wanglab/gogpt-training-data huggingface dataset:
Protein: Protein FRG1 (FSHD region gene 1 protein) (Q14331)
Organism: Homo sapiens (Human)
Function: Binds to mRNA in a sequence-independent manner. May play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. May be involved in mRNA transport. May be involved in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B.
Subcellular location: Nucleus, Cajal body {ECO:0000269|PubMed:15060122, ECO:0000269|PubMed:17103222, ECO:0000269|PubMed:21699900}. Nucleus, nucleolus {ECO:0000269|PubMed:15060122, ECO:0000269|PubMed:20970242, ECO:0000269|PubMed:21699900}. Cytoplasm {ECO:0000269|PubMed:20970242, ECO:0000269|PubMed:21699900}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:20970242}. Note=Localization changes during myogenesis from mainly cytoplasmic in undifferentiated myoblasts, to strongly nucleolar in early myotubes and back to cytoplasmic 5 days post-differentiation (PubMed:20970242). Localized at the Z-line in the sarcomere of matured myotubes 8 days post-differentiation (PubMed:20970242). {ECO:0000269|PubMed:20970242}.
Interaction partners:
- Pre-mRNA-splicing factor CWC22 homolog
- Protein FRG2
- Double homeobox protein 4-like protein 2
- Pre-mRNA-processing-splicing factor 8
- Small nuclear ribonucleoprotein F
- Corepressor interacting with RBPJ 1
- Peptidylprolyl isomerase domain and WD repeat-containing protein 1
- WD repeat-containing protein 70
- Pre-mRNA-splicing factor SPF27
- Small nuclear ribonucleoprotein Sm D1
Sequence:
MAEYSYVKSTKLVLKGTKTKSKKKKSKDKKRKREEDEETQLDIVGIWWTVTNFGEISGTIAIEMDKGTYIHALDNGLFTLGAPHKEVDEGPSPPEQFTAVKLSDSRIALKSGYGKYLGINSDGLVVGRSDAIGPREQWEPVFQNGKMALLASNSCFIRCNEAGDIEAKSKTAGEEEMIKIRSCAERETKKKDDIPEEDKGNVKQCEINYVKKFQSFQDHKLKISKEDSKILKKARKDGFLHETLLDRRAKLKADRYCK
Protein: N-glycosidase Npun_R5314 (EC 3.2.2.-) (Riboflavin biosynthesis intermediates N-glycosidase) (B2J4E5)
Organism: Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Function: Catalyzes the hydrolysis of the N-glycosidic bond in the first two intermediates of riboflavin biosynthesis, which are highly reactive metabolites, yielding relatively innocuous products. Thus, can divert a surplus of harmful intermediates into relatively harmless products and pre-empt the damage these intermediates would otherwise do. May act on other substrates in vivo. Has no activity against GTP, nucleoside monophosphates or ADP-ribose.
Interaction partners:
- Riboflavin biosynthesis protein RibD
Sequence:
MTIYFYKVWQPYGCFSNFSPHGIHIQDTYWATVEHYYQAQKFVGSKDAAIIPLIHAAATPEEAAALGRCSTRQLRRDWDLVKTQIMREAVLKKFLTHADIREVLLKTGDELLVENSPTDSFWGCGANKAGLNHLGKTLMSVREEIRNLLSLTGIYE
Protein: Uncharacterized protein Rv2091c (P9WLJ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein Rv1109c
- Conserved alanine valine rich protein
- Conserved protein
- Cell envelope integrity protein Cei
- Conserved protein
- Possible conserved membrane protein
- Probable conserved transmembrane protein
- Probable conserved transmembrane protein
- Uncharacterized protein
- Uncharacterized protein Rv0481c
Sequence:
MSGPQGSDPRQPWQPPGQGADHSSDPTVAAGYPWQQQPTQEATWQAPAYTPQYQQPADPAYPQQYPQPTPGYAQPEQFGAQPTQLGVPGQYGQYQQPGQYGQPGQYGQPGQYAPPGQYPGQYGPYGQSGQGSKRSVAVIGGVIAVMAVLFIGAVLILGFWAPGFFVTTKLDVIKAQAGVQQVLTDETTGYGAKNVKDVKCNNGSDPTVKKGATFECTVSIDGTSKRVTVTFQDNKGTYEVGRPQ
Protein: RNA-binding region RNP-1 domain-containing protein (Q54F26)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNPDFTVYVSNISLKANTKTVSDFFSFCGRIVNLFLRNDPTGSSQQAIVVFESDSAAKTALLLTNALIVDKVIQVVQFTPELEFDLTQQFSQQQQFNNLSGEQQPQQQQYVSQPQEDIVNREHSVPDNERSKTSVVASIIAAGYSVGQDAAIKARQVDEEHMISLKLKVGAEAVKAKANEIDNNLHISESAAAIKGAVVERANALDERFQISGFFKSASDMISQQASNLMKAAEENSTVSPIVNKVSSFGTFIKQEVQQIQTETSQAIDEKNKEKGINSSNDTELQQQQQQQQQQPEQPEQHSNIDFSKEQ
Protein: Tubercidin resistance protein (Q4Q661)
Organism: Leishmania major
Interaction partners:
- Succinyl-diaminopimelate desuccinylase-like protein
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MECINQESASARSATNVASGVDEPAVAAVPFSPLQVELQRPDPLSKSLCETVQRSQSSASNAAEANDTDVPPLLGGDPAAAHSSSIISSHDASFYNSLMVSRAENLDALESCTSRTGRNLISQSAGAAAERYAQEQSPSAELRLSTPRRRLAPNSAVSQGGKEEVAPNVEAETASQQHVSSGAAVRAVESVVAAAGPHSVGAEDHSSGSQAHAHECLTSPAGNVKTLEGLLDWRAHLSAWQQSVGTQESHHTDGNNNTVKHMCNDQASERNMVGRVNRKGALASEGSQVSSRSECLQGCHGGCHRTPAASSSSPSTDAITSAESNAAGGDTIAVTHNPQGQHSHPPSGAASQTEVVDAFFTKESSSASSSHPRSPAQVDGHPWSTQLSAHLEQHFSTGDNLATQAPPTAHVTIIDGRVLRERGGTGKSGRPRGAGSPTLSLSRCVEGIGLEDHHPPNSTGHSSPYSHSALPHGVERRSWVRSALPPSAPTHILLHSSPVGGFDGCRSRDNCNNPHSGSNKSTIGSAGIQRQHSREASLSQATPRTPESWRHRVKAMPPMAKPLRELAVEEKYPVFSVPVDEETNKAVVAFVSGLVLLICLVFICAM
Protein: Exported protein family 3 (C6KTE9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNYFLSLFNVSLFFLLIFKYSYKNIVKKDLQDKFNKSIITINIASRILTENNKKWYKKYIYTSIFSGNKNPQKRERKNEEENQKDNTKVDNDNNMGNEMENHIDDSIDDPMDDLMNDKWEHHNSLEDRIKEYYTLTDPSDGEENNSFFKKLKLIMNILDEVHSDLLINNSVTDGSIFSPELVPISVLSTMTLACPPIGTVTLPYITNRINFLNRYEGQNIHTEHDLKIFK
Protein: Caffeyl-CoA reductase-Etf complex subunit CarD (EC 1.3.1.108) (Electron transfer flavoprotein small subunit) (ETFSS) (Electron transfer flavoprotein subunit beta) (Beta-ETF) (H6LGM7)
Organism: Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
Function: Caffeyl-CoA reductase-Etf complex catalyzes the reduction of caffeyl-CoA to yield hydrocaffeyl-CoA. It couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. The electron transfer flavoprotein (Etf) mediates the electron transfer between the different donors and acceptors. The complex can also reduce 4-coumaroyl-CoA and feruloyl-CoA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23479729}.
Interaction partners:
- Caffeyl-CoA reductase-Etf complex subunit CarE
- Caffeyl-CoA reductase-Etf complex subunit CarC
- Lactate dehydrogenase
- Caffeyl-CoA-synthetase CarB2
- 2-enoate reductase Enr2
- Putative geranylgeranyl reductase
- Oxidoreductase
- Aldehyde dehydrogenase, iron-sulfur subunit
- FAD-dependent pyridine nucleotide-disulfide oxidoreductase
- Acyl-CoA synthetase
Sequence:
MRILVCAKQVPDTNEVKIDPKTGTMIREGVPSILNPDDANALEAALVIKDENPGTEVIVMTMGPPQASEMLRECLAMGADEAYLLSDRAFGGADTWATSATLAAGIKKVKKVDLVLAGRQAIDGDTAQVGSQIAQRLKMPVVTYVEDIKIEDKKAIVHRQMEDGYEVIEVQLPCLLTCVKELNDPRYMSVGGIMDAYEQPITIWNHEDIGLSPEACGLNASPTQVFRSFSPPAKGGGEMITGTTVNEVAGSLVSKLKEKHII
Protein: Probable glutamine amidotransferase (Q9I6J4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable glutamine synthetase
- Probable glutamine synthetase
- Putrescine--pyruvate aminotransferase
- Metallo-beta-lactamase domain-containing protein
- L,D-TPase catalytic domain-containing protein
- Outer membrane assembly lipoprotein YfiO
- PNPLA domain-containing protein
- FAD dependent oxidoreductase domain-containing protein
- Probable oxidoreductase
- FAD dependent oxidoreductase domain-containing protein
Sequence:
MSRLPLIGVTACTKQIGLHPYHIAGDKYLRAVVNGAGGLPLIIPALGESIDQAALLDSVDGLLFTGSPSNVEPRHYSGPASEPGTLHDSDRDATTLPLVRAAIDAGIPVLGICRGFQEMNVAFGGSLHQKVHEVGTFMDHREPADQPLEVQYAPRHAMHVQPGGVLAGIGLPSEFQVNSIHGQGVDRLAPGLRVEALAPDGLVEAISVEGAKAFALGVQWHPEWQVLTNPNYLAIFQAFGKACSKRAGQR
Protein: N-acetylglucosamine-6-sulfatase (EC 3.1.6.14) (Glucosamine-6-sulfatase) (G6S) (Q8BFR4)
Organism: Mus musculus (Mouse)
Subcellular location: Lysosome {ECO:0000250}.
Interaction partners:
- Beta-glucuronidase
- Beta-hexosaminidase subunit alpha
- Beta-hexosaminidase subunit beta
- Beta-galactosidase
- Alpha-N-acetylglucosaminidase
- Heparan-alpha-glucosaminide N-acetyltransferase
- Cathepsin Z
- Formylglycine-generating enzyme
Sequence:
MRLPSAAGPRPGRPRRLPALLLLPLLGGCLGLVGAARRPNVLLLLTDDQDAELGGMTPLKKTKALIGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKAWQKIQEPYTFPAILKSVCGYQTFFAGKYLNEYGAPDAGGLEHIPLGWSYWYALEKNSKYYNYTLSINGKARKHGENYSVDYLTDVLANLSLDFLDYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFQNVIAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIRFLDDAFRRRWQTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQMDGMSLLPILKGDRNLTWRSDVLVEYQGEGRNVTDPTCPSLSPGVSQCFPDCVCEDAYNNTYACVRTLSSLWNLQYCEFDDQEVFVEVYNITADPDQITNIAKSIDPELLGKMNYRLMMLQSCSGPTCRTPGVFDPGYRFDLRLMFNSHGSVRTRRFSKHPL
Protein: Actin-related protein 3 (Actin-like protein 3) (P32390)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity). May be involved in cytokinesis.
Subcellular location: Cytoplasm, cytoskeleton, actin patch.
Interaction partners:
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 1
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2
- Actin
- Actin-binding protein wsp1
- Profilin
- Protein dip1
Sequence:
MASFNVPIIMDNGTGYSKLGYAGNDAPSYVFPTVIATRSAGASSGPAVSSKPSYMASKGSGHLSSKRATEDLDFFIGNDALKKASAGYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALAASWTSSKVTDRSLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEPDSSLKTAERIKEECCYVCPDIVKEFSRFDREPDRYLKYASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFLTPLPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIHRSEMLSGAKSGGVDVNVISHKRQRNAVWFGGSLLAQTPEFGSYCHTKADYEEYGASIARRYQIFGNSL
Protein: Alba DNA/RNA-binding protein (At1g76010/T4O12_22) (Q93VA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein GAMETOPHYTE DEFECTIVE 1
- Ribonuclease MRP protein subunit POP4
- Uncharacterized protein At2g34160
- Ribonucleases P/MRP protein subunit POP1
- Alba DNA/RNA-binding protein
- Emb|CAB72159.1
- AT3G14870 protein
- At2g32130)
- At1g53380
- F28N24.3 protein)
Sequence:
MDKYQRVVKPKADTPIDANEIRITSQGRARNYITYAMTLLQDKGSTEVVFKAMGRAINKTVTIVELIKRRIPDLHQNTSIGSTDITDTWEPTEEGLLPLETTRHVSMITITLSKIELNTSSVGYQCPIPIELVKPMGDIDYEGREGSPGGRGRGRGRGRGRGRGRGGRGNAYVNVEHEDGGWEREQSYGRGRGRGRGRSSRGRGRGGYNGPPNEYDAPQDGGYGYDAPHEHRGYDDRGGYDAPPQGRGGYDGPQGRGGYDGPQGRRGYDGPPQGRGGYDGPSQGRGGYDGPSQGRGGYDGPSQGRGGYDGPQGRGRGRGRGRGGRGRGGGRGGDGGFNNRSDGPPVQAAA
Protein: Kinesin-like protein (A0A1D8PKA4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Kinesin-like protein
- Kinesin-like protein
- Ase1p
- Probable kinetochore protein NUF2
- Kinesin-like protein
- Spindle assembly checkpoint component MAD2
- Dynein heavy chain, cytoplasmic
- Serine/threonine/tyrosine protein kinase
- Tubulin alpha chain
- Protein kinase
Sequence:
MSYPNSLGSPATVTSTSVPTAKQSSISVAVRVRPFTEAESNRLVKIDNDDVFLGDGCLTSDNNNNNNNSNSNGNGNGNGSSAANSSGASTSRRAIFNTLGGLRKIINVVDDRMLIFDPPETNPLTKMQRNAFPNSFKGSRIREHRFVFDRLFDEDCTQDQVYRNTTQPLLDSVLDGYNATVFAYGATGCGKTHTISGTPEDPGVIFLTMKELYNRIEELKDTKIIDISLSYLEIYNETIRDLLNPMTQCKNLVIREDANNKISVSNLSRHRPNSVEEVMQLILEGNKNRTCSPTEANATSSRSHAVLQINVIQKDRTGDITEEHTFATLSIIDLAGSERAAATKNRGARLNEGANINKSLLALGNCINALCDPRRRNHVPYRDSKLTRLLKFSLGGNCKTVMIVCVSPSSQHYDETLNTLKYADRAKEIKTKLIRNQHNLDRHVGSYLKMITEQKQEIEELRARESKMVESTINKRKDLESKVFKILFESLESTRKAIAKQNQEKWKKYFILAKRKLLLSQKIETELVLEQRDDIDINSLSIASGNESESVFKIYDLCEQLISKIEYQLPQLESQYSQPTDLDYILEDSAMQTLKRLQDEEGWTEHHSAIYRQSIQSMKREVHTDLLLYSSILYDNLIHDLSIFFYIPREIGNFINNISNPTSLNEANQELLYNMTLGLENLLNGEFDSAMEHYAMDYMKNKVESENQTQTQNQNQNQNQNQNQNQNQNQNQNQVNSYNPDESMMSIDNDIIPIKKQRILSPPRQLKKPKKSTQIPPITRINNINSGGSGGNGNSKLKKPSHWGDRDKSDLMYDTSMEENSLITSEINFDEPDGGGTPVARSSPPPPLPPLVSSNKPPNVHNILADVNELDLPFNPTIESSPTQVPTSKLIPPTGTATITDRDDIDNSNININGNGNGNGNANNFTNKRLLTDLKRSRSSSLMSNKKIMMNFTDSKLPLLNKQAASKISNDN
Protein: Leucine-rich repeat-containing protein sog2 (O94294)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Barrier septum. Cell tip. {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Serine/threonine-protein kinase nak1
- Maintenance of ploidy protein mob2
- Serine/threonine-protein kinase orb6
- Cell polarity protein mor2
- Mo25-like protein
- Serine/threonine-protein kinase ppk11
- Enhancer of rudimentary homolog 1
- Dual specificity protein kinase lkh1
- Metallothionein expression activator
- Casein kinase II subunit beta-2
Sequence:
MSAHEVSSTKNSEIERIIKEAEDAGPENALTLDLSHLNLRELPYEQLERIQGRIARLALGHNFIKSIGPEILKFTRLRYLNIRSNVLREFPESLCRLESLEILDISRNKIKQLPESFGALMNLKVLSISKNRLFELPTYIAHMPNLEILKIENNHIVFPPPHIANNDLQDSDMQLFIANIKGYLSRNESVFRTRSESTVSAALSASANLSHSEENDSSVVDSYLFSAPSDTSHAVSPGMLTFVTPSPHSHSPAGHQQSTPKSTLSKTNENSEGTLYDSNVAHGCTHPPSLNQLNKFHLDASPRQARPRRSVSLATGLNSPSVSKPPSSATGPLYHSPQSSLTNSSVASADVQERTHNTNGASPIQDQISEFTDQHQNPSNNDAASTQSILKTAPTQLSASAKTSAISLPEVAKKERNRSNSTNDDYSSTRLPSSVLHRLEALKEARKLSEQLPNRIFAQDPHPSPRLKKEETHENGSNLTNDSVNSYFSNIGGSEVEMKHSAFEKTLESSRGILFSLSQVQQALRQQLLFCSNPVVLDSMRHVLHTANVQIKRLILCFEDTQQSNDGTANINSIVNASLSCISSFRKLIEVTKKFLNELTSRADVRYVRLLLLILFDAAKELQNALVPLSPSQPHSGNNIFADQVRQSPTSMIRTASGLTNRIVSVEKPASVMNPEIDKQIQDQVALATNSAMSVLTLLIDAVPKNNQPDLVNENIAPNLISKLRELGSLSAAACDVTRKLKHRLLTFQTNPEELEWQLFLDDTQAFVKSIIAVANLAKALSSEYTFQKSVLAGLSAATRSTKDLTILLSSSARHYTESSLATPVPLMSPIARVPATPLSAALGSAAQSITSPLIMSPAAIPASAYSTNKIDYFTDADGNVEGLQR
Protein: BcDNA.GH02901 (MIP13254p) (Pudgy, isoform A) (Pudgy, isoform B (EC 6.2.1.3)) (Pudgy, isoform C) (Pudgy, isoform D) (Q9VXZ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- FI08446p
- CG9503-PA
Sequence:
MNPAAQLLRMRSATAFGSAATRSITTNRRQRTTSTASAQRERTQSVSETDKFLHYSPEDGYYKTSPFDPVTIPNVPLHEYVWRDFKKWERRTAAVCVITDRQYTFAQMRDASAAFAVRLQTKFNLQKPDVLAICLPNLPEYPIATLGAIEAGLTVTTVNPVYTPDEIARQLTFSGAKFLVGTVSGFATLSQASKLVGRQIPIAVVRTSAEEALPEGAIDFSELTSTQNVRYEDLKAPKEASADDMVFLPFSSGTTGLPKGVMLSHNNITSNCEQVQASLPLDLMGPQNTLPGVLPFFHIYGLTVVMLSKLGQGCRLATMPCFKPDDFMRSLDKYQGSILNLVPPIALFMINHPKLTQETAPHLKVVMSGAAPIGQHDVERFLNKFPNTVFKQGYGMTEASPVVLLTPEGNKVYASTGVLPASTEAKIVPLDGSDAKGVGPRTTGELCVRGPQVMAGYLNNDEANQVTFYPGNWLRSGDVAFYDEDGLFYITDRMKELIKVKGFQVPPAELEAVLRDHPKILEAAVFGIPHEFNGEAPRAIVVLRQGEKASAEEISAYVAERVAHYKKLEGGVIFVDEVPKNPTGKILRRELKEKFSD
Protein: Cell wall integrity and stress response component 2 (P53832)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane; Single-pass membrane protein.
Interaction partners:
- RHO1 GDP-GTP exchange protein 2
- Protein SLG1
- Cell wall integrity sensor MID2
- RHO1 GDP-GTP exchange protein 1
- Cell wall integrity and stress response component 3
- Protein MTL1
- GTP-binding protein RHO1
- Protein kinase C-like 1
- Serine/threonine-protein kinase BCK1/SLK1/SSP31
- Mitogen-activated protein kinase SLT2/MPK1
Sequence:
MHLDLIHKSFILVWLIYIRAALADQFTYKACYSASDIRKLGLTYKGVYEYQSVSYCQNECPGQAVVALFNGTGCYCGGSVAQLQSLTQVDSSKCDVSCAGWPYQNCGGSSAMNVYINNAASTADSTSSTATSTSTTSSSSTSVSSKTSTKLDTKTSTSSSATHSSSSSSTTSTTTSSSETTTSSSSSSSSSSTSTTSTTSTTSSTTSTSSSPSTTSSSTSASSSSETSSTQATSSSTTSTSSSTSTATVTSTPSSTSIGTSTHYTTRVVTQSVVSQANQQASTIFTTRTSVYATVSSTSSSTSSLLNGKSSSSKSKGLSGGAIAGVVVGVVCGTVALLALALFFFVWKKRRQSSQHVDLEETKQYQPYSLGDADANPVIPPSASSTNWHIPSRNNTALSKNTASTFATYDLPTRAPGGRDSIITGDAHNISKRSHFPSVVYEEPPSIYNGNQRFSATSLPDMMEERQLHIVNPDNVSSNIGSNVSDGDDDYDDAKDSNNSSLR
Protein: DUF3456 domain-containing protein (Q381R4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYARLSNTSQSYYSIISKIFQLLAIIGSISLVEAATVGDPLFRIHEPTYAFLDCSACIAFAGHLGRRMNESIRYGGRGGATFLSSHRLGKDNKLKRRDYATSELRGAEVLEKICNDSLFDDYALHFRADMRIRVYDNGESEYPLAQHYSKEDSRILKAVKTKAVHVFCTRVMDEEEDAMTSLVREVELLSELEQRLCGGYLEMRNITAPPFPVEKAVTAVCVGVEPSIEAEVRRLEKYEKWQASISKGTSQDKMKGAEGAESVVVKGVQYSKDDPLSFTVLRKPNAKSNGDTTEGGSDAAEDVRKQPDKDSVFMNFDL
Protein: NEDD8-activating enzyme E1 regulatory subunit (Q54JM3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Regulatory subunit of the dimeric uba3-nae1 E1 enzyme. E1 activates nedd8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a nedd8-uba3 thioester and free AMP. E1 finally transfers nedd8 to the catalytic cysteine of ube2m (By similarity).
Interaction partners:
- NEDD8-activating enzyme E1 catalytic subunit
- NEDD8-conjugating enzyme Ubc12
- Large ribosomal subunit protein uL1
- Molybdopterin synthase catalytic subunit
- COP9 signalosome complex subunit 5
Sequence:
MSTSTTDTDKYDRQLRLWGEDGQSKLERSHILLLNGSATGTETLKNLVLPGIGSFTVVDNKKVTESDLGNNFFVERSSLGKPRATVVCELLRELNDRVKGFSVEECPIHLINNNISFFKDFSLVVANRLSEEALLTLSQYLTEQNIPLLITNSYGYIGYLRISTPEHQIIESKPDDPIDDLRIYNPFKQLVDMADALELDKLNTQQHSHVPYVLLLIKFLKEWRSTHNDKMPETRAEKDEFKKFFNSHSWSADEMNFVEGIQNLLKYIQPPRVPGDVQNLLKDPKTNITENSDDFWVLVAALKEFMTNNDNTLPLHGNVPDMTSETHNFIQLQKGYQEKALADLSEFSGYVDQILTKVGKSSISSDLVKKFCKNTRFLNIIRYRTISEEYNQPKTNLIKSELEQADTVMVFYILLRGIDKFYKTYHKYPGSSDDFESDIPLLKTVITQYLAEINISNDLVKDDYIAEFVRFGGSELHNIASLMGGVTSQEIIKLITHQYTPLNNTFIFNGINSTAGSYNL
Protein: Mothers against decapentaplegic homolog 9 (MAD homolog 9) (Mothers against DPP homolog 9) (SMAD family member 9) (SMAD 9) (Smad9) (Smad8) (O54835)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD) (By similarity). Has been shown to be activated by activin type I receptor-like kinase-2 (ALK-2) which stimulates heteromerization between SMAD9 and SMAD4. ALK-2 binds TGF-beta, activin and BMP.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}.
Interaction partners:
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 5
- Bone morphogenetic protein receptor type-1A
- Bone morphogenetic protein receptor type-2
- Activin receptor type-1
- Mothers against decapentaplegic homolog 1
- Serine/threonine-protein kinase receptor
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog 3
Sequence:
MHPSTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQSLGPAPPSSPGHVFPQSPCPTSYPQSPGSPSESDSPYQHSDFRPVCYEEPLHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKVFNNQLFAQLLAQLLAQSVHHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
Protein: Isopentenyl-diphosphate Delta-isomerase 1 (EC 5.3.3.2) (Isopentenyl pyrophosphate isomerase 1) (IPP isomerase 1) (IPPI1) (O35760)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:O35586}.
Interaction partners:
- Diphosphomevalonate decarboxylase
- Geranylgeranyl pyrophosphate synthase
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Squalene monooxygenase
- Lanosterol 14-alpha demethylase
- Methylsterol monooxygenase 1
- Lanosterol synthase
- Farnesyl pyrophosphate synthase
- Squalene synthase
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Sequence:
MPEINASNLDEKQVQLLAEMCILIDENDNKIGADTKKNCHLNENIDKGLIHRAFSVFLFNTENKLLLQQRSDAKITFPGCFTNSCCSHPLNNPGELEENDAMGVKRAAQRRLKAELGIPLEEVDLNEMNYLTRIYYKAQSDGIWGEHEIDYILFLRKNVTLNPDPNEIKSYCYVSKEELKEILKKEARGEIKLTPWFKIIADAFLFKWWDNLNHLSPFVDHEKIHRM
Protein: Liquid facets, isoform G (Liquid facets, isoform L) (M9PEM7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MQVNVAGLRRNIKNLAHNYSDAQVKVREATSNDPWGPSAAIMSEIAELTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKENIFAIQTLREFVYFEEGKDQGTHVREKAKQLVTLLKDDERLKNERVKAQKAKERFAQNPSGFGSDGYIDGPSQRDLPPGWQEEPPKSVSELEMVRPQTAGEEELQLQLAMAMSREEAEQEEAKRRSDDVRLQLALSQSEQDFKDPNGRPIPAPKKEEQQSHLLDLLDISLGATSISSPPLGAAGGAPTAVVDPWAMPGPRAPSQLSDPWSGTSSPQVDPWNPSAAPRTILGAGVPMTSAPLGAGNDAWGARTQSPSVASGSSNEGWLQSNGNANQNGRGATPAGPPAEGWLIKSTAVGALGAAPINHAANNGSSSSDPWLAEPAASAAGGAAAVGLADPWAPGAASQTGAGALDDPWKALGTGAIKKQSPEFDEFDLITNRNKSEHSNSNASNNNNASLLDDMDPLSANYGNGGINSSMHPSTGATAKKSIKDAHSFLGENSALVNLDNLIKPIAPQTQTGNQPAYNPFSDNVVPPKTNLFQQQQPAVPSINQLKQQAPFSVSMNQDPWAPVMGGVSTTSQPSMEAWTLK
Protein: Crossover junction endodeoxyribonuclease RuvC (EC 3.1.21.10) (Holliday junction nuclease RuvC) (Holliday junction resolvase RuvC) (Q92M90)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00034}.
Interaction partners:
Sequence:
MQNTIRIIGIDPGLRRTGWGVIETLGNSLRFVASGTVTSDGELDLASRLCQLHDGLAEVVHGYQPHEAAVEQTFVNKDATATLKLGQARGIAMLVPARAGLRVAEYAPNAVKKAVIGVGHGEKQQIHMMLKVLMPKAEFKGNDAADALAIAICHAHNRQAVTSRLAALAG
Protein: Forkhead box protein P2 (Q6TKS2)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MMQESATETISNSSMNQNGMSTLSSQLDAGSRDGRSSGDTSTEVSTVELLHLQQQQALQAARQLLLQQQTSGLKSPKGSEKQRPLQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQALLQQQQAVMLQQQQLQEFYKKQQEQLHLQLLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHPGKQAKEQQQQQQLAAQQLVFQQQLLQMQQLQQQQHLLNLQRQGLISIPPGQSALPVQSLPQAGLSPAEIQQLWKEVTGVHSMEDNGIKHGGLDLTTNNSSSTTSSTTSKASPPITHHSIVNGQSSVLNARRDSSSHEETGASHTLYGHGVCKWPGCESVCEDFGQFLKHLNNEHALDDRSTAQCRVQMQVVQQLEIQLSKERERLQAMMTHLHMRPSEPKPSPKPLNLVSSVTMSKNMLETSPQSLPQTPTTPTAPVTPITQGPSVITPASVPNVGAIRRRHSDKYNIPMSSEIAPNYEFYKNADVRPPFTYATLIRQAIMESSDRQLTLNEIYSWFTRTFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEVEYQKRRSQKITGSPTLVKNIPTSLGYGAALNASLQAALAESSLPLLSNPGLINNASSGLLQAVHEDLNGSLDHIDSNGNSSPGCSPQPHIHSIHVKEEPVIAEDEDCPMSLVTTANHSPELEDDREIEEEPLSEDLE
Protein: Pre-mRNA-splicing factor RBM22 (RNA-binding motif protein 22) (Q22412)
Organism: Caenorhabditis elegans
Interaction partners:
- TPR_REGION domain-containing protein
- Protein BUD31 homolog
- Uncharacterized protein T27F2.1
- Pre-mRNA-splicing factor SYF1
- Tr-type G domain-containing protein
- Pleiotropic regulator 1
- Cell division cycle 5-like protein
- Protein isy-1
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor 8 homolog
Sequence:
MSMSKSSYSQYNRKNWEDSDFPILCETCLGNNPYMRMMKDKYGRECKICERPFTTFRWQPGKGARYKNTELCQTCAKVKNVCQTCMFDLEYGLPVQVRDHELQIADNIPKQGANRDFFLQNVERTLGQGDGTQPIAQIANNMDQAAHDRLRRMGRTQPYYKRNAPHICSFFVKGECKRGEECPYRHEKPTDPDDPLSRQNIRDRYYGTNDPVAEKILNRAAAAPTLSPPADTTITTLYIGNLGPSGAQQVTEKDLNDFFYQYGDIRCLRVLTEKGCAFIEFTTREAAERAAERSFNKTFIKGKRLTIRWGEPQAKRAADNSNYVTPVPSVPILPVPDGLAPSTSSQQRFTGSMPRPPAPPTFAAPRSLVVPNVRPVKAGESSGASSSSSIYYPSQDPTRLGAKGDVIE
Protein: Small nuclear ribonucleoprotein D3 polypeptide (A0A8I5ZKE3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGVELRMLTSLKTKLERIMRSEPKTKYPVIPPALLYNPASSFSPSGPVDAISMSNITVTYRDGRVAQLEQVYIRGSKIRFLILPDMLKNAPMLKSMKNKNQGSGAGRGKAAILKAQVAARGRGRGMGRGNIFQKRR