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Protein

Protein VPRBP

Gene

VPRBP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • histone kinase activity (H2A-T120 specific) Source: UniProtKB

GO - Biological processi

  • B cell differentiation Source: UniProtKB
  • cell competition in a multicellular organism Source: UniProtKB
  • histone H2A-T120 phosphorylation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein ubiquitination Source: UniProtKB-UniPathway
  • transcription, DNA-templated Source: UniProtKB-KW
  • V(D)J recombination Source: UniProtKB
  • 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

ReactomeiR-HSA-983168. 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
Proteomesi
  • UP000005640 Componenti: 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

  • cytoplasm Source: UniProtKB-SubCell
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi194K → R: Abolishes serine/threonine-protein kinase kinase activity. 1 Publication1
Mutagenesisi361D → A: Abolishes serine/threonine-protein kinase kinase activity. 1 Publication1
Mutagenesisi363K → A: Abolishes serine/threonine-protein kinase kinase activity. 1 Publication1

Organism-specific databases

DisGeNETi9730.
OpenTargetsiENSG00000145041.
PharmGKBiPA142670621.

Polymorphism and mutation databases

BioMutaiVPRBP.
DMDMi147742890.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002874731 – 1507Protein VPRBPAdd BLAST1507

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei202PhosphoserineCombined sources1
Modified residuei255PhosphoserineCombined sources1
Modified residuei701N6-acetyllysineBy similarity1
Modified residuei828PhosphoserineCombined sources1
Modified residuei888PhosphothreonineCombined sources1
Modified residuei895PhosphoserineCombined sources1
Modified residuei898PhosphoserineCombined sources1
Modified residuei979PhosphoserineCombined sources1
Modified residuei1000PhosphoserineCombined sources1
Modified residuei1328PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Y4B6.
PaxDbiQ9Y4B6.
PeptideAtlasiQ9Y4B6.
PRIDEiQ9Y4B6.

PTM databases

iPTMnetiQ9Y4B6.
PhosphoSitePlusiQ9Y4B6.

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

BgeeiENSG00000145041.
CleanExiHS_VPRBP.
GenevisibleiQ9Y4B6. HS.

Organism-specific databases

HPAiHPA036142.
HPA052445.
HPA053203.

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. Interacts 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
vprP059282EBI-9915372,EBI-9210238From a different organism.
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. 118 interactors.
DIPiDIP-47048N.
IntActiQ9Y4B6. 38 interactors.
MINTiMINT-4947153.
STRINGi9606.ENSP00000393183.

Structurei

Secondary structure

11507
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1076 – 1078Combined sources3
Beta strandi1081 – 1087Combined sources7
Beta strandi1096 – 1101Combined sources6
Beta strandi1107 – 1112Combined sources6
Beta strandi1115 – 1121Combined sources7
Turni1122 – 1124Combined sources3
Beta strandi1127 – 1132Combined sources6
Beta strandi1140 – 1143Combined sources4
Beta strandi1147 – 1153Combined sources7
Beta strandi1158 – 1165Combined sources8
Beta strandi1167 – 1169Combined sources3
Beta strandi1171 – 1176Combined sources6
Beta strandi1180 – 1184Combined sources5
Beta strandi1186 – 1188Combined sources3
Beta strandi1191 – 1196Combined sources6
Beta strandi1199 – 1204Combined sources6
Turni1205 – 1207Combined sources3
Beta strandi1210 – 1214Combined sources5
Turni1217 – 1219Combined sources3
Beta strandi1234 – 1239Combined sources6
Beta strandi1242 – 1245Combined sources4
Turni1246 – 1249Combined sources4
Beta strandi1250 – 1254Combined sources5
Beta strandi1259 – 1262Combined sources4
Beta strandi1270 – 1275Combined sources6
Beta strandi1278 – 1281Combined sources4
Turni1282 – 1284Combined sources3
Beta strandi1287 – 1290Combined sources4
Helixi1292 – 1294Combined sources3
Beta strandi1297 – 1301Combined sources5
Beta strandi1305 – 1313Combined sources9
Beta strandi1329 – 1338Combined sources10
Turni1339 – 1341Combined sources3
Beta strandi1344 – 1349Combined sources6
Beta strandi1351 – 1359Combined sources9
Beta strandi1361 – 1363Combined sources3
Beta strandi1365 – 1371Combined sources7
Turni1375 – 1378Combined sources4
Beta strandi1382 – 1388Combined sources7
Beta strandi1482 – 1485Combined sources4
Beta strandi1501 – 1504Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WA0X-ray2.31G/H1418-1507[»]
4CC9X-ray2.47A1058-1396[»]
4P7IX-ray2.60C/D1447-1507[»]
4PXWX-ray1.72A/B1039-1401[»]
4Z8LX-ray2.60A/D1057-1396[»]
5AJAX-ray2.65A1058-1396[»]
5JK7X-ray3.49C/E1045-1396[»]
ProteinModelPortaliQ9Y4B6.
SMRiQ9Y4B6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini562 – 593ChromoAdd BLAST32
Domaini846 – 878LisHPROSITE-ProRule annotationAdd BLAST33
Repeati1091 – 1130WD 1Add BLAST40
Repeati1133 – 1174WD 2Add BLAST42
Repeati1176 – 1213WD 3Add BLAST38
Repeati1215 – 1247WD 4Add BLAST33
Repeati1248 – 1290WD 5Add BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni141 – 500Protein kinase-likeAdd BLAST360
Regioni1091 – 1290WD repeat-like regionAdd BLAST200
Regioni1418 – 1507Interaction with NF2Add BLAST90

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1242 – 1249DWD box 18
Motifi1278 – 1285DWD box 28

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1396 – 1500Asp/Glu-rich (acidic)Add BLAST105

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

eggNOGiKOG1832. Eukaryota.
ENOG410XR8C. LUCA.
GeneTreeiENSGT00390000005874.
HOGENOMiHOG000007026.
HOVERGENiHBG108659.
InParanoidiQ9Y4B6.
KOiK11789.
OMAiGYESKQE.
OrthoDBiEOG091G0128.
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.
IPR033270. VPRBP/DCAF1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR13129. PTHR13129. 1 hit.
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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051486267N → D.Corresponds to variant rs3749318dbSNPEnsembl.1
Natural variantiVAR_051487378L → F Does not affect serine/threonine-protein kinase kinase activity. 1 PublicationCorresponds to variant rs17712228dbSNPEnsembl.1
Natural variantiVAR_0514881031L → P.Corresponds to variant rs9835229dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02549887Missing in isoform 2. 1 Publication1
Alternative sequenceiVSP_025499225 – 673Missing in isoform 3. 1 PublicationAdd BLAST449

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005276810.1. XM_005276753.4. [Q9Y4B6-1]
XP_005276812.1. XM_005276755.4. [Q9Y4B6-1]
XP_011532575.1. XM_011534273.2. [Q9Y4B6-1]
XP_011532576.1. XM_011534274.2. [Q9Y4B6-1]
XP_011532577.1. XM_011534275.2. [Q9Y4B6-1]
XP_011532578.1. XM_011534276.2. [Q9Y4B6-1]
XP_011532579.1. XM_011534277.2. [Q9Y4B6-1]
XP_016863035.1. XM_017007546.1. [Q9Y4B6-1]
XP_016863036.1. XM_017007547.1. [Q9Y4B6-1]
XP_016863037.1. XM_017007548.1. [Q9Y4B6-1]
XP_016863038.1. XM_017007549.1. [Q9Y4B6-1]
XP_016863039.1. XM_017007550.1. [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.
UCSCiuc032rnn.1. human. [Q9Y4B6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005276810.1. XM_005276753.4. [Q9Y4B6-1]
XP_005276812.1. XM_005276755.4. [Q9Y4B6-1]
XP_011532575.1. XM_011534273.2. [Q9Y4B6-1]
XP_011532576.1. XM_011534274.2. [Q9Y4B6-1]
XP_011532577.1. XM_011534275.2. [Q9Y4B6-1]
XP_011532578.1. XM_011534276.2. [Q9Y4B6-1]
XP_011532579.1. XM_011534277.2. [Q9Y4B6-1]
XP_016863035.1. XM_017007546.1. [Q9Y4B6-1]
XP_016863036.1. XM_017007547.1. [Q9Y4B6-1]
XP_016863037.1. XM_017007548.1. [Q9Y4B6-1]
XP_016863038.1. XM_017007549.1. [Q9Y4B6-1]
XP_016863039.1. XM_017007550.1. [Q9Y4B6-1]
UniGeneiHs.716623.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WA0X-ray2.31G/H1418-1507[»]
4CC9X-ray2.47A1058-1396[»]
4P7IX-ray2.60C/D1447-1507[»]
4PXWX-ray1.72A/B1039-1401[»]
4Z8LX-ray2.60A/D1057-1396[»]
5AJAX-ray2.65A1058-1396[»]
5JK7X-ray3.49C/E1045-1396[»]
ProteinModelPortaliQ9Y4B6.
SMRiQ9Y4B6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115079. 118 interactors.
DIPiDIP-47048N.
IntActiQ9Y4B6. 38 interactors.
MINTiMINT-4947153.
STRINGi9606.ENSP00000393183.

PTM databases

iPTMnetiQ9Y4B6.
PhosphoSitePlusiQ9Y4B6.

Polymorphism and mutation databases

BioMutaiVPRBP.
DMDMi147742890.

Proteomic databases

EPDiQ9Y4B6.
PaxDbiQ9Y4B6.
PeptideAtlasiQ9Y4B6.
PRIDEiQ9Y4B6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335891; ENSP00000338857; ENSG00000145041. [Q9Y4B6-3]
ENST00000423656; ENSP00000393183; ENSG00000145041. [Q9Y4B6-1]
ENST00000504652; ENSP00000421724; ENSG00000145041. [Q9Y4B6-2]
GeneIDi9730.
KEGGihsa:9730.
UCSCiuc032rnn.1. human. [Q9Y4B6-1]

Organism-specific databases

CTDi9730.
DisGeNETi9730.
GeneCardsiVPRBP.
HGNCiHGNC:30911. VPRBP.
HPAiHPA036142.
HPA052445.
HPA053203.
neXtProtiNX_Q9Y4B6.
OpenTargetsiENSG00000145041.
PharmGKBiPA142670621.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1832. Eukaryota.
ENOG410XR8C. LUCA.
GeneTreeiENSGT00390000005874.
HOGENOMiHOG000007026.
HOVERGENiHBG108659.
InParanoidiQ9Y4B6.
KOiK11789.
OMAiGYESKQE.
OrthoDBiEOG091G0128.
PhylomeDBiQ9Y4B6.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiVPRBP. human.
GeneWikiiVPRBP.
GenomeRNAii9730.
PROiQ9Y4B6.

Gene expression databases

BgeeiENSG00000145041.
CleanExiHS_VPRBP.
GenevisibleiQ9Y4B6. HS.

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.
IPR033270. VPRBP/DCAF1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR13129. PTHR13129. 1 hit.
SMARTiSM00667. LisH. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF50978. SSF50978. 2 hits.
PROSITEiPS50896. LISH. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 133 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.