wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase 6 (EC 3.4.19.12) (Deubiquitinating enzyme 6) (Proto-oncogene TRE-2) (RN-tre) (Ubiquitin thioesterase 6) (Ubiquitin-specific-processing protease 6) (P35125)
Organism: Homo sapiens (Human)
Function: Deubiquitinase with an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety. Catalyzes its own deubiquitination. In vitro, isoform 2, but not isoform 3, shows deubiquitinating activity. Promotes plasma membrane localization of ARF6 and selectively regulates ARF6-dependent endocytic protein trafficking. Is able to initiate tumorigenesis by inducing the production of matrix metalloproteinases following NF-kappa-B activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19077034}. Cytoplasm. Endosome. Note=Localizes to the plasma membrane and to filamentous structures within the cell corresponding to ARF6 regulated tubular endosomes. Activation of RAC1 and CDC42 can direct the relocalization of USP6 to the plasma membrane in a manner that depends on the integrity of the actin cytoskeleton.
Interaction partners:
- Cell division cycle protein 16 homolog
- Tuberin
- Hamartin
- TBC1 domain family member 7
- TBC1 domain family member 20
- Ubiquitin carboxyl-terminal hydrolase 14
- TBC1 domain family member 25
- Queuine tRNA-ribosyltransferase catalytic subunit 1
Sequence:
MDMVENADSLQAQERKDILMKYDKGHRAGLPEDKGPEPVGINSSIDRFGILHETELPPVTAREAKKIRREMTRTSKWMEMLGEWETYKHSSKLIDRVYKGIPMNIRGPVWSVLLNIQEIKLKNPGRYQIMKERGKRSSEHIHHIDLDVRTTLRNHVFFRDRYGAKQRELFYILLAYSEYNPEVGYCRDLSHITALFLLYLPEEDAFWALVQLLASERHSLPGFHSPNGGTVQGLQDQQEHVVPKSQPKTMWHQDKEGLCGQCASLGCLLRNLIDGISLGLTLRLWDVYLVEGEQVLMPITSIALKVQQKRLMKTSRCGLWARLRNQFFDTWAMNDDTVLKHLRASTKKLTRKQGDLPPPAKREQGSLAPRPVPASRGGKTLCKGYRQAPPGPPAQFQRPICSASPPWASRFSTPCPGGAVREDTYPVGTQGVPSLALAQGGPQGSWRFLEWKSMPRLPTDLDIGGPWFPHYDFEWSCWVRAISQEDQLATCWQAEHCGEVHNKDMSWPEEMSFTANSSKIDRQKVPTEKGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKSVAPLKLRRTIAKYAPKFDGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDGRPDWEVAAEAWDNHLRRNRSIIVDLFHGQLRSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMDLEITVIKLDGTTPVRYGLRLNMDEKYTGLKKQLRDLCGLNSEQILLAEVHDSNIKNFPQDNQKVQLSVSGFLCAFEIPVPSSPISASSPTQIDFSSSPSTNGMFTLTTNGDLPKPIFIPNGMPNTVVPCGTEKNFTNGMVNGHMPSLPDSPFTGYIIAVHRKMMRTELYFLSPQENRPSLFGMPLIVPCTVHTRKKDLYDAVWIQVSWLARPLPPQEASIHAQDRDNCMGYQYPFTLRVVQKDGNSCAWCPQYRFCRGCKIDCGEDRAFIGNAYIAVDWHPTALHLRYQTSQERVVDKHESVEQSRRAQAEPINLDSCLRAFTSEEELGESEMYYCSKCKTHCLATKKLDLWRLPPFLIIHLKRFQFVNDQWIKSQKIVRFLRESFDPSAFLVPRDPALCQHKPLTPQGDELSKPRILAREVKKVDAQSSAGKEDMLLSKSPSSLSANISSSPKGSPSSSRKSGTSCPSSKNSSPNSSPRTLGRSKGRLRLPQIGSKNKPSSSKKNLDASKENGAGQICELADALSRGHMRGGSQPELVTPQDHEVALANGFLYEHEACGNGCGDGYSNGQLGNHSEEDSTDDQREDTHIKPIYNLYAISCHSGILSGGHYITYAKNPNCKWYCYNDSSCEELHPDEIDTDSAYILFYEQQGIDYAQFLPKIDGKKMADTSSTDEDSESDYEKYSMLQ
Protein: Ankyrin 2 (FI18613p1) (Q9NCP8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVTENGAQGDGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLESDTRGKVRLPALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKEGQDEVAAVLIENGAALDAATKKGFTPLHLTAKYGHIKVAQLLLQKEADVDAQGKNGVTPLHVACHYNNQQVALLLLEKGASPHATAKNGHTPLHIAARKNQMDIATTLLEYGALANAESKAGFTPLHLSSQEGHAEISNLLIEHKAAVNHPAKNGLTPMHLCAQEDNVNVAEILEKNGANIDMATKAGYTPLHVASHFGQANMVRFLLQNGANVDAATSIGYTPLHQTAQQGHCHIVNLLLEHKANANAQTVNGQTPLHIARKLGYISVLDSLKTITKEDETAAAPSQAEEKYRVVAPEAMHESFMSDSEEEGGEDNMLSDQPYRYLTVDEMKSLGDDSLPIDVTRDERMDSNRMTQSAEYASGVPPTIGEEVISPHKTQVYGSSPKATVDGVYIANGSGHDEPPHVGRKLSWKSFLVSFLVDARGGAMRGCRHSGVRMIIPSRSTCQPTRVTCRYVKPQRTMHPPQLMEGEALASRVLELGPCSTKFIGPVVMEVPHFASLRGKEREIIILRSDNGETWREHTIDNSEEIIHDVLQQCFEPEEIAQLEEQAGNHVCRFVTYDFPQYFAVVSRIRQEVHAIGPEGGMVSSTVVPQVQAVFPQGALTKKIKVGLQVNLFKPRKGVAPEKLRKISVNHVPKKKRFSLIW
Protein: PH-sensitive chloride channel 1, isoform U (X2JGQ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGCVFEAAKEQPHKPRSRQLRRNQCRGKAEKAAAGTRGKVAVRGNNDKPAEDIKIKDNYQQNHKTQTETQTEVAAVVAIATDAGAETETETEAEAQKEPATGPEHLKAAAQVLLTIRQARQENNKHSSSQVAETHKDEGEDALARQGSIVDTAAGRIGIDIAATTIQVAERHEDGQHWQQHNVRRRRRQPDPAAHPASITKLSAISLHFHALAALAKTLQKHEDLSPVQDRQPLAYRAWQEHPYAETQMPATMSAAIIANVGATAAATSAAAFQYLGQHYKHYSQSISFYAASSVLLMLCYLTTASTAAATQSETGALDKHPIFDESSSDKEILDLLLEKKRYDKRLLPPVNGTLTVNVNVLLLSLASPDESSLKYEVEFLLNQQWNDPRLQYGNKSHYDFLNALHHHDSIWTPDTYFIMHGDFKDPIIPMHFALRIFRNGTITYAMRRHLILSCQGSLHIFPFDDPKCSFSMESISYEEAQIKYVWKNDEDTLRKSPSLTTLNAYLIKNQTTACDQNSWRGNYSCLQVELTFTRDRAYYFTTVFIPGIILVTSSFITFWLEWNAVPARVMIGVTTMLNFFTTSNGFRSTLPVVSNLTAMNVWDGVCMCFIYASLLEFVCVNYVGRKRPLHNVVYRPGENPVTQRLPAVLSRIGVILASPLFFKFTAVYQGEKRQNAGAPNEIVACTTCGGSNSPCTHSANNGCATETCFVQVRKKEPPHPIRVAKTIDVIARITFPTAYAIFLIFFFVHYKGFS
Protein: Helicase sen1 (EC 3.6.4.-) (Q92355)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-dependent 5'->3' DNA/RNA helicase required for the expression and maturation of diverse classes of non-protein-coding RNAs like precursor tRNAs, rRNAs and small nuclear (snRNA) and nucleolar (snoRNA) RNAs. Directs RNA polymerase II transcription termination on snoRNAs as well as on several short protein-coding genes. May also play a role in transcription-coupled nucleotide excision repair (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized RNA-binding protein C3H8.09c
- Rpb7-binding protein seb1
- DNA-directed RNA polymerase II subunit rpb1
- Uncharacterized protein C4G9.04c
- Transcription elongation factor spt5
- Ribonuclease H
- Exosome complex component rrp45
- Transcription elongation factor spt4
- Protein air1
- Set1 complex component swd2
Sequence:
MAENLSDQDCFEKLSSSKEGQHWFCSGLLTQYIQPTFFWFAHDETPSFKWVLNAYHERLRSCTSCIQAYYELRNESLAKGSYSFTGFSITDLQEKWNKWDIIRVLEDFKALEDETIDFTSLPCLIFETLLNPKLFTCKNIYKNAIDAFNGLLSDWCSNIFLPGYLLFFYEASHPDVLEWVHSFFKENTEIRISSATVDAVFNTVVFESQNSSDSDCNFVSISSPEFWERTYMFLELLPLQSITAACESILKDYLLNLVKTSESLSSQQMSCLRICCNSSSFWSAADSFKEVSSFLKNLLKNVTATPFEVSDMNWAYIIASFFRTCLNDFVSVFPEWLKGFVEEKRTIGFIIYSVLDALFDLLSLDYSSPSFLNNTLSLMNANSITILQDYPEYMLKLRLHSLLYDIAFISWSHKAITKNPSFVFDPSYELSPFWKLDNLQEEKISDVLFSKISSCCFAHDIEISENSTPSGTMVQFAELWQVMSEYISGFLKGFSEKSSTEISNMLGDSSKFDTVVSFLLSPTQPLYVSAFHIVQIITNCTKNRNEALKKLVAMDFRGIVHGLADAVLNWQSILSFFPALRIMRFLSITNKSLSSDNSAFTENDIPTLGAYWQCIWNILDLVFSNVARWSLNNPADTVKALMKLTLKFVDDLFQNDGIFIKLLAKFDSLILLGETSESLFSFIMWLKINDLELRGIVINSLCKLFTKFSNFDYLFEDRTVTFLTDFIIRKQKAHLSADQCKQLANVLTQASPEAKTVLEQHRLSEMRKTKKQTELTNSAHVIKPSPTPQITVKQNTTKSSSAPRMGMLEQLKQEYLTKRNFESKLKSSAVSSRKPTFNEVKPANLLAEDLSDNEDDIDRKQGLFSLAKANKIPEIRQQERRQVQLLSNSTIKMHPSQIRMMTNRNVANVKARLFPSMTDFYKEILSWEPANQSPNPVLKFHKLDGKIIDSFKTVEHYMEVLQPMIFMECWSQIQSTKLDLKFSPVEGIMVERTAVNNFVDIGVSVAPKDLYGYPLYDTEVVSLAFNKEDASSMKGLCCFAKVERIVRQTNGVLVVLRTLPSMEILNKLQGNCALWFLKLTNLATFTRQYAGIRGLPYFHLADDIIRARPCSQPVKHSSSEIKAAMKRYQVNEPQAKAIMCALDNNGFTLIQGPPGTGKTKTIIGIISALLVDLSRYHITRPNQQSKSTESKQQILLCAPSNAAVDEVLLRLKRGFLLENGEKYIPRVVRIGNPETINVSVRDLSLEYQTEKQLLEVNQGAIDLGSLQELTRWRDTFYDCIQKIEELEKQIDVARDVAEDTKSLGKELQNKINEKNLAEQKVEELQSQSFTKNKEVDLLRKKAQKAILKQADVVCATLSGSGHDLVAHSSLNFSTVIIDEAAQAVELDTIIPLRYGAKKCILVGDPNQLPPTVLSKKAASLNYSQSLFVRIQKNFSNQMCLLSIQYRMHPDISHFPSKKFYDSRLEDGDNMAEKTQQVWHVNPKFTQYRLFDVRGKERTSNTMSTYNLEEVEYLVNMVDELLNKFPDVNFTGRIGVITPYRSQLHELRRAFKVKYGKSFMSTIDIQTVDGFQGQEKDIIFFSCVKSYSKHGIGFLRDFRRLNVALTRARSSLLIIGNMETLKTDDLWGSLVDDALSRKLVESPHIDSEGRLITISRTSEKRMKNEEFVEPPSKKLANSEPSKEIRQRS
Protein: monogalactosyldiacylglycerol synthase (EC 2.4.1.46) (Q7XZR6)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Plastid, chloroplast membrane {ECO:0000256|ARBA:ARBA00046299}.
Interaction partners:
Sequence:
MESSYKFMVKHVQLWKVAFHTTSPRWVHCFYLAALASFYAKKVEAGLKKYKPDIIISVHPLMQHIPLWVLKWQGLQNRVVFVTVITDLNTCHPTWFHADVNRCYCPSEEVAKRAALDDLQPSQIRVFGLPIRPSFCRAVLVKDDLRKELELDPELPAVLLMGGGEGMGPVKKTAKALGESLFDEELGKPIGQLIVICGRNKTLSSSLQALEWKIPIKVRGFETQMEKWMGACDCIITKAGPGTIAEALIRGLPIILNDFIPGQEVGNVPYVVDNGAGVFSKSSRETAKLVARWFGPDSDELKRMSEKALKLAQPEAVFDIVRDIHELSREQGVISQISSSLTSSFFIPSPETTPIQLM
Protein: Basement membrane proteoglycan (H9G349)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKRSSTVLAALLALLLVATNDAARHRKYRQTYQDIDSDDDDTSDVQITVFPSEKEVRDGRDVSFECRARTSDNSVYPTVRWARVGGPLPSSAHDSGGRLTINPVQLSDAGTYICVSDYNGNTVEARATLSVVSYGPQEVSNGLRQAGQCMADEKACGNNECVKNDYVCDGEPDCRDRSDEANCPAISRTCEPNEFKCNNNKCVQKMWLCDGDDDCGDNSDELNCNAKPSSSDCKPTEFQCHDRRQCVPSSFHCDGTNDCHDGSDEVGCVQPTVVDPPQTNLQVPRGTTFSLTCKAVAVPEPYINWRLNWGPVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKGRVLATPDCIVRVVDDPRPQPPQPPTAPPQRASCDTRGAVTPYPNNYGTCECKSQVTGPNCDQCKPGAFHLSEKSPEGCLKCFCFGVSNDCRSSGHYRTKDRLMFAGDAEGVTISDIEERTIDRNTPFSFFKTGYLTFDGTTDGVAKYWRLPQRFLGDKVTAYGGKMEFEIEFSGSGHHSSEPMVVLKGNQNILVHRVRNQEHVLRSDSPVRITVETYETNYEQLNGAAATREDLLMVLADLDAFLIRATHVAHQTSTSLGDVSWEIAVDRYTPDGLALEVEQCVCPPGYLGTSCEDCAPGYERSGYGPYLGTCVPIQPRHQQCGPGAVAPTAPAQGQCQCKASVIGPNCDRCAPNSFGLAPTNPQGCIPCFCSGVTQQCSASSYRRTSVSIDYARGDRDQLELTTSDSRQPYSPQTRAELSGQAIEFRSFEEARGQTLYWKLPEKFLGDKVTSYGGTLEYTFKFSGNGNSDQSADVILRGNDIALQYKHREPFYADRENKVQIKIIETSWQRVDGQQATREHLLMTLADLDTLLIKSTYNDDCTDSQLLSANLEFAEPYGQGLTAAEVEQCICPPGYVGTSCEDCAPGYSRTGGGLYLGLCEKCECNGHASQCDKEYGYCLDCQHNTEGDQCERCKPGFVGDARRGTPNDCQPEATRAPCHCNNHSPRGCDSFGRCLLCEHNTEGTHCERCKKGYYGDATKGSPYDCTPCPCPGASDCYLDNEGQVACRICPAGLQGRLCNECAPGYTRSNKPAGRVCEPIGQVTNEDITFVQKPHEVLRVRIMEPKRQIALPGDRVHWICQVTGYTTEKIHVEWTKVGEMSLPPNAKAYDGYLVLKGVEAENAGQYRCTATTITQYATDDALLTISKRISGRPPQPVIDPPHLVVNEGEPAAFRCWVPGIPDCQITWHREQLGGPLPHGVYQTGNALKIPQSQLHHAGRYICSAANQYGTGQSPPAVLEVKKPVIPPKVDPIRQTVDRDQPARFKCWVPGNSNVQLRWSRPGGAPLPSGVQEQQGILHIPRASDQEVGQYVCTATDPSDNTPLQSEPVQLNIRDPAPPQRGAAPQIDPPNQTVNVNDPAQFRCWVPGQPRAQLKWSRKDGRPLPNGILERDGFLRIDKSQLHDAGEYECTSTEPDGSTQLSPPARLNVNQPQAIQPQVDPPVQTVNEGEPSRIRCWVPGHPNIQLQFVKRGRRPLPAHARFSQGNLEIPRTLKSDEDEYICIATDPTTNRPVESNPARVIVKSPIRPIIDPAEQTVPEGSPFKIRCYVPGHPSVQLTFRRVSGQLNEDADENNGLLAVQRAELTDEGDYICTARDPDTGAPIDSTPATVHVTNAAAPPQVEAQGTPPRPVATPPLLSVAPGSPARFNCVAHSDTPARIRWGFREENGPLPEHVNQDGDDIVISEAGDRNVGEYVCSATNDFGTGVADPVRLEVTEDQEPPTAVVEPRTWNGKPGERHQFRCITTGSPTPKITWTGPNGSPLPHDVTPLEPNILDFSNGRSELNGDYTCTASNPIGEASDHGNVNIGPSLTVKTNPPGPKLIVTVGEPLQVKCEAFGAPGDPEPEVEWLHDPGPERGDLPDDFKPVTISEQFIRHPNVGLGNAGVYTCKGSSAHATATKNIYIEVVEPSRIATVSILGGSSQWFDQGEKGELICTATGSSLVDRLEWEKVDDQLPTDVEEHNEPGLLHFPSFKNSYAGEYRCNGYRNNEIIASAAVHVHSSANADDEPKVEIEPPRVRVVSQGDNIVLKCSVQGAENGEHFKWALLRGGSLVRQLGTEPTLEITKADPSNDFGVYRCNVEDNNGLVIGSAFTAVSVGQQDKSHAQIVKFDDKSDASFTCPIYSVPGSKVDWTYENGDLPSKAVPNGNKIEIKEFDDASAGTYVCKVSFDGNVVEGFVTAQMFVPDTIIQVLLEVSSESPQIGDRAWFDCKVTGDPSAVISWTKEGNDDLPPNAQVTGGRLLFTDLKEDNAGVYRCVAKTKAGPLQTRTVLNVGSGKRKRKHLGNRRGRRLRHRRRNAQNGPLSRKTRTTTKLFGSWF
Protein: BRCA1 associated protein 1 (H0Y8E8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
GSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSIRPIQGSQGSSSPVEKEVVEATDSREKTGMVRPGEPLSGEKYSPKLPIARGALLLARPDQRCNAGFWQELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ
Protein: Rifin (Q8I4Q0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKMKHVYFKVLLLFSLPLNILVTLHHVDKKTNDYRPYTLTYTKLENTITSSRLLCECDTYAATNYDNDPEVKKVMQQFDEHTTQRLLEYNEHMIKKRKECKEQCDKDIRKIILNDKIEKQLKEKFSSALQTDIGANYLPKCTCEKSLSDKVEKTCLKCGGLLGGGITPTVGFFSTIVTYLLTDAAAKQAGILAAKKVSVEAGIQTFIQQLSDMSNLHVLIGHKLVNLITPKTVGNIMELSKTIHETLQSTCFAAEPRINDVMTILCSTDSYIFDAQYLQQQVANIATKAAEEGAKAGALASQNAEANTWSLGTISNFFFTNSAGIAFTTIVLIAIILLITYLILHYRKKKENEEKTTIYKIIKGIDMFYYVDVYR
Protein: Growth hormone (Q0QBD2)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MMAAGPRTSLLLAFTLLCLPWTQVVGAFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDVTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEAGCAF
Protein: (2E)-enoyl-[ACP] glycyltransferase (EC 4.3.2.11) ((2E)-unsaturated fatty acyl-[ACP] glycyltransferase) (Long-chain fatty acyl-CoA thioesterase FcoT) (EC 3.1.2.-) (Palmitoyl-CoA hydrolase) (EC 3.1.2.2) (P9WM67)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Thiesterase that shows a preference for long chain fatty acyl groups. In vitro, cleaves the thioester linkage of palmitoyl-CoA, stearoyl-CoA, lauroyl-CoA and hexanoyl-CoA. Contains low levels of trans-enoyl hydratase activity.
Interaction partners:
- (3R)-3-[(carboxymethyl)amino]fatty acid oxygenase/decarboxylase
- Acyl carrier protein Rv0100
- Isonitrile lipopeptide synthase
- Uncharacterized PPE family protein PPE1
- Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase FadD10
Sequence:
MSHTDLTPCTRVLASSGTVPIAEELLARVLEPYSCKGCRYLIDAQYSATEDSVLAYGNFTIGESAYIRSTGHFNAVELILCFNQLAYSAFAPAVLNEEIRVLRGWSIDDYCQHQLSSMLIRKASSRFRKPLNPQKFSARLLCRDLQVIERTWRYLKVPCVIEFWDENGGAASGEIELAALNIP
Protein: Decapping nuclease (EC 3.6.1.-) (A0A024RCW8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367113}.
Interaction partners:
Sequence:
MDPRGTKRGAEKTEVAEPRNKLPRPAPSLPTDPALYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPTNGPGPNFDLRDGYPDRYQPRDEEVQERLDHLLCWLLEHRGRLEGGPGWLAEAIVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPNARAQRLARPPLLRELMYMGYKFEQYMCADKPGSSPDPSGEVNTNVAFCSVLRSRLGSHPLLFSGEVDCTDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPNVVAGFRNPDGFVSSLKTFPTMKMFEYVRNDRDGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHQDAPYAFLPIWYVEAMTQDLPSPPKTPSPK
Protein: Cysteine-rich PDZ-binding protein (Cysteine-rich interactor of PDZ three) (Cysteine-rich interactor of PDZ3) (Q792Q4)
Organism: Rattus norvegicus (Rat)
Function: Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10570482}. Synapse {ECO:0000269|PubMed:10570482}. Cell projection, dendritic spine {ECO:0000269|PubMed:10570482}. Note=Colocalizes with DLG4 in asymmetric synapses.
Interaction partners:
- Disks large homolog 4
- Armc7 protein
- Transmembrane protein 247
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 1
- Splicing factor 3b, subunit 2
- Pre-mRNA-processing-splicing factor 8
- Splicing factor 3B subunit 3
Sequence:
MVCEKCEKKLGRVITPDTWKDGARNTTESGGRKLNENKALTSKKARFDPYGKNKFSTCRICKSSVHQPGSHYCQGCAYKKGICAMCGKKVLDTKNYKQTSV
Protein: Succinyl-CoA:glutarate CoA-transferase (EC 2.8.3.-) (Dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase SUGCT) (Succinate--hydroxymethylglutarate CoA-transferase) (EC 2.8.3.13) (Q7TNE1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the succinyl-CoA-dependent conversion of glutarate to glutaryl-CoA. Can use different dicarboxylic acids as CoA acceptors, the preferred ones are glutarate, succinate, adipate, and 3-hydroxymethylglutarate (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9HAC7}.
Interaction partners:
- Citramalyl-CoA lyase, mitochondrial
- Glutaryl-CoA dehydrogenase, mitochondrial
Sequence:
MLWMLARAVAFRRPGRGLAGGRGLWTGRPQSDCDSMKPLEGVRILDLTRVLAGPFATMNLGDLGAEVIKVERPGAGDDTRSWGPPFVNTESTYFLSVNRNKKSIAVNIKDPRGVRIVKELAAICDVFVENYVPGKLSEMGLGYEDIDKIAPHIIYCSITGYGQTGPMSHRAGYDAIASAMSGLMHITGPEDGDPVRPGVAMTDLATGLFAYGAIMAGLLQRYRTGKGLFIDCNLLSSQVACLTQVAANYLIGQKEAKRWGTAHGSIVPYQAFKTKDGYLVIGAGNNQQFAVVCKILNLPELIDDCKYRTNHLRVQNRKELVKILSARFAEEVTAKWLCLFEGSGIPYGPINSLKDVFSEAQVLHNGLVMEMNHPTVGKISVPGPAVRYSKFKMSEAKPPPLLGQHTRHILKEVLRYDEGAIEKLLCSGVIEQHETK
Protein: Pre-B lymphocyte protein 3 (N27C7-2) (Protein VPreB3) (Q9UKI3)
Organism: Homo sapiens (Human)
Function: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells.
Interaction partners:
- Immunoglobulin lambda-like polypeptide 1
- B-cell antigen receptor complex-associated protein alpha chain
- B-cell antigen receptor complex-associated protein beta chain
- Fc receptor-like A
- B-lymphocyte antigen CD19
- T-cell leukemia/lymphoma protein 1A
- B-lymphocyte antigen CD20
- Tyrosine-protein kinase Blk
- B-cell differentiation antigen CD72
- B-cell receptor CD22
Sequence:
MACRCLSFLLMGTFLSVSQTVLAQLDALLVFPGQVAQLSCTLSPQHVTIRDYGVSWYQQRAGSAPRYLLYYRSEEDHHRPADIPDRFSAAKDEAHNACVLTISPVQPEDDADYYCSVGYGFSP
Protein: Lantibiotic lichenicidin VK21 A1 (LchA1) (P86475)
Organism: Bacillus licheniformis
Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually, LchA1 exhibits activity towards B.subtilis L1 (IC(50)=9 uM), Rhodococcus sp. SS2 (IC(50)=9 uM), M.luteus B1314 (IC(50)=1.2 uM), B.megaterium VKM41 (IC(50)=1.8 uM), S.aureus 209p (IC(50)=3.1 uM), B.pumilus 2001, B.globigii I, B.amyloliquefaciens I, M.smegmatis 1171 and M.phlei 1291. However, when combined with LchA2, it displays much stronger activity against B.subtilis L1 (IC(50)=0.64 uM), Rhodococcus sp. SS2 (IC(50)=0.64 uM), M.luteus B1314 (IC(50)=0.09 uM), B.megaterium VKM41 (IC(50)=0.12 uM) and S.aureus 209p (IC(50)=0.64 uM). The activity of the combined LchA1 and LchA2 peptides is strongest at a molar ratio of 1. Even when applied at 17-fold concentration of the highest IC(50) values for Gram-positive bacteria, neither the individual nor the combined peptides display activity against Gram-negative bacteria P.aeruginosa PAO1, P.putida I-97 or E.coli C600.
Subcellular location: Secreted {ECO:0000269|PubMed:20578714, ECO:0000305}.
Interaction partners:
Sequence:
MSKKEMILSWKNPMYRTESSYHPAGNILKELQEEEQHSIAGGTITLSTCAILSKPLGNNGYLCTVTKECMPSCN
Protein: OCIA domain-containing protein 2 (Q9D8W7)
Organism: Mus musculus (Mouse)
Subcellular location: Endosome {ECO:0000305}.
Interaction partners:
Sequence:
MASVSTHGNQEKSPHLPPLSKQSLLFCPKSKLHIHRGEIAKIIRECQEESFWKRALPFSLISMLVTQGLVHQGYLAANPRFGSLPKVALAGLLGFGLGKASYIRVCQSKFHSFEDQLRGAGFGPEHNRHCLLTCEDCKTRRGLSEKAGSQPSAS
Protein: Probable enoyl-CoA hydratase EchA7 (Enoyl hydrase) (Unsaturated acyl-CoA hydratase) (Crotonase) (P71540)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable acyl-CoA dehydrogenase FadE13
- Acyl-CoA dehydrogenase FadE12
- Probable biotin-dependent acyl-coenzyme A carboxylase beta2 subunit
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit
- Exopolyphosphatase
- Uncharacterized lipoprotein LprP
- Acyl-CoA dehydrogenase FadE7
- Probable acyl-CoA dehydrogenase FadE23
- Possible acyl-CoA dehydrogenase FadE19
- Probable acyl-CoA dehydrogenase FadE1
Sequence:
MDSPVDYAGPAACGGPFARLTLNSPHNRNALSSTLVSQLHQGLSAAEADPAVRLVVLGHTGGTFCAGADLSEAGGGGGDPYRMAVARAREMTALLRAIVESPLPVVGAINGHVRAGGFGLVGACDMVVAGPESTFALTEARIGVAPAIISLTLLPKLSPRAAARYYLTGEKFGAREAADIGLITMAADDVDAAVAALVADVGRGSPQGLAASKALTTAAVLEGFDRDAERLTEESARLFVSDEAREGMLAFLQKRPPRWVQPATMRAAD
Protein: V-type proton ATPase subunit B, kidney isoform (V-ATPase subunit B 1) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 1) (P15313)
Organism: Homo sapiens (Human)
Function: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Essential for the proper assembly and activity of V-ATPase. In renal intercalated cells, mediates secretion of protons (H+) into the urine thereby ensuring correct urinary acidification. Required for optimal olfactory function by mediating the acidification of the nasal olfactory epithelium (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:16769747, ECO:0000269|PubMed:29993276}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q91YH6}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase 116 kDa subunit a 4
- V-type proton ATPase subunit F
- V-type proton ATPase subunit E 2
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit d 2
- V-type proton ATPase 116 kDa subunit a 3
Sequence:
MAMEIDSRPGGLPGSSCNLGAAREHMQAVTRNYITHPRVTYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGALQDLAPDTAL
Protein: snRNA-activating protein complex subunit 3 (Small nuclear RNA-activating complex polypeptide 3) (Q7JUY8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- LD18233p
- PSEA-binding protein 45kD
- Transcription initiation factor IIB
- LD18062p1
- Transcription initiation factor IIA subunit 2
- TATA-box-binding protein
- Transcription initiation factor IIA subunit 1
- TBP-related factor
- General transcription factor IIF subunit 1
- General transcription factor IIF subunit 2
Sequence:
MDTTYITTNPALSLRDFLADYQKKISGTADEVPFFLQKNPVLVDVSESCSLDLIESPDDSSIAVFQPAADKCRPTFSPPQENQHVPSTFTALSQHKDKSRKCPFGRTQYSHKLNPTPTDSPNLHIDACGELELTVRLYRPPRAYHRGFKVEIPVFAEEFVCLGSNYLTELRDKISCVCNGKRFVDISDDPDAPLPSIDTNPGYFFINDTFYNDQRNPDNPDYSKTVLQWAARANGVNGETLKVESMEGKRFIDLTVSPGSPLHYLHHGNCEHLFVISQVEVLTPLSKRPDRSLYPYPHAFSTFNRRTCYMCGIRSYSFIVNQSRRQLHDPSYLCRRCFLSFFYVDGVKLGQFKAYRMYDHVELEGEEEDIKQQNLPS
Protein: Calcium and integrin-binding family member 2 (Q568Z7)
Organism: Rattus norvegicus (Rat)
Function: Calcium- and integrin-binding protein that plays a role in intracellular calcium homeostasis (By similarity). Acts as a auxiliary subunit of the sensory mechanoelectrical transduction (MET) channel in hair cells (By similarity). Essential for mechanoelectrical transduction (MET) currents in auditory hair cells and thereby required for hearing (By similarity). Regulates the function of hair cell mechanotransduction by controlling the distribution of transmembrane channel-like proteins TMC1 and TMC2, and by regulating the function of the MET channels in hair cells (By similarity). Required for the maintenance of auditory hair cell stereocilia bundle morphology and function and for hair-cell survival in the cochlea (By similarity). Critical for proper photoreceptor cell maintenance and function (By similarity). Plays a role in intracellular calcium homeostasis by decreasing ATP-induced calcium release (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Z309}. Cell projection, stereocilium {ECO:0000250|UniProtKB:O75838}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q9Z309}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q9Z309}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9Z309}. Note=Colocalizes with ITGA7 at the myotendinous junctions (MTJ) and at the neuromuscular junctions (NMJ) (By similarity). Located mainly in stereocilia and at the apical surface of hair cells of the cochlea (By similarity). Localizes in the cuticular plate along and at the tip of the stereocilia of vestibular sensory hair cells (By similarity). {ECO:0000250|UniProtKB:O75838, ECO:0000250|UniProtKB:Q9Z309}.
Interaction partners:
- Transmembrane channel-like protein
- LHFPL tetraspan subfamily member 5 protein
- Transmembrane channel-like protein
- Transmembrane inner ear
- USH1 protein network component sans
- Protocadherin-15
- Myosin VIIA
- Whirlin
- USH1 protein network component harmonin.
- Clarin-1
Sequence:
MGNKQTIFTEEQLDNYQDCTFFNKKDILKLHARFYELAPNLVPMDYRKSPIVHVPMSLIIQMPELRENPFKERIVEAFSEDGEGNLTFNDFVDMFSVLCESAPRELKANYAFKIYDFNTDNFICKEDLELTLARLTKSELDEDEVVLVCDKVIEEADLDGDGKLGFADFEDMIAKAPDFLSTFHIRI