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Database: UniProt
Entry: H3A1N3_LATCH
LinkDB: H3A1N3_LATCH
Original site: H3A1N3_LATCH 
ID   H3A1N3_LATCH            Unreviewed;      5051 AA.
AC   H3A1N3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=RCR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012249};
DE            EC=2.3.2.33 {ECO:0000256|ARBA:ARBA00012249};
GN   Name=MYCBP2 {ECO:0000313|Ensembl:ENSLACP00000003554.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000003554.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000003554.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.;
CC         EC=2.3.2.33; Evidence={ECO:0000256|ARBA:ARBA00000333};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}.
CC   -!- SIMILARITY: Belongs to the RING-Cys relay (RCR) family.
CC       {ECO:0000256|ARBA:ARBA00005415}.
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DR   EMBL; AFYH01032547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01032548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01032549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01032550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01032551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01032552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01032553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01032554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01032555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01032556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7897.ENSLACP00000003554; -.
DR   Ensembl; ENSLACT00000003586.1; ENSLACP00000003554.1; ENSLACG00000003166.1.
DR   eggNOG; KOG1428; Eukaryota.
DR   GeneTree; ENSGT00940000155756; -.
DR   HOGENOM; CLU_000063_0_0_1; -.
DR   InParanoid; H3A1N3; -.
DR   OMA; MAHPGCG; -.
DR   TreeFam; TF313151; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000003166; Expressed in chordate pharynx and 6 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR   GO; GO:0016198; P:axon choice point recognition; IEA:Ensembl.
DR   GO; GO:0048677; P:axon extension involved in regeneration; IEA:Ensembl.
DR   GO; GO:0048066; P:developmental pigmentation; IEA:Ensembl.
DR   GO; GO:0021986; P:habenula development; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042068; P:regulation of pteridine metabolic process; IEA:Ensembl.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR   CDD; cd19799; Bbox2_MYCBP2; 1.
DR   CDD; cd16463; RING-H2_PHR; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.120.820; PHR domain; 2.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR004939; APC_su10/DOC_dom.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR012983; PHR.
DR   InterPro; IPR038648; PHR_sf.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45943; E3 UBIQUITIN-PROTEIN LIGASE MYCBP2; 1.
DR   PANTHER; PTHR45943:SF1; E3 UBIQUITIN-PROTEIN LIGASE MYCBP2; 1.
DR   Pfam; PF08005; PHR; 2.
DR   Pfam; PF00415; RCC1; 1.
DR   Pfam; PF13540; RCC1_2; 1.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM01337; APC10; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR   PROSITE; PS00626; RCC1_2; 1.
DR   PROSITE; PS50012; RCC1_3; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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   REPEAT          831..886
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          887..937
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          2753..2846
FT                   /note="Filamin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT   DOMAIN          4045..4223
FT                   /note="DOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51284"
FT   DOMAIN          4810..4861
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          808..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2976..3002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3122..3165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3191..3252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3299..3318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3364..3389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3421..3462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3544..3569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2988..3002
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3129..3165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3196..3233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3428..3455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   5051 AA;  555520 MW;  4C6D1E8BCF37D0A3 CRC64;
     MGSGSGSGLG PGAQSDCRSR YQLLLSGKAL AERYRRIYTA AISDKDQGIQ QGRNKKILGK
     KKLKRKQKSK SKVKARTKGD NLEGTFSVPD IKLHSNPSAF NVYCNVRQCV LEWQRKEASL
     ALALKNSVLS GDSDSDEEEE SKELPVKLPK IVGIGLCGVF ELIKETRFSH PSLCHRSLQA
     LLDMLQGQQP EGLQSEPTDV LESLFQLLLE TTIRSTGLND SMAQSLTALS CACLFSLVVA
     WGDTGKTLQA ISAILTNNGS HACQTIQVPT ILNSLQRSVQ AVLVGKIQIQ DWFNNGIKKA
     SLMHKWALKE VTVDEDEHCL LQSDGSFLYL LCRNGLYRVG SGYSGTVRGH VYSFTSNIRN
     RKDKRSWLGF AKGFLLYREL VRIAGTFQAK FWSVDALDSL KSIITELTLC HQTEGQNILF
     TDGEYINQIA ASKDDGFVVR IYATSTESVL QQELQLKLAR KCLHACGISL FDLEKDLHII
     NSIASSFMGW LIELRTPGTG FDDDSAVLGA GREFALMKTA AGKIYYTGKY QSLGIKQGGP
     AAGKWVELPI TKSPKIVQFS VGHDGSHALL VAEDGSVFFT GSSSKGEDGE STKSRRQAKP
     YKPKKMIKME GKVALYTACN NGSSSVLTKD GELYMFGKDA IYCDSSNLVI ELKGHFVTQV
     AMGKAHACVL TKNGEVWTFG VNNKGQCGRD TGSMNQGGKA PPKKKNSGTV SLRDIIYQLD
     LDEKDEKAMM CPPGMHKWKL DQCMVCTACG DCTGYGPSCV SSGRPDRVPG GICGCGSGES
     GCSVCGCCKA CARELDGQEA RQNLQCGPCP TRSQHRRASS VTSRRKEATN KQKTKFGGGG
     DGSGERGEKD ASKTTTYPPG AVRFDCELRA VQVSCGFHHS VILMENGDVY TFGYGQHGQL
     GHGDVNSRGA PTLVQGLPGP STQVTAGSNH TAVLLTDGQV STFGSFSKKK LKQNPSPTTT
     SYLLKKKKKN QTDSAVKTPG PAVGLFVFLG GGPVTAVYPM PEKWEVQGVT LPSRSENKPH
     VLPILDMPYW NAKPAPMPNI GAKYGRKATW IGASGDQTFL RIDEALINSH VLATSEIFAS
     KQIIVCVYIN VSVREPSIHM IFDKSLHHHE GGPTNVHVLT HTKQPLRIFS NTENNNSAPK
     TRTPPHTHTQ CIYIALIGTE AAGLTVACSV ERRDLSARNL KIKQTKLKIL GAPAVAATKR
     PGIPFGAHSH PKMRLNSSPG TSSDEKALAL VDFSFSKDPV FDVLWRFMSD TREFWCYNSV
     VADARLPSVS DMQTRCSILS PELALPIGPK AFTTRSHGAL HVLACIHILS SCSFSNRWWF
     SRPALSPPEH VARTMASGYA VLGLFRSHGG GWGYSAHSVE AIRFCADTDI LLGGLGLFGG
     RGEYTAKIKL FELGPDGGDH ETDGDLLAET DVLAYDCAAR EKYAMMFDEP VILQSGWWYV
     AWARVSGPSS DCGSHGQASI TTDDGVIFQF KSSKKSNNGT DVNAGQIPQL LYRLPSSDGN
     GSKGKQQTSE PVHILKKSFA RTVSVECFES LLSILHWSWT TLVLGVEELR GLKGYQYIAT
     LLDLERLKFV GTCCLRLLRV YTCEIYPISE YYMFSMCTTG HAHVFYNRNA LPVKEVSTVL
     IYLCELVVPL NFFCAIAICF LINLRFTSVA TKAVVEETSK LAECIGKTRS LLKGVDHCMV
     KLDNDPQGYH SQPLALLEAV LQECHNTFTA CFHSFYPTPA LQWACLCDLL NCLDQTSSSR
     LLAAVMSALC HTSVKLTSIL PIAYDGEVLL RTLAKQASTE NDSALAHRFP LLVAQMEKLS
     QKKENEENLT GITSFREVLE KMLVIVVLPV RKSLRQEMEL FSPHLVSNTC GLLASIVCEL
     TVLALGSEKY RKLLLTPSLH KSSPNRFTKT SQGRSWNTGN GSPDAICFMV DKPGVVVVGF
     CVYGGGGIHE YELEVLVDDS ENTGDSSHSH RWTTLELVKG TYSTDDSSSD MAEIRLDKAV
     PLKENVKYAV RLRNYGSRTA NGDGGMTTVQ CPDGVTFTFS TCSLSSNGTN QTRGQIPQIL
     YYRFVCFCGV KQADINLNRR KNYSFVLHVL HKRIIQYPSC VHNIDIETER QRDLKYSIVF
     FAIMTCNFFF WFCRSEYDGD LQSQLLSKAN EEDKNCSRAL SVVGAVARAA KDLLHRAVAV
     DASLASLLKY SDRQTDRSNL TLDVGLAQLP PSRVKRGNTS ESFLSSCIIM SSVLGFPSRR
     GVDLNLGVVC ICISLCLFKN KTKQKKKTTA TFIICYTTVI EKKPTQVEIA DDIPELLSSS
     SLFSMLLPLI LAYIGPVAAT IPKAAVEVFG LVQQLLPAVA ALNQKYAPPA FNPNQSTDSA
     TGNMPEQGLS ACTTSNHYAV VESDHPYKPA SVAQYKVSFP ECVRWMTIEF DPQCGTGQPE
     DVLRLLIPSR AFQNSGFASK QTAVPDSLNS WIELKKFSCS SGWPTTVLVL PGKVHSFYKL
     TQNKTCTMQL CFDVLGADNL PHKESIPTPT PEQNKEAEPK MRVYSVAKIF KMSQSWRHSP
     FFFSGNEALF SLETASDYVK DEKACFFGFK CIAVGYEFSP GTDEFFSGII QLEKELAYLG
     SVCAAALMKK DLALPIGSEL EEDLEILEES ALQVCKAHSG ILGKGLVLSH SPTILEALEG
     NLPIHIHTNE HSFLEDFIAC VPGSSGGRLA RWLQPDSYAD PQKTSLLLNK DDIRCSWPVT
     ITVLTKDQYG DVVHVPNMKV EVKAIPVSQK KTSVQQENIK KLQRIPGSPA IASSSSDLTF
     GGLPSPKLEA SYEPVIVKEA RYIAVTMMKA YENYSFEELR FASPTPKRPS ENMLIRANND
     GSYSANWTPG AVGLYTVHVT IDGIEIDAGL EVEVKDPPKG MIPPGTQLVK PKVEPQPSKV
     RVFVAKDSAG LRIRSHPSLQ SEQIGIVKVN GTITFIDEIH NDDGVWLRLN DETVKKYVPN
     MNGYTEAWCL SFNQHLGKSL LVPVDNREKK MYRKSATSLL RGQKNPPTAS PPSLPGEKSP
     LSRPPPPPIF LFYRANTIGS RSSDSSSKPF LNPGLRWMLE DIECNIQNKS SKRQAPFVFG
     QPLSFQPPQP QLLTKPCYFV STVHIGANFC IHWWVLVLGG GAARLRSLQE FFFGINMVNA
     PPRSRAESPA PGSRSSSPKQ KALPGGKSSP SSVSSPRSLS PHDKSLPQKV VQENLHSEVV
     EVCTSSTLKA NGSESIEENG DVKHAEDNSS KVHFSIGKAP SKEEQDTRAS PKVSRKSTTR
     HVRPKKAVEP AKQAMSPSVA ECARAVFAAF LWHEGIVHDA MACSSFLKFN PELSKEHAPI
     RSNLTSQQSA DEKETKLKNR HSLEISSALN MFNISPHGPD ISKMGSINKN KVLSMLKEPP
     LHEKCEDAKA ESTSDDAPGP HQTTSKSKSP LPLTLQHLVA FWEDISLATI KAATQNMIFP
     SPGSSAVLKK KENEKDNRRY KKEKKKKDKS EVRPREMAQL AMGGPEKDTI CELCGESHPY
     PVTYHMRQAH PGCGRYAGGQ GYNSIGHFCG GWAGNCGDGG IGGSTWYLVC DRCREKYLRE
     KQAAAREKSV RQRRQEKKKR GEPLNPRGKK NIDLWLRNEK YSAWIEKSST SLINDVSSPV
     ALLKLDFTDT SLYRDPTKVD VGFVAEIILH EMKHKGKGSE ANNTKMSGEI SSKICTCAQS
     GVSRSNSAAE PSILCYHPPK PFLSQLPSLR EGISEDLPAK MTCLYLQTLA RYCINNCSLG
     NTIEESSSSV EARWGGGGGI SGVITKTLFN NFSVSGSIPL LKRKKEENNH PTYQLLQMHA
     PMSLRSLKHS ALPARVKAVP RRRVNSGDAE ILICYSDNSA RQLTKDLIAS EIMSLAEVGS
     SLLRHPSPEL SRLISAHSSL CKGERNFQWP VLAFVIQHHD LEGLEVAMKH ALRKSACRVF
     AMEAFNWLLC SVIQTTSLHD ILWHFVASLT PSPVSQPLGG GEKDTRVCEH PLSDIVIAGE
     AAHPLPHTFH HLLQTISDLM MSLPGGSALQ QMALRCWSLK FKQSDHQFLH QSNVFHHINN
     ILSKSDDGDS EESFNISVQS GYEAMNQIQP SKCSRPNNEL CMVTCLKDLT AIVDIKTSSR
     PAMIGSLTDG STETFWESGD EDKNKTKSIT VSCVKGINAH YISVHVDNSR DLGNKVTSMA
     FLTGKTVEEL CRIKQMDLDS RHIGWVTCEV PGGESHVIKI ELKGPENTLR VRQVKVLGWK
     DGESIKIAGQ IAASVAQQKN CEAETLRVFR LITSQVFGKL MSNGLPIHAL LLIDNAGAHP
     GPESLKAADR SIRAPSDADL KEHMVGIIFS RSKLTNLQKQ VCTHIVQAIR MEATRVREEW
     EHAISSKENA NSQPSDEDAS SDAYCFELLS MVLALSGSNV GRQYLAQQLT LLQDLFSLLH
     TASPRVQRQV TSLLRRVLPE VTPACLASII GVKALPPADI SDIIHSTEKG DWNKLGILDM
     LLGCIAKALT VQLKAKGTTI TGTAGTAAEG GSSNVMNGYV LKNKNKKKLY GLVVLCLVSS
     SLSNSSQILV SFPLNDSSGS LPPFLLSFLP PPPPNSYIRR GENHWWMKGS TPTQIAEIII
     KLVKDMGAGH LSEAWSRVTK NAIAETIIAL TKMEEEHRSP VRCIATTRLW LALASLCVLD
     QDHVDRLSSG RWMVLMCIPN PMCDNHDDGE TAAIILCNVC GNLCTDCDRF LHLHRRTRTH
     QRQVFKEEEE AIKVDLHEGC GRTKLFWLMA LADSKTMKAM VEFRENTGKP TSSSNEACRF
     CGSRSGTELS AVGSVCSDPD CQEYAKAACS KTHPCGHICG GVKNEEQCLP CLHGCDKSTS
     SLKQDADDMC MICFTEALSA APAVQLDCSH VFHLQCCRRV LENRWIGPRI TFGFLACPIC
     KNTVNHPRLK DLLDPIRQLY EDVRKKALMR LEYEGLHKSV RFYNDPAGFA MNRYAYYVCY
     KCKKKYINRL NTKLGKHFHI RELYCRDCKD PCTASATQMC PKHGTDFLEY KCRYCCSVAV
     FFCFGTTHFC NACHDDFQRI TSIPKEELPR CPAGPRGKQV EGTECPLHVV HPPTGEEFAL
     GCGVCRNAHT F
//
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