UniProt: U4PBJ5

Database: UniProt
Entry: U4PBJ5_CAEEL

LinkDB:  U4PBJ5_CAEEL 
Original site:  U4PBJ5_CAEEL

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   NCBI-Gene (1)   
   WORMBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (17)   
   InterPro (9)   
   Pfam (5)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (27)   

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ID   U4PBJ5_CAEEL            Unreviewed;      4179 AA.
AC   U4PBJ5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=eel-1 {ECO:0000313|EMBL:CDH93238.1,
GN   ECO:0000313|WormBase:Y67D8C.5b};
GN   ORFNames=CELE_Y67D8C.5 {ECO:0000313|EMBL:CDH93238.1}, Y67D8C.5
GN   {ECO:0000313|WormBase:Y67D8C.5b};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CDH93238.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CDH93238.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CDH93238.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00034494}.
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DR   EMBL; BX284604; CDH93238.1; -; Genomic_DNA.
DR   RefSeq; NP_001294466.1; NM_001307537.1.
DR   SMR; U4PBJ5; -.
DR   EPD; U4PBJ5; -.
DR   EnsemblMetazoa; Y67D8C.5b.1; Y67D8C.5b.1; WBGene00022069.
DR   GeneID; 177084; -.
DR   AGR; WB:WBGene00022069; -.
DR   WormBase; Y67D8C.5b; CE48624; WBGene00022069; eel-1.
DR   OrthoDB; 5396290at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00022069; Expressed in germ line (C elegans) and 6 other cell types or tissues.
DR   ExpressionAtlas; U4PBJ5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd14306; UBA_VP13D; 1.
DR   Gene3D; 6.10.250.1630; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR   InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR025527; HUWE1/Rev1_UBM.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR041969; VP13D_UBA.
DR   PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF06012; DUF908; 2.
DR   Pfam; PF06025; DUF913; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF14377; UBM; 3.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|EPD:U4PBJ5,
KW   ECO:0007829|PeptideAtlas:U4PBJ5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDH93238.1};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1436..1475
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          3843..4179
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          810..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1120..1141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2034..2065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2373..2555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2799..2944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3003..3039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3594..3662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2179..2218
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        493..517
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..542
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..851
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2395..2416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2457..2510
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2511..2525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2526..2554
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2799..2813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2844..2879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2884..2898
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2920..2940
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3598..3614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        4146
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   4179 AA;  465687 MW;  467CD73DB2CC4FE7 CRC64;
     MKIDDAEPSS SSSGSDMPPA SATLLRNIVA TKNDEDFIAA INKGREVHAV MGKTELYKWT
     EVLNRCDEIL EKAVHKNEFG NLQCDHDTVL KNHAVAIVRF TVLLFECTSS RRIYKSVDRI
     LALLESTDMD LLAEVLRLLQ VMGKRSKFLS TRIPQKEQHA LAQRLTAIAQ CWGGKLRTVK
     MAECLKREPK LPMLFPFTYT DAKQRTIIVE QPKFQKDESV GELITRTVAQ ISPPVSSDSV
     PSQQFSKEDL YCLLSRVRML VTFEDWHHRF KCLIVRLLSV STLVYCRLGG TDETTLSSLL
     YSGFIEEIVE MLKSDREADT QQDHNLHDAI QTEALSTLCS IVTYEKEPKI TQILEALSAG
     SYHGFLSVMT RQIVDELKSN NLGKTGKPSV SLATALFSFI YHLASIEPGG DTLVGSGLTQ
     TLLSVIGFHE LPIECITFGT RCARIIDLFT TIDVTSFKAN NGMEICVNRV VHEINECRKE
     QPFMIDISYD MPFEEEPEPR DDQEAHEEPE DESDERNPVD QEAPVPIEVD APLPPASPIA
     APAPVPVASA STSSDSKIKG GPWEEVQMNG ATCHQQRSGL IKGLLTFIKR AIGDVQFQDI
     MKHLMEGDLP EALMHILSNA EYYSPSLFHQ SAHLITNFVY QFPEELSSIQ RRHVPYVIFQ
     SLLRKELPNS KDVITTLGNV FTAMCLNERG LRQFKSYDPF NQIFRIVLSV KFLVTLRKKR
     SAEVFESAQA IGGALDDLMR HYPDLKHDML KSIIVILDLL DEIGRNPPAG VELVPTLTKT
     MARSVVFSPN NSSLLPREAR EARELRIQQL QREIPEQADE RVGGDVEEEP MEVEDAEDSD
     VDEEDNEMSM DEMSGEAPAP PAAPSPKPTK PFEYGAGMMC EDANGKKILP IGDYMLLIAR
     VVETMMTQSP SQKITEEFID ECVMQKIMKL CHLPCITNEA THATYIGSIA NIIKHIVKAG
     YQSQRNGPDV GPKLMSAIVG EFIKTINPLF EVNNGDFSAM NQAESRKATL LMHLDEKLVE
     KTLVELNSII PTLLNLNKSP MSSTYNPQDH RTRIYETWKM PEGMKLYGML RKLSRMLCWE
     YELVQTLKPT IRTAATQTEG EMLSDQPADT HLDVEVMPPW DEDSVDEQQK RDEAKEPRWK
     AAGVSQEEHD FWIKNKPLQD IVSKSHAMVK DLLNSMGKTI NVNNPRRPRI RDTPPLPLAA
     SHCISMIFSS IYKDLKWEPP VQNAATSPMA YGRYIELLTQ LNHSLFENGR CSNPALPQNF
     YTSGCHKAFF ELFSDKIIPF LGDNMPEGVE QTMEEWCRLA VKLTDRNTIV SSDNWQRRDR
     QSADFDTNKY LKLVCRDMFN AYKQFFEKMA QMPDWELKSL KKVCENAFSV FKEVAKNLVE
     ETEATTAATE AVNAAAAPAP ADAPAAEWGP GALRIPPVAV EPAPAPVAVN PAAAADPHED
     TIVMLMDLGF SRDIVLYALE STRNADEAAN YLLAHGNEIP LQDAANPFRD DLLNQVLREA
     GAEMIAGANT PNADEIELQL NAQFAEHQGY ELVRIAQRVL RDAGAEQIGL QIMEAYPDES
     VDVAAEQLIN DVMDRVRNPR SSYEENIAQP LIPPLSQLKI EQDVSLNSAC KQLFPLVKRL
     LLVSNDTIHP CAELIVSIFP AMTEEWRKEH LIAEICGEDL KNMAKSLVEQ EVDENGRPKQ
     HDVARTMTNR LHFAVLIFDK ISEEYVQWID ANGMTEVMLT SLEYLVERFK SVDYYQSLIT
     RIICWNDFYA KTHRLIVRRA YLKSLSPSLV WSYQSYEEDA LRRRADYSSG EKKWVPYDAA
     SQKTLNDAFF AGVRGVKCTL KRGVRPNKKV DVDFASMKQG DGTSRENIKA ELPPTVEVSI
     PDLMDAEAKL SWSEDQNDRF LDLSTQILRT GALDPKCSHS MLSFIARLTR SHRNAVRFME
     KDGVEAILRL RARCAITYPF LVSIIIRNCI DDDALLGHIY EKTIRGYIAV PTQPPASMSE
     YAAGKSKDFA DTLNFMAPLS TRNPLVFTEA MNKLARMNGS LILPMIKEKK PTLSVSSTAG
     GASTSSSSAP PPPPPLTSSS SHTVVENNSR AEKIVSMMLS EVLNGEFPTV GQTRMLSQEK
     ILQILAEIVK SYPSLAIIIA ETQAEGRSAL HSLIDTYIIA PIEKIETTNA LKTLIAVISA
     SQNSLKAQEL LVLDVKNALA SYSEKASELR VDLAKLQLDK ESEEREEATT SLKKQETEVL
     SKISELCSII IIMCQSCPAH HHHHHSSTDR NNRERSSQNA IMKMFHKKRM CADLVKTIHC
     LQLSTKVSLD TVNQILKTLD TLLEGSTTTT SATITGPRSL MDIVAGRREQ RREAAAGGIM
     NEREIDTIFQ RDGLAFDGEM ENLLRRLQGD HWRGNSVQRG AGQVAEEEEG SETYEERERS
     DSPSESSEHA GDEEVRDDAV ETGDGEVDMA DAQDAPLAAP DAPPGINLVD EIMQQVQRDV
     EDDEEDEDGD QNEHEAEEDD HDREDEDDED DDDDEDEEEE AEDDDQDEDD VRHVEQNPEP
     LARRLFEEDD DDEEDDDGDE DGDSMEDDVQ RLDLDDDYFD MGGPFDAQRM DDMIFPPSFG
     RPAVTSFADL FRDDFDFLPP YRAERRPLAR GSHLGGVISE HPLMTRPPAE NDVSRRPNTN
     IRAEILQMHT RSSLHRQNAI RRTTTEAREL EAISRGIRMG ELPAGRMLVR GTTTHGDGGV
     HTSFFDHIFD IRPSNVAFSR SGAYRSYNTG DRDERRDIRA SQVPTCLERL ESYSLSMEPV
     SSRFVTVIVN SHLNKIHAAR EAQIKKEAEI KAKAKKDAEA AKKAAEDKKK AAEAPAPAPS
     AEQSDSPASP DAPAPAPEEI GLATPAATNT TNTVSESVAP NASTRGDDTL TTPAAAQVED
     QASEDQHIEE EPMEVGEDDG AAEAPQSSAA TAASSVAGTE EIEDVERQAV EDHVPEIQDN
     DDTLPYEGAV EHAPAQAPEE NVMPEEFRAI LGDIIIPDGV DPAFLAALPE EMRAEVIRDY
     QRQQRAERAS RPVPAAQPVA VNPNAPAGGE AAQGEGQAEQ PAAAVVPLVE PIDPVFLNAL
     PPELQEEVLA EHERRLREAE EQQRRQNAPP APVVEMDGAA VIASLPANER AQVLAEMDDA
     ELAGLPADMQ NEARRARAQH VEPNMLRYHR LLFRGGVGGA PGAIGTVRAR TNARAAANAG
     PSVGQNAGNA IQAPPDQPHL LDRESILTLC LLYLVDNNRV PHTRLQKVLR SACVNQTTCD
     FIVWCLLALL DKASEANTDD EEILSNVPAW LDSIAVSGVG HNERAIRISE NAQKISIHSM
     LAIPMCKNIL DLLANIARAY PGNFLPLILR HGAKPTDTPK QAPSFAQFWT MVQNTTKVPK
     SKDWTATPEQ QLEECPLGQM LNSLRKPIMA KSPLKEKVLK VASQIMVTLP MDTLKLLGND
     ESRKPLAEKL EFVIQVMTTG SCSTEGLADG LTILSEAMRS LSDSTSVDIY EHLFLAVSKL
     GGELLPQVDR LIVELDEAQK KEEVSSVAPS DQPTSSKTAQ LVVDTSAAGR VATGRFDGER
     LVIDGDQNMR LQMSSCKELQ LPAVTVLTDK GGAQYALLSA LQTLVKVRNH MKAIRKDKAK
     RAKDAEKKLK EKETPSTSAP AAPAAPATAP TAPAAPDAPV ENNEVPEPAA ELEEVNDEEP
     RISERLSSLE SLWNSLSECL LRLGKASDPH AVLALQPAAE AFFLVHASQQ NKLKAKDAEA
     KRKESQAASS SAAAAVASSV SHDGLREDLD PDTAKLIEFA EKHRQVLNQA LRQNNAVLSA
     GGPFAILTQF PKLLDFDVKR KYFRKELTKL EPSMPRYRRN DVSVQVSRNR VFSDSFRELF
     RLRPSEWKNR FYIIFQGEEG QDAGGLLREW FSVITREIFN PNYALFITAP GDMVTYMINK
     ASYINPEHLD YFKFVGRLIA KSVFEHKYLD CYFTRAFYKH ILNLPVRYQD LESEDPAFFK
     SLDFLLQNPI DDLALDLTFS TEVEEFGVRS VRDLKPNGRK IEVNDANKDE YVKLVCQMKM
     TGSIRKQLDA FLTGFYEIIP KDLISMFNEQ ELELLISGLP TVDIDDMAAN TDYKGFQKTS
     THIQWFWRAL RSFEKEDKAK FLQFVTGTSK VPLQGFASLE GMNGVQKFSI HMDSRGGDRL
     PAAHTCFNQL DLPQYESYEK LRQSLLLAIR ECTEGFGFA
//

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