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Q13620

- CUL4B_HUMAN

UniProt

Q13620 - CUL4B_HUMAN

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Protein
Cullin-4B
Gene
CUL4B, KIAA0695
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.6 Publications

Pathwayi

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. UV-damage excision repair Source: UniProt
  2. cell cycle Source: UniProtKB
  3. histone H2A monoubiquitination Source: UniProt
  4. positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  5. positive regulation of protein catabolic process Source: Ensembl
  6. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-4B
Short name:
CUL-4B
Gene namesi
Name:CUL4B
Synonyms:KIAA0695
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:2555. CUL4B.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. Cul4B-RING E3 ubiquitin ligase complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: HPA
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:300354]: A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti213 – 2131T → I in MRXS15; uncertain pathological significance. 2 Publications
VAR_032273
Natural varianti572 – 5721R → C in MRXS15. 2 Publications
VAR_032274
Natural varianti745 – 7451V → A in MRXS15. 2 Publications
VAR_032275

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 584Missing: Distributed in cytoplasm. Fails to promote cell proliferation. No binding to KPNA2, KPNA4 and KPNA1. 1 Publication
Mutagenesisi55 – 551K → A: No impairment in nuclear localization. 1 Publication
Mutagenesisi56 – 561K → A: Disrupts nuclear localization and does not bind KPNA2, KPNA4, KPNA1; when associated with A-57. Disrupts nuclear localization. 1 Publication
Mutagenesisi57 – 571R → A: Disrupts nuclear localization and does not bind KPNA2, KPNA4, KPNA1; when associated with A-56. Disrupts nuclear localization. 1 Publication
Mutagenesisi58 – 581K → A: No impairment in nuclear localization. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi300354. phenotype.
Orphaneti85293. Cabezas syndrome.
PharmGKBiPA27051.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 913913Cullin-4B
PRO_0000393946Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491Phosphothreonine2 Publications
Modified residuei53 – 531Phosphoserine1 Publication
Modified residuei146 – 1461Phosphoserine2 Publications
Modified residuei193 – 1931Phosphoserine1 Publication
Cross-linki859 – 859Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) By similarity

Post-translational modificationi

Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13620.
PaxDbiQ13620.
PRIDEiQ13620.

PTM databases

PhosphoSiteiQ13620.

Miscellaneous databases

PMAP-CutDBQ13620.

Expressioni

Gene expression databases

ArrayExpressiQ13620.
BgeeiQ13620.
CleanExiHS_CUL4B.
GenevestigatoriQ13620.

Organism-specific databases

HPAiCAB017786.
HPA003046.
HPA011880.

Interactioni

Subunit structurei

Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes that seem to be formed of DDB1, CUL4A or CUL4B, RBX1 and a variable substrate recognition component which seems to belong to a protein family described as DCAF (Ddb1- and Cul4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Component of the DCX(DTL) complex with the putative substrate recognition component DTL. Component of the DCX(DDB2) complex with the putative substrate recognition component DDB2. Part of a complex with RBX1 and TIP120A/CAND1. Interacts with RBX1 GRWD1, MLST8, SMU1, TLE2, TLE3, VPRBP, DDA1, DCAF6, DCAF17, DDB2, DCAF8, TIP120A/CAND1 and TMEM113. Interacts with cyclin E and with importins alpha-1 (KPNA2), alpha-3 (KPNA4), alpha-5 (KPNA1) and beta-1 (KPNB1). May interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76 and WDR5.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAND1Q86VP63EBI-456067,EBI-456077
DDB1Q1653115EBI-456067,EBI-350322
RBX1P628774EBI-456067,EBI-398523

Protein-protein interaction databases

BioGridi114028. 314 interactions.
DIPiDIP-31609N.
IntActiQ13620. 34 interactions.
MINTiMINT-4774381.
STRINGi9606.ENSP00000384109.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi210 – 2123
Helixi215 – 22814
Helixi237 – 25014
Helixi253 – 27018
Helixi271 – 2766
Helixi282 – 30625
Helixi308 – 3125
Turni315 – 3173
Helixi324 – 33512
Turni336 – 3383
Helixi340 – 35819
Helixi365 – 37713
Helixi381 – 3844
Helixi386 – 40722
Helixi410 – 43021
Helixi434 – 4363
Helixi437 – 44812
Helixi450 – 4523
Helixi453 – 46614
Helixi470 – 48011
Helixi486 – 50722
Beta strandi511 – 5133
Helixi515 – 53319
Helixi538 – 54912
Helixi841 – 86020
Beta strandi861 – 8655
Helixi866 – 87611
Helixi883 – 89513
Beta strandi898 – 9014
Beta strandi908 – 9114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DO7NMR-A826-913[»]
4A0CX-ray3.80C/E192-913[»]
4A0LX-ray7.40E/H192-913[»]
4A64X-ray2.57A/B/C/D206-557[»]
ProteinModelPortaliQ13620.
SMRiQ13620. Positions 206-913.

Miscellaneous databases

EvolutionaryTraceiQ13620.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi55 – 584Nuclear localization signal1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 193191Ser-rich
Add
BLAST

Sequence similaritiesi

Belongs to the cullin family.

Phylogenomic databases

eggNOGiCOG5647.
HOVERGENiHBG003619.
KOiK10609.
OMAiLQKGLNH.
OrthoDBiEOG75TMB5.
PhylomeDBiQ13620.
TreeFamiTF101153.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13620-2) [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

MMSQSSGSGD GNDDEATTSK DGGFSSPSPS AAAAAQEVRS ATDGNTSTTP    50
PTSAKKRKLN SSSSSSSNSS NEREDFDSTS SSSSTPPLQP RDSASPSTSS 100
FCLGVSVAAS SHVPIQKKLR FEDTLEFVGF DAKMAEESSS SSSSSSPTAA 150
TSQQQQLKNK SILISSVASV HHANGLAKSS TTVSSFANSK PGSAKKLVIK 200
NFKDKPKLPE NYTDETWQKL KEAVEAIQNS TSIKYNLEEL YQAVENLCSY 250
KISANLYKQL RQICEDHIKA QIHQFREDSL DSVLFLKKID RCWQNHCRQM 300
IMIRSIFLFL DRTYVLQNSM LPSIWDMGLE LFRAHIISDQ KVQNKTIDGI 350
LLLIERERNG EAIDRSLLRS LLSMLSDLQI YQDSFEQRFL EETNRLYAAE 400
GQKLMQEREV PEYLHHVNKR LEEEADRLIT YLDQTTQKSL IATVEKQLLG 450
EHLTAILQKG LNNLLDENRI QDLSLLYQLF SRVRGGVQVL LQQWIEYIKA 500
FGSTIVINPE KDKTMVQELL DFKDKVDHII DICFLKNEKF INAMKEAFET 550
FINKRPNKPA ELIAKYVDSK LRAGNKEATD EELEKMLDKI MIIFRFIYGK 600
DVFEAFYKKD LAKRLLVGKS ASVDAEKSML SKLKHECGAA FTSKLEGMFK 650
DMELSKDIMI QFKQYMQNQN VPGNIELTVN ILTMGYWPTY VPMEVHLPPE 700
MVKLQEIFKT FYLGKHSGRK LQWQSTLGHC VLKAEFKEGK KELQVSLFQT 750
LVLLMFNEGE EFSLEEIKQA TGIEDGELRR TLQSLACGKA RVLAKNPKGK 800
DIEDGDKFIC NDDFKHKLFR IKINQIQMKE TVEEQASTTE RVFQDRQYQI 850
DAAIVRIMKM RKTLSHNLLV SEVYNQLKFP VKPADLKKRI ESLIDRDYME 900
RDKENPNQYN YIA 913
Length:913
Mass (Da):103,982
Last modified:May 18, 2010 - v4
Checksum:i3E58C5868FDF0700
GO
Isoform 2 (identifier: Q13620-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MMSQSSGSGDGNDDEATTSKDG → MFPT

Note: Contains a N-acetylmethionine at position 1. Contains a phosphoserine at position 8. Contains a phosphoserine at position 10.

Show »
Length:895
Mass (Da):102,299
Checksum:i25B25D253C1C2B71
GO
Isoform 3 (identifier: Q13620-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-196: Missing.
     197-203: LVIKNFK → MIDPDFA

Show »
Length:717
Mass (Da):84,017
Checksum:iD50E2D33B73E6CB9
GO

Sequence cautioni

The sequence AAK16812.1 differs from that shown. Reason: Frameshift at position 115.
The sequence AAB67315.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031L → P.1 Publication
Corresponds to variant rs61759504 [ dbSNP | Ensembl ].
VAR_032272
Natural varianti213 – 2131T → I in MRXS15; uncertain pathological significance. 2 Publications
VAR_032273
Natural varianti572 – 5721R → C in MRXS15. 2 Publications
VAR_032274
Natural varianti745 – 7451V → A in MRXS15. 2 Publications
VAR_032275

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 196196Missing in isoform 3.
VSP_039084Add
BLAST
Alternative sequencei1 – 2222MMSQS…TSKDG → MFPT in isoform 2.
VSP_039085Add
BLAST
Alternative sequencei197 – 2037LVIKNFK → MIDPDFA in isoform 3.
VSP_039086

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691S → R in BAG53936. 1 Publication
Sequence conflicti126 – 1261E → G in CAD97843. 1 Publication
Sequence conflicti142 – 1421S → P in BAG53936. 1 Publication
Sequence conflicti196 – 1961K → N in AAK16812. 1 Publication
Sequence conflicti265 – 2651E → G in BAG53936. 1 Publication
Sequence conflicti268 – 2681I → M in AAK16812. 1 Publication
Sequence conflicti485 – 4851G → D in CAD97843. 1 Publication
Sequence conflicti664 – 6641Q → QVK in AAK16812. 1 Publication
Sequence conflicti727 – 7271L → I in AAR13073. 1 Publication
Sequence conflicti727 – 7271L → I in AAH36216. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY365125 mRNA. Translation: AAR13073.1.
AF212995 mRNA. Translation: AAK16812.1. Frameshift.
AK123688 mRNA. Translation: BAG53936.1.
AK299081 mRNA. Translation: BAH12944.1.
AK315037 mRNA. Translation: BAG37520.1.
BX537787 mRNA. Translation: CAD97843.1.
AC002476 Genomic DNA. Translation: AAB67315.1. Sequence problems.
AL451005, AC002476 Genomic DNA. Translation: CAI41370.1.
CH471107 Genomic DNA. Translation: EAX11877.1.
BC036216 mRNA. Translation: AAH36216.1.
AB014595 mRNA. Translation: BAA31670.2.
U58091 mRNA. Translation: AAC50548.1.
CCDSiCCDS35379.1. [Q13620-2]
CCDS43987.1. [Q13620-1]
RefSeqiNP_001073341.1. NM_001079872.1. [Q13620-1]
NP_003579.3. NM_003588.3. [Q13620-2]
UniGeneiHs.102914.

Genome annotation databases

EnsembliENST00000371322; ENSP00000360373; ENSG00000158290. [Q13620-1]
ENST00000404115; ENSP00000384109; ENSG00000158290. [Q13620-2]
GeneIDi8450.
KEGGihsa:8450.
UCSCiuc004esv.3. human. [Q13620-1]
uc004esw.3. human. [Q13620-2]

Polymorphism databases

DMDMi296439468.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY365125 mRNA. Translation: AAR13073.1 .
AF212995 mRNA. Translation: AAK16812.1 . Frameshift.
AK123688 mRNA. Translation: BAG53936.1 .
AK299081 mRNA. Translation: BAH12944.1 .
AK315037 mRNA. Translation: BAG37520.1 .
BX537787 mRNA. Translation: CAD97843.1 .
AC002476 Genomic DNA. Translation: AAB67315.1 . Sequence problems.
AL451005 , AC002476 Genomic DNA. Translation: CAI41370.1 .
CH471107 Genomic DNA. Translation: EAX11877.1 .
BC036216 mRNA. Translation: AAH36216.1 .
AB014595 mRNA. Translation: BAA31670.2 .
U58091 mRNA. Translation: AAC50548.1 .
CCDSi CCDS35379.1. [Q13620-2 ]
CCDS43987.1. [Q13620-1 ]
RefSeqi NP_001073341.1. NM_001079872.1. [Q13620-1 ]
NP_003579.3. NM_003588.3. [Q13620-2 ]
UniGenei Hs.102914.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DO7 NMR - A 826-913 [» ]
4A0C X-ray 3.80 C/E 192-913 [» ]
4A0L X-ray 7.40 E/H 192-913 [» ]
4A64 X-ray 2.57 A/B/C/D 206-557 [» ]
ProteinModelPortali Q13620.
SMRi Q13620. Positions 206-913.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114028. 314 interactions.
DIPi DIP-31609N.
IntActi Q13620. 34 interactions.
MINTi MINT-4774381.
STRINGi 9606.ENSP00000384109.

PTM databases

PhosphoSitei Q13620.

Polymorphism databases

DMDMi 296439468.

Proteomic databases

MaxQBi Q13620.
PaxDbi Q13620.
PRIDEi Q13620.

Protocols and materials databases

DNASUi 8450.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371322 ; ENSP00000360373 ; ENSG00000158290 . [Q13620-1 ]
ENST00000404115 ; ENSP00000384109 ; ENSG00000158290 . [Q13620-2 ]
GeneIDi 8450.
KEGGi hsa:8450.
UCSCi uc004esv.3. human. [Q13620-1 ]
uc004esw.3. human. [Q13620-2 ]

Organism-specific databases

CTDi 8450.
GeneCardsi GC0XM119658.
H-InvDB HIX0017025.
HGNCi HGNC:2555. CUL4B.
HPAi CAB017786.
HPA003046.
HPA011880.
MIMi 300304. gene.
300354. phenotype.
neXtProti NX_Q13620.
Orphaneti 85293. Cabezas syndrome.
PharmGKBi PA27051.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5647.
HOVERGENi HBG003619.
KOi K10609.
OMAi LQKGLNH.
OrthoDBi EOG75TMB5.
PhylomeDBi Q13620.
TreeFami TF101153.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

EvolutionaryTracei Q13620.
GeneWikii CUL4B.
GenomeRNAii 8450.
NextBioi 31618.
PMAP-CutDB Q13620.
PROi Q13620.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13620.
Bgeei Q13620.
CleanExi HS_CUL4B.
Genevestigatori Q13620.

Family and domain databases

Gene3Di 1.10.10.10. 2 hits.
InterProi IPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view ]
SMARTi SM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view ]
SUPFAMi SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEi PS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint."
    Higa L.A., Mihaylov I.S., Banks D.P., Zheng J., Zhang H.
    Nat. Cell Biol. 5:1008-1015(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH CDT1.
  2. "Molecular cloning of a full-length cullin, CUL4B and identification of its interacting proteins."
    Du M., Zu Z., Sansores-Garcia L., Wu K.K.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Chondrocyte, Teratocarcinoma and Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal liver.
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] (ISOFORM 1).
    Tissue: Testis.
  8. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-913 (ISOFORMS 1/2).
    Tissue: Brain.
  9. "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.
  10. "cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family."
    Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.
    Cell 85:829-839(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 626-913.
  11. "Covalent modification of all members of human cullin family proteins by NEDD8."
    Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N., Kato S., Tanaka K.
    Oncogene 18:6829-6834(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION.
  12. "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: INTERACTION WITH RBX1.
  13. "TIP120A associates with cullins and modulates ubiquitin ligase activity."
    Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.
    J. Biol. Chem. 278:15905-15910(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIP120A, IDENTIFICATION IN A COMPLEX WITH RBX1 AND TIP120A.
  14. "Involvement of CUL4 ubiquitin E3 ligases in regulating CDK inhibitors Dacapo/p27Kip1 and cyclin E degradation."
    Higa L.A., Yang X., Zheng J., Banks D., Wu M., Ghosh P., Sun H., Zhang H.
    Cell Cycle 5:71-77(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CYCLIN E.
  15. "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 AND RBX1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  16. "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 VPRBP; DDA1; DCAF6; DCAF17; DDB2 AND DCAF8.
  17. "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation."
    Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.
    Nat. Cell Biol. 8:1277-1283(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DTL; DDB2; TMEM113; WDR5B; WDR82; WDR26; GRWD1; WDR51B; SNRNP40; DCAF8; WDR61; WDR76; WDR5; SMU1; TLE2 AND TLE3.
  18. "Mutation in CUL4B, which encodes a member of cullin-RING ubiquitin ligase complex, causes X-linked mental retardation."
    Zou Y., Liu Q., Chen B., Zhang X., Guo C., Zhou H., Li J., Gao G., Guo Y., Yan C., Wei J., Shao C., Gong Y.
    Am. J. Hum. Genet. 80:561-566(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRXS15.
  19. "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A."
    Guerrero-Santoro J., Kapetanaki M.G., Hsieh C.L., Gorbachinsky I., Levine A.S., Rapic-Otrin V.
    Cancer Res. 68:5014-5022(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  20. "mTORC1 signaling requires proteasomal function and the involvement of CUL4-DDB1 ubiquitin E3 ligase."
    Ghosh P., Wu M., Zhang H., Sun H.
    Cell Cycle 7:373-381(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MLST8.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-53; SER-146 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Characterization of nuclear localization signal in the N terminus of CUL4B and its essential role in cyclin E degradation and cell cycle progression."
    Zou Y., Mi J., Cui J., Lu D., Zhang X., Guo C., Gao G., Liu Q., Chen B., Shao C., Gong Y.
    J. Biol. Chem. 284:33320-33332(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KPNA2; KPNA4; KPNA1 AND KPNB1, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF LYS-55; LYS-56; ARG-57; LYS-58 AND 55-LYS--LYS-58.
  24. "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 THR-49 AND SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  25. "A novel nonsense mutation in CUL4B gene in three brothers with X-linked mental retardation syndrome."
    Badura-Stronka M., Jamsheer A., Materna-Kiryluk A., Sowinska A., Kiryluk K., Budny B., Latos-Bielenska A.
    Clin. Genet. 77:141-144(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, INVOLVEMENT IN MRXS15.
  26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-10 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Solution structure of the winged helix-turn-helix motif of human cul-4b."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 826-913.
  31. "Mutations in CUL4B, which encodes a ubiquitin E3 ligase subunit, cause an X-linked mental retardation syndrome associated with aggressive outbursts, seizures, relative macrocephaly, central obesity, hypogonadism, pes cavus, and tremor."
    Tarpey P.S., Raymond F.L., O'Meara S., Edkins S., Teague J., Butler A., Dicks E., Stevens C., Tofts C., Avis T., Barthorpe S., Buck G., Cole J., Gray K., Halliday K., Harrison R., Hills K., Jenkinson A.
    , Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Varian J., West S., Widaa S., Mallya U., Moon J., Luo Y., Holder S., Smithson S.F., Hurst J.A., Clayton-Smith J., Kerr B., Boyle J., Shaw M., Vandeleur L., Rodriguez J., Slaugh R., Easton D.F., Wooster R., Bobrow M., Srivastava A.K., Stevenson R.E., Schwartz C.E., Turner G., Gecz J., Futreal P.A., Stratton M.R., Partington M.
    Am. J. Hum. Genet. 80:345-352(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MRXS15 ILE-213; CYS-572 AND ALA-745, VARIANT PRO-103.
  32. "A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation."
    Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C., O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M., Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J.
    , Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M., Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P., Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R., Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R., de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M., Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U., Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M., Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T., Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C., Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L., Futreal P.A., Stratton M.R.
    Nat. Genet. 41:535-543(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MRXS15 ILE-213; CYS-572 AND ALA-745.

Entry informationi

Entry nameiCUL4B_HUMAN
AccessioniPrimary (citable) accession number: Q13620
Secondary accession number(s): B1APK5
, B3KVX4, B7Z5K8, Q6PIE4, Q6UP07, Q7Z673, Q9BY37, Q9UEB7, Q9UED7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 140 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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