wanglab/gogpt-training-data huggingface dataset:
Protein: Protein argonaute-2 (Q9VUQ5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for RNA interference (RNAi); double-stranded RNA induces potent and specific gene silencing. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger.
Subcellular location: Nucleus {ECO:0000269|PubMed:26257286}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:17178403, ECO:0000269|PubMed:26257286}.
Interaction partners:
- Endoribonuclease Dcr-2
- LD06392p
- Endoribonuclease Dcr-1
- Ribonuclease 3
- Staphylococcal nuclease domain-containing protein 1
- Fragile X messenger ribonucleoprotein 1 homolog
- LD07162p
- Transcription initiation factor TFIID subunit 11
- LD23072p
- Protein argonaute-1
Sequence:
MGKKDKNKKGGQDSAAAPQPQQQQKQQQQRQQQPQQLQQPQQLQQPQQLQQPQQQQQQQPHQQQQQSSRQQPSTSSGGSRASGFQQGGQQQKSQDAEGWTAQKKQGKQQVQGWTKQGQQGGHQQGRQGQDGGYQQRPPGQQQGGHQQGRQGQEGGYQQRPPGQQQGGHQQGRQGQEGGYQQRPSGQQQGGHQQGRQGQEGGYQQRPPGQQQGGHQQGRQGQEGGYQQRPSGQQQGGHQQGRQGQEGGYQQRPPGQQQGGHQQGRQGQEGGYQQRPPGQQQGGHEQGRQGQEGGYQQRPSGQQQGGHQQGRQGQEGGYQQRPSGQQQGGHQQGRQGQEGGYQQRPSGQQQGGHQQGRQGQEGGYQQRPPGQQPNQTQSQGQYQSRGPPQQQQAAPLPLPPQPAGSIKRGTIGKPGQVGINYLDLDLSKMPSVAYHYDVKIMPERPKKFYRQAFEQFRVDQLGGAVLAYDGKASCYSVDKLPLNSQNPEVTVTDRNGRTLRYTIEIKETGDSTIDLKSLTTYMNDRIFDKPMRAMQCVEVVLASPCHNKAIRVGRSFFKMSDPNNRHELDDGYEALVGLYQAFMLGDRPFLNVDISHKSFPISMPMIEYLERFSLKAKINNTTNLDYSRRFLEPFLRGINVVYTPPQSFQSAPRVYRVNGLSRAPASSETFEHDGKKVTIASYFHSRNYPLKFPQLHCLNVGSSIKSILLPIELCSIEEGQALNRKDGATQVANMIKYAATSTNVRKRKIMNLLQYFQHNLDPTISRFGIRIANDFIVVSTRVLSPPQVEYHSKRFTMVKNGSWRMDGMKFLEPKPKAHKCAVLYCDPRSGRKMNYTQLNDFGNLIISQGKAVNISLDSDVTYRPFTDDERSLDTIFADLKRSQHDLAIVIIPQFRISYDTIKQKAELQHGILTQCIKQFTVERKCNNQTIGNILLKINSKLNGINHKIKDDPRLPMMKNTMYIGADVTHPSPDQREIPSVVGVAASHDPYGASYNMQYRLQRGALEEIEDMFSITLEHLRVYKEYRNAYPDHIIYYRDGVSDGQFPKIKNEELRCIKQACDKVGCKPKICCVIVVKRHHTRFFPSGDVTTSNKFNNVDPGTVVDRTIVHPNEMQFFMVSHQAIQGTAKPTRYNVIENTGNLDIDLLQQLTYNLCHMFPRCNRSVSYPAPAYLAHLVAARGRVYLTGTNRFLDLKKEYAKRTIVPEFMKKNPMYFV
Protein: 2-oxoglutarate receptor 1 (Alpha-ketoglutarate receptor 1) (G-protein coupled receptor 80) (G-protein coupled receptor 99) (P2Y purinoceptor 15) (P2Y15) (P2Y-like GPCR) (P2Y-like nucleotide receptor) (Q96P68)
Organism: Homo sapiens (Human)
Function: Receptor for alpha-ketoglutarate. Seems to act exclusively through a G(q)-mediated pathway (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15141213, ECO:0000269|PubMed:36919698}; Multi-pass membrane protein {ECO:0000255}. Note=Upon itaconate binding, internalizes via endocytosis in a beta-arrestin dependent manner. {ECO:0000269|PubMed:36919698}.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate synthase
Sequence:
MNEPLDYLANASDFPDYAAAFGNCTDENIPLKMHYLPVIYGIIFLVGFPGNAVVISTYIFKMRPWKSSTIIMLNLACTDLLYLTSLPFLIHYYASGENWIFGDFMCKFIRFSFHFNLYSSILFLTCFSIFRYCVIIHPMSCFSIHKTRCAVVACAVVWIISLVAVIPMTFLITSTNRTNRSACLDLTSSDELNTIKWYNLILTATTFCLPLVIVTLCYTTIIHTLTHGLQTDSCLKQKARRLTILLLLAFYVCFLPFHILRVIRIESRLLSISCSIENQIHEAYIVSRPLAALNTFGNLLLYVVVSDNFQQAVCSTVRCKVSGNLEQAKKISYSNNP
Protein: Uncharacterized protein YBR138C (P38277)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized protein YHR202W
Sequence:
MEKDQIQPRVLESVDTNSLSLLSSNTSSNMNSNTNNKLSIIASDISTGSVLSRPLTPPVVQDIENNSMLQWQFEKKEFIFDSNSTPSKQAKPLQRNSPYQGNSQSENQNQQLLNVRKRRSQLIGAKPKIPSKLYQSVSKLDLIDDKSFTSLPIAPPCNIETNEDDSGNNEYNNNKKRPRLNPVNELRVHNNKRNRYVSYGPSLDTKNYELTENTSQDIPPLVLVEDYIPYTQSKSTKKMVSISDLKSKLSKRRDNHIPLRVKNSYSEINKETNRNSFEPNSLTLIPHILRNTEENRDESNNPLDFIKEEIEISDISIPNSIENMVVNLVNIPSSNKSYDDLYLSELNVHSQLRKCVICEKALYEISSRLLNSGYYKEIVCEQCTVRYEEAAKIFENCEFESSMDESNLSSGTFSDLENSAEPFHLSTDVPKKINRHIEDNKIDLKKEISKKKDSFSKELIERLQLQLLENDKSIKHHFNKDAMGSKSMNWFLEARRKLKWKWRINGLLPHFLRNQNSDRLNFQP
Protein: Ski-like protein (Ski-related oncogene) (Ski-related protein) (Q60665)
Organism: Mus musculus (Mouse)
Function: May have regulatory role in cell division or differentiation in response to extracellular signals.
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 3
- E3 ubiquitin-protein ligase Arkadia
- Nuclear receptor corepressor 1
- Nuclear receptor corepressor 2
- Mothers against decapentaplegic homolog 7
- E3 ubiquitin-protein ligase SMURF2
- Homeobox protein TGIF1
- Paired amphipathic helix protein Sin3a
Sequence:
MENLQSKFSLVQGSNKKLNGMEDDGSPPVKKMMTDIHANGKTLTKVKKEHLDDYGDASVEPDGEHAKRNRVSLPETLNLNPSLKHTLAQFHLSSQSSLGGPAAFSARYSQESMSPTVFLPLPSPQVLPGPLLIPSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQRLCNALLRPRTFPQNGSILPAKSSLAQLKETGSAFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYLGTPEEKKLKIILEEMKEKFSMRNGKRIQSKTDTPSGMELPSWYPVIKQEGDHVPQTHSFLHPSYYLYMCDKVVAPNVSLTSAASQSKEATKAETSKSTSKQSEKPHESSQHQKTVSYPDVSLEEQEKMDLKTSRELYSCLDSSISNNSTSRKKSESAVCSLVRGTSKRDSEDSSPLLVRDGEDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPSKD
Protein: Putative flavin carrier protein 3 (FAD transporter 3) (TRP-like ion channel FLC3) (P53121)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be responsible for the transport of FAD into the endoplasmic reticulum lumen, where it is required for oxidative protein folding.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16717099}; Multi-pass membrane protein {ECO:0000269|PubMed:16717099}.
Interaction partners:
- Uncharacterized membrane protein YGL140C
- Regulator of rDNA transcription protein 6
Sequence:
MRFLQVYKSSALIGLIILLASKVNLAEAKRKLVATSLVTCMENSQLSANSFDVVFNPDDRSLHYDLDMSTQIDSYIFADIDVYAYGFKIITKNVDLCSINWKQFCPVHPGNIQIDSIEYISSEYVNEIPGIAYQVPDIDAYARVKITNNVSEYLACIQIYFSNGKTVSQIGVKWATAVVAGIGLLLSAILSTFGNSTAASHISANTMSLFLYFQSVVVVAMQHVHRVPPIAAAWAENLVWSMGLIRISFMQRIFRWYVQSTGGTPSLYLTSTSMSVLAQRSWQYLMELPLIKRATNVLYGNANTLIFRGIKRLGYKMGIENTSIVCTGFTFFVLCGYVLAGFIIVFKCCVELATRLGWIQKARFWEFRKQWRMILKGALLRYIYIGFVQLTILSFWEFTERDSPAVIVIACLFILLSCGLMLWAAWRTVFFARRSVALYNNPAALLYGDEYVLHKYGFFYTMFNANHYWWNIVLLSYIFVKSLLVGFAQASGQTQVLFMFILDLFYFVAIIYYKPYLDRPTNIMNILIATVTVVNSFLFMFFSDLFNQSYKVAAIMGWIFFIMNAAFSFILLMMILAFAGMMLFSKNPDLRFKPAKDDRTSFQRNTMKPEGTVNRSVANELLALGNVAKDHDDNSDYESNDTGVNDELKQAQDETTPTTVTSSDDNKPTFSEKILSKFSRPKNENASTDALRVEAPKQQTFPHNLTNLSRENLSTLGSKPYPGHTRSQSDAHNGLINSFEEEDTSSNTDPFHDSTEGDLLDTSSSDGGFRSQNYVRDDSINSLGNNKQPLRKPPGFFDEGFM
Protein: Secretory carrier-associated membrane protein 4 (Secretory carrier membrane protein 4) (Q9C6X2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in membrane trafficking.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Proline-rich family protein
- Beclin-1-like protein
- Protein MICRORCHIDIA 3
- GDSL esterase/lipase At4g26790
- Peptidyl-prolyl cis-trans isomerase CYP19-1
- Small ribosomal subunit protein uS7z
Sequence:
MNRHHDPNPFDEDEEIVNPFSKGGGRVPAASRPVEYGQSLDATVDIPLDNMNDSSQKQRKLADWEAELRKKEMDIKRREEAIAKFGVQIDDKNWPPFFPIIHHDIAKEIPVHAQKLQYLAFASWLGIVLCLVFNVIATMVCWIKGGGVKIFFLATIYALIGCPLSYVLWYRPLYRAMRTDSALKFGWFFFTYLIHIGFCIVAAIAPPIFFHGKSLTGVLAAIDVISDSLLAGIFYFIGFGLFCLESLLSLWVLQKIYLYFRGNK
Protein: Protein YIF1 (A6NGW1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368073}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU368073}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU368073}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU368073}.
Interaction partners:
Sequence:
MAYHSGYGAHGSKHRARAAPDPPPLFDDTSGGYSSQPGGYPATGADVAFSVNHLLGDPMANVAMAYGSSIASHGKDMVHKELHRFVSVSKLKYFFAVDTAYVAKKLGLLVFPYTHQNWEVQYSRDAPLPPRQDLNAPDLYIPTMAFITYVLLAGMALGIQKRMILSVLTGLLFGSDGYYVALAWTSSALMYFIVRSLRTAALGPDSMGGPVPRQRLQLYLTLGAAAFQPLIIYWLTFHLVR
Protein: tRNA intron endonuclease catalytic domain-containing protein (Q383V5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MASGSGRGEGVGEHRPNPIVRVVGVNGPLFVCEDSSVLSKFPQMYKKDYSGPHLGVEELEYLSEFVSIEFITAEDRQYWASLRMRHEFSCRVYRHLTDKMGLFLRHGSQFGAAFIGYRDLKDHGNCLVYFGPLSQLSATAAARVAASVGKEAWVVEEFPIKATGCLSVSKIESYWGPSGQGGNSVCGDKGGKCVKKRRLSYTPIVQL
Protein: Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' beta isoform (AtB' beta) (PP2A, B' subunit, beta isoform) (O04376)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The B regulatory subunit may modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment (By similarity). Required for the formation of the PP2A holoenzyme that positively regulates brassinosteroid signaling by dephosphorylating and activating BZR1.
Subcellular location: Nucleus {ECO:0000269|PubMed:26517938}. Cytoplasm {ECO:0000269|PubMed:26517938}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''epsilon
- Serine/threonine protein phosphatase 2A regulatory subunit B''beta
- Serine/threonine protein phosphatase 2A regulatory subunit B''alpha
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma
Sequence:
MFKKIMKGGHRKPSKSEANEPSSYGIGLPDNRSGPGSNVVVSHASRGALVNSSPSPVTATPPPPPLGSVEPLPLFRDVPVSERQTLFLRKLQNCCFLFDFTDTIKNARDKEIKRQTLLELVDFIQSGSSKISESCQEEMIKMISVNIFRSLPPASHENTGQEPADPEEEEPYLEPSWPHLQLVYELLLRYVVSTDTDTKVAKRYIDHSFVLKLLDLFDSEDPREREYLKTILHRIYGKFMVHRPFIRKAINNIFYRFIYETERHSGIGELLEILGSIINGFALPMKEEHKLFLIRVLIPLHKPKPIVVYHQQLSYCIVQFVEKDYKLADTVIRGLLKYWPVTNCSKENLFLGELEEVLEATQPVEFQRCMVPLFQQIGRCLTSSHFQVAERALFLWNNEHIVGLIAQNRSVILPIIYPTLEKNIQSHWNQAVHGLTTNIKKMFMEMDPELFEECQRQYEEKQAKSKEVEEQRQYTWKRLAEAAAERDGGGGEEDHMITS
Protein: Carboxylic ester hydrolase (EC 3.1.1.-) (Q32Q55)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Beta-glucuronidase
- Cytidine deaminase
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 2B1
- Carboxylesterase 1D
- UDP-glucuronosyltransferase 2B15
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase 2B37
Sequence:
MGLKQIHARLTTAACGLLLLLQVQGQDSLSPIRTTHTGQILGSLIHMKGLDVGVHSFLGIPFAKPPIGPLRFAPPEAPEPWSGVRDGTSHPAMCLQDITAMNMQAFKLLKLTLPLIPMSEDCLYLNIYTPNHAHEGSNLPVMVWIHGGALVIGMASLYDGSMLAAMENVVVVTIQYRLGVLGFFSTGDQHARGNWGYLDQVAALHWVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSRGLFHGAIMESGVALMSSLISVSSDVVYRTVANLSGCEQVDSKALVNCLRGKSEEEIMSINKAFRIISGIVDGIFLPRHPKELLASADFHPIPSIIGVNNDEYGWIIPSSMTTTDSKKKMDRQMVQAILQKRVAQMMWPPEFSDLLLEEYMGDSEDPQFLQVQFKEMMEDFTFVIPALQVAHFQRSNAPVYFYEFQHRPSFFKDSKPPHVKADHGDEILFIFRSFWGGTQVDLTEEEELLSRRMMKYWANFARQGNPNSEGLPYWPVFDHDEQYLQLDTQPAVGRALKAKRLQFWTKTLPEKIRELKDTEDRHTEL
Protein: tRNA-dihydrouridine(16) synthase (EC 1.3.1.-) (U16-specific dihydrouridine synthase) (U16-specific Dus) (tRNA-dihydrouridine synthase C) (P33371)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. DusC specifically modifies U16 in tRNAs.
Interaction partners:
- dCTP deaminase
Sequence:
MRVLLAPMEGVLDSLVRELLTEVNDYDLCITEFVRVVDQLLPVKVFHRICPELQNASRTPSGTLVRVQLLGQFPQWLAENAARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPAHLPVSVKVRLGWDSGEKKFEIADAVQQAGATELVVHGRTKEQGYRAEHIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKYNEPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLSYLRKEYDEATELFQHVRVLNNSPDIARAIQAIDIEKL
Protein: ATP-dependent dethiobiotin synthetase BioD 1 (EC 6.3.3.3) (DTB synthetase 1) (DTBS 1) (Dethiobiotin synthase 1) (P13000)
Organism: Escherichia coli (strain K12)
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid. In another study both CTP and GTP (but not ITP, TTP or UTP) can partially replace ATP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}.
Interaction partners:
- 8-amino-7-oxononanoate synthase
- Biotin synthase
- Malonyl-[acyl-carrier protein] O-methyltransferase
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Pimeloyl-[acyl-carrier protein] methyl ester esterase
- ATP-dependent dethiobiotin synthetase BioD 2
- Bifunctional ligase/repressor BirA
- Thiamine-monophosphate kinase
- Riboflavin biosynthesis protein RibD
- 2-amino-3-ketobutyrate coenzyme A ligase
Sequence:
MSKRYFVTGTDTEVGKTVASCALLQAAKAAGYRTAGYKPVASGSEKTPEGLRNSDALALQRNSSLQLDYATVNPYTFAEPTSPHIISAQEGRPIESLVMSAGLRALEQQADWVLVEGAGGWFTPLSDTFTFADWVTQEQLPVILVVGVKLGCINHAMLTAQVIQHAGLTLAGWVANDVTPPGKRHAEYMTTLTRMIPAPLLGEIPWLAENPENAATGKYINLALL
Protein: Albumin (A0A0C4DGB6)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEPTMRIRERK
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q9VXP1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- FI05221p
- RING-type E3 ubiquitin transferase
Sequence:
MEEPKSVPTAELPSTSTGASSSSSTLSNNVSYDKIAWTRDITEPLAEESSTSQLRPLGTSIPTNSTASELKKSNTSYSFTGDYLSGGNKADLKGGYPFGGTDTDTKANEKDKEKEHTADDSLYECNICLDTAKDAVVSMCGHLFCWPCLHQWLLTRPNRKLCPVCKAAVDKDKVIPLYGRNSTHQEDPRNKVPPRPAGQRTEPDPVPGFPGFGFGDGFHMSFGIGAFPFGFITSTLNFGEPRPPAANRGTRQYEDEQTLSKLFSYLAVVWILWLFYA
Protein: Ranatuerin-2SEb (P85058)
Organism: Lithobates sevosus (Dusky gopher frog) (Rana sevosa)
Function: Mast cell degranulating peptide. Causes histamine release from rat peritoneal mast cells in vitro. Has antibacterial activity against the Gram-negative bacterium E.coli K12 and Gram-positive bacterium M.luteus NCT C2665.
Subcellular location: Secreted {ECO:0000269|PubMed:16386333}.
Interaction partners:
Sequence:
AIMDTIKDTAKTVAVGLLNKLKCKITGC
Protein: Cysteine/serine-rich nuclear protein 1 (CSRNP-1) (Axin-1 up-regulated gene 1 protein) (Protein URAX1) (TGF-beta-induced apoptosis protein 3) (TAIP-3) (Q96S65)
Organism: Homo sapiens (Human)
Function: Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity (By similarity). May have a tumor-suppressor function. May play a role in apoptosis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Growth arrest and DNA damage-inducible protein GADD45 beta
- Homeobox protein MSX-1
Sequence:
MTGLLKRKFDQLDEDNSSVSSSSSSSGCQSRSCSPSSSVSRAWDSEEEGPWDQMPLPDRDFCGPRSFTPLSILKRARRERPGRVAFDGITVFYFPRCQGFTSVPSRGGCTLGMALRHSACRRFSLAEFAQEQARARHEKLRQRLKEEKLEMLQWKLSAAGVPQAEAGLPPVVDAIDDASVEEDLAVAVAGGRLEEVSFLQPYPARRRRALLRASGVRRIDREEKRELQALRQSREDCGCHCDRICDPETCSCSLAGIKCQMDHTAFPCGCCREGCENPMGRVEFNQARVQTHFIHTLTRLQLEQEAESFRELEAPAQGSPPSPGEEALVPTFPLAKPPMNNELGDNSCSSDMTDSSTASSSASGTSEAPDCPTHPGLPGPGFQPGVDDDSLARILSFSDSDFGGEEEEEEEGSVGNLDNLSCFHPADIFGTSDPGGLASWTHSYSGCSFTSGVLDENANLDASCFLNGGLEGSREGSLPGTSVPPSMDAGRSSSVDLSLSSCDSFELLQALPDYSLGPHYTSQKVSDSLDNIEAPHFPLPGLSPPGDASSCFLESLMGFSEPAAEALDPFIDSQFEDTVPASLMEPVPV
Protein: Histone-lysine N-methyltransferase Clr4 (AFU_orthologue AFUA_1G11090) (C8VT24)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
Sequence:
MLVDLTIDSDPEEQPRLVSRLPFISEYHNNQELIGLSCSLDDGSIPNPLIKSLGRQTLAHRTLSPSPHTKNSTIPFKRKSDADSAESGSESSYASAVAYPQKAKTRTTNVSSRNPVGHDSLSGPFKRVGAGPGTGAARQARQIPASAPSLASSSGTDSAAGHYAPSPAPETLRVVIPSPSVQLKKEIDSAERLPDAEVKTPEITGMSEKYYPTDALERRAMRGAYPAARKTNRAGVPLVIGTPGPFLTEKNRRPVIDLLCKNLQKKLASIKGPAVTVAKADEKRLAKATTGFEFINEYKLREGVAPISKEFQSGCSCETICLPDRCQCLAQEEDSEERIIAYKRARDNPRFMVLRPEFMKRTSMIFECNSLCGCEEKCWNRVVQLGRTIRLEIFHTGARGFGLRSLDTIRAGQFIDLYLGEVITTSKADQREKIANTRNAPSYLFSLDFLVDDESSYVVDGANYGAATRFINHSCNPNCRMFPVSRTHGDDYLYDLAFFALREIKPGTELTFDYNPGMERVDKLDPNAVPCLCGEPNCRGQLWATERKKAR
Protein: ULP1-interacting protein 4 (Q08926)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16407407}; Peripheral membrane protein {ECO:0000269|PubMed:16407407}. Mitochondrion outer membrane {ECO:0000269|PubMed:16407407}. Nucleus envelope {ECO:0000269|PubMed:16407407}.
Interaction partners:
- ULP1-interacting protein 3
- Protein FUN14
- Protein HBT1
- Inactive diphosphatase DCS2
- Mitochondrial outer membrane protein OM45
Sequence:
MVTIVFDHPAEDFPELKIAGEFTNWEGVPMKINTSSGKWEYKFDESSVTKHNDKDKVHFKFIDQNGNWFADDEYPKEVDEHSNENNVATLNNEEDGGSAGEEKDEGDKTAHNTNENGSELYYEGPETPTPSLKGNVTFPSPKTAISQDGSAFAKETTRKERKYEHAPLNEVPVERDPKEENKELSPNFSQEQTENKQDKGLDNLSEGNDNDNTRVNEDTDVTDTQESEHEINGSDTENTDMSEQEEIQKIDKPADQNAKSIVKEGDANTEDYESVLKKLLGALGRFFGSWFSWLTTKMSSSEAS
Protein: Angiotensinogen (Serpin A8) [Cleaved into: Angiotensin-1 (Angiotensin 1-10) (Angiotensin I) (Ang I); Angiotensin-2 (Angiotensin 1-8) (Angiotensin II) (Ang II); Angiotensin-3 (Angiotensin 2-8) (Angiotensin III) (Ang III) (Des-Asp[1]-angiotensin II); Angiotensin-4 (Angiotensin 3-8) (Angiotensin IV) (Ang IV); Angiotensin 1-9; Angiotensin 1-7; Angiotensin 1-5; Angiotensin 1-4] (P01017)
Organism: Bos taurus (Bovine)
Function: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.
Subcellular location: Secreted {ECO:0000305|PubMed:13403900}.
Interaction partners:
Sequence:
MAPAGLSLGAAILCLLAWAGLAAGDRVYVHPFHLLVYSKSNCDQLEKPSVETPPDPTFTPVPIQTKSSAVDEEALWEQLVRATEKLEAEDRLRASEVGLLLNFMGFHMYKTLSETWSVASGAVFSPVALFSTLTSFYVGALDPTASRLQAFLGVPGEGQGCTSRLDGHKVLSSLQTIQGLLVAQGGASSQARLLLSTVVGLFTAPGLHLKQPFVQSLSSFAPITLPRSLDLSTDPNLAAEKINRFMQSVTGWNMGRALTAVSPDSTLLFNAYVHFQGKMKGFSLLPGLKEFWVDNTTSVSVPMLSGTGIFHFWSDSQNNLSVTRVPLSANTYLLLIQPHHTPDLRKVEALTFQHNFLTRMKNLSPRAIHLTMPQLTLKASYDLQDLLAQAKLPTLLGAEANLSKISDANLRVGKVLNSVLFELKADGEQAPESVPQPAGPEALEVTLNSPFLLAVLERSSGALHFLGRVSRPLSAE
Protein: Thioredoxin domain-containing protein 3 (3'-5' exonuclease NME8) (EC 3.1.-.-) (NME/NM23 family member 8) (Spermatid-specific thioredoxin-2) (Sptrx-2) (Q715S9)
Organism: Rattus norvegicus (Rat)
Function: Probably required during the final stages of sperm tail maturation in the testis and/or epididymis, where extensive disulfide bonding of fibrous sheath (FS) proteins occurs. May be involved in the reduction of disulfide bonds within the sperm FS components. In vitro, it has neither NDP kinase nor reducing activity on disulfide bonds (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12909633}. Note=In spermatozoa, it is an integral component of the FS.
Interaction partners:
- Dynein axonemal intermediate chain 1
- Dynein axonemal intermediate chain 2
- Dynein axonemal heavy chain 5
- Outer dynein arm-docking complex subunit 1
- Dynein axonemal intermediate chain 3
- Dynein axonemal heavy chain 1
- Dynein, axonemal, heavy chain 9
- Dynein axonemal intermediate chain 4
- Dynein axonemal heavy chain 17
- Dynein, axonemal, heavy chain 11
Sequence:
MASKKREVQLQSVVNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNELNEDELLHFVVAEADSIVTLQPFRDKCEPVFLFSLNGKIIAKIQGANAPLINRKVIALIDEEKKIAAGEMARPQYVEIPLVDSLDEEYGEVHYESNVEVYNMAVINPDAVLMRKNLEIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRLSCVLIISQGEDTEVIEEEALPQSDDEEEPDPLEEPHVRFAPMLVKKKRDSLQEYMDRQHMSDYCHVEDDAVKVSKFIDILFPDFKTMKSTNVQRTLGLLYPEVCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSVERWKELIGPKTVEEAYASHPDSLCVRFASGNFPVNQFYGSSSKAAAETEIEHFFPPQSTLALIKPHVSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAVGEWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTESNFEN
Protein: LRP2-binding protein (Q9D4C6)
Organism: Mus musculus (Mouse)
Function: May act as an adapter that regulates LRP2 function.
Subcellular location: Cytoplasm {ECO:0000250}. Note=Detected in a vesicular staining pattern close to the plasma membrane and throughout the cytoplasm. {ECO:0000250}.
Interaction partners:
Sequence:
MKLSSEKLPKNPFSLSQYAAKQQKFFQWKKEKPDYYLHANLVDTALQFLKERIRRGDAMAYFLRGQLYFEEGWYEEALAQFEEIQEKDHQAIYQLGVMYYDGLGTIANAEKGVNYMRKILDSSCPQTMHLKFAAAYNLGRAYFEGKGVKRSDEEAERLWLLAADNGNPKASVKAQSILGLFYSMKEPKELEKAFFWHSEACGNGSLESQGALGLMYFYGQGIRQDTDAALHCLREAAERGNVYAQGTLVEYYYKMKFFTKCVSFSKRIADYDEVHDIPMIAHVTDCLPEFIIKGMAMAAFYHGRCLQLGLGIMKDEESAKHYYSKACRLNPTLADELHSLLIHQRI
Protein: Fe2OG dioxygenase domain-containing protein (Q9U3P9)
Organism: Caenorhabditis elegans
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- Protein aurora borealis
- Alpha-ketoglutarate-dependent dioxygenase AlkB-like domain-containing protein
- BTB domain-containing protein
- TPR_REGION domain-containing protein
- Uncharacterized protein
- Cecropin-A
- Major sperm protein
- Anther-specific protein BCP1-like
- CLIP domain-containing serine protease
Sequence:
MYFNEEKAKRIGERFEGGKLAKKVHKSIEQLKRHDPDVQISTEPTKYLLVSNSSILCGVSLEELEEIFLPLDELAEFIVYPNKRSYSFVQCSSIEKSIQVRTELHGLIPPSLKNSHQPFAISYVENLPEATKCEDFRPANLKIIEEYVSSDLEKELVDLVTNHPSVQSLKHRAVVHFGHVFDYSTNSASEWKEADPIPPVINSLIDRLISDKYITERPDQVTANVYESGHGIPSHYDTHSAFDDPIVSISLLSDVVMEFKDGANSARIAPVLLKARSLCLIQGESRYRWKHGIVNRKYDVDPRTNRVVPRQTRVSLTLRKIRRKPCECEWKEFCDWDRKGEMSVPSNEDLALKLENSYVSDVYENIASHFDETRHSSWKAVKQFINEIPRGSVMYDVGCGNGKYLIPKDGLLKIGCDMCMGLCDIARKKDCHVARCDALALPFRYESADAAISIAVLHHIATFERRKRLIEELLRVVKPGSKICVTVWSMDQSQSEYAKMRGNKDDVAAAPAVSSEETQTTNRLKVHDGKDFEQQDVLVPWTIDQKGETFLRYYHVFREGEAEKLIESVQGCKLISVEKEQGNYIIIAKKI
Protein: Apical asparagine-rich protein AARP (Q8IFN2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MWKFITIIIFSIYYIDGKSILRNNKSHNNLPISKTNEEEEGKININNLKPIKQHDNIIEDVHIKENKFISIKNKDKNGSFIDLSMRYNEKESDNDEEEEEDEEDNEDNNTNNNNNNNNNNNNDDDHHNDDDHHDNNDNHDNDNNDNNNNNNDNNNNNNDNNNNNNDNNNNSSAAFTALPPPPPPVPPPPPPTLTPSGIVGNVLSTFVSHGLKLIGVP