014
This is version 109 of the entry and version 3 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3