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Q8IWT3

- CUL9_HUMAN

UniProt

Q8IWT3 - CUL9_HUMAN

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Protein

Cullin-9

Gene

CUL9

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

Functioni

Core component of a Cul9-RING ubiquitin-protein ligase complex, a complex that mediates ubiquitination and subsequent degradation of BIRC5 and is required to maintain microtubule dynamics and genome integrity. Acts downstream of the 3M complex, which inhibits CUL9 activity, leading to prevent ubiquitination of BIRC5 (PubMed:24793696). Cytoplasmic anchor protein in p53/TP53-associated protein complex. Regulates the subcellular localization of p53/TP53 and subsequent function (PubMed:12526791, PubMed:17332328).3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1363 – 13708ATPSequence Analysis
Zinc fingeri2070 – 212051RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri2140 – 220364IBR-typeAdd
BLAST
Zinc fingeri2236 – 226530RING-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. microtubule cytoskeleton organization Source: UniProtKB
  2. protein ubiquitination Source: UniProtKB
  3. regulation of mitosis Source: UniProtKB
  4. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-9
Short name:
CUL-9
Alternative name(s):
UbcH7-associated protein 1
p53-associated parkin-like cytoplasmic protein
Gene namesi
Name:CUL9
Synonyms:H7AP1, KIAA0708, PARC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:15982. CUL9.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cullin-RING ubiquitin ligase complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164718328.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25172517Cullin-9PRO_0000119815Add
BLAST

Post-translational modificationi

In vitro, self-ubiquitination in the presence of E1, E2 and ubiquitin.
Neddylated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ8IWT3.
PaxDbiQ8IWT3.
PRIDEiQ8IWT3.

PTM databases

PhosphoSiteiQ8IWT3.

Expressioni

Tissue specificityi

Ubiquitously expressed in all tissues with highest expression in testis brain and kidney.1 Publication

Gene expression databases

BgeeiQ8IWT3.
ExpressionAtlasiQ8IWT3. baseline and differential.
GenevestigatoriQ8IWT3.

Organism-specific databases

HPAiHPA016434.

Interactioni

Subunit structurei

Part of a Cul9-RING complex at least composed of CUL9 and RBX1. Interacts with CUL7: interaction with CUL7 component of the 3M complex leads to inhibition of CUL9 activity. The CUL7-CUL9 heterodimer seems to interact specifically with TP53. Forms a complex with p53/TP53 in the cytoplasm of unstressed cells. Interacts with UBCH7 and UBCH8.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TP53P046373EBI-311123,EBI-366083

Protein-protein interaction databases

BioGridi116736. 9 interactions.
IntActiQ8IWT3. 8 interactions.
MINTiMINT-6615845.
STRINGi9606.ENSP00000252050.

Structurei

Secondary structure

1
2517
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi376 – 3827
Beta strandi388 – 3936
Beta strandi403 – 4086
Beta strandi411 – 4133
Beta strandi416 – 4205
Turni421 – 4244
Beta strandi425 – 4295
Helixi431 – 4333

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JUFNMR-A366-466[»]
ProteinModelPortaliQ8IWT3.
SMRiQ8IWT3. Positions 375-438, 1866-1953, 1997-2417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IWT3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1143 – 1322180DOCPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1649 – 169143Sequence AnalysisAdd
BLAST
Coiled coili2365 – 238521Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1661 – 168929Glu-richAdd
BLAST

Domaini

The IBR domain is required for interaction with UBCH7 and UBCH8.

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation
Contains 1 DOC domain.PROSITE-ProRule annotation
Contains 1 IBR-type zinc finger.Curated
Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2070 – 212051RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri2140 – 220364IBR-typeAdd
BLAST
Zinc fingeri2236 – 226530RING-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG48148.
GeneTreeiENSGT00700000104406.
InParanoidiQ8IWT3.
KOiK11970.
OMAiTKHEWRP.
OrthoDBiEOG70S74H.
PhylomeDBiQ8IWT3.
TreeFamiTF101154.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.10.10. 4 hits.
2.30.30.30. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR004939. APC_su10/DOC_dom.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021097. CPH_domain.
IPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR008979. Galactose-bd-like.
IPR014722. Rib_L2_dom2.
IPR011991. WHTH_DNA-bd_dom.
IPR002867. Znf_C6HC.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF03256. APC10. 1 hit.
PF11515. Cul7. 1 hit.
PF00888. Cullin. 1 hit.
PF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00884. Cullin_Nedd8. 1 hit.
SM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 4 hits.
SSF49785. SSF49785. 1 hit.
SSF75632. SSF75632. 2 hits.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
PS51284. DOC. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IWT3) [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
MVGERHAGDL MVPLGPRLQA YPEELIRQRP GHDGHPEYLI RWSVLKCGEV
60 70 80 90 100
GKVGVEEGKA EHILMWLSAP EVYANCPGLL GERALSKGLQ HEPAGVSGSF
110 120 130 140 150
PRDPGGLDEV AMGEMEADVQ ALVRRAARQL AESGTPSLTA AVLHTIHVLS
160 170 180 190 200
AYASIGPLTG VFRETGALDL LMHMLCNPEP QIRRSAGKML QALAAHDAGS
210 220 230 240 250
RAHVLLSLSQ QDGIEQHMDF DSRYTLLELF AETTSSEEHC MAFEGIHLPQ
260 270 280 290 300
IPGKLLFSLV KRYLCVTSLL DQLNSSPELG AGDQSSPCAT REKSRGQREL
310 320 330 340 350
EFSMAVGNLI SELVRSMGWA RNLSEQGMSP PRPTRSIFQP YISGPSLLLP
360 370 380 390 400
TIVTTPRRQG WVFRQRSEFS SRSGYGEYVQ QTLQPGMRVR MLDDYEEISA
410 420 430 440 450
GDEGEFRQSN NGIPPVQVFW QSTGRTYWVH WHMLEILGPE EATEDKASAA
460 470 480 490 500
VEKGAGATVL GTAFPSWDWN PMDGLYPLPY LQPEPQKNER VGYLTQAEWW
510 520 530 540 550
ELLFFIKKLD LCEQQPIFQN LWKNLDETLG EKALGEISVS VEMAESLLQV
560 570 580 590 600
LSSRFEGSTL NDLLNSQIYT KYGLLSNEPS SSSTSRNHSC TPDPEEESKS
610 620 630 640 650
EASFSEEETE SLKAKAEAPK TEAEPTKTRT ETPMAQSDSQ LFNQLLVTEG
660 670 680 690 700
MTLPTEMKEA ASEMARALRG PGPRSSLDQH VAAVVATVQI SSLDTNLQLS
710 720 730 740 750
GLSALSQAVE EVTERDHPLV RPDRSLREKL VKMLVELLTN QVGEKMVVVQ
760 770 780 790 800
ALRLLYLLMT KHEWRPLFAR EGGIYAVLVC MQEYKTSVLV QQAGLAALKM
810 820 830 840 850
LAVASSSEIP TFVTGRDSIH SLFDAQMTRE IFASIDSATR PGSESLLLTV
860 870 880 890 900
PAAVILMLNT EGCSSAARNG LLLLNLLLCN HHTLGDQIIT QELRDTLFRH
910 920 930 940 950
SGIAPRTEPM PTTRTILMML LNRYSEPPGS PERAALETPI IQGQDGSPEL
960 970 980 990 1000
LIRSLVGGPS AELLLDLERV LCREGSPGGA VRPLLKRLQQ ETQPFLLLLR
1010 1020 1030 1040 1050
TLDAPGPNKT LLLSVLRVIT RLLDFPEAMV LPWHEVLEPC LNCLSGPSSD
1060 1070 1080 1090 1100
SEIVQELTCF LHRLASMHKD YAVVLCCLGA KEILSKVLDK HSAQLLLGCE
1110 1120 1130 1140 1150
LRDLVTECEK YAQLYSNLTS SILAGCIQMV LGQIEDHRRT HQPINIPFFD
1160 1170 1180 1190 1200
VFLRHLCQGS SVEVKEDKCW EKVEVSSNPH RASKLTDHNP KTYWESNGST
1210 1220 1230 1240 1250
GSHYITLHMH RGVLVRQLTL LVASEDSSYM PARVVVFGGD STSCIGTELN
1260 1270 1280 1290 1300
TVNVMPSASR VILLENLNRF WPIIQIRIKR CQQGGIDTRV RGVEVLGPKP
1310 1320 1330 1340 1350
TFWPLFREQL CRRTCLFYTI RAQAWSRDIA EDHRRLLQLC PRLNRVLRHE
1360 1370 1380 1390 1400
QNFADRFLPD DEAAQALGKT CWEALVSPLV QNITSPDAEG VSALGWLLDQ
1410 1420 1430 1440 1450
YLEQRETSRN PLSRAASFAS RVRRLCHLLV HVEPPPGPSP EPSTRPFSKN
1460 1470 1480 1490 1500
SKGRDRSPAP SPVLPSSSLR NITQCWLSVV QEQVSRFLAA AWRAPDFVPR
1510 1520 1530 1540 1550
YCKLYEHLQR AGSELFGPRA AFMLALRSGF SGALLQQSFL TAAHMSEQFA
1560 1570 1580 1590 1600
RYIDQQIQGG LIGGAPGVEM LGQLQRHLEP IMVLSGLELA TTFEHFYQHY
1610 1620 1630 1640 1650
MADRLLSFGS SWLEGAVLEQ IGLCFPNRLP QLMLQSLSTS EELQRQFHLF
1660 1670 1680 1690 1700
QLQRLDKLFL EQEDEEEKRL EEEEEEEEEE EAEKELFIED PSPAISILVL
1710 1720 1730 1740 1750
SPRCWPVSPL CYLYHPRKCL PTEFCDALDR FSSFYSQSQN HPVLDMGPHR
1760 1770 1780 1790 1800
RLQWTWLGRA ELQFGKQILH VSTVQMWLLL KFNQTEEVSV ETLLKDSDLS
1810 1820 1830 1840 1850
PELLLQALVP LTSGNGPLTL HEGQDFPHGG VLRLHEPGPQ RSGEALWLIP
1860 1870 1880 1890 1900
PQAYLNVEKD EGRTLEQKRN LLSCLLVRIL KAHGEKGLHI DQLVCLVLEA
1910 1920 1930 1940 1950
WQKGPNPPGT LGHTVAGGVA CTSTDVLSCI LHLLGQGYVK RRDDRPQILM
1960 1970 1980 1990 2000
YAAPEPMGPC RGQADVPFCG SQSETSKPSP EAVATLASLQ LPAGRTMSPQ
2010 2020 2030 2040 2050
EVEGLMKQTV RQVQETLNLE PDVAQHLLAH SHWGAEQLLQ SYSEDPEPLL
2060 2070 2080 2090 2100
LAAGLCVHQA QAVPVRPDHC PVCVSPLGCD DDLPSLCCMH YCCKSCWNEY
2110 2120 2130 2140 2150
LTTRIEQNLV LNCTCPIADC PAQPTGAFIR AIVSSPEVIS KYEKALLRGY
2160 2170 2180 2190 2200
VESCSNLTWC TNPQGCDRIL CRQGLGCGTT CSKCGWASCF NCSFPEAHYP
2210 2220 2230 2240 2250
ASCGHMSQWV DDGGYYDGMS VEAQSKHLAK LISKRCPSCQ APIEKNEGCL
2260 2270 2280 2290 2300
HMTCAKCNHG FCWRCLKSWK PNHKDYYNCS AMVSKAARQE KRFQDYNERC
2310 2320 2330 2340 2350
TFHHQAREFA VNLRNRVSAI HEVPPPRSFT FLNDACQGLE QARKVLAYAC
2360 2370 2380 2390 2400
VYSFYSQDAE YMDVVEQQTE NLELHTNALQ ILLEETLLRC RDLASSLRLL
2410 2420 2430 2440 2450
RADCLSTGME LLRRIQERLL AILQHSAQDF RVGLQSPSVE AWEAKGPNMP
2460 2470 2480 2490 2500
GSQPQASSGP EAEEEEEDDE DDVPEWQQDE FDEELDNDSF SYDESENLDQ
2510
ETFFFGDEEE DEDEAYD
Length:2,517
Mass (Da):281,229
Last modified:January 4, 2005 - v2
Checksum:i42387A55DCC52EAF
GO
Isoform 2 (identifier: Q8IWT3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     418-527: Missing.

Note: No experimental confirmation available.

Show »
Length:2,407
Mass (Da):268,362
Checksum:iF41FAF09CC71656C
GO

Sequence cautioni

The sequence BAC85207.1 differs from that shown. Reason: Intron retention.
The sequence BAC86090.1 differs from that shown. Reason: Intron retention.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti527 – 5271E → G in CAH18696. (PubMed:17974005)Curated
Sequence conflicti663 – 6631E → K in AAN61516. (PubMed:12526791)Curated
Sequence conflicti1171 – 11711E → K in CAH18328. (PubMed:17974005)Curated
Sequence conflicti1230 – 12301M → T in CAH18328. (PubMed:17974005)Curated
Sequence conflicti1268 – 12681N → S in CAH18328. (PubMed:17974005)Curated
Sequence conflicti1277 – 12771R → H in CAH18328. (PubMed:17974005)Curated
Sequence conflicti1830 – 185728Missing in CAH18696. (PubMed:17974005)CuratedAdd
BLAST
Sequence conflicti2049 – 20491L → P in CAH18696. (PubMed:17974005)Curated
Sequence conflicti2058 – 20592HQ → PL in CAH18696. (PubMed:17974005)Curated
Sequence conflicti2345 – 23451V → VV in CAI20204. (PubMed:14574404)Curated
Sequence conflicti2345 – 23451V → VV in EAX04163. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2058 – 20581H → P.
Corresponds to variant rs2273709 [ dbSNP | Ensembl ].
VAR_048844
Natural varianti2180 – 21801T → I.
Corresponds to variant rs11962520 [ dbSNP | Ensembl ].
VAR_048845

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei418 – 527110Missing in isoform 2. 1 PublicationVSP_009573Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145132 mRNA. Translation: AAN61516.1.
AJ318215 mRNA. Translation: CAC85756.1.
CR749511 mRNA. Translation: CAH18328.1.
CR749841 mRNA. Translation: CAH18696.1.
AL133375 Genomic DNA. Translation: CAI20204.1.
CH471081 Genomic DNA. Translation: EAX04163.1.
AK125228 mRNA. Translation: BAC86090.1. Sequence problems.
AK129649 mRNA. Translation: BAC85207.1. Sequence problems.
AB014608 mRNA. Translation: BAA31683.3.
BC002879 mRNA. Translation: AAH02879.2.
CCDSiCCDS4890.1. [Q8IWT3-1]
PIRiT00350.
RefSeqiNP_055904.1. NM_015089.3. [Q8IWT3-1]
XP_006715094.1. XM_006715031.1. [Q8IWT3-3]
UniGeneiHs.485434.

Genome annotation databases

EnsembliENST00000252050; ENSP00000252050; ENSG00000112659. [Q8IWT3-1]
GeneIDi23113.
KEGGihsa:23113.
UCSCiuc003ouk.3. human. [Q8IWT3-1]

Polymorphism databases

DMDMi57015409.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145132 mRNA. Translation: AAN61516.1 .
AJ318215 mRNA. Translation: CAC85756.1 .
CR749511 mRNA. Translation: CAH18328.1 .
CR749841 mRNA. Translation: CAH18696.1 .
AL133375 Genomic DNA. Translation: CAI20204.1 .
CH471081 Genomic DNA. Translation: EAX04163.1 .
AK125228 mRNA. Translation: BAC86090.1 . Sequence problems.
AK129649 mRNA. Translation: BAC85207.1 . Sequence problems.
AB014608 mRNA. Translation: BAA31683.3 .
BC002879 mRNA. Translation: AAH02879.2 .
CCDSi CCDS4890.1. [Q8IWT3-1 ]
PIRi T00350.
RefSeqi NP_055904.1. NM_015089.3. [Q8IWT3-1 ]
XP_006715094.1. XM_006715031.1. [Q8IWT3-3 ]
UniGenei Hs.485434.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JUF NMR - A 366-466 [» ]
ProteinModelPortali Q8IWT3.
SMRi Q8IWT3. Positions 375-438, 1866-1953, 1997-2417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116736. 9 interactions.
IntActi Q8IWT3. 8 interactions.
MINTi MINT-6615845.
STRINGi 9606.ENSP00000252050.

PTM databases

PhosphoSitei Q8IWT3.

Polymorphism databases

DMDMi 57015409.

Proteomic databases

MaxQBi Q8IWT3.
PaxDbi Q8IWT3.
PRIDEi Q8IWT3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252050 ; ENSP00000252050 ; ENSG00000112659 . [Q8IWT3-1 ]
GeneIDi 23113.
KEGGi hsa:23113.
UCSCi uc003ouk.3. human. [Q8IWT3-1 ]

Organism-specific databases

CTDi 23113.
GeneCardsi GC06P043149.
HGNCi HGNC:15982. CUL9.
HPAi HPA016434.
MIMi 607489. gene.
neXtProti NX_Q8IWT3.
PharmGKBi PA164718328.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG48148.
GeneTreei ENSGT00700000104406.
InParanoidi Q8IWT3.
KOi K11970.
OMAi TKHEWRP.
OrthoDBi EOG70S74H.
PhylomeDBi Q8IWT3.
TreeFami TF101154.

Miscellaneous databases

ChiTaRSi CUL9. human.
EvolutionaryTracei Q8IWT3.
GeneWikii PARC_(gene).
GenomeRNAii 23113.
NextBioi 44317.
PROi Q8IWT3.
SOURCEi Search...

Gene expression databases

Bgeei Q8IWT3.
ExpressionAtlasi Q8IWT3. baseline and differential.
Genevestigatori Q8IWT3.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.25.10.10. 4 hits.
2.30.30.30. 1 hit.
2.60.120.260. 1 hit.
InterProi IPR004939. APC_su10/DOC_dom.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021097. CPH_domain.
IPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR008979. Galactose-bd-like.
IPR014722. Rib_L2_dom2.
IPR011991. WHTH_DNA-bd_dom.
IPR002867. Znf_C6HC.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF03256. APC10. 1 hit.
PF11515. Cul7. 1 hit.
PF00888. Cullin. 1 hit.
PF01485. IBR. 2 hits.
[Graphical view ]
SMARTi SM00884. Cullin_Nedd8. 1 hit.
SM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 4 hits.
SSF49785. SSF49785. 1 hit.
SSF75632. SSF75632. 2 hits.
PROSITEi PS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
PS51284. DOC. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 786-791; 2419-2431 AND 2432-2445, INTERACTION WITH TP53, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
    Tissue: Cervix carcinoma.
  2. "UbcH7 associated protein, H7AP1. A new member of the Parkin/Ariadne E3 ubiquitin Ligase (PAUL) family."
    Rose S.A., Ardley H.C., Tan N.G., Scott G.B., Markham A.F., Robinson P.A.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Amygdala and Testis.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] OF 1-662 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-662 (ISOFORMS 1/2).
    Tissue: Chondrocyte and Thymus.
  7. "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 765-2517 (ISOFORM 1).
    Tissue: Brain.
  8. "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] OF 1554-2517 (ISOFORM 1).
    Tissue: Lung.
  9. "The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1."
    Moynihan T.P., Ardley H.C., Nuber U., Rose S.A., Jones P.F., Markham A.F., Scheffner M., Robinson P.A.
    J. Biol. Chem. 274:30963-30968(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBCH7 AND UBCH8.
  10. "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 CUL7.
  11. Cited for: FUNCTION, INTERACTION WITH CUL7; RBX1 AND TP53, NEDDYLATION.
  12. "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 CUL7 AND RBX1.

Entry informationi

Entry nameiCUL9_HUMAN
AccessioniPrimary (citable) accession number: Q8IWT3
Secondary accession number(s): O75188
, Q5TCY3, Q68CP2, Q68D92, Q8N3W9, Q9BU56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: January 4, 2005
Last modified: October 29, 2014
This is version 125 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, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3