wanglab/gogpt-training-data huggingface dataset:
Protein: Heat shock factor protein 5 (Heat shock transcription factor family member 5) (Zgc:162225) (A4QNW9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAMDCDYSLLNVNINYHNFPAKLWRLTNNPQNSSVFWSPTGESLIVDQQQFEVDLLTPIKLDNKPFKTSNFTSFIRQLNLYGFKKIFDGSPRDKHRNRHHFYNPNFRRGQPELLVHLKRLTLSKKTKTKIGEKESCRPLSRGQQKTQRNPAEENRGSAQLSGGAAHQQPEYEQSPMTGHSWIFPCADASSFYSNTGLPLSVYPYSSMPVGPHSGPAFLFPQDIPHHLSYPAGLYSPVCQCCTHTQADQAGGNQTSHLSYSHYAYYPNYSVSHQQSSFQPTNWPVHHVSEQRGDMNLDRAFRMVDDFQGLSNVRIVQVGPPVKPQLISNPPLYTIPSAPKAQSVSLQSIETMTFSPPKDTDTYEDHSQIKADLESLEQLKDGGLSFKVTIENVKEENIRNELQINTHRSSFWTDSDF
Protein: Cilia- and flagella-associated protein 36 (Coiled-coil domain-containing protein 104) (Q8C6E0)
Organism: Mus musculus (Mouse)
Function: May act as an effector for ARL3.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96G28}. Cytoplasm {ECO:0000250|UniProtKB:Q96G28}. Cell projection, cilium, flagellum {ECO:0000305}.
Interaction partners:
- ADP-ribosylation factor-like protein 3
Sequence:
MAAEEEDEVEWVVESIAGFLRGPDWSIPILDFVEQKCEVFDDEEESKLTYTEIHQEYKELVEKLLESYLKEIGINEDQFQEACTSPLAKTRTSQAILQPVLAAEDFTIFKAMMVQKNIEMQLQAIRIIQERNGVLPDCLTDGADVVSDLEQEEMKILREVLRKSKEEYDQEEERKRKKQSSEAKMEELPVYTSEAEKMSNSQGDGEHFVQPPSEVKVHFANQSVQPLARKMELLPETSSLTQKGLKIPGLEHASMEGPIANLSALGTEELRQREHYLKQKRDKLLSMRKDTRTKQIQNTEQKGKPTREAEEMTEKPEMTAEEKQTLLKRRLLAEKLKEEVINK
Protein: Acetolactate synthase isozyme 2 small subunit (EC 2.2.1.6) (ALS-II) (Acetohydroxy-acid synthase II small subunit) (AHAS-II) (P0ADG1)
Organism: Escherichia coli (strain K12)
Interaction partners:
- L-threonine dehydratase biosynthetic IlvA
- Branched-chain-amino-acid aminotransferase
- Acetolactate synthase isozyme 1 small subunit
- Acetolactate synthase isozyme 1 large subunit
- Dihydroxy-acid dehydratase
- Ketol-acid reductoisomerase
- Acetolactate synthase isozyme 3 large subunit
- Acetolactate synthase isozyme 3 small subunit
- 3-isopropylmalate dehydrogenase
- L-threonine dehydratase catabolic TdcB
Sequence:
MMQHQVNVSARFNPETLERVLRVVRHRGFHVCSMNMAAASDAQNINIELTVASPRSVDLLFSQLNKLVDVAHVAICQSTTTSQQIRA
Protein: 60 kDa heat shock protein, mitochondrial (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (Q54J97)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- 10 kDa heat shock protein, mitochondrial
- Heat shock 70 kDa protein, mitochondrial
- Chaperonin Cpn10 family protein
- Translocase of outer mitochondrial membrane
- GrpE protein homolog, mitochondrial
- Luminal-binding protein 2
- T-complex protein 1 subunit theta
- Mitochondrial-processing peptidase subunit alpha-1
- Iron-sulfur cluster assembly protein
- Luminal-binding protein 1
Sequence:
MFRQIANKSTKFGLRNYSTGKDIKFGAECRALMLRGVEQLAAAVEVTLGPKGRNVILDQPFGQPKITKDGVTVAKHIEFADRHINLGAQLVKGVASSQNDQSGDGTTTATILTRAIFAEGCKAVAAGMNPMDLWRGINFAVEKVVGELKTISRPISSTEEISQVATISANGDKVIGNLIANAMEKIGKEGVITVQDGKTLKDELEIIEGMKFDQGFISRYFINDAKEQKCEFDDPVILVVDGKISNVQQLVPILELVHSKHKKLVIIADNIEGDALSALIFNKMRGLQVCAVKAPGFGDLKRVNLQDIAVISGAQVISEELGVRLEDVDITMLGSAKKITIDSDSTIILDGAGDKAAIQERVELIRESLTRTTSDYDKTQLETRLAKIGGGVAVIRVGGASEVEVGEKKDRITDALNATKAAVEEGIVPGGGTALLYSTLALKKIKMDNFDQTIGVKIVRDALLIPCKTIANNAGVEGSVVIGRLLSKRDFEYGYNAQKGVYENMIQAGIIDPTKVVRTALIDAASVASLMTTTEAMVVEIKKDTPMPQMPPQMDY
Protein: E3 ubiquitin-protein ligase RGLG4 (EC 2.3.2.27) (RING domain ligase 4) (Q9SAL0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses E3 ubiquitin-protein ligase in vitro. Acts as upstream modulator of jasmonate (JA) signaling in response to various stimuli, such as JA-inhibited root growth, JA-inductive gene expression, coronatine-mediated pathogen susceptibility, wound-stimulated expression of JA-responsive genes and wound-induced JA biosynthesis. Controls fumonisin B1 (FB1)-triggered programmed cell death (PCD) by modulating the JA signaling pathway. May mediate salicylic acid (SA) suppression of JA signaling in FB1-induced responses. May mediate the formation of 'Lys-48'-linked multiubiquitin chains. Mediates the polyubiquitination and subsequent proteasomal degradation of the target protein GRXS17.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25788731}. Nucleus {ECO:0000269|PubMed:25788731}.
Interaction partners:
- Two-on-two hemoglobin-3
Sequence:
MTMGNFLKRFGSGKSRSSRNMTLGTTSSQSHEPSPSDPSLSLADNTNATKKKYALIPDRFSSLDQVSKALREAGLESSNLILGVDFTKSNEWTGKTSFDGKCLHALGETSNPYEKAIFVIGQTLAPFDEDNLIPCFGFGDSTTHDEEVFGFHSDNSPCHGFEEVLACYKRIAPNLRLSGPTSYGPLIDAAVDIVEKNNGQFHVLVIVADGQVTRGTDMAEGELSQQEKTTIDAIVNASSYALSIVLVGVGDGPWEDMRKFDDKIPKREFDNFQFVNFTEIMTRNSPESAKETAFALAALMEIPFQYQAAIELRLLGKQTGLAKTIVPRPPPIPYTPPTNAELPSTASPASPEQTQSCPICLTNRKDVAFSCGHMTCGDCGSKISNCPICRVRITNRLKLYT
Protein: TRANSCRIPTION INITIATION FACTOR TFIID (TFIID-1) (Q8ST28)
Organism: Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- TRANSCRIPTION INITIATION FACTOR TFIID 70kDa SUBUNIT
- B-related factor 1
- TRANSCRIPTION INITIATION FACTOR TFIID 111kDa SUBUNIT
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 5
- Similarity to TRANSCRIPTION INITIATION FACTOR TFIID 30kDa SUBUNIT
- Transcription initiation factor TFIID subunit 13
- TAFII55 protein conserved region domain-containing protein
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 9
Sequence:
MDAPDISYEHQETSVPNRSGIIPTLQNVVATVNLSCKLDLKNIALRARNAEYNPKRFAAVIMRIREPKTTALIFASGKMVITGAKSEKSSRMAAQRYAKIIHKLGFNATFDDFKIQNIVSSCDIKFSIRLEGLAYAHSNYCSYEPELFPGLIYRMVKPKIVLLIFVSGKIVLTGAKVRDDIYQAFNNIYPVLIQHRKA
Protein: Alpha-mannosidase (EC 3.2.1.-) (Q38BY8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Phospholipase B-like
- Phospholipase B-like
Sequence:
MLTLGMHTLQLLSLILYFAATVFVPALKVPSKAVVHLVAHTHSDLGWLKTVDQYTYGLNNSIQFADVTTIINSVVEGLLANPERKFTYVEIGFFSRWWSRQSVSMREKVRGLVANGQLQFANGGWCMHDEATTHYIDMIDQTTLGHRWLLRELNVVPLVGWQADAFGHSATQASLLTSRAGFNGTFFARIDYREYEDRVKRGGRQFWWDASPSLPDLKTFAEANLHATYCSAAGYKWDLADQLESARTFTQADDIIDDNASERYNVPVVLKHFKDEVARSLQATRGANVMWTMGCDFTYMVSEFWFGKMDKLIKIANDDGEFTVRYSTPYEYMMAKLDEAVNAKIKYETSTGDFFPYASAAHEFWTGFYSSRPTLKRLIRMLSSYWVASRQLQFLAGVPSGDLPLLSDALAIAQHHDAVTGTARQHVTFDYVKRLVAGYNDDFSVRLRTALTGRLFNLSNVSHCLLSNVSACDATATGLAKKGSKLTVMVWNPSVHPNVNTFLQIPVPRRDIRVEGNGVKSFSVYGSPTQVSDYSNVNANWQPYTIGIILSLGKTSSLTLSTPGKYDIPRKESHVGYSLKSVVSRDRRGGFTLTSDHLKVRFGVNGRLKSIEVLSVGQEVLVEHDWCYFKSSRGEDPSGISGGAYIMRPVSDNVCEPISTDKVESIIIDETIGIVEQRFGNDLVQRVILHGDTVDLEFTSLGIPVKDGFGRELVARFSTSVNNSGIFYTDSNGREMQRREVDKRRNYPFVQTESVAGNYYPVSSLIFINDTETQFNVFTDAAMGGTSINNGEVLLTTHRRLLLDDQKGVSEPLNETEFITAYEGDPSMNEKGRGKHYGNPLRVRGTLTISVGRSGPSAMRRVREQLDEKYFSPIAVYSTGSTPNLNCSLELTQISPSVQIITTQLLNKTTLLLRIAHRYAVGEDDERSKSVEVELRSLIPNELDYNVESIDEVSLTTNTLLRNGLDTVVLKPMDVRTFLFHMREHKWRGMSMSCTGV
Protein: mRNA-capping enzyme (HCE) (MCE1) [Includes: mRNA 5'-triphosphate monophosphatase (EC 3.6.1.74) (mRNA 5'-phosphatase); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase)] (O55236)
Organism: Mus musculus (Mouse)
Function: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate.
Subcellular location: Nucleus.
Interaction partners:
- mRNA cap guanine-N
- Transcription elongation factor SPT5
- DNA-directed RNA polymerase II subunit RPB1
- Poly
- Nuclear cap-binding protein subunit 2
- Cap-specific mRNA
- Cap-specific mRNA
- Nuclear cap-binding protein subunit 1
- DNA-directed RNA polymerase II subunit RPB3
Sequence:
MAYNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMSLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERSPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDIEEAPPPPVLPDWCFEDEDEEDEDEDGKKDSEPGSSASFSKRRKERLKLGAIFLEGITVKGVTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDKVNGQAVPRYLIYDIIKFNAQPVGDCDFNIRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRPKQFFDINISRKLLEGNFAKEVSHEMDGLIFQPIGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEGLLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRIDKSFPNAYNTAMAVCNSISNPVTKEMLFEFIDRCAAAAQGQKRKYPLDPDTELMPPPPPKRLHRPT
Protein: Small ribosomal subunit protein eS21z (40S ribosomal protein S21-1) (Q9M337)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein uS2z
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein eS19z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS28x
- Large ribosomal subunit protein uL4y
Sequence:
MENDAGQVTELYIPRKCSATNRMITSKDHASVQLNIGHLDANGLYTGQFTTFALCGFVRAQGDADSGVDRLWQKKKVEAKQQ
Protein: RNA-binding protein 4B (RNA-binding motif protein 30) (RNA-binding motif protein 4B) (RNA-binding protein 30) (Q9BQ04)
Organism: Homo sapiens (Human)
Function: Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA (By similarity).
Subcellular location: Nucleus. Nucleus, nucleolus.
Interaction partners:
Sequence:
MVKLFIGNLPREATEQEIRSLFEQYGKVLECDIIKNYGFVHIEDKTAAEDAIRNLHHYKLHGVNINVEASKNKSKASTKLHVGNISPTCTNQELRAKFEEYGPVIECDIVKDYAFVHMERAEDAVEAIRGLDNTEFQGKRMHVQLSTSRLRTAPGMGDQSGCYRCGKEGHWSKECPVDRTGRVADFTEQYNEQYGAVRTPYTMGYGESMYYNDAYGALDYYKRYRVRSYEAVAAAAAASAYNYAEQTMSHLPQVQSTTVTSHLNSTSVDPYDRHLLPNSGAAATSAAMAAAAATTSSYYGRDRSPLRRAAAMLPTVGEGYGYGPESELSQASAATRNSLYDMARYEREQYVDRARYSAF
Protein: B-cell CLL/lymphoma 9 protein (B-cell lymphoma 9 protein) (Bcl-9) (Q9D219)
Organism: Mus musculus (Mouse)
Function: Promotes beta-catenin's transcriptional activity. Involved in signal transduction through the Wnt pathway (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15371335}.
Interaction partners:
- Catenin beta-1
- Pygopus 2
- Pygopus homolog 1
- Lymphoid enhancer-binding factor 1
- Transcription factor 7-like 2
- Transducin-like enhancer protein 1
- B-cell CLL/lymphoma 9-like protein
- Transducin-like enhancer protein 3
- LIM domain-binding protein 1
- Transducin-like enhancer protein 4
Sequence:
MHPSNPKVRSSPSGNTQSSPKSKQEVMVRPPTVMSPSGNPQLDSKFSNQGKPGGSASQSQPSPCDSKSGGHTPKALPGPGGSMGLKNGAGNGAKGKGKRERSISADSFDQRDPGTPNDDSDIKECNSADHIKSQESQHTPHSMTPSTATAPRSSTPSHGQTPAPEPISAQKTPAKVVYVFSTEMANKAAEAVLKGQVETIVSFHIQNISNSKSERSTAPLNTQIPTLRNDPKPLPQQPPAPANQDQNSSQNARLQPTPPIQAPAPKPTAAPRPLDRESPGVENKLIPPVGSPGSSTPLPPDGTGPNSTPNNRAVTPVSQGSNSSSADPKAPPPPPVSGGEPPTLGENPDGLSQEQLEHRERSLQTLRDIQRMLFPDEKEFTAGQTGGPQQNTGVLDGPQKKPDGPIQAMMSQSQSLGKGPGPRTDVGAPFGPQGHRDVPFSPDEMVPPNMSSQSGPIGPDHLDHMTPEQIAWLKLQQEFYEEKRRKQEQVVVQQCSLQDMMVHQHGPRGVVRGPPPPYQMAPGEGWAPGAEPFPDGINISHSLPPRGMAPHPNMPGSQMRLPGFAGMINSEMEGPNVPNPASRPGLSGVSWPDDVPKIPDGRNFPPGQGVFSGPGRGERFPNPQGLSEEMFQQQLAEKQLALPPGMSMEGIRPGMEMNRMIPGSQRHMEPGSNPIFPRIPVEGPLSPSRGDFPKGMPPQIGPGRELEFGMVPGGMKGEVNLNVNMGSSSQMIPQKMREAGAGPEEMMKLRPGSSEMLPAQQKMVPLPFGEHPQQEYGVGPRPFLPMSQGPGSNSGLRNLREPIGPDQRTNSRLSHMPPLPLNPSSNPTSLSTAPPVQRGLGRKPLDISVAGSQVHSPGINPLKSPTMHQVQSPMLGSPSGNLKSPQTPSQLAGMLAGPAAAASIKSPPVLGSAAASPVHLKSPSLPAPSPGWTSSPKPPLQSPGIPPNHKAPLTMASPAMLGSVESGGPPPPTASQPASVNIPGSLPSSTPYPMPPEPTLSQNPLSIMMSRMSKFAMPSSTPLYHDAIKTVASSDDDSPPARSPNLPSMNSMPGMGINTQNPRISGPNPVVPMPTLSPMGMTQPLSHSNQMPSPNAMGPSIPPHGVPMGPGLMSHNPIMGHGSQEPPMVPQGRMGFPQGFPPVQSPPQQVPFPHNGPTGGQGNFPGGIGFPGEGPLGRPSNLPQSSADPALCKPGGPGAPDSFTVLGNSMPSVFTDPDLQEVIRPGATGIPEFDLSRIIPSEKPSQTLQYFPRGEVPGRKQPQGPGPGFSHMQGMMSDQAPRMGLALPGMGGPGPVGTPDIPLGTSPSMPGHNPMRPPAFLQQGMMGPHHRMMSPAQSTVPGPATLMTNPAAAVGMIPGKDRGPAGLYTHPGPVGSPGMMMSMQGMMGPQQNIMIPPQMRPRGMAADVGMGGFSQGPGNPGNMMF
Protein: AAA+ ATPase domain-containing protein (PEX6) (G5EFR8)
Organism: Caenorhabditis elegans
Interaction partners:
- Peroxisomal ATPase PEX1
- TPR_REGION domain-containing protein
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PEX13
- Peroxisome assembly protein 12
- Putative peroxisomal biogenesis factor 19
- Peroxisomal biogenesis factor 11
- Probable phytanoyl-CoA dioxygenase
- Bifunctional glyoxylate cycle protein
- ATPase asna-1
Sequence:
MVCREEFFKFYFRILFSKNEAKRIRKLLWNEEVELKIVVDQSGASINTLSIHPVTCWSLGILDSQLVKTSFTITTDHGKSSNIERVMKVQTSTSVKIGSLRISRCDVFNLFGPDLVKNVAVDNITPNFKFHETPIPISEDAKLSLMRQPSVAKNIRLEKHHLKQILKSANVFYKNDVIRITNYNAYTDKTTHLFYKLDVSSSPCIMDSSTAVYETSAVSQSLPFSNFLLKNSLTSSMRTTVFRMTQIYSAQKTISKKALVLLVTGASGSGKRLMSRVFASETHRNFFEVDGYEMVCENASTSEAKWTSWWEKAKLLQNCVLFIRNSNVLAIDQFNALDRRILQYMEQKLSEPSKITVIFSCNTDTMSSMPANVKNLALYTFSAEFMDENDRKTWLQYYLNEKLANHVAKKTSGFTLAELEKLVKNGKKVKIEEKEEKVYEDLIDKRNSNFADAIGAPKIPNVRWEDVGGLEETKQTVLESIRTNLFGSRALKRSGIILYGSPGCGKTLIAKAVATEFKIAFLSVKGPELLNKYVGQSEENLRKVFERAKQASPCVIFFDEIDSLAPNRGRNGDSGGVIDRIVSQLLAELDKLHNSPLTKVFVMGATNRPDLLDNSLMTPGRFDKLVEVKPGEDVESKTKILEAVSRKMRFEEDVDLREIASKVDEKMSGAQLFSIISNAGMAAIVETIQSIEDGKTENQSIRVAQRHLLESVKRFHETKY
Protein: Valine N-monooxygenase 2 (EC 1.14.14.38) (Cytochrome P450 79D2) (Isoleucine N-monooxygenase 2) (EC 1.14.14.39) (Q9M7B7)
Organism: Manihot esculenta (Cassava) (Jatropha manihot)
Function: Involved in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Can use L-valine or L-isoleucine as substrate.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:D5JBW8}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAMNVSTTATTTASFASTSSMNNTAKILLITLFISIVSTVIKLQKRASYKKASKNFPLPPGPTPWPLIGNIPEMIRYRPTFRWIHQLMKDMNTDICLIRFGKTNVVPISCPVIAREILKKHDAVFSNRPKILCAKTMSGGYLTTIVVPYNDQWKKMRKVLTSEIISPARHKWLHDKRAEEADQLVFYINNQYKSNKNVNVRIAARHYGGNVIRKMMFSKRYFGKGMPDGGPGPEEIMHVDAIFTALKYLYGFCISDYLPFLEGLDLDGQEKIVLNANKTIRDLQNPLIEERIQQWRSGERKEMEDLLDVFITLQDSDGKPLLNPDEIKNQIAEIMIATIDNPANAVEWAMGELINQPELLAKATEELDRVVGKDRLVQESDIPNLNYVKACAREAFRLHPVAYFNVPHVAMEDAVIGDYFIPKGSWAILSRYGLGRNPKTWPDPLKYDPERHLNEGEVVLTEHDLRFVTFSTGRRGCVAALLGTTMITMMLARMLQCFTWTPPPNVTRIDLSENIDELTPATPITGFAKPRLAPHLYPTSP
Protein: L23A ribosomal protein natural variant (Q0ZHI2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPPKKPTEKSAKPGDKKPEQKKTAAAPAAGKKEAAPSAAKPAAAAPKKAAAPAAKKAAPAAKKPATAGAAAKKPAAVKTTAAAKAKSKDAKKKVLAGKKPQSVPAKLSAKARAAAKAKKGVKPVTKPAKGTAKAKAVALLNAKKVQKKIIKGAFGTRARKIRANVHFRRPTTLKLPRSPKYPRKSVPTRNRMDAYNIIKYPLTTEAAMKKIEDNNTLVFLTHLRANKSHVRAAVRKLYDIKVAKVNVLIRPDGQKKAYVRLARDYDALDIANKIGII
Protein: SD03967p (Q8T9E6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Carnitine O-octanoyltransferase, isoform A)
- Niemann-Pick type C-1a, isoform A
- LP12374p
Sequence:
MTLLPDIKASDAACCVGGANSDASSSSGVCSLKGHHGDPDSGCLGINCCTTAASSELSIDETSSTSSRGSCELTSKVTNDLNGFQSPNYHQAVAHANFDHCDPVDIQFADVRYTVKKFSFPERKFVTKEILHGLNGSFRSGELTAIMGPSGAGKSTLLNVMSGFCSTGVSGDIRVNRKPMAPSSERFRQMLCYIHQDDLLRPQLLVGEIMLLAAHLKLGFKVTKAYKMDLIKHILSLLGLDHRYNVPTGKLSGGQKKRLAIALELISNPPVLYLDEPTTGLDSSSCSSCVALLKKLASQGHTIVCTIHQPSALIFEMFDKLYTVVDGHCMYQGPVRELVPFLADQQLVCPSYHNPADYLLEVAVGEHQRDLNELIHAANKKYYEDVDRHRYMSSDDMARLVESIKENMGGKAVVKTSEALAAFAAAQFSSFDYVKPSPQELALEEIKALSGGPESADPDLLEKNLRPQPQPLAKAGELARPPNAIRSASFLMQYVLLMQRILICAKRNYFLLLARIFSHIFIGVVFGYLYMNVGNNAQSVLGNYVYLYGSTLLLVYTGKMAVVLTFPLEIDMLTREHFNRWYKLGPYFLSLISFEIPFQSLCTAMYIIISVHLTGNDATDSFRIYYFMLLGIMASLSAQAWGFFVGATLPTKLAVFLGPILAVMFSVFGFCTRYIDITPLFRWMWHLSYFRAGFHGALNAIYGMDRPFLECPETAMYCHFRSPKVFLKYMMISDVHMSDCLILMGIVIGVMHVLTLITLWHKLNKR
Protein: Matrix metallopeptidase 25b (Matrix metalloproteinase-25) (E7F1N5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- A disintegrin and metalloproteinase with thrombospondin motifs 15
- ADAM metallopeptidase with thrombospondin type 1 motif, 15b.
Sequence:
MSFSGYLGLVYLTCPMLVFFSAVHSAPVKDQYSRGVDWLSRYGYLPPLDPRTGQLQSKDGIERAIREMQRFAGLKETGKLDSDTLTLMNTPRCSLPDIIGIEDKLKKRRRKRYATTGLRWTKSDITWSVQNYPSVHKRLTPTQVDPIISYALKAWSDVTNLNFYGASSSEKDRADIRISFARSLHDDGYPFDGKGGTLAHAFFPGESDVAGDTHFDDDEIWTYLDESGTDLFAVAVHEFGHALGLSHSSSSPSIMKPYYQGSVGDVGSYILPDDDREAIQSLYGRKISSPTPSPNKPTSHLPKPPATYPKGPVKPDPSIQNRCEGGFDAVANLRGEVFFFKGPYFWRIQRTGSLVSFQPAHIKNFWMGLPPTTNKVDAVYERKVDNAIIFFIGSQYWVFKNTEVLPGYPRPLSDWGMITQDGRKVMRVDAAFIWAHNGKTYIFSGGEFWRFSEGRETELRGPDTGYPRNTNLWKGAPSNPDDVITWGQGDAYFFKDNSYWVLKNGEMDQTSVTKKSTAVDWMMCQQETTKAPESPRRREGVNCYCDNSAGLQMSVSAWLLLITALLHIGFNSQ
Protein: ITSN1 protein (Q6GMY7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAQFPTPFGGSLDIWAITVEERAKHDQQFHSLKPISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQLPSALPPVMKQQPVAISSAPAFGMGGIASMPPLTAVAPVPMGSIPVVGMSPTLVSSVPTAAVPPLANGAPPVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASVPPVAEWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGISVISSTSVDQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKKKKK
Protein: Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 3, mitochondrial (UDP-3-O-acyl-GlcNAc deacetylase 3) (EC 3.5.1.108) (Protein LIPID X C3) (AtLpxC3) (UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase 3) (P0DKB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21709257, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Probable UDP-3-O-acylglucosamine N-acyltransferase 2, mitochondrial
- Probable UDP-3-O-acylglucosamine N-acyltransferase 1, mitochondrial
- Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial
- Probable lipid-A-disaccharide synthase, mitochondrial
- Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial
- Probable tetraacyldisaccharide 4'-kinase, mitochondrial
- Is a member of the PF|00364 Biotin-requiring enzymes family
- adenylate kinase
- Uncharacterized protein At2g34110
- Uncharacterized protein
Sequence:
MRLPVTVKATKPSFLVIWIRYSSAASSPTVSLNPSGRLQQTLAGSVEVKGKSLHSGKFSTVKLNPEIAGAGRFFEFRSRFIPASIEFAQESPLCTTLLKDELKIRTVEHLLSALEAKGVDNCRIQIESESSDDREVEVPIFDGSAKEWVDAIQGVGINAAQNHDGESVEKMVAHVNKPVYVCKNDTFVAAFPALETRITCGIDFPQVPAIGCQWFSWRPIHESSFAKDIASSRTFCVYEEVERMREAGLIKGGSLDNAIVCSAEHGWMNPPLRFDDEACRHKILDLIGDLSLVSRGGNGGLPVAHIVAYKAGHALHTDLARHLTMD
Protein: eIF5-mimic protein 1 (Basic leucine zipper and W2 domain-containing protein 2) (Q9Y6E2)
Organism: Homo sapiens (Human)
Function: Translation initiation regulator which represses non-AUG initiated translation and repeat-associated non-AUG (RAN) initiated translation by acting as a competitive inhibitor of eukaryotic translation initiation factor 5 (EIF5) function. Increases the accuracy of translation initiation by impeding EIF5-dependent translation from non-AUG codons by competing with it for interaction with EIF2S2 within the 43S pre-initiation complex (PIC) in an EIF3C-binding dependent manner.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21745818}.
Interaction partners:
- eIF5-mimic protein 2
Sequence:
MNKHQKPVLTGQRFKTRKRDEKEKFEPTVFRDTLVQGLNEAGDDLEAVAKFLDSTGSRLDYRRYADTLFDILVAGSMLAPGGTRIDDGDKTKMTNHCVFSANEDHETIRNYAQVFNKLIRRYKYLEKAFEDEMKKLLLFLKAFSETEQTKLAMLSGILLGNGTLPATILTSLFTDSLVKEGIAASFAVKLFKAWMAEKDANSVTSSLRKANLDKRLLELFPVNRQSVDHFAKYFTDAGLKELSDFLRVQQSLGTRKELQKELQERLSQECPIKEVVLYVKEEMKRNDLPETAVIGLLWTCIMNAVEWNKKEELVAEQALKHLKQYAPLLAVFSSQGQSELILLQKVQEYCYDNIHFMKAFQKIVVLFYKADVLSEEAILKWYKEAHVAKGKSVFLDQMKKFVEWLQNAEEESESEGEEN
Protein: Putative increased recombination centers protein 11 (Q12479)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YOR012W
Sequence:
MTWMVKLLRQMISMQSQYGAALGATCLLHYLTTSLSIRFFFHDLTVRKHEVMPLGMDYYYLYAIGKDPSHPEIRGSVRKILEKYKTKADKANCALALEAISEHARSVYEYFGFKTYLVFQFGVGEVNSKGEPDPQGKGFTAYLMLYHKDADTIFHA
Protein: Large ribosomal subunit protein uL15 (60S ribosomal protein L27a) (P41092)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein eS10B
- Large ribosomal subunit protein eL20
- Ubiquitin-ribosomal protein eL40 fusion protein
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein P2
- Small ribosomal subunit protein eS4
Sequence:
MSNIKRKKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGMHHHRINFDKYHPGYFGKVGMRNFHLRRQHKFRPEINLDKLWSLVGAEKFAELEKEKSTKAPVIDLVKFGYYKLLGRGHLPARPVIVKAKYFSKKAEDKIKKAGGVCLLSA
Protein: Stardust, isoform J (EC 2.7.4.8) (M9NG38)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQANSSRSNLSAQSSGTPSASTISSSQGKQQVVELSGYVIILVENVEGKIKLYGSPPDRDNLEVGDEILEVNGLTLENISRTEVIRHIHDCIKSCTICLRVRKKNDSRLAWDIGNSVQDAFVIAVEEHARERLQRLAALNRVTPVDITQLSKKLLEDVIVHQASDVHSYSTSASAAAIASSSNRSQQQQQQQQQHQLLSAAYELQQQQQLQLQQQQQQQNSPTSSISIGRTELLLGDQSLRQDPRGNRRRSGSSIVVLDGDDLKPCLPDDYISGQHHLNHQQQLQLQQQLQQQHPLQQQHYRTHSGDIREIDQEMLTMLSVNQDNGPHREMAVDCPDTFIARNKTPPRYPPPRPPQKQHQATTAMAATQVAQQQTPSHKLQATLSSDPNGNSNSNNNSHIVGISSSSSSNNSSITDDFLCVVDGLYQGRKDTASPSSSAFDEVMSKHTLDSFGSIAYRHLHQQHQATSNGNSSSNTSNTNSNTNSNTNSNSNTNGNTSNNTAVSTKTATVTKTGVSSSNSNSNSLNSSNSSMHTSSSSSGHSSNIASATSSSSATSSSTVPDDLSLAPPGYEVSQQQQQQHLVATPVTMLLPPMAKHRELPVDVPDSFIEMVKTTPRYPPPAHLSSRGSLLSNGSASTAHTTLSSMGVAPSPVTATAAAAASASAACATTAVAAAAVSGVADGDARRVADELNGNAKPVPPPRDHLRVEKDGRLVNCSPAPQLPDRRAPGNASSGSSGATTHPLQHQQIAQIVEPTLEQLDSIKKYQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPLFYLLEERLKPAKIKAQVKDTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: Serine/threonine-protein kinase receptor (EC 2.7.11.30) (Q8ITX8)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}.
Interaction partners:
Sequence:
MPYQHADSMNCENESSCRQGRSFRGGIGMCCCSTNNCNMPDLIEMVNPSLKKDSDNSALLWASTPSNMDLESLDKFPFYWIIIIALSVILCIALLILAYVGWKFQQNKKEEIKKQQKIKFDMEKTDALEAGNVPLVEPEEEMIEMVETPKELPITDFQLISKGRFGKVFKAQYTPDSGEKRLVAVKKLNEFQKASFLAEKRIFDELNEYPKWYKSIVEFVCAEKIGDEYWIVTEFHERLSLYELLKNNVISITSANRIIMSMIDGLQFLHDDRPYFFGHPKKPIIHRDIKSKNILVKSDMTTCIADFGLARIYSYDIEQSDLLGQVGTKRYMSPEMLEGATEFTPTAFKAMDVYSMGLVMWEVISRTKLHQTDEPPNYQMPFQVIGFDPTIGLMRNYVVSKKERPQWRDEIIKHEYMSLLKKVTEEMWDPEACARITAGCAFARVWNHIMSSPDSSEGYHSGSSMKNRGVDDVEQSEKPEGIEEMQHYHASSPSKRQHPSPNPFFDSCPPPPPIPVILENGGILQPDNAEPEPEELPDLPIVEKIYDIATNMLFSREELDLMNAQRQVEYEAGADTRASTPTPSGTFGTFTT