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Q14999 (CUL7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cullin-7

Short name=CUL-7
Gene names
Name:CUL7
Synonyms:KIAA0076
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1698 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of a probable SCF-like E3 ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably plays a role in the degradation of proteins involved in endothelial proliferation and/or differentiation By similarity. Seems not to promote polyubiquitination and proteasomal degradation of TP53. In vitro, complexes of CUL7 with either CUL9 or FBXW8 or TP53 contain E3 ubiquitin-protein ligase activity. In complex with FBXW8, mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Ref.8 Ref.9 Ref.14

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Part of a SCF-like complex consisting of CUL7, RBX1, SKP1, FBXW8 and GLMN isoform 1. Interacts with a complex of SKP1 and FBXW8, but not with SKP1 alone. Interacts with CUL9. Interacts with FBXW8; interaction is mutually exclusive of binding to CUL9 or TP53. Interacts with TP53; the interaction preferentially involves tetrameric and dimeric TP53. The CUL7-CUL9 heterodimer seems to interact specifically with TP53. Interacts with CUL1; the interactions seems to be mediated by FBXW8 By similarity. Interacts with SV40 Large T antigen; this interaction seems to inhibit CUL7. Component of a SCF-like complex composed of SV40 Large T antigen, CUL7, SKP1, RBX1, and FBXW8. Interacts with OBSL1. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.14 Ref.15

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Golgi apparatus. Note: Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. Ref.8 Ref.14

Tissue specificity

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. Ref.16

Post-translational modification

According to a report, may not be neddylated despite the conserved consensus site for neddylation at Lys-1576 (Ref.9).

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Belongs to the cullin family.

Contains 1 DOC domain.

Sequence caution

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

Ontologies

Keywords
   Biological processHost-virus interaction
Ubl conjugation pathway
   Cellular componentCytoplasm
Golgi apparatus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dwarfism
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from sequence or structural similarity. Source: UniProtKB

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

positive regulation of dendrite morphogenesis

Inferred from genetic interaction Ref.14. Source: UniProtKB

protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

proteolysis

Non-traceable author statement Ref.5. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

vasculogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCul7-RING ubiquitin ligase complex

Inferred from direct assay Ref.14. Source: UniProtKB

Golgi apparatus

Inferred from direct assay Ref.14. Source: UniProtKB

anaphase-promoting complex

Non-traceable author statement Ref.5. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TP53P046374EBI-308606,EBI-366083

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14999-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14999-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16981698Cullin-7
PRO_0000119802

Regions

Domain814 – 993180DOC
Region360 – 460101Interaction with TP53

Amino acid modifications

Modified residue3391Phosphoserine Ref.10
Cross-link1576Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) Potential

Natural variations

Alternative sequence11M → MSRGFWLAEPLAGTGPHPAP VAADSRGCSSVPRRHAPSRL SVSTPSRGPGARM in isoform 2.
VSP_046105
Alternative sequence1941G → GEGQCGEEGKAGEGLGRLRD SQDTVAGASDLIR in isoform 2.
VSP_046106
Natural variant6161S → G.
Corresponds to variant rs7774330 [ dbSNP | Ensembl ].
VAR_048841
Natural variant8131Q → R. Ref.1 Ref.2 Ref.4
Corresponds to variant rs9381231 [ dbSNP | Ensembl ].
VAR_026121
Natural variant8521R → Q.
Corresponds to variant rs34574340 [ dbSNP | Ensembl ].
VAR_048842
Natural variant10141L → R in 3M1. Ref.16
VAR_026122
Natural variant12461Q → G in 3M1; requires 2 nucleotide substitutions. Ref.16
VAR_026123
Natural variant12461Q → H.
Corresponds to variant rs36071170 [ dbSNP | Ensembl ].
VAR_048843
Natural variant14641H → P in 3M1; impairs the ability to interact with RBX1, thus hampers the assembly of polyubiquitin chains. Ref.16
VAR_026124

Secondary structure

............... 1698
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: EC9EED17E98FC9A1

FASTA1,698191,161
        10         20         30         40         50         60 
MVGELRYREF RVPLGPGLHA YPDELIRQRV GHDGHPEYQI RWLILRRGDE GDGGSGQVDC 

        70         80         90        100        110        120 
KAEHILLWMS KDEIYANCHK MLGEDGQVIG PSQESAGEVG ALDKSVLEEM ETDVKSLIQR 

       130        140        150        160        170        180 
ALRQLEECVG TIPPAPLLHT VHVLSAYASI EPLTGVFKDP RVLDLLMHML SSPDYQIRWS 

       190        200        210        220        230        240 
AGRMIQALSS HDAGTRTQIL LSLSQQEAIE KHLDFDSRCA LLALFAQATL SEHPMSFEGI 

       250        260        270        280        290        300 
QLPQVPGRVL FSLVKRYLHV TSLLDQLNDS AAEPGAQNTS APEELSGERG QLELEFSMAM 

       310        320        330        340        350        360 
GTLISELVQA MRWDQASDRP RSSARSPGSI FQPQLADVSP GLPAAQAQPS FRRSRRFRPR 

       370        380        390        400        410        420 
SEFASGNTYA LYVRDTLQPG MRVRMLDDYE EISAGDEGEF RQSNNGVPPV QVFWESTGRT 

       430        440        450        460        470        480 
YWVHWHMLEI LGFEEDIEDM VEADEYQGAV ASRVLGRALP AWRWRPMTEL YAVPYVLPED 

       490        500        510        520        530        540 
EDTEECEHLT LAEWWELLFF IKKLDGPDHQ EVLQILQENL DGEILDDEIL AELAVPIELA 

       550        560        570        580        590        600 
QDLLLTLPQR LNDSALRDLI NCHVYKKYGP EALAGNQAYP SLLEAQEDVL LLDAQAQAKD 

       610        620        630        640        650        660 
SEDAAKVEAK EPPSQSPNTP LQRLVEGYGP AGKILLDLEQ ALSSEGTQEN KVKPLLLQLQ 

       670        680        690        700        710        720 
RQPQPFLALM QSLDTPETNR TLHLTVLRIL KQLVDFPEAL LLPWHEAVDA CMACLRSPNT 

       730        740        750        760        770        780 
DREVLQELIF FLHRLTSVSR DYAVVLNQLG ARDAISKALE KHLGKLELAQ ELRDMVFKCE 

       790        800        810        820        830        840 
KHAHLYRKLI TNILGGCIQM VLGQIEDHRR THQPINIPFF DVFLRYLCQG SSVEVKEDKC 

       850        860        870        880        890        900 
WEKVEVSSNP HRASKLTDHN PKTYWESNGS AGSHYITLHM RRGILIRQLT LLVASEDSSY 

       910        920        930        940        950        960 
MPARVVVCGG DSTSSLHTEL NSVNVMPSAS RVILLENLTR FWPIIQIRIK RCQQGGIDTR 

       970        980        990       1000       1010       1020 
IRGLEILGPK PTFWPVFREQ LCRHTRLFYM VRAQAWSQDM AEDRRSLLHL SSRLNGALRQ 

      1030       1040       1050       1060       1070       1080 
EQNFADRFLP DDEAAQALGK TCWEALVSPV VQNITSPDED GISPLGWLLD QYLECQEAVF 

      1090       1100       1110       1120       1130       1140 
NPQSRGPAFF SRVRRLTHLL VHVEPCEAPP PVVATPRPKG RNRSHDWSSL ATRGLPSSIM 

      1150       1160       1170       1180       1190       1200 
RNLTRCWRAV VEKQVNNFLT SSWRDDDFVP RYCEHFNILQ NSSSELFGPR AAFLLALQNG 

      1210       1220       1230       1240       1250       1260 
CAGALLKLPF LKAAHVSEQF ARHIDQQIQG SRIGGAQEME RLAQLQQCLQ AVLIFSGLEI 

      1270       1280       1290       1300       1310       1320 
ATTFEHYYQH YMADRLLGVV SSWLEGAVLE QIGPCFPNRL PQQMLQSLST SKELQRQFHV 

      1330       1340       1350       1360       1370       1380 
YQLQQLDQEL LKLEDTEKKI QVGLGASGKE HKSEKEEEAG AAAVVDVAEG EEEEEENEDL 

      1390       1400       1410       1420       1430       1440 
YYEGAMPEVS VLVLSRHSWP VASICHTLNP RTCLPSYLRG TLNRYSNFYN KSQSHPALER 

      1450       1460       1470       1480       1490       1500 
GSQRRLQWTW LGWAELQFGN QTLHVSTVQM WLLLYLNDLK AVSVESLLAF SGLSADMLNQ 

      1510       1520       1530       1540       1550       1560 
AIGPLTSSRG PLDLHEQKDI PGGVLKIRDG SKEPRSRWDI VRLIPPQTYL QAEGEDGQNL 

      1570       1580       1590       1600       1610       1620 
EKRRNLLNCL IVRILKAHGD EGLHIDQLVC LVLEAWQKGP CPPRGLVSSL GKGSACSSTD 

      1630       1640       1650       1660       1670       1680 
VLSCILHLLG KGTLRRHDDR PQVLSYAVPV TVMEPHTESL NPGSSGPNPP LTFHTLQIRS 

      1690 
RGVPYASCTA TQSFSTFR 

« Hide

Isoform 2 [UniParc].

Checksum: 3CFC980A4E8C4EB2
Show »

FASTA1,782199,750

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
[9]"PARC and CUL7 form atypical cullin RING ligase complexes."
Skaar J.R., Florens L., Tsutsumi T., Arai T., Tron A., Swanson S.K., Washburn M.P., DeCaprio J.A.
Cancer Res. 67:2006-2014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CUL9; SKP1; FBXW8; RBX1 AND TP53, LACK OF NEDDYLATION.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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.
[12]"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.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
[15]"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.
[16]"Identification of mutations in CUL7 in 3-M syndrome."
Huber C., Dias-Santagata D., Glaser A., O'Sullivan J., Brauner R., Wu K., Xu X., Pearce K., Wang R., Giovannucci Uzielli M.L., Dagoneau N., Chemaitilly W., Superti-Furga A., Dos Santos H., Megarbane A., Morin G., Gillessen-Kaesbach G., Hennekam R.C.M. expand/collapse author list , Van der Burgt I., Black G.C.M., Clayton P.E., Read A., Le Merrer M., Scambler P.J., Munnich A., Pan Z.-Q., Winter R., Cormier-Daire V.
Nat. Genet. 37:1119-1124(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS 3M1 ARG-1014; GLY-1246 AND PRO-1464, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001161842.1. NM_001168370.1.
NP_055595.2. NM_014780.4.
UniGeneHs.520136.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JNGNMR-A360-460[»]
ProteinModelPortalQ14999.
SMRQ14999. Positions 360-435, 829-969, 1212-1648.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115159. 25 interactions.
DIPDIP-31618N.
DIP-60187N.
IntActQ14999. 10 interactions.
STRING9606.ENSP00000265348.

PTM databases

PhosphoSiteQ14999.

Polymorphism databases

DMDM160370003.

Proteomic databases

PaxDbQ14999.
PRIDEQ14999.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265348; ENSP00000265348; ENSG00000044090. [Q14999-1]
ENST00000535468; ENSP00000438788; ENSG00000044090. [Q14999-2]
GeneID9820.
KEGGhsa:9820.
UCSCuc003otq.3. human. [Q14999-1]

Organism-specific databases

CTD9820.
GeneCardsGC06M043006.
HGNCHGNC:21024. CUL7.
HPACAB015449.
HPA030095.
HPA030096.
MIM273750. phenotype.
609577. gene.
neXtProtNX_Q14999.
Orphanet2616. 3M syndrome.
PharmGKBPA134897835.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG48148.
HOGENOMHOG000024831.
HOVERGENHBG103792.
InParanoidQ14999.
KOK10613.
OMAQIRSRGV.
OrthoDBEOG70S74H.
PhylomeDBQ14999.
TreeFamTF101154.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

BgeeQ14999.
CleanExHS_CUL7.
GenevestigatorQ14999.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
2.60.120.260. 1 hit.
InterProIPR004939. 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]
PfamPF03256. APC10. 1 hit.
PF11515. Cul7. 1 hit.
PF00888. Cullin. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
SSF49785. SSF49785. 1 hit.
SSF75632. SSF75632. 2 hits.
PROSITEPS50069. CULLIN_2. 1 hit.
PS51284. DOC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14999.
GeneWikiCUL7.
GenomeRNAi9820.
NextBio36986.
PROQ14999.
SOURCESearch...

Entry information

Entry nameCUL7_HUMAN
AccessionPrimary (citable) accession number: Q14999
Secondary accession number(s): B4DYZ0, F5H0L1, Q5T654
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM