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Database: UniProt
Entry: A0A1S3WKU8_ERIEU
LinkDB: A0A1S3WKU8_ERIEU
Original site: A0A1S3WKU8_ERIEU 
ID   A0A1S3WKU8_ERIEU        Unreviewed;      2324 AA.
AC   A0A1S3WKU8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   18-JUN-2025, entry version 43.
DE   SubName: Full=Cullin-9 {ECO:0000313|RefSeq:XP_016046907.1};
GN   Name=CUL9 {ECO:0000313|RefSeq:XP_016046907.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016046907.1};
RN   [1] {ECO:0000313|RefSeq:XP_016046907.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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DR   RefSeq; XP_016046907.1; XM_016191421.1.
DR   FunCoup; A0A1S3WKU8; 1108.
DR   STRING; 9365.ENSEEUP00000005270; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   InParanoid; A0A1S3WKU8; -.
DR   OrthoDB; 1431934at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd20347; BRcat_RBR_CUL9; 1.
DR   CDD; cd20359; Rcat_RBR_CUL9; 1.
DR   CDD; cd16624; RING-HC_RBR_CUL9; 1.
DR   FunFam; 1.20.120.1750:FF:000014; Cullin 9; 1.
DR   FunFam; 2.60.120.260:FF:000046; Cullin 9; 1.
DR   FunFam; 3.30.230.130:FF:000009; Cullin 9; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 3.30.230.130; Cullin, Chain C, Domain 2; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR004939; APC_su10/DOC_dom.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR056405; ARM_CUL7_CUL9.
DR   InterPro; IPR047561; BRcat_RBR_CUL9.
DR   InterPro; IPR021097; CPH_domain.
DR   InterPro; IPR055486; CUL7/CUL9_N.
DR   InterPro; IPR045093; Cullin.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047560; Rcat_RBR_CUL9.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR047562; RING-HC_RBR_CUL9.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22771:SF2; CULLIN-9; 1.
DR   Pfam; PF03256; ANAPC10; 1.
DR   Pfam; PF24742; ARM_CUL7_CUL9; 1.
DR   Pfam; PF11515; Cul7; 1.
DR   Pfam; PF23168; CUL7_CUL9_N; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM01337; APC10; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF75632; Cullin homology domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 2.
PE   3: Inferred from homology;
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          954..1133
FT                   /note="DOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51284"
FT   DOMAIN          1355..1622
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   DOMAIN          1877..2094
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          1881..1928
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          2047..2090
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          275..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1244..1277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2254..2324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..596
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..616
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1244..1256
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2272..2303
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2313..2324
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2324 AA;  260005 MW;  64CE893568D1D742 CRC64;
     MVRERRTGDF MVPLGPQLQA YPEELIRQRP GHDGHPEYLI RWSVLKCGES SRVDVEEGKA
     EHILMWLSAP EVYANCPMLL GERTLSKGPQ LESVGSPGSF PRDPGGLDDV AMGELEADVR
     ALVRRATRQL AEGGASSLTA AVLHTVHVLS AYASIGPLTG VFRETGALDL LMHMLCNPEP
     QIRRSAGKML QALAAHNAGS RAHVLLSLSQ QDGIEQHMDF DSCYTLLELF AETTSSEEHC
     MAFESIHLPQ IPGKLLFSLV KRYLCVTSLL DQLNSSPEPG AGDQASASSR EELGLKKSRG
     QRELEFSMAV GNLISELVRS LGWARNLSEQ GTSPPRPARS IFQPCMSSPS LLLPTSTFTA
     TPRKPGWAFR PRSEFSSRSG YGEYMQQTLR PGMRVRMLDD YEEISAGDEG EFRQSNNGVP
     PVQVFWQSTG RTYWVHWHML EILGPEEAVE DTAPAAVKKE EEAAMLGTAF PSWDWKPVDG
     LYSLPYLQPE PQKNEELGYL TQAEWWELLF FIKKLDACEQ QPIFQSLREK LDETLSEKAL
     GEISVPIEVA EGLLRVLSSR FEGSTLSDLL SSQIYTKYGL PRDELSSSSS SHSPSSTPDP
     EEEFRSEASF SEEEAESPQG KAERPEAEAE PAIVKTEPPM AQSDSQLFNQ LLKTEGMALP
     PEMKEAADEM ARALRGPGPR SSLHQHVAAI VATVQIPILD SNLQLSGLYA LSQAVEEVTE
     RDHPLVRPDR SLRYAVILLL CTWAAVVETP GAEGQDGSLE LLMRSLVGDS SAELLLDLER
     MLCQEDSSGS TVGPLLKRLQ QETQPFLLLL RTLDAPGPNK TLLLTALRVM TQLLDHPEAM
     VLPWHEVLEP CLNCLSGPNS DSEIVQVLLC FLHRLASVHK DYAVVLCCLG AKETLSKVPD
     KHSDQLLLAC ELEHLVTACE KHAQLYSKLT SSILAGCIQM VLGQIEDHRR TQQPINIPFF
     DVFLRHLCQG SSVEVKEDKC WEKVEVSSNP HRASKLTDRN PKTYWESNGS TGSHYITLHM
     HRGVLVRQLT LLVASEDSSY MPARVMVFGG DSASCISTEL NTVNVLPSAT RVVLLENLNR
     FWPIIQIRIK RCQQGGIDTR VRGVEVLGPK PTFWPLFREQ LCRRTCLFYT IQAQAWSQDI
     AEDRKRLLQL CPRLNRVLRH EQNFADRFLP DEEAAQALGK TCWEALVSPL VQNITSPDAE
     GVSSLGWLLD QYLEQRESSQ NPLSRAASFA SRVRRLCHLL VHVEPPPGPS PEPSPQPFSK
     NSKGRDRSPG PSPILPSSSL RNITQCWLSV VQEQVSRFLA AAWRAPDFVP RYCKLYERLQ
     RAGSELFGPR AAFTLALRSG FSGALLQQSF LTAAHMSEQF ARHIDQQIQG GLIGGAHGVD
     MLGQLQRHLE PIMVLSGLEL ATTFEHFYQH YMADRLLSLG SNWLEGAVLE QIGFCFPNRL
     PQQMLQSLST SEELQRQFHV YQLQQFDKLL LEQGNKEEQG LEEEEEEEEE ETEKKLFIEE
     PSPTASILVL SPRCWPVSPL CYLYHPRKCL PIEFCDALDR FSNFYIQSQN HPVLDVGPHR
     RLQWTWLGRA ELQFGNQTLH VSTVQMWLLL HFNHTEEVSI ETLLKKSDLT GELLLQALLP
     LTSETGPLTL HEGQDFPPGG ILRLREPEPQ ACNEALWLIP PQMYLNVEED EGRILEQKRN
     LLSCLLVRIL KAQGERGLHI DQLVFLVLEA WKKGPNPPGS LGHTVAGGVA CSSTDVLSCI
     LHLLGQGYVQ RRDDRPQILI YGIPEPTGPC RGQADIPFCG SQASKTSKPS PKAVATLASL
     QLPAGRTMSP QEVEGLMEQT VRQVQETLNL QPDVAQHLLA HSHWGAEQLL QSYSENPEPL
     LLAAGLCVPQ AQDAPTRPDH CPVCVSPLEP DSSLPSLCCR HYCCKSCWNE YLTTRIEQNL
     VLNCTCPIAD CSAQPTGAFI RAIVSSPEVI SKYEKALLRG YVESCSNLTW CTNPQGCDRI
     LCRQGLGCGT TCSKCGWASC FTCSFPEAHY PASCGHMSQW VDDGGYYDGM SVEAQSKHLA
     KLISKRCPSC QAPIEKNEGC LHMTCAKCKH GFCWRCLKSW KPNHKDYYNC SAMVSKAARQ
     EKRFQDYNER CTFHHQARDF AVNLRHQVSA IHEVPPPRSF TFLSDACRGL EQARKVLAYA
     CVYSFYNQDT EHMDVVEQQT ESLELHTNAL QILLEENLLR CRDLASSLRL LRADCLNTGL
     ELLRRIQERL LAILQHSTQD FRVGLQSPSL EVREVKGSNM PAMPPQGSSG VEVEEEEEEE
     EDDVPEWQQD EFDDSFSDDE ESENLDRDTF FFGDEEEEDD EAYD
//
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