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Protein

Cullin-7

Gene

CUL7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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: 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 - Biological processi

  • epithelial to mesenchymal transition Source: UniProtKB
  • Golgi organization Source: UniProtKB
  • IRE1-mediated unfolded protein response Source: Reactome
  • microtubule cytoskeleton organization Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • placenta development Source: UniProtKB
  • positive regulation of dendrite morphogenesis Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • proteolysis Source: UniProtKB
  • regulation of mitotic nuclear division Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: InterPro
  • vasculogenesis Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-381038. XBP1(S) activates chaperone genes.
R-HSA-983168. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21024. CUL7.

Subcellular locationi

GO - Cellular componenti

  • 3M complex Source: UniProtKB
  • anaphase-promoting complex Source: UniProtKB
  • centrosome Source: UniProtKB
  • Cul7-RING ubiquitin ligase complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • Golgi apparatus Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • 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)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:273750
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1014 – 10141L → R in 3M1. 1 Publication
Corresponds to variant rs61752334 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121918229 [ dbSNP | Ensembl ].
VAR_026124
Natural varianti1588 – 15881L → P in 3M1. 1 Publication
Corresponds to variant rs759300846 [ dbSNP | Ensembl ].
VAR_071120

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MalaCardsiCUL7.
MIMi273750. phenotype.
Orphaneti2616. 3M syndrome.
PharmGKBiPA134897835.

Polymorphism and mutation databases

BioMutaiCUL7.
DMDMi160370003.

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 – 3391PhosphoserineCombined sources
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

EPDiQ14999.
MaxQBiQ14999.
PaxDbiQ14999.
PeptideAtlasiQ14999.
PRIDEiQ14999.

PTM databases

iPTMnetiQ14999.
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

BgeeiENSG00000044090.
CleanExiHS_CUL7.
GenevisibleiQ14999. HS.

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
TP53P046375EBI-308606,EBI-366083

Protein-protein interaction databases

BioGridi115159. 654 interactions.
DIPiDIP-31618N.
DIP-60187N.
IntActiQ14999. 11 interactions.
STRINGi9606.ENSP00000438788.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JNGNMR-A360-460[»]
ProteinModelPortaliQ14999.
SMRiQ14999. Positions 360-435.
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

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00780000121942.
HOGENOMiHOG000024831.
HOVERGENiHBG103792.
InParanoidiQ14999.
KOiK10613.
OMAiTNILGGC.
OrthoDBiEOG091G0053.
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.
IPR031223. CUL7.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR008979. Galactose-bd-like.
IPR014722. Rib_L2_dom2.
[Graphical view]
PANTHERiPTHR22771:SF3. PTHR22771:SF3. 2 hits.
PfamiPF03256. ANAPC10. 1 hit.
PF11515. Cul7. 1 hit.
PF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM01337. APC10. 1 hit.
SM00884. Cullin_Nedd8. 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. AlignAdd to basket

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

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
Corresponds to variant rs61752334 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121918229 [ dbSNP | Ensembl ].
VAR_026124
Natural varianti1588 – 15881L → P in 3M1. 1 Publication
Corresponds to variant rs759300846 [ dbSNP | Ensembl ].
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:
EMBLi
GenBanki
DDBJi
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.4. human. [Q14999-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JNGNMR-A360-460[»]
ProteinModelPortaliQ14999.
SMRiQ14999. Positions 360-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115159. 654 interactions.
DIPiDIP-31618N.
DIP-60187N.
IntActiQ14999. 11 interactions.
STRINGi9606.ENSP00000438788.

PTM databases

iPTMnetiQ14999.
PhosphoSiteiQ14999.

Polymorphism and mutation databases

BioMutaiCUL7.
DMDMi160370003.

Proteomic databases

EPDiQ14999.
MaxQBiQ14999.
PaxDbiQ14999.
PeptideAtlasiQ14999.
PRIDEiQ14999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265348; ENSP00000265348; ENSG00000044090. [Q14999-1]
ENST00000535468; ENSP00000438788; ENSG00000044090. [Q14999-2]
GeneIDi9820.
KEGGihsa:9820.
UCSCiuc003otq.4. human. [Q14999-1]

Organism-specific databases

CTDi9820.
GeneCardsiCUL7.
GeneReviewsiCUL7.
HGNCiHGNC:21024. CUL7.
HPAiCAB015449.
HPA030095.
HPA030096.
MalaCardsiCUL7.
MIMi273750. phenotype.
609577. gene.
neXtProtiNX_Q14999.
Orphaneti2616. 3M syndrome.
PharmGKBiPA134897835.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00780000121942.
HOGENOMiHOG000024831.
HOVERGENiHBG103792.
InParanoidiQ14999.
KOiK10613.
OMAiTNILGGC.
OrthoDBiEOG091G0053.
PhylomeDBiQ14999.
TreeFamiTF101154.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-381038. XBP1(S) activates chaperone genes.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiCUL7. human.
EvolutionaryTraceiQ14999.
GeneWikiiCUL7.
GenomeRNAii9820.
PROiQ14999.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000044090.
CleanExiHS_CUL7.
GenevisibleiQ14999. HS.

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.
IPR031223. CUL7.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR008979. Galactose-bd-like.
IPR014722. Rib_L2_dom2.
[Graphical view]
PANTHERiPTHR22771:SF3. PTHR22771:SF3. 2 hits.
PfamiPF03256. ANAPC10. 1 hit.
PF11515. Cul7. 1 hit.
PF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM01337. APC10. 1 hit.
SM00884. Cullin_Nedd8. 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]
ProtoNetiSearch...

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: September 7, 2016
This is version 163 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

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.