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Q14999

- CUL7_HUMAN

UniProt

Q14999 - CUL7_HUMAN

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Protein

Cullin-7

Gene

CUL7

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

Functioni

Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695). Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5 (PubMed:24793696). Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1 (PubMed:21572988, PubMed:24362026). Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradatation, thereby affecting cell proliferation and differentiation (PubMed:24362026). Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development (PubMed:20139075). Does not promote polyubiquitination and proteasomal degradation of p53/TP53 (PubMed:16547496, PubMed:17332328). While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions.8 Publications

Pathwayi

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. endoplasmic reticulum unfolded protein response Source: Reactome
  4. epithelial to mesenchymal transition Source: UniProtKB
  5. Golgi organization Source: UniProtKB
  6. microtubule cytoskeleton organization Source: UniProtKB
  7. mitotic cytokinesis Source: UniProtKB
  8. placenta development Source: UniProtKB
  9. positive regulation of dendrite morphogenesis Source: UniProtKB
  10. protein ubiquitination Source: UniProtKB
  11. proteolysis Source: UniProtKB
  12. regulation of mitosis Source: UniProtKB
  13. ubiquitin-dependent protein catabolic process Source: InterPro
  14. vasculogenesis Source: UniProtKB
  15. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-7
Short name:
CUL-7
Gene namesi
Name:CUL7
Synonyms:KIAA0076
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:21024. CUL7.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmperinuclear region. Golgi apparatus
Note: Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus (PubMed:24793695). CCDC8 is required for centrosomal location (PubMed:24793695).1 Publication

GO - Cellular componenti

  1. 3M complex Source: UniProtKB
  2. anaphase-promoting complex Source: UniProtKB
  3. centrosome Source: UniProtKB
  4. Cul7-RING ubiquitin ligase complex Source: UniProtKB
  5. cytoplasm Source: UniProtKB
  6. cytosol Source: Reactome
  7. Golgi apparatus Source: UniProtKB
  8. nucleus Source: HPA
  9. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

Pathology & Biotechi

Involvement in diseasei

3M syndrome 1 (3M1) [MIM:273750]: An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1014 – 10141L → R in 3M1. 1 Publication
VAR_026122
Natural varianti1246 – 12461Q → G in 3M1; requires 2 nucleotide substitutions. 1 Publication
VAR_026123
Natural varianti1464 – 14641H → P in 3M1; impairs the ability to interact with RBX1, thus hampers the assembly of polyubiquitin chains. 1 Publication
VAR_026124
Natural varianti1588 – 15881L → P in 3M1. 1 Publication
VAR_071120

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi273750. phenotype.
Orphaneti2616. 3M syndrome.
PharmGKBiPA134897835.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16981698Cullin-7PRO_0000119802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei339 – 3391Phosphoserine1 Publication
Cross-linki1576 – 1576Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)Sequence Analysis

Post-translational modificationi

According to a report, may not be neddylated despite the conserved consensus site for neddylation at Lys-1576.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14999.
PaxDbiQ14999.
PRIDEiQ14999.

PTM databases

PhosphoSiteiQ14999.

Expressioni

Tissue specificityi

Highly expressed in fetal kidney and adult skeletal muscle. Also abundant in fetal brain, as well as in adult pancreas, kidney, placenta and heart. Detected in trophoblasts, lymphoblasts, osteoblasts, chondrocytes and skin fibroblasts.1 Publication

Developmental stagei

Highly expressed in invasive placental villi during first trimester.1 Publication

Gene expression databases

BgeeiQ14999.
CleanExiHS_CUL7.
GenevestigatoriQ14999.

Organism-specific databases

HPAiCAB015449.
HPA030095.
HPA030096.

Interactioni

Subunit structurei

Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1. Part of a Cul7-RING complex consisting of CUL7, RBX1, SKP1 and FBXW8. Interacts with a complex of SKP1 and FBXW8, but not with SKP1 alone. Interacts with CUL9; leading to inhibit CUL9 activity. Interacts with FBXW8; interaction is mutually exclusive of binding to CUL9 or p53/TP53. Interacts with p53/TP53; the interaction preferentially involves tetrameric and dimeric p53/TP53. The CUL7-CUL9 heterodimer seems to interact specifically with p53/TP53. Interacts with CUL1; the interactions seems to be mediated by FBXW8. Interacts with SV40 Large T antigen; this interaction seems to inhibit CUL7. Interacts with OBSL1.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TP53P046374EBI-308606,EBI-366083

Protein-protein interaction databases

BioGridi115159. 30 interactions.
DIPiDIP-31618N.
DIP-60187N.
IntActiQ14999. 10 interactions.
STRINGi9606.ENSP00000265348.

Structurei

Secondary structure

1
1698
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi360 – 3623
Beta strandi363 – 3664
Helixi367 – 37610
Beta strandi382 – 3854
Beta strandi397 – 4037
Beta strandi407 – 4148
Turni415 – 4184
Beta strandi419 – 4246
Helixi425 – 4273
Beta strandi428 – 4303

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JNGNMR-A360-460[»]
ProteinModelPortaliQ14999.
SMRiQ14999. Positions 360-435, 1214-1648.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14999.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini814 – 993180DOCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni360 – 460101Interaction with TP53Add
BLAST

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation
Contains 1 DOC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG48148.
GeneTreeiENSGT00700000104406.
HOGENOMiHOG000024831.
HOVERGENiHBG103792.
InParanoidiQ14999.
KOiK10613.
OMAiTFEHYYQ.
OrthoDBiEOG70S74H.
PhylomeDBiQ14999.
TreeFamiTF101154.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR004939. APC_su10/DOC_dom.
IPR016024. ARM-type_fold.
IPR021097. CPH_domain.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR008979. Galactose-bd-like.
IPR014722. Rib_L2_dom2.
[Graphical view]
PfamiPF03256. APC10. 1 hit.
PF11515. Cul7. 1 hit.
PF00888. Cullin. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF49785. SSF49785. 1 hit.
SSF75632. SSF75632. 2 hits.
PROSITEiPS50069. CULLIN_2. 1 hit.
PS51284. DOC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14999-1) [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
MVGELRYREF RVPLGPGLHA YPDELIRQRV GHDGHPEYQI RWLILRRGDE
60 70 80 90 100
GDGGSGQVDC KAEHILLWMS KDEIYANCHK MLGEDGQVIG PSQESAGEVG
110 120 130 140 150
ALDKSVLEEM ETDVKSLIQR ALRQLEECVG TIPPAPLLHT VHVLSAYASI
160 170 180 190 200
EPLTGVFKDP RVLDLLMHML SSPDYQIRWS AGRMIQALSS HDAGTRTQIL
210 220 230 240 250
LSLSQQEAIE KHLDFDSRCA LLALFAQATL SEHPMSFEGI QLPQVPGRVL
260 270 280 290 300
FSLVKRYLHV TSLLDQLNDS AAEPGAQNTS APEELSGERG QLELEFSMAM
310 320 330 340 350
GTLISELVQA MRWDQASDRP RSSARSPGSI FQPQLADVSP GLPAAQAQPS
360 370 380 390 400
FRRSRRFRPR SEFASGNTYA LYVRDTLQPG MRVRMLDDYE EISAGDEGEF
410 420 430 440 450
RQSNNGVPPV QVFWESTGRT YWVHWHMLEI LGFEEDIEDM VEADEYQGAV
460 470 480 490 500
ASRVLGRALP AWRWRPMTEL YAVPYVLPED EDTEECEHLT LAEWWELLFF
510 520 530 540 550
IKKLDGPDHQ EVLQILQENL DGEILDDEIL AELAVPIELA QDLLLTLPQR
560 570 580 590 600
LNDSALRDLI NCHVYKKYGP EALAGNQAYP SLLEAQEDVL LLDAQAQAKD
610 620 630 640 650
SEDAAKVEAK EPPSQSPNTP LQRLVEGYGP AGKILLDLEQ ALSSEGTQEN
660 670 680 690 700
KVKPLLLQLQ RQPQPFLALM QSLDTPETNR TLHLTVLRIL KQLVDFPEAL
710 720 730 740 750
LLPWHEAVDA CMACLRSPNT DREVLQELIF FLHRLTSVSR DYAVVLNQLG
760 770 780 790 800
ARDAISKALE KHLGKLELAQ ELRDMVFKCE KHAHLYRKLI TNILGGCIQM
810 820 830 840 850
VLGQIEDHRR THQPINIPFF DVFLRYLCQG SSVEVKEDKC WEKVEVSSNP
860 870 880 890 900
HRASKLTDHN PKTYWESNGS AGSHYITLHM RRGILIRQLT LLVASEDSSY
910 920 930 940 950
MPARVVVCGG DSTSSLHTEL NSVNVMPSAS RVILLENLTR FWPIIQIRIK
960 970 980 990 1000
RCQQGGIDTR IRGLEILGPK PTFWPVFREQ LCRHTRLFYM VRAQAWSQDM
1010 1020 1030 1040 1050
AEDRRSLLHL SSRLNGALRQ EQNFADRFLP DDEAAQALGK TCWEALVSPV
1060 1070 1080 1090 1100
VQNITSPDED GISPLGWLLD QYLECQEAVF NPQSRGPAFF SRVRRLTHLL
1110 1120 1130 1140 1150
VHVEPCEAPP PVVATPRPKG RNRSHDWSSL ATRGLPSSIM RNLTRCWRAV
1160 1170 1180 1190 1200
VEKQVNNFLT SSWRDDDFVP RYCEHFNILQ NSSSELFGPR AAFLLALQNG
1210 1220 1230 1240 1250
CAGALLKLPF LKAAHVSEQF ARHIDQQIQG SRIGGAQEME RLAQLQQCLQ
1260 1270 1280 1290 1300
AVLIFSGLEI ATTFEHYYQH YMADRLLGVV SSWLEGAVLE QIGPCFPNRL
1310 1320 1330 1340 1350
PQQMLQSLST SKELQRQFHV YQLQQLDQEL LKLEDTEKKI QVGLGASGKE
1360 1370 1380 1390 1400
HKSEKEEEAG AAAVVDVAEG EEEEEENEDL YYEGAMPEVS VLVLSRHSWP
1410 1420 1430 1440 1450
VASICHTLNP RTCLPSYLRG TLNRYSNFYN KSQSHPALER GSQRRLQWTW
1460 1470 1480 1490 1500
LGWAELQFGN QTLHVSTVQM WLLLYLNDLK AVSVESLLAF SGLSADMLNQ
1510 1520 1530 1540 1550
AIGPLTSSRG PLDLHEQKDI PGGVLKIRDG SKEPRSRWDI VRLIPPQTYL
1560 1570 1580 1590 1600
QAEGEDGQNL EKRRNLLNCL IVRILKAHGD EGLHIDQLVC LVLEAWQKGP
1610 1620 1630 1640 1650
CPPRGLVSSL GKGSACSSTD VLSCILHLLG KGTLRRHDDR PQVLSYAVPV
1660 1670 1680 1690
TVMEPHTESL NPGSSGPNPP LTFHTLQIRS RGVPYASCTA TQSFSTFR
Length:1,698
Mass (Da):191,161
Last modified:October 23, 2007 - v2
Checksum:iEC9EED17E98FC9A1
GO
Isoform 2 (identifier: Q14999-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSRGFWLAEPLAGTGPHPAPVAADSRGCSSVPRRHAPSRLSVSTPSRGPGARM
     194-194: G → GEGQCGEEGKAGEGLGRLRDSQDTVAGASDLIR

Note: No experimental confirmation available.

Show »
Length:1,782
Mass (Da):199,750
Checksum:i3CFC980A4E8C4EB2
GO

Sequence cautioni

The sequence BAA07551.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti616 – 6161S → G.
Corresponds to variant rs7774330 [ dbSNP | Ensembl ].
VAR_048841
Natural varianti813 – 8131Q → R.3 Publications
Corresponds to variant rs9381231 [ dbSNP | Ensembl ].
VAR_026121
Natural varianti852 – 8521R → Q.
Corresponds to variant rs34574340 [ dbSNP | Ensembl ].
VAR_048842
Natural varianti1014 – 10141L → R in 3M1. 1 Publication
VAR_026122
Natural varianti1246 – 12461Q → G in 3M1; requires 2 nucleotide substitutions. 1 Publication
VAR_026123
Natural varianti1246 – 12461Q → H.
Corresponds to variant rs36071170 [ dbSNP | Ensembl ].
VAR_048843
Natural varianti1464 – 14641H → P in 3M1; impairs the ability to interact with RBX1, thus hampers the assembly of polyubiquitin chains. 1 Publication
VAR_026124
Natural varianti1588 – 15881L → P in 3M1. 1 Publication
VAR_071120

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MSRGFWLAEPLAGTGPHPAP VAADSRGCSSVPRRHAPSRL SVSTPSRGPGARM in isoform 2. 1 PublicationVSP_046105
Alternative sequencei194 – 1941G → GEGQCGEEGKAGEGLGRLRD SQDTVAGASDLIR in isoform 2. 1 PublicationVSP_046106

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38548 mRNA. Translation: BAA07551.2. Different initiation.
AK302668 mRNA. Translation: BAG63902.1.
AL355385, AL136304 Genomic DNA. Translation: CAI13779.1.
AL136304, AL355385 Genomic DNA. Translation: CAI19793.1.
BC033647 mRNA. Translation: AAH33647.1.
CCDSiCCDS4881.1. [Q14999-1]
CCDS55003.1. [Q14999-2]
RefSeqiNP_001161842.1. NM_001168370.1. [Q14999-2]
NP_055595.2. NM_014780.4. [Q14999-1]
UniGeneiHs.520136.

Genome annotation databases

EnsembliENST00000265348; ENSP00000265348; ENSG00000044090. [Q14999-1]
ENST00000535468; ENSP00000438788; ENSG00000044090. [Q14999-2]
GeneIDi9820.
KEGGihsa:9820.
UCSCiuc003otq.3. human. [Q14999-1]

Polymorphism databases

DMDMi160370003.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38548 mRNA. Translation: BAA07551.2 . Different initiation.
AK302668 mRNA. Translation: BAG63902.1 .
AL355385 , AL136304 Genomic DNA. Translation: CAI13779.1 .
AL136304 , AL355385 Genomic DNA. Translation: CAI19793.1 .
BC033647 mRNA. Translation: AAH33647.1 .
CCDSi CCDS4881.1. [Q14999-1 ]
CCDS55003.1. [Q14999-2 ]
RefSeqi NP_001161842.1. NM_001168370.1. [Q14999-2 ]
NP_055595.2. NM_014780.4. [Q14999-1 ]
UniGenei Hs.520136.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JNG NMR - A 360-460 [» ]
ProteinModelPortali Q14999.
SMRi Q14999. Positions 360-435, 1214-1648.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115159. 30 interactions.
DIPi DIP-31618N.
DIP-60187N.
IntActi Q14999. 10 interactions.
STRINGi 9606.ENSP00000265348.

PTM databases

PhosphoSitei Q14999.

Polymorphism databases

DMDMi 160370003.

Proteomic databases

MaxQBi Q14999.
PaxDbi Q14999.
PRIDEi Q14999.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265348 ; ENSP00000265348 ; ENSG00000044090 . [Q14999-1 ]
ENST00000535468 ; ENSP00000438788 ; ENSG00000044090 . [Q14999-2 ]
GeneIDi 9820.
KEGGi hsa:9820.
UCSCi uc003otq.3. human. [Q14999-1 ]

Organism-specific databases

CTDi 9820.
GeneCardsi GC06M043006.
GeneReviewsi CUL7.
HGNCi HGNC:21024. CUL7.
HPAi CAB015449.
HPA030095.
HPA030096.
MIMi 273750. phenotype.
609577. gene.
neXtProti NX_Q14999.
Orphaneti 2616. 3M syndrome.
PharmGKBi PA134897835.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG48148.
GeneTreei ENSGT00700000104406.
HOGENOMi HOG000024831.
HOVERGENi HBG103792.
InParanoidi Q14999.
KOi K10613.
OMAi TFEHYYQ.
OrthoDBi EOG70S74H.
PhylomeDBi Q14999.
TreeFami TF101154.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_18273. XBP1(S) activates chaperone genes.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTracei Q14999.
GeneWikii CUL7.
GenomeRNAii 9820.
NextBioi 36986.
PROi Q14999.
SOURCEi Search...

Gene expression databases

Bgeei Q14999.
CleanExi HS_CUL7.
Genevestigatori Q14999.

Family and domain databases

Gene3Di 2.30.30.30. 1 hit.
2.60.120.260. 1 hit.
InterProi IPR004939. APC_su10/DOC_dom.
IPR016024. ARM-type_fold.
IPR021097. CPH_domain.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR008979. Galactose-bd-like.
IPR014722. Rib_L2_dom2.
[Graphical view ]
Pfami PF03256. APC10. 1 hit.
PF11515. Cul7. 1 hit.
PF00888. Cullin. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
SSF49785. SSF49785. 1 hit.
SSF75632. SSF75632. 2 hits.
PROSITEi PS50069. CULLIN_2. 1 hit.
PS51284. DOC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-813.
    Tissue: Bone marrow.
  2. "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] (ISOFORM 2), VARIANT ARG-813.
    Tissue: Testis.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [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] (ISOFORM 1), VARIANT ARG-813.
    Tissue: Eye.
  5. "CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex."
    Dias D.C., Dolios G., Wang R., Pan Z.Q.
    Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH SKP1; FBXW8 AND RBX1.
  6. "Targeted disruption of p185/Cul7 gene results in abnormal vascular morphogenesis."
    Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C., DeCaprio J.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBX1, IDENTIFICATION IN A COMPLEX WITH SKP1; FBXW8; RBX1 AND GLMN.
  7. "Simian virus 40 large T antigen's association with the CUL7 SCF complex contributes to cellular transformation."
    Kasper J.S., Kuwabara H., Arai T., Ali S.H., DeCaprio J.A.
    J. Virol. 79:11685-11692(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SV40 LARGE ANTIGEN, IDENTIFICATION IN A SFC(CUL7)-LIKE COMPLEX.
  8. "Dimerization of CUL7 and PARC is not required for all CUL7 functions and mouse development."
    Skaar J.R., Arai T., DeCaprio J.A.
    Mol. Cell. Biol. 25:5579-5589(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CUL9.
  9. "Cytoplasmic localized ubiquitin ligase cullin 7 binds to p53 and promotes cell growth by antagonizing p53 function."
    Andrews P., He Y.J., Xiong Y.
    Oncogene 25:4534-4548(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RBX1 AND TP53, SUBCELLULAR LOCATION.
  10. Cited for: FUNCTION, INTERACTION WITH CUL9; SKP1; FBXW8; RBX1 AND TP53, LACK OF NEDDYLATION.
  11. "Clinical, molecular and histopathological features of short stature syndrome with novel CUL7 mutation in Yakuts: new population isolate in Asia."
    Maksimova N., Hara K., Miyashia A., Nikolaeva I., Shiga A., Nogovicina A., Sukhomyasova A., Argunov V., Shvedova A., Ikeuchi T., Nishizawa M., Kuwano R., Onodera O.
    J. Med. Genet. 44:772-778(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN 3M1.
  12. "The CUL7 E3 ubiquitin ligase targets insulin receptor substrate 1 for ubiquitin-dependent degradation."
    Xu X., Sarikas A., Dias-Santagata D.C., Dolios G., Lafontant P.J., Tsai S.C., Zhu W., Nakajima H., Nakajima H.O., Field L.J., Wang R., Pan Z.Q.
    Mol. Cell 30:403-414(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Exome sequencing identifies CCDC8 mutations in 3-M syndrome, Suggesting that CCDC8 Contributes in a Pathway with CUL7 and OBSL1 to Control Human Growth."
    Hanson D., Murray P.G., O'Sullivan J., Urquhart J., Daly S., Bhaskar S.S., Biesecker L.G., Skae M., Smith C., Cole T., Kirk J., Chandler K., Kingston H., Donnai D., Clayton P.E., Black G.C.
    Am. J. Hum. Genet. 89:148-153(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OBSL1.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi morphology and dendrite patterning."
    Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E., Gygi S.P., Harper J.W., Bonni A.
    PLoS Biol. 9:E1001060-E1001060(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FBXW8 AND OBSL1, SUBCELLULAR LOCATION.
  18. "Ubiquitin ligase cullin 7 induces epithelial-mesenchymal transition in human choriocarcinoma cells."
    Fu J., Lv X., Lin H., Wu L., Wang R., Zhou Z., Zhang B., Wang Y.L., Tsang B.K., Zhu C., Wang H.
    J. Biol. Chem. 285:10870-10879(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  19. "The CUL7/F-box and WD repeat domain containing 8 (CUL7/Fbxw8) ubiquitin ligase promotes degradation of hematopoietic progenitor kinase 1."
    Wang H., Chen Y., Lin P., Li L., Zhou G., Liu G., Logsdon C., Jin J., Abbruzzese J.L., Tan T.H., Wang H.
    J. Biol. Chem. 289:4009-4017(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FBXW8.
  20. Cited for: FUNCTION, IDENTIFICATION IN THE 3M COMPLEX, SUBCELLULAR LOCATION.
  21. "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin to maintain genome integrity."
    Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W., Xiong Y.
    Mol. Cell 54:805-819(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL9.
  22. "The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53."
    Kaustov L., Lukin J., Lemak A., Duan S., Ho M., Doherty R., Penn L.Z., Arrowsmith C.H.
    J. Biol. Chem. 282:11300-11307(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 360-460, INTERACTION WITH TP53.
  23. Cited for: VARIANTS 3M1 ARG-1014; GLY-1246 AND PRO-1464, TISSUE SPECIFICITY.
  24. Cited for: VARIANT 3M1 PRO-1588.

Entry informationi

Entry nameiCUL7_HUMAN
AccessioniPrimary (citable) accession number: Q14999
Secondary accession number(s): B4DYZ0, F5H0L1, Q5T654
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 23, 2007
Last modified: October 29, 2014
This is version 143 of the entry and version 2 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 6
    Human chromosome 6: 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

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