wanglab/gogpt-training-data huggingface dataset:
Protein: AT01735p (Q8IHH1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
Interaction partners:
Sequence:
MAVKVQFEIGHTSKLRSKKTPHPQAFTHDWEIYVQGVNKADISAFVEKVVFVLHESFPKPKRVVKEPPYAIQESGYAGFLLPVEIYFRNRDEPKRIVYQYDLVLQSTGPPQHHVEVKTHIFEAPSEEFRTKLMRGGGVPVFGANIGAGSLARTLSPSVGSGETAHSNEMSGVKAKGVPGTISMNSDLNTGKKHKSRSEDPGKSNAFSALFGPPITKTSVTANNMAQVPVSKHSPEAKSAAVGGKGVFHEGREKASKDRDKSSGGDKPREKDKKDRHGRDKDRKSSKSGDGKHERDKEKSKKDKSRDKEREREQGSGNTTSANALTVATSVGTAGGLVKHTASPKPGKPNEMGAPSPKKTANDSAAGAVAPTSRSKERDEHKSVKSESKDKERSSSKKSKKDKKDKDKQRDESKDKRMPKDERPGQSDSPASGNLQSAHLQQQSQVASTGKATPTSVGSNSSSSMVSNIGKQKEEATGKHSEKAAESKGDKSTSNGNATDTKKSHKHKKKEKSKDKEKERNDRDKDKDKERDKDKLKEREKDKQHVTGSEKSSTVDPSPKLEGASPATEGGAPDKTPVSASASSGSKKEKHKKSKEKSSGKDEKRQREAVDKQADTKHTGKSQQSQSGQSKTPSNLDLSDMDSAQSAPDLAATNALAAAAAATLQHSDSSNSSFPDLPARSSSQQKPTKGNTGSGKETKSTVKEHKGKSKQNDKTLEKNTDKTEKPDKTPDPKVDKSEKSEKEDKKRNRRSSQSSNSGSGAGVTGAFIEPPVKASKKEQGKAGEKSKSPSLRPPRETNSTGTGGGTPNAGAGFLAPPSSSPSNNHSAAVAASLNNNNNNNNNNTNSNSSHSPGEMTTPGQLQLPTEYLSELQELHHKIMTLQDNEELQHVVEMIAATGCYEITHKTFDFDLCKLDRGTVQRLQEFLATSVS
Protein: Poly(U)-binding-splicing factor hfp (68 kDa poly(U)-binding-splicing factor) (PUF60 homolog) (Protein half pint) (Q8T6B9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Splicing factor that regulates oogenesis and controls both mitosis and mRNA localization in the germline by regulating mRNA splicing of a subset of genes within the ovary. Probably acts by regulating the alternative splice site selection of the otu transcript. Also regulates the alternative splicing of eIF4E1 and grk, while it is not involved in the splicing of par-1, sqd and psq.
Subcellular location: Nucleus {ECO:0000269|PubMed:11879639}.
Interaction partners:
- LD21442p
- Probable U2 small nuclear ribonucleoprotein A'
- P-element somatic inhibitor, isoform C
- Deubiquitinase otu
- U1 small nuclear ribonucleoprotein A
- Splicing factor 3A subunit 2
- Splicing factor 3B subunit 3
- U2 snRNP-associated SURP motif-containing protein
- Survival of motor neuron-related-splicing factor 30
- ATP-dependent RNA helicase DHX15 homolog
Sequence:
MGSNDRASRSPRSDDQREISDMPATKRTRSDSGKSTDSKIPYLSQPLYDLKQTGDVKFGPGTRSALLGLLGGALPKLSSEQHDLVSKAKKYAMEQSIKMVLMKQTLAHQQQQLATQRTQVQRQQALALMCRVYVGSISFELKEDTIRVAFTPFGPIKSINMSWDPITQKHKGFAFVEYEIPEGAQLALEQMNGALMGGRNIKVGRPSNMPQAQQVIDEVQEEAKSFNRIYVASIHPDLSEEDIKSVFEAFGPILYCKLAQGTSLHTHKGYGFIEYANKQAMDEAIASMNLFDLGGQLLRVGRSITPPNALACPTTNSTMPTAAAVAAAAATAKIQALDAVASNAVLGLSQNTPVMAAGAVVTKVGAMPVVSAATSAAALHPALAQAAPALLPPGIFQAPTPVAPSLLGVPAGLQPLQAVVPTLPPPALLATPTLPMTVGGVGVGLVPTVATLAGAEASKGAAAAAALSAAANNAAVTAANLSENIKKAHEKQQEELQKKLMDEGDVQTLQQQENMSIKGQSARQLVMQRLMRPVDSRVIILRNMVGPEDVDETLQEEIQEECSKFGTVSRVIIFNEKQTENEDDDEAEIIVKIFVEFSAGAEAMRGKEALDGRFFGGRRVVAELYDQGIFDQGDLSG
Protein: Fructose-1,6-bisphosphatase 1 class 2 (FBPase 1 class 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1 class 2) (P0A9C9)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Is likely to be involved in gluconeogenesis during growth on glycerol. Also displays a low activity toward glucose 1,6-bisphosphate, and no activity against ribulose 1,5-bisphosphate, fructose 2,6-bisphosphate, or fructose 1-phosphate.
Subcellular location: Cytoplasm.
Interaction partners:
- Fructose-1,6-bisphosphatase class 1
- Transketolase 1
- Fructose-bisphosphate aldolase class 2
- Transketolase 2
- Transaldolase A
- Glucose-6-phosphate isomerase
- Transaldolase B
- ATP-dependent 6-phosphofructokinase isozyme 2
- ATP-dependent 6-phosphofructokinase isozyme 1
- Glycerol kinase
Sequence:
MRRELAIEFSRVTESAALAGYKWLGRGDKNTADGAAVNAMRIMLNQVNIDGTIVIGEGEIDEAPMLYIGEKVGTGRGDAVDIAVDPIEGTRMTAMGQANALAVLAVGDKGCFLNAPDMYMEKLIVGPGAKGTIDLNLPLADNLRNVAAALGKPLSELTVTILAKPRHDAVIAEMQQLGVRVFAIPDGDVAASILTCMPDSEVDVLYGIGGAPEGVVSAAVIRALDGDMNGRLLARHDVKGDNEENRRIGEQELARCKAMGIEAGKVLRLGDMARSDNVIFSATGITKGDLLEGISRKGNIATTETLLIRGKSRTIRRIQSIHYLDRKDPEMQVHIL
Protein: Envelope glycoprotein B (gB) (F5HB81)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Envelope glycoprotein that forms spikes at the surface of the virion envelope. Participates in viral entry through an RGD motif that binds ITGAV-ITGB3. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04032}.
Interaction partners:
Sequence:
MTPRSRLATLGTVILLVCFCAGAAHSRGDTFQTSSSPTPPGSSSKAPTKPGEEASGPKSVDFYQFRVCSASITGELFRFNLEQTCPDTKDKYHQEGILLVYKKNIVPHIFKVRRYRKIATSVTVYRGLTESAITNKYELPRPVPLYEISHMDSTYQCFSSMKVNVNGVENTFTDRDDVNTTVFLQPVEGLTDNIQRYFSQPVIYAEPGWFPGIYRVRTTVNCEIVDMIARSAEPYNYFVTSLGDTVEVSPFCYNESSCSTTPSNKNGLSVQVVLNHTVVTYSDRGTSPTPQNRIFVETGAYTLSWASESKTTAVCPLALWKTFPRSIQTTHEDSFHFVANEITATFTAPLTPVANFTDTYSCLTSDINTTLNASKAKLASTHVPNGTVQYFHTTGGLYLVWQPMSAINLTHAQGDSGNPTSSPPPSASPMTTSASRRKRRSASTAAAGGGGSTDNLSYTQLQFAYDKLRDGINQVLEELSRAWCREQVRDNLMWYELSKINPTSVMTAIYGRPVSAKFVGDAISVTECINVDQSSVNIHKSLRTNSKDVCYARPLVTFKFLNSSNLFTGQLGARNEIILTNNQVETCKDTCEHYFITRNETLVYKDYAYLRTINTTDISTLNTFIALNLSFIQNIDFKAIELYSSAEKRLASSVFDLETMFREYNYYTHRLAGLREDLDNTIDMNKERFVRDLSEIVADLGGIGKTVVNVASSVVTLCGSLVTGFINFIKHPLGGMLMIIIVIAIILIIFMLSRRTNTIAQAPVKMIYPDVDRRAPPSGGAPTREEIKNILLGMHQLQQEERQKADDLKKSTPSVFQRTANGLRQRLRGYKPLTQSLDISPETGE
Protein: Sperm head and tail associated protein (C4P6S0)
Organism: Mus musculus (Mouse)
Function: Plays a role during spermatogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19686095}. Note=Localized to the peri-acrosomal region of the round spermatids as well as the heads and tails of the elongated spermatids and spermatozoa. Redistributed within the head during sperm capacitation.
Interaction partners:
Sequence:
MNSSPPFLLKISAPSTSPQADCPNNYSFPPESPSSCRKGFTPVLTLEVPVAPGKDFNDHLSCNAGLSPNAGNRFTNPPYSREPFSCLTISSPCLPRRIPTPPPPPPVLSSPPPPERCPFEPFSPLLGRLYRQEPAGSSSPCFDRFSLQGSPSPHQRNLCCNYIDSPESQRSCPPSPRLCYVTSPPLIHQAPRASPVTSPELTHITLETGPVISTPLMPGSQGNYSIISPLLTHRPLRPGLAISPPLAHRSVETRPLTPASISHRGPHCPSRRSYNDPPLSSASSPPSGNPYHDNPMPPNSCEPKPQLDVPLGKNGCGPPLSSQAGMSGSPISPQEGCIHYSHLCPDSQISAPRSPFCVINLPPESAGSPSSSLPQALQKPCVGSFLWEPGGNSYLLLTPGTIISGPSCTTGPPLPQCPNPSPYFPSPLNNQCVAPPQSPRGYNEPRPPTSAPPQMKSPKSPESRRNPYKCRSLDNTPHHTPPSHSKSHKTNTCPQPPSQSFGLFSPCMEPAITTTSNSCPKEPPPETAVLKTVAPTSCPHSSPCNPALPSRYPKSSPHVPPPVSPCNTHMYSVVPPTSHLSPLSSPLNQSIPLPQPAVLPCGTYSAPRGPPSHIKSVAPPCSTHIYSFIPLRTPFDPRCLPVVPRARFCPTTVPCGIHTYAVTSPVPLNNPSQIPYSCSLPPSKTSSTCSTSVSSTIVCSDYQSSDSQINHQNKSQSPNKNSSLHNQSKSPLRRGAFQSRSRSRSSSPLQSSTQDRNESTNMGVKHHKRSRKQSQSPADGKIESQSKSLQHRKSVGQIKSPHSKKK
Protein: BK channel (H8ESD8)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGEIYSPSQSKGFNQPYGYPMNCNLSRVFMEMTEEDRKCLEERKYWCFLLSSITTFCASMILVVIWRVVTHLCCQRREKEFVEPIPAPEAVQINMNGSKHAPSETDPFLKQQEEKHLGWMTEAKDWAGELISGQSLTGRFLVLLVFILSIGSLIIYFYDASFQNFQVETCIPWQDSPSQQIDLGFNIFFLVYFFIRFIAASDKVWFLLEMYSWIDFFTIPPSFVAIYLQRNWLGFRFLRALRLMTVPDILQYLNILKTSSSIRLTQLVTIFVAVCLTGAGLVHLLENSGDFFKGFINPHRITYADSVYFVLVTMSTVGYGDIYCTTLCGRLFMIFFILFGLAMFASYVPEIADLIGNRQKYGGEYKGEHGKKHIVVCGHITYDSVSHFLQDFLHEDRDDVDVEVVFLHRVVPDLELEGLFKRHFTKVEFFTGTVMDSLDLSRVKIGDADACLVLANKYSTNPDAEDAANIMRVISIKNYSSDIRVIVQLMQYHNKAYLLNIPSWDWKRGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSQTTPDWLNLYLCGAGMEMYTDTLSHSFVGMTFPEAVDLLFNRLGLLLLAIELKDEENKECNIAINPGPHIVIQPQTQGFFIAQSADEVKRAFFWCKQCHDDIKDVSLIKKCKCKNLALFRRNTKHSTAAREKNAKISDYSDFDALFYQNDARATDVLQQFQPQAPAGPMGHLGQQVQLRMINQQRPSSGGRRNSMSIPPDGRGVDFSKDFEQQFQDMKYDSTGMFHWCPSRNLEDCVLERHQAAMTVLNGHVVVCLFADQDSPLIGLRNFIMPLRSSNFHYHELKHVVIVGDLEYLRKEWKTLYNLPKISILNGSPLSRADLRAVNINLCDMCVIISARVPNTEDTTLADKEAILASLNIKAMQFDDTLGFFPMRHQTGDRSPLGSPISMQKKGAKFGTNVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAISVLDSLMSTTYFNDSALTLIRTLVTGGATPELELILAEGAGLRGGYSTPETLSNRDRCRIAQISLQDNPYDGVVHNTTYGAMFTIALRRYGQLCIGLYRLHDQDNPDSMKRYVITNPPAELRIKNTDYVYVLEQFDPGLEYEPGKRHF
Protein: Aminopeptidase YpdE (EC 3.4.11.-) (P77585)
Organism: Escherichia coli (strain K12)
Function: Has a broad aminopeptidase activity on non-blocked peptides by progressively cleaving amino acids off the peptide substrate. Aminopeptidase activity stops at the residue before the first proline in the peptide. Cannot cleave when proline is the first N-terminal residue.
Interaction partners:
- Aminopeptidase YpdF
- Multiphosphoryl transfer protein 1
- Uncharacterized protein YgfM
- Fructose-like permease IIC component 1
- PTS system fructose-like EIIB component 1
Sequence:
MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAIDVLPVGNVRMAARQLQPVRITTREECKIPGLLDGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRVMGKAFDDRLGCYLLVTLLRELHDAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFDYGAANHRQIGNGPMLVLSDKSLIAPPKLTAWVETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDILQMQQLLSALIQRLTRETVVQLTDFR
Protein: Arginine transporter 1 (Amino acid transporter 1) (Apicomplexan amino acid transporter 1) (TgApiAT1) (Major facilitator superfamily domain-containing protein) (Novel putative transporter 1) (TgNPT1) (S8EZA7)
Organism: Toxoplasma gondii (strain ATCC 50611 / Me49)
Function: Selective L-arginine transporter that is essential for parasite survival and virulence. Does not require other inorganic ions such as sodium, chloride, potassium or calcium.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28205520}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAGLLSSCCGRVYALLPDSAHPSAQQKTPFGVNRYVLLVIYMIYALLTSSVYFGWRSMSAMLFKSGQFSWVCTGESADTSPEEGETDYLCALQDTKVQSLFTIAMACHFTCSAVAGYLLDTVGPKAVALLGQTFNALAWILLAFSGPNFRSVYPAFVFMGAGADVSVYPTLLIVNLFPGSTALIMATLGACISLSFFVPLVLRTMWESTGISFEAVCIGYAVAGPILCAVVAFFFIPFKAFKGVDNFSACVEAEKLANSPTAQSSPKAVDSPPCDEGASSRGRLAVSHNTERTAPDDEQEKDNTERISLSDLACDPRFKKQKVSFSSQAFTFLYFGICLYFTVCGWVMAYYQEAAGRFLCNDAEYTLEILTPLSTIPCLLFGVVINRIGIMPVILMLNTIGLLTYVCVVAAESVVAQYFSVIFFFMYISIFTTQMYVFVESTFDSAHFGKLIGVASLIGGLLSLISNVLYGDVTVGMLNGDTRPVVIALLAVIILMYPILLAMRTKRNRKKQMEQEDIRSRVLELKAAHAADAA
Protein: Matrix metalloproteinase-14b precursor (EC 3.4.24.80) (Membrane-type matrix metalloproteinase 1 beta) (Q7T2J1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MIWSGFTRLLLLIFVCAHRSSSKQDMKPEAWLQQYGYLPPGDLRTHTARSPQSVPSAIAAMQRFYGLTVTGNLDANTLEAMKRPRCGVPDKFGSELKSNLRKKRYAIQGLKWDKNEITFCIQNYTPKVGEYETFEAIRKAFKVWESVTPLRFREISYSDIRDKVVDFADIMLFFADGFHGDASPFDGEGGFLAHAYFPGNGIGGDTHFDAAEPWTIGNKDLLGNDVFLVAVHELGHALGMEHSNDPSAIMAPFYQWMETDHFVLPDDDRKGIQKLYGPGSGGHPRPPVSPETPHHTPYPTPYRPGGPSYGPNICEGHFDTIGIFRGEMFVFKGKWFWRVRNNQVMENYPMPIGHFWRGLPTDINAAYEREDGKFVFFKGDRHWVFTESNLEPGYPKVLGELGTGVPKDKLDAALLYTPTGYTYFFRGNKYYRYNEDTHSVDPDYPKPISKWQGVPDNIKAAFMSRDQGYTYFYKANKYWKFNNQLLKVEPGYPKSALKDWMGCPNEDSNTGGGGSDRDRERERERERERERERERAREREREQDRTNEVDKTEEEGKKEETEVLIIEVEDAPSSRGGAAAVVVPLMLLVCVIFTLGALLFFRRYGTPRRLLYCQRSLLDKV
Protein: Uncharacterized transporter C3H1.06c (Q10072)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MNPSSSPNRSLNPTRGLNLYSTGNEVTWFSSTVDEVNELKPAKSKAFSISAQDQIYGTSSLKSRFSTHEASSEKDDSSDFTLVLPSNRMYIVIPGLMLSIFLSALDQTVITTAIPTIVANLDGGSSYSWIGTAYTLAQTSILPFCGIMSEVVGRKIVLYTSIVLFLFGSAMCGAAQNMLWLVLCRAVQGIGGGGITSLVTIVIADITPLQTRPYYTGCMGVTWGLASVMGPLIGGAISQKASWRWIFFINLPTGGLSLALLIFFLNLVPKPTVSFRVFLRDFDFVGIITITTGVVLFLVGLNIGSTTGHWAHANVLCYLIFGILCIAGFVVNEFYTTRTRIITPSAFKTLSLTSVMVTSFLHYYIVSTITYYIPVYFQNIKGDGPLMSGVHTLSLAVVSSLLSAVSGMGIGKLKNYRYPMIGGWIVLLAGTGSMIAIYYNTDISRTMGFLALTAVGTGNLFQPNLIAVQASVPPALIATSCSAFMLLRNMGASVGISMGAVIYDQQLTTLLKGTKYSAGLSYSQIASIPNVSEKNFVFNAYANAIRMIWIVNCPVAGVGMLLSFFTKQEKLSQSVTEYKEKDKGFKDAP
Protein: Neuroplastin b precursor (Zgc:77326) (Q6NZV3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MMLSYSGILALFLVHGNVMLPYVSSQNAGFVKSPMSEVKLTGDAFELYCDVVGNPVPEIQWWYADINRADSFKQLWDGARKRRVSINTASGANVVSVLAISRLTLEDAGIYECRASNDPRRNDMRQNPAITWIRTQATITVLQRPRINASDQEILQPKSSKTSQDPPEPIVLKCNLTNSHSTHQETFWMKNGQEISSSRTQRKHTEFRLNKPRTDDSGEYMCVYTFKSAPNANASIEVKACPEIIGHKRSENKKEGENATLYCKSAGYPHPVWTWRKKVGRDSYMDIDNSTGRFFIVNRENFTELSILDLDIRTDPGEYFCNASNIIGFTNSSTILRVRSHLAPLWPFLGVLAEIIILVVIIVVYEKRKKPDEVFEDDEPVTTMKTNSTNNHKDKNVRQRNTN
Protein: Pcdha2 protein (Protocadherin alpha 2) (B9EJ92)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MPSLRGGPEVRQCLLLLLPFLAAWEAGNGQLHYSVPEEAKHGTFVGRIAQDLGLELTELVPRLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVRDINDNPPRFPMTEKTIQFSESRSLDSRFPLEGASDADIGVNALLSYKLSPSELFFLDVQTSDELSQSLFLVLGKSLDREEDAEVKLLLVATDGGKPELTGTVQILIKVLDVNDNEPTFPQSVYKVQLLENTANGTLVMKLNASDADEGSNSEIVYSLGSDVSSTTRTKFQIDPNSGEVRTKGELDYEERTSYEIQVIASDKGTPAMSGHCKISVKLVDINDNTPEVSITSLSLPVQENAPLGAVIALISVSDRDSGVNGQVTCSLSPHVPFKLVSTFKNYYSLVLDSALDREATADYKVMVTARDGGSPSLRATASVSVEVADVNDNAPVFAQPEYTVFVKENNPPGAHIFTVSAMDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLQFQVTARDAGVPALGSNVTLQVFVLDENDNAPLLLPQGAVGVGGSVSELVPRSVGSGHVVTKVRAVDADSGYNAWLSYELQSTVGMRSLFRVGLYTGEISTTRALDEVDAPRQRLLVLVKDHGEPSLTATATVLVSLVENSQAPKTSSRALVDAAGQEASLVTVNVYLVIAICAVSSLLVLTLLLYTALRCSAMPTDGACAPGRPMLVCSSAVGSWSYSQQRRQRVCSGEGPPKTDLMAFSPSLSQGPESAEERQPPLEAEYLGKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPEPKKQTQVSFLPRRKGEASQPRQ
Protein: AMP deaminase (EC 3.5.4.6) (M9MS55)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNFNRMDTAHRLRVDVRLYGGSMGNQLNDKGTASSTPTISSDDLSDLADSPVDEKAEADVEVTNEISAPYEVPQFPIEQIEKKLQIQRHLNEKQATGPRPVATAAVLATNRESSSSTEGRESAVTMERNDADINFQRVSISGEDTSGVPLEDLERASTLLIEALRLRSHYMAMSDQSFPSTTARFLKTVKLKDRINNLPVKEVSDIIRKMSVANIQESADVHLRHSPMKITNPWNVEFPNDEDFKIKPLNGVFHIYENDDESSEIKYEYPDMSQFVNDMQVMCNMIADGPLKSFCYRRLCYLSSKYQMHVLLNELRELAAQKAVPHRDFYNTRKVDTHIHAASCMNQKHLLRFIKKTLKNNANEVVTVTNGQQMTLAQVFQSMNLTTYDLTVDMLDVHADRNTFHRFDKFNSKYNPIGESRLREVFLKTDNYLNGKYFAQIIKEVAFDLEESKYQNAELRLSIYGKSPDEWYKLAKWAIDNDVYSSNIRWLIQIPRLFDIFKSNKMMKSFQEILNNIFLPLFEATARPSKHPELHRFLQYVIGFDSVDDESKPENPLFDNDVPRPEEWTYEENPPYAYYIYYMYANMTVLNKFRQSRNMNTFVLRPHCGEAGPVQHLVCGFLMAENISHGLLLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLNYHRNPLPEYLARGLIISLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSSCDMCELARNSVMMSGFPHAIKQQWLGPIYYEDGIMGNDITRTNVPEIRVAYRYETLLDELSNIFKVNQTCSIADMNAT
Protein: Cytochrome P450 85A1 (AtCYP85A1) (3-dehydroteasterone synthase) (EC 1.14.14.179) (Brassinosteroid-6-oxidase 1) (BR6ox 1) (C6-oxidase 1) (Castasterone synthase) (EC 1.14.14.179) (Teasterone synthase) (EC 1.14.14.179) (Typhasterol synthase) (EC 1.14.14.179) (Q9FMA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the C6-oxidation step in brassinosteroids biosynthesis. Converts 6-deoxocastasterone (6-deoxoCS) to castasterone (CS). May also convert 6-deoxoteasterone (6-deoxoTE) to teasterone (TE), 3-dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo-3-DHT) to 3-dehydroteasterone (3DT, 3-DHT), and 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY). Required for the initiation of female gametogenesis (megagametogenesis).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 734A1
- 3-epi-6-deoxocathasterone 23-monooxygenase CYP90C1
- 3-epi-6-deoxocathasterone 23-monooxygenase CYP90D1
- Steroid 5-alpha-reductase DET2
- Cytochrome P450 85A2
- 7-dehydrocholesterol reductase
- Delta
- Delta
- Protein BRASSINAZOLE-RESISTANT 2
- Protein BRASSINAZOLE-RESISTANT 1
Sequence:
MGAMMVMMGLLLIIVSLCSALLRWNQMRYTKNGLPPGTMGWPIFGETTEFLKQGPNFMRNQRLRYGSFFKSHLLGCPTLISMDSEVNRYILKNESKGLVPGYPQSMLDILGTCNMAAVHGSSHRLMRGSLLSLISSTMMRDHILPKVDHFMRSYLDQWNELEVIDIQDKTKHMAFLSSLTQIAGNLRKPFVEEFKTAFFKLVVGTLSVPIDLPGTNYRCGIQARNNIDRLLRELMQERRDSGETFTDMLGYLMKKEGNRYPLTDEEIRDQVVTILYSGYETVSTTSMMALKYLHDHPKALQELRAEHLAFRERKRQDEPLGLEDVKSMKFTRAVIYETSRLATIVNGVLRKTTRDLEINGYLIPKGWRIYVYTREINYDANLYEDPLIFNPWRWMKKSLESQNSCFVFGGGTRLCPGKELGIVEISSFLHYFVTRYRWEEIGGDELMVFPRVFAPKGFHLRISPY
Protein: RNA guanine-N7 methyltransferase activating subunit (Protein FAM103A1) (RNA guanine-7 methyltransferase activating subunit) (RNMT-activating mRNA cap methyltransferase subunit) (RNMT-activating mini protein) (RAM) (Q9BTL3)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Promotes the recruitment of the methyl donor, S-adenosyl-L-methionine, to RNMT. Regulates RNMT expression by a post-transcriptional stabilizing mechanism. Binds RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:22099306}.
Interaction partners:
- mRNA cap guanine-N
- Eukaryotic translation initiation factor 4E
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 3
- Eukaryotic translation initiation factor 4E type 2
- Nuclear cap-binding protein subunit 1
- Protein argonaute-2
- Eukaryotic translation initiation factor 4E type 3
- Fragile X messenger ribonucleoprotein 1
- Eukaryotic translation initiation factor 4E type 1B
Sequence:
MTDTAEAVPKFEEMFASRFTENDKEYQEYLKRPPESPPIVEEWNSRAGGNQRNRGNRLQDNRQFRGRDNRWGWPSDNRSNQWHGRSWGNNYPQHRQEPYYPQQYGHYGYNQRPPYGYY
Protein: Gim5A protein (Q38DM9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSLPPDKTLFGSHSQRLVAVAQFCSLVSAGVAGSKHYTLVARSACALAKVLANYLCLSRLKGSYLLLREVSPSSVRRRLHSSPSWFTGVMRVLTMLAMLLFRITDKIALLANEGVLSNNICFYTSRLIPSLLFYCNLMQTMTSAALLKAVRPISFEATDTRNVFRKRYYLQGVLSFLEGVGLMTYAMTLFPRGVPPLAMTLHEKHLLTHWLAVAASSFPPALSVSTTTQGLIGLAATLPSFFMSP
Protein: Calpain-2 catalytic subunit (EC 3.4.22.53) (Calcium-activated neutral proteinase 2) (CANP 2) (Calpain M-type) (Calpain-2 large subunit) (Millimolar-calpain) (M-calpain) (Q92178)
Organism: Gallus gallus (Chicken)
Function: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250}.
Interaction partners:
- Talin-1
- Talin 2.
- Uncharacterized protein.
- BH3-interacting domain death agonist
- Calpain-1 catalytic subunit
- Uncharacterized protein
- Bcl-2 homologous antagonist/killer
Sequence:
MAGMAAALAKERAAAAGAGRHGQAVPYLGQDFGALRRECLQGGRLFHDPSFPAGPAALGYRELGPNSYKTKGVVWCRPTELCSCPRFIAGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPRDQSFQDEYAGIFHFQFWQYGEWVDVVVDDRLPTKNGELLFVHSAEGSEFWSALLEKAYAKLNGSYEALSGGTTTEGFEDFTGGIAEWYELQKAPPNLFKIIQKALQKGSLLGCSIDITSAAETEAVTSQKLVKGHAYSVTGAEEVNFRGSIQKLIRIRNPWGEVEWTGKWNDNCPNWSGVDPEVRERLTRRHEDGEFWMAFNDFLRHYSRLEICNLTPDTLASDRYKKWSLLKLDGNWRRGATAGGCRNYPNTFWTNPQYLIKLEEEDEDPDDPEGGCTFLIGLIQKHRRKQRKMGEDMHTIGFAIYEVPPEFSGQTNIHLSKNFFLTNKAREKSNTFINLREVLNRFKLPAGEYIIVPSTFEPNLNGDFCLRVFSEKNANSTVIDDEIEANFEETEIDEDDIEPSFKKLFGQLAGSDAEISAFELRSILNKILAKRQDIKSDGFSIETCKIMVDLLDNDGSGKLGLKEFHTLWTKIQKYQKIYREIDVDRSGTMNSYEMRRALEAAGFKLSCQLHQIIVARFADEDLIIDFDNCVRCLIRLETLYKMFRKLDTEKTGTIELNLINWLFFTVI
Protein: RE17452p (Q8SZ43)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTLLGPSAPGMAFMMKKKKYKFNVEVQLQDLVEVALVNEVLFAKIRLLDGGSFQEYSSREEVRNHRVEWNRSFEFPCKMSANASTGVLDPCHLRISIRKEMKGGRSYYKLGFIDLNLAEFAGAGLTSRRFLLEGYDSRHRLDNSMLRVSIKMHMLSGDILFKAPTPNLKSKQSKPSIDDFSNAATGVGLQIPTATALPSIGGGSGGASVSLGGSGVTLGGIPGNQSLPGTRPVSTTKEEDIDNQALIAAIVTDSGLSESSESGVTLTTDNLQQHGSVVVANPISPVTQALPQLGIIGSNNYGTTGGAIGFTGAGNATLIEMGHSRNSSNTSQMSKGSGYSSFSHSQHSRQSSEGDSGHARNPSSGSLVISETGSLDRTKSSGEKRKKGALDDGPRVSDRVEETRVNPDSLIDEILKDTKLDQLEESAETSGLQLYIARDGTASLGGHEVKSSVRAGALKQVVMQDRR
Protein: Splicing factor 1 (A0A8I6G7I2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367126}.
Interaction partners:
Sequence:
MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHTLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAELGEAPVPASVGSTSGPATTPLASAPRPAAPASNPPPPSLMSTTQSRPPWMNSGPSENRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMDQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGTPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMIPPRSSDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGKAA
Protein: Diacylglycerol kinase beta (DAG kinase beta) (EC 2.7.1.107) (Diglyceride kinase beta) (DGK-beta) (Q6NS52)
Organism: Mus musculus (Mouse)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). Has a higher activity with long-chain diacylglycerols like 1,2-di-(9Z-octadecenoyl)-sn-glycerol compared to 1,2-didecanoyl-sn-glycerol (By similarity). Specifically expressed in brain, it regulates neuron-specific morphological changes including neurite branching and neurite spine formation.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:20657643}; Peripheral membrane protein {ECO:0000305|PubMed:20657643}. Cell membrane {ECO:0000269|PubMed:20657643}; Peripheral membrane protein {ECO:0000305|PubMed:20657643}. Cytoplasm {ECO:0000305|PubMed:20657643}. Note=Translocation to the plasma membrane is induced by phorbol esters. {ECO:0000250|UniProtKB:Q9Y6T7}.
Interaction partners:
- Lipoprotein lipase
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Adenylate cyclase type 5
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
- Phospholipase D2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
Sequence:
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDFEGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPNVKSKPALLSGGLRMNKGAITPPRSSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIIGQMMHVAEYLEWDVTELNPILHEMMEEIDYDRDGTVSLEEWIQGGMTTIPLLVLLGLENNVKDDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVKSKKNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQTTLHNKCASHLKPECDCGPLKDHILPPTTICPVVLTMPSAGASVPEERQSTAKKEKSSSQQPNKATDKNKMQRANSVTMDGQGLQITPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGLHFFRDVPDFRVLACGGDGTVGWILDCIEKANVVKHPPVAILPLGTGNDLARCLRWGGGYEGENLMKILKDIESSTEIMLDRWKFEVTPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFHIMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIAILNIPSMHGGSNLWGESKKKRSHRRIEKKGSDKRPTLTDAKELKFASQDLSDQLLEVVGLEGAMEMGQIYTGLKSAGRRLAQCSSVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPMLMGPPPKTGLFCSLIKRTRNRSKE