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Database: UniProt
Entry: A0A6P8GE31_CLUHA
LinkDB: A0A6P8GE31_CLUHA
Original site: A0A6P8GE31_CLUHA 
ID   A0A6P8GE31_CLUHA        Unreviewed;      2518 AA.
AC   A0A6P8GE31;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   18-JUN-2025, entry version 22.
DE   SubName: Full=Cullin-9 isoform X5 {ECO:0000313|RefSeq:XP_031435316.1};
GN   Name=LOC105897402 {ECO:0000313|RefSeq:XP_031435316.1};
OS   Clupea harengus (Atlantic herring).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes; Clupeoidei;
OC   Clupeidae; Clupea.
OX   NCBI_TaxID=7950 {ECO:0000313|Proteomes:UP000515152, ECO:0000313|RefSeq:XP_031435316.1};
RN   [1] {ECO:0000313|RefSeq:XP_031435316.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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_031435316.1; XM_031579456.2.
DR   GeneID; 105897402; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000515152; Chromosome 13.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 1.20.1310.10; Cullin Repeats; 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; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
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; IPR044066; TRIAD_supradom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR22771:SF4; CULLIN 7-RELATED; 1.
DR   PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 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   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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; 1.
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:UP000515152};
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          1215..1394
FT                   /note="DOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51284"
FT   DOMAIN          1635..1887
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   DOMAIN          2148..2366
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          2319..2362
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          52..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1515..1553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2019..2048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..75
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..314
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..688
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1525..1539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1540..1551
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2024..2048
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2518 AA;  281501 MW;  59A2A28F52D8D374 CRC64;
     MVGERRNGNL LVQLGPRQQA YPEELIRQRR THDGQTEYLI RWTLLAVEDG TGTGGAEVAG
     SVSSGSGAGG SGGSTSGESK AESILMWMST EDVYANCPTL LGKRKAPAQE EEESPSSSGG
     GGGSFRPPDV TFDEVELSDM KTDVVNLVRR ARKQMAKTSE FAISLTHTIH VLSAYASIGS
     LVGVFKETGA LDLLMELLCN KERQTRRSAG KMLRALASHD AGSRAYVLLS LSQQDGIEQH
     MDFDNRFTLL ELFAETTSSE EHGISFEGIH LPQIPGKLLF SLVKRYLCVT SLMDKLNTAG
     SESSIEPSSS SPSSVASDQT RLQREFEFTM AMANLISELV RVMGWDRNRQ LPMCLPSQTG
     SGASDDASED EGCPRRMLRS IFQPRFTASA SLTAATAAAM ATASGATPPV APVSAAPTKK
     KVANDFKTRV DFSTRSSYVE YVQDNLKSGM MVRMLEDYEE VSSGDEGEFR YSNDGSPPVQ
     VYWNSLSRTY WVHWHMIEIL GSGTSGQSEK ETQEKASTLT ETLKLTAVSQ TFFSKPPGGL
     YSLPYLCEDE REDGAQLSRA EWWEVLFFIK KLEPEQQQEV NHILRQNLDE AQMSELDEVS
     LLQLCVTGEV VRKILHYLKQ TLQSSCLGDL LCSQAFAKHY LRRGGAGLQD EDPLTAAATL
     LGGRRSPPSS SSSSGIAVSS SSAMGSVSKK PKKEPATEGG SEGGGGSDTE SELPTEDETK
     YPEDLEEKMK AFNSPKVQGK KTALEKMGEV VDMMRKGGSG SDAGRQLAAI KVMIKLLEEE
     GPQEKRTLCD SAQAIRDKVL KLLVEMIGSQ VKVDAVAALR LTRALMLKYE WRVSFATEGG
     VKAILSSMQE FSTCTQVQQI ALATLKVITG ASKHDMRSVG SCVPLSESGT QMMLEIFASI
     GSATPEGSKG LLSTIPNAIE LMLNTPRCSL SVCNGLLVVI MLISSHKSLA EQLVACGISP
     VLKKCLSSQR SETTTLAIIA LNHISMVHKL EKKESKEELE FKDTELKMLV VSLKSMTATK
     EVVQTLEQLL CDSAHLEDEK NEVTYNRDTF QDLVCLMDQH RVDRALQLSI LRILCKFLDN
     YQEDLLPWHE SIEPCLSSMT AFINDRDVVQ QFIRFLFRLA SLNKDYAVVM CRLGTKDALV
     KALDKHSTNL LLVTELKDLI SDCEKYASLY KKMTTSVLAG CIQMVLGHIE EHRRSHQPIN
     IPFFDVFLRN LCQGDLPPYH LCTAQLKSFL RSSVELKEDK CWEKVEVSSN HHRVNKLTDK
     NPKTYWESNG CTGSHFINIY MHKGVVIRQL AVLVASEDSS YMPARILVQG GDDPASINTE
     LNTVNVPPSA SRIVLLENMT RFWSIVQIRI KRCQQGGIDT RVHGFEVLGP KPTFWPVFKE
     QLCCRTYLFY TTKAHTWCQE ILEDKTQLLQ LFNKLNSALK HEQMFADRFL PDAEAAEALG
     RTCWEALITP IVQSITISEL PVLSPLAWLL SEYLDNAESS KRYKTRAAIF NSRVRRLTHL
     LVHVDTSRID TEELKPPVKS KGINRSKDLK NGKEGKNKEA VVPPSSSSAV KPKMKNTSSI
     AGIALCWQGV VQRQVKKFLD STCSLPDFVE RYRAMYLRLK NAMEELFGQQ TAFVLALRQG
     FSAALLQLSI LTAMHVSERF AQYIDLMIQE SCGDSGSVET IRQLQQFLEP MLFLSGLELA
     NTFEHFYRHY LGDRLLGQSK VWLESAVIEQ IGSCFPNRFP QQMLTNLRES EELQQEFHLY
     RLQQLDKTLQ DLDEEMMEEQ SSEPEDDSEV KVLVLSPRCW AVSPPCFLDD PNKHFPAQLC
     SYLTEFTNFY SSSQSIYSLN HSKPRRLQWT WLGHAELHYD SCTLYVSTLQ MYILLQFNNQ
     EDLNMETLQK DTGLTMAVIA HALQPLTGDK GILTQDPEKG VLQLNQRVLS QGSSAQSFCH
     LLPKQTYLNV DEDSARTLER KRNYIYCLIV QIMKAEREMH IDNLVFRVLD TCWKKEALHS
     PGGVRFSCST TDVLSCVIHV ISKGYVRRNE DSPHILEFLP EDPSTPQKGQ AQFSFSNTDL
     KNSSSSTKAD ISLGDESVLA QRPEDGVLEA VLFSMGRTMS QEDVLQLMQR TVQQVAGTLS
     LDLDCAQHLL VHCKWNVDLL IQRYTDDPDT LVLAAGLKIR NPQPPPSPSV QCPVCLVAQS
     GGSEPAPTLC CNHYCCRSCW QEYLTARIEQ NLVMNCNCPI TDCRSQPTSQ FFYNILTDKD
     TISKYENALL RGYVECCSNL TWCTNPLGCD QILCKENIGS MGTCSKCCWS SCFSCNFPEA
     HYPASCSHMS QWMDDGGYYD GMTMEAQSKH LAKLISKRCP SCQAQIEKNE GCLHMTCAKC
     NHGFCWRCLK PWKPTHKDYY NCSAMVSKAA RQEKKFQDYN ERCTFHNQAK DFAISLENKV
     SSINEALQMK SLTFVIDACK ILAQARKVLA YSCVYSYYNQ DTEKMDVMEQ QTEALDLHTN
     ALQILLEETL LQCTDLASCV RLLKPEHLNT GLELIRRIQE RLVAILQHST QVEVGEGL
//
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