wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-binding protein NOB1 (Q9N3D3)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037125}.
Interaction partners:
- Uncharacterized protein byn-1
- Serine/threonine-protein kinase RIO2
- Protein LTV1 homolog
- Pre-rRNA-processing protein TSR1 homolog
- Serine/threonine-protein kinase RIO1
- Ubiquitin-like domain-containing protein
- Small ribosomal subunit protein uS7
- RNA-binding protein pno-1
- 26S rRNA
- Small ribosomal subunit protein uS11
Sequence:
MTNKEKPIKHLVIDTCAIIANRNLHALADHYYAPPQILDELRSSAARKLWNTLPFEVTLREPTQTALRAVIDASKTTGDFQSLSMVDIKMIALTYDLHRQYVAENDVAETTEDDEKKNIEDLSAKVEQVTVGENTEDTKEEEIEENEESEDSAVSEGSESSESSESFDEDGWITQDNIEETLKKLGAFEIEENMLVGCLTTDFALQNVLLAMNLSLVSLSGYRIRKLKSFVLRCRTCFSTTSVMTKEFCPACGHKTLHKCAVSVDEDGNQQLHINWNRMANRRGLVYTLANPKGGKHATNERLFEDQPMPHMRMAKIHMDPLADGPFSVHDVTSRSAMLGVRTINNRAKQNRNPNESKRGGRRK
Protein: Pliceosome associated protein-like protein (T23J18.18) (Q9LPY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein At3g23325
- Nuclear protein-like
- Splicing factor 3B subunit 4
- At2g32600/T26B15.16
- Small nuclear ribonucleoprotein Sm D2
- Uncharacterized protein At4g14342
- Splicing factor SF3a60 homolog
- RNA-binding
- Splicing factor 3B subunit 6-like protein
- PHD finger-like domain-containing protein 5A
Sequence:
MTFRFPISFLKNLEISYIDQFYFPIFYLLQINVRSLFSQQHPNMTAHSIVAHVDSVLPKKSREIDRRRRRRKRKKKNKASQADVDAMDVSKSLSSTPTGIETPDAIELRKEQRKEPDRALYQVLEEKGESVVAPGTLLRTTHTYVIKTGTQDKTGTKRVDLLRGQKTDRVDFSLQPEELDAMGNVLQYEEAREEEK
Protein: Aminodeoxyfutalosine synthase (AFL synthase) (Aminofutalosine synthase) (EC 2.5.1.120) (Menaquinone biosynthetic enzyme MqnE) (Q727U8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Chorismate dehydratase
- Cyclic dehypoxanthine futalosine synthase
- 1,4-dihydroxy-6-naphtoate synthase
- 4-hydroxybenzoate polyprenyltransferase
- Thiazole synthase
- 3-octaprenyl-4-hydroxybenzoate carboxy-lyase family protein
- Response regulator
- Flagellar basal body rod protein FlgB
- Anti-sigma factor, putative
- Phosphomethylpyrimidine synthase
Sequence:
MLDTDHYARLGLGEIRDKVMAGHRLSYDDGLRLFACPDITAIGALAHHVRTRLHGDRTYYVVNRQVNYTNICVNGCLFCAFQRERGQQGAFALTPDEMVARVMDDGGVPFSEVHIVGGCHPDLPLEWFEDVIRRIHAARPSIVVKAFTAVEIAHFAKLAGIDTEEVLRRLKAAGLSQLPGGGAEIFAPDVRQRICPRKIDAEAWLRVAGEAHRLGIGTNCTMLFGHLESEADRVDHLCRLRAQQDETGGFTCFIPLPFLTENSLLKLPPERVGQHVGLDRLRTVAVSRLMLDNIAHIKAYWVMMGVKLAQVALHYGANDLDGTIVEEKIGHMAGSDAVQAMTIAQLEDMIRRSGFTPVRRDTHFNPVEEARA
Protein: ATP-dependent permease PDR15 (Q04182)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Oligomycin resistance ATP-dependent permease YOR1
- Transcription factor PDR3
- Transcription factor PDR1
- Pleiotropic ABC efflux transporter of multiple drugs
- ATP-dependent permease PDR10
- Hexose transporter HXT9
- Hexose transporter HXT14
- Hexose transporter HXT11
- DNA damage-inducible protein 1
- Inositolphosphotransferase 1
Sequence:
MSSDIRDVEERNSRSSSSSSSSNSAAQSIGQHPYRGFDSEAAERVHELARTLTSQSLLYTANSNNSSSSNHNAHNADSRSVFSTDMEGVNPVFTNPDTPGYNPKLDPNSDQFSSTAWVQNMANICTSDPDFYKPYSLGCVWKNLSASGDSADVSYQSTFANIVPKLLTKGLRLLKPSKEEDTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNSHGFKIAKDSIVSYNGLSSSDIRKHYRGEVVYNAESDIHLPHLTVYQTLFTVARMKTPQNRIKGVDREAYANHVTEVAMATYGLSHTRDTKVGNDLVRGVSGGERKRVSIAEVAICGARFQCWDNATRGLDSATALEFIRALKTQADIGKTAATVAIYQCSQDAYDLFDKVCVLDDGYQLYFGPAKDAKKYFQDMGYYCPPRQTTADFLTSITSPTERIISKEFIEKGTRVPQTPKDMAEYWLQSESYKNLIKDIDSTLEKNTDEARNIIRDAHHAKQAKRAPPSSPYVVNYGMQVKYLLIRNFWRMKQSASVTLWQVIGNSVMAFILGSMFYKVMKKNDTSTFYFRGAAMFFAILFNAFSCLLEIFSLYETRPITEKHRTYSLYHPSADAFASVLSEMPPKLITAVCFNIIFYFLVDFRRNGGVFFFYFLINVIATFTLSHLFRCVGSLTKTLQEAMVPASMLLLAISMYTGFAIPKTKILGWSIWIWYINPLAYLFESLMINEFHDRRFPCAQYIPAGPAYQNITGTQRVCSAVGAYPGNDYVLGDDFLKESYDYEHKHKWRGFGIGMAYVVFFFFVYLILCEYNEGAKQKGEMVVFLRSKIKQLKKEGKLQEKHRPGDIENNAGSSPDSATTEKKILDDSSEGSDSSSDNAGLGLSKSEAIFHWRDLCYDVPIKGGQRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGNIFVDGRLRDESFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPSSVSIEEKNRYVEEVIKILEMQQYSDAVVGVAGEGLNVEQRKRLTIGVELAARPKLLVFLDEPTSGLDSQTAWDTCQLMRKLATHGQAILCTIHQPSAILMQQFDRLLFLQKGGQTVYFGDLGEGCKTMIDYFESKGAHKCPPDANPAEWMLEVVGAAPGSHATQDYNEVWRNSDEYKAVQEELDWMEKNLPGRSKEPTAEEHKPFAASLYYQFKMVTIRLFQQYWRSPDYLWSKFILTIFNQVFIGFTFFKADRSLQGLQNQMLSIFMYTVIFNPILQQYLPSFVQQRDLYEARERPSRTFSWLAFFLSQIIVEIPWNILAGTIAYCIYYYAVGFYANASAAGQLHERGALFWLFSIAFYVYIGSMGLLMISFNEVAETAAHMGTLLFTMALSFCGVMATPKVMPRFWIFMYRVSPLTYMIDALLALGVANVDVKCSNYEMVKFTPPSGTTCGDYMASYIKLAGTGYLSDPSATDICSFCAVSTTNAFLATFSSHYYRRWRNYGIFICYIAFDYIAATFLYWLSRVPKKNGKISEKPKK
Protein: Stress-activated protein kinase JNK (dJNK) (EC 2.7.11.24) (Protein basket) (P92208)
Organism: Drosophila melanogaster (Fruit fly)
Function: Responds to activation by environmental stress by phosphorylating a number of transcription factors, primarily components of AP-1 such as Jra and also the transcriptional repressor aop, and thus regulates transcriptional activity. Component of the immune response activated by bacterial infection, and is involved in wound healing and in dorsal closure, a morphogenetic movement during embryogenesis. Functions in the systematic response to wounding acting downstream of the Hayan-phenoloxidase PPO1 cascade. Exhibits cytoprotective activity in neuronal cells in response to wounding to the integument. Controls the expression of a phosphatase, puckered, at the edges of wounded epidermal tissue and in the dorsal epithelium during dorsal closure. Regulates the activity of SREBP in neurons and thereby the accumulation of lipids in glia. Plays a role in positively regulating the expression of DIP2 independently of AP-1, thereby ensuring proper axon guidance in mushroom bodies.
Subcellular location: Nucleus {ECO:0000269|PubMed:18456458, ECO:0000269|PubMed:25836674}. Cytoplasm {ECO:0000269|PubMed:18456458}.
Interaction partners:
- protein-tyrosine-phosphatase
- Transcription factor Jra
- mitogen-activated protein kinase kinase
- Dual specificity mitogen-activated protein kinase kinase hemipterous
- Transcription factor kayak, isoforms A/B/F
- Ras-related protein Rac1
- Connector of kinase to AP-1, isoform E
- Forkhead box protein O
- Tumor necrosis factor family member eiger
- Ras-related protein Rac2
Sequence:
MTTAQHQHYTVEVGDTNFTIHSRYINLRPIGSGAQGIVCAAYDTITQQNVAIKKLSRPFQNVTHAKRAYREFKLMKLVNHKNIIGLLNAFTPQRNLEEFQDVYLVMELMDANLCQVIQMDLDHDRMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKADCTLKILDFGLARTAGTTFMMTPYVVTRYYRAPEVILGMGYTENVDIWSVGCIMGEMIRGGVLFPGTDHIDQWNKIIEQLGTPSPSFMQRLQPTVRNYVENRPRYTGYSFDRLFPDGLFPNDNNQNSRRKASDARNLLSKMLVIDPEQRISVDEALKHEYINVWYDAEEVDAPAPEPYDHSVDEREHTVEQWKELIYEEVMDYEAHNTNNRTR
Protein: TOG domain-containing protein (B3CJ34)
Organism: Caenorhabditis elegans
Interaction partners:
- ABC transporter domain-containing protein
- Eukaryotic translation initiation factor 2-alpha kinase gcn-2
- Large ribosomal subunit protein eL19
- Uncharacterized GTP-binding protein C02F5.3
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Eukaryotic translation initiation factor 2 subunit 1
- Small ribosomal subunit protein uS4
Sequence:
MSDDEIKSEHVQEKTENLSEEDALKEEIRRFSSAVSNPSLRAHGMAYAALTKLIERRSTEIPAQFVKGLVKMSIANSIRLYGQPKSFQAVSKLLQVLAKRDPISTLKSLLQTITTALPIIPNLTESHSLSQVPTMKWLLACLDGNSCAENAVEIFGALGAIAYWMSASDKAWRVFTKKLAQLFAKNPEISNVFTAKIGEFSKENPEKSLALISAFGALGAAKTPEIAPIFVEIFTKSQLLPKLRPPQFFVTRISKFAVFLQKSPDFETNLLPNMKKALLRSPEVAIFGIRGLLEHISFSLDFCAQDLLKSTISSLCNTDPEIREAGIGIVVALSRKSEISVIQKILNTLLDQFSAAKASEIKCSLMEGVGAIAKVVEAQDIDKIAEDVISKTAKADKESHDGTIEAQWNAAAEWAIRLSKPAISLTNAFKEASKLAPAVKYIGYRVLADILERRSMTSLPEGIDVKPLLTELETGPKGELCSIGLALLILRTTKKGSIEHTKAWSRASHAEALLKEKPLSQTKWQEAIAWAKLVELVILDRPVVNKTAPPSYSLPSIKPLSLLLFWPNWKVRQQASKSLLRILSTENALFAEALADLIFSETTNGTIDQLLRRVPGCPTPVDSWQVPGEWYVSTLRLLLTPKEPELDKLAIHTLLLASVQRLVEVDGSVWLRWVHEHRESKTWQASEVFRETAIQNVLQCKDRGVRNTALVTLIALHDERLRADLWKHVDASIKQLEVTDYGRITEQEISIYKCAEGQLYNTRVLDFDEAAGIKGTKGTSIQDQMAEIQLIRELAAKRQKEGKLSAKQKQVMEKELAAEKDTRDALRELYVTAEAKLDECRAMVAADAAGAFARPEILFEYCMPLTRSLLVSEEAARLFLAYRDACFEHSDDYLEELVGSNWLRVIGAHHRIPGWNDEFLDSALKRMFSLLNERAFVIDSGDDDDDEPVIFDDEIVGANHLTLLYPMIRIILKNSQRFSDNSRQDALQLLQSAIHKKFLRDRDVLNLPMEHYASMLFEHFSLDSGATNAFKATQQLFRLANDTNDIGDRVIGMVREILAYVGNEQPSVRGAALEILGAPHLLMRIVVELGIEQSISKEILVRIHVARHDPIEAVSEIAERLWIENHLQVKQVIGAMLVDECVSPSPLVRQSAAHAMVTFIEEHPNEMPAILTKFDETYKDLVLIREPIYDDVGRLQREAIDESDRRSGIGQTLVLLAGLCRQEEAEQLIRIVAPDGLSDRAQECRNELRNAAVETIRRHGAACMLRLLPLLEKLSDETPAQDDNRRQGLVVLLGTLAQYIDSTEKVKGIVARLVEALGTPSQTVQESVSRCLAPLVPKIRQDAKDLVSKLQWTLFEAETYGERRGAAYGIAGLMKGMGIIALKDTDLLGSIHKNMEDKKSPKHREGGLLALEILCCTIGKLFEPYILKALPSLLITFGDTDSNVRQSAEDTARAMMASMTVYGTKLVLPVLIVAIDDDSWRTKCAATELLGSMAFCAPRQLSACLPNIVPKLIEILADSSSKVQKSGEKALQQIARVVRNPEILGVTNQLMAGLLDPANKTSAALQAVLNTKFIHYIDAPSLALMMPIVRRAFEDRLSETRRVAAQIISNIYSLTENKDMEPYLAHMVPGLQRSLLDPVPEIRAVSARALGAVVSKSGGSTSENLRAQVIPWLKEKLVSPQSTVDRSGAAQGLCEVLAGAGTEQLEYVMPEIIHATESTDVSAETRDGYILMYIYLPMTFGDRFVPYLPQVVPPILKALADENEYVRASALKAGQRLISQYCSHARKLLLPQLQLALMDENWRIRYASVQLIGDFLFNISGITGKSTSSTADEDDTMGMEQAGKVIVRALGQKDRDRVLAGLYLTRSDVALVVRQAAGHVWKMVVSNTPRTLREVTKILFEMVVDSLASTCDERQQMGARCLGELVRKMGDKVINDILPVLDANQKSEEVAKRVGVAIALHEIIGNMSKEVTNHYLGAIVAPVRRAICDESELVREAAADTFTVLYHVVGNEALDEIICPLLEQLTPEQDHILAGLCDVMRQNSRSMLPYLLPKLTKPPVNVHALCSLASVSGDSLSRQLPKVLDALLAACETNDESDPMIESCEKVVIAVTDEDGIPVLVDYLIQKASQDENVPAAVLLSTFIAKSGVSLAEMAEEVLPGLLNLYTSPNPQIVDHAIAAAVALTQSMDQRELLSVLPVVKKAINIIVAGAKGQQIPGFTHPKSLQPLVVMLRESILQGQIEMKALAAECLGMVVKVSDVAALKAHVVNITGPLIRVLGDRFPANVKLPIIETLSKLLDKVDAMLRPFLPQLQSTFLKALQEPTSRPVRLAAGGALARLLKLHPKPEATMTELLKLLATSTDQQLIESSLATARALIATCGQKMSPTTIDEIYRVTELIYSENVENPTELDASLTACSGALLGETIAQKSDWKTAQNCVLSGIESPSTSARGRQAKACALQQLCSSNGDELWASEANSACRSAFTSAFTSPDPIVASAALRGASHVLKVSIDRDLMSAVARSLNHASTDVRKTAGIALGHVGHSADLPNDILKLIVPQLINGCKESNSQVRAASELALVHALKMTQNEDRFEAYRNTLEGVVQRNLDETRVSLARVVRAGDVDLEPLDTILNVY
Protein: 3,5,7-trioxododecanoyl-CoA synthase (EC 2.3.1.206) (Olivetol synthase) (EC 4.4.1.-) (Polyketide synthase-1) (Tetraketide synthase) (B1Q2B6)
Organism: Cannabis sativa (Hemp) (Marijuana)
Function: Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity. Polyketide synthase responsible for olivetol biosynthesis, from a C(12)-polyketide, probably 3,5,7-trioxododecanoyl-CoA. Catalyzes the first step in the cannabinoids biosynthetic pathway. The preferred substrate is hexanoyl-CoA, but accepts also CoA esters with C4 to C8 aliphatic side chains. When using malonyl-CoA and hexanoyl-CoA as substrates, produces undetermined compounds distinct form olivetol or olivetolic acid that could be hexanoyl triacetic acid lactone (HTAL) and pentyl diacetic acid lactone (PDAL). Produces olivetolic acid when acting in concert with olivetolic acid cyclase (OAC).
Interaction partners:
Sequence:
MNHLRAEGPASVLAIGTANPENILLQDEFPDYYFRVTKSEHMTQLKEKFRKICDKSMIRKRNCFLNEEHLKQNPRLVEHEMQTLDARQDMLVVEVPKLGKDACAKAIKEWGQPKSKITHLIFTSASTTDMPGADYHCAKLLGLSPSVKRVMMYQLGCYGGGTVLRIAKDIAENNKGARVLAVCCDIMACLFRGPSESDLELLVGQAIFGDGAAAVIVGAEPDESVGERPIFELVSTGQTILPNSEGTIGGHIREAGLIFDLHKDVPMLISNNIEKCLIEAFTPIGISDWNSIFWITHPGGKAILDKVEEKLHLKSDKFVDSRHVLSEHGNMSSSTVLFVMDELRKRSLEEGKSTTGDGFEWGVLFGFGPGLTVERVVVRSVPIKY
Protein: MADS-box protein FBP24 (Floral-binding protein 24) (Q9ATE5)
Organism: Petunia hybrida (Petunia)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
Sequence:
MIIMGRGKIEVKRIENKTSRQVTFSKRRAGLLKKTHELSVLCDAQIGLIIFSSKGKLFEYCSQPHSMSQIISRYLQTTGASLPVEDNRVQLYDEVAKMRRDTLNLQLSLQRYKGDDLSLAQYEELNELEKQLEHALNKIRARKLELMQQQMENLKKTEKMLEKENHDMYQWLMNNQMYKQESAAMDHEDHHHHHEHQQAITELNLLGEQPLLSHFTFFGDQEQPSTSTVNHFASISLTSPPANSISPYRLQPSHPNLQDSHVHGPSYD
Protein: RE48687p (Q8IGQ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- very-long-chain enoyl-CoA reductase
Sequence:
MQPVLEVSIYTLLKMAFIWQLISAAIYLVGLLTIGVFLYDNLKSLVSIIKAVLEPYFQPHLPRTLVDKFGQWAVVTGATDGIGKEYARELARQGINLVLISRTKEKLIAVTNEIESQYKVKTKWIAADFAKGREVYDQIEKELAGIDVGILVNNVGMMYEHPESLDLVSEDLLWNLLTVNMGSVTMLTRKILPQMIGRRKGAIVNLGSSSELQPLPNMTVYAASKKFVTYFSKALELEVAEHNIHVQLVMPNFVVTKMNAYTDRVMQGGLFFPNAYTFARSAVFTLGKTSETNGFWTHGIQYAIMKLAPLPIRTYLGHQLFKRLRIEALEQKQKKLKLT
Protein: Zinc finger and BTB domain-containing protein 46 (BTB-ZF protein expressed in effector lymphocytes) (BZEL) (BTB/POZ domain-containing protein 4) (Zinc finger protein 340) (Q86UZ6)
Organism: Homo sapiens (Human)
Function: Functions as a transcriptional repressor for PRDM1.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Basic leucine zipper transcriptional factor ATF-like 3
- Chemokine XC receptor 1
Sequence:
MNNRKEDMEITSHYRHLLRELNEQRQHGVLCDVCVVVEGKVFKAHKNVLLGSSRYFKTLYCQVQKTSEQATVTHLDIVTAQGFKAIIDFMYSAHLALTSRNVIEVMSAASFLQMTDIVQACHDFIKAALDISIKSDASDELAEFEIGASSSSSTEALISAVMAGRSISPWLARRTSPANSSGDSAIASCHDGGSSYGKEDQEPKADGPDDVSSQPLWPGDVGYGPLRIKEEQVSPSQYGGSELPSAKDGAVQNSFSEQSAGDAWQPTGRRKNRKNKETVRHITQQVEDDSRASSPVPSFLPTSGWPFSSRDSNADLSVTEASSSDSRGERAELYAQVEEGLLGGEASYLGPPLTPEKDDALHQATAVANLRAALMSKNSLLSLKADVLGDDGSLLFEYLPRGAHSLSLNEFTVIRKKFKCPYCSFSAMHQCILKRHMRSHTGERPYPCEICGKKFTRREHMKRHTLVHSKDKKYVCKVCSRVFMSAASVGIRHGSRRHGVCTDCAGRGMAGPLDHGGGGGEGSPEALFPGDGPYLEDPEDPRGEAEELGEDDEGLAPEDALLADDKDEEDSPRPRSPPGGPDKDFAWLS
Protein: Cysteine-rich receptor-like protein kinase 21 (Cysteine-rich RLK21) (EC 2.7.11.-) (Q3E9X6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- CDPK-related kinase 2
- CDPK-related kinase 3
- CDPK-related kinase 7
- CDPK-related kinase 5
- PHD finger-like protein
Sequence:
MQKNKMVDLRAIFWFVVISSCAVAAPTCIQRSDFFKANGPYDINLRAMLSSLPSRVKDNEGFYKTPFKPGPNIAHGLGMCSRGTTTQDCSDCITSVSHTLLHTCPNQAEAIDWSSGDSLCLVRYSNHLINGSLDEDIIWAEYIEYKYNTSFGQTNLTEFKSTWQALMDRVINKVDGSLYANSIQELGSFPFRSIYAIAQCNKDLTKLNCEKCLQHLRIDNRSCCRGIQVGYIARTSCFMRWDLQPFLGLFINGMLPTPPSELDNGHSNTTKKDGKNISTGSIVAIAVVSVVVSTVLLALGYAVSRRRKAYQSFASENGYFSVSRRPRRPYGTASPDDATDDLTASSGSLRFDFRAIKAATSNFHKSNKLGHGGFGAVYKGMFPNGTEVAAKRLSKPSDQGEPEFKNEVLLVARLQHKNLVGLLGFSVEGEEKILVYEFVPNKSLDHFLFDPIKRVQLDWPRRHNIIEGITRGILYLHQDSRLTIIHRDLKASNILLDAEMNPKIADFGLARNFRVNQTEANTGRVVGTFGYMPPEYVANGQFSTKSDVYSFGVLILEIIGGKKNSSFHQIDGSVSNLVTHVWRLRNNGSLLELVDPAIGENYDKDEVIRCIHIGLLCVQENPDDRPSMSTIFRMLTNVSITLPVPQPPGFFFRERSEPNPLAERLLPGPSTSMSFTCSVDDASITSVRPR
Protein: Dynein axonemal assembly factor 8 (Dynein axonemal-associated protein 1) (Q8IYS4)
Organism: Homo sapiens (Human)
Function: In cyliated cells, dynein axonemal particle-specific protein required for deployment of ODA to the axoneme. Interacts with outer dynein arm (ODA) subunits.
Subcellular location: Dynein axonemal particle {ECO:0000269|PubMed:33263282}. Cytoplasm {ECO:0000269|PubMed:31429579}.
Interaction partners:
Sequence:
MASNDKGMAPSLGSPWASQMGPWDAILKAVKDQLPSLDSDSPLSDYGEEELFIFQRNQTSLIPDLSEELAEDPADGDKSRAWVAAAEESLPEPVLVPAELATEPGCRQNTRTKDASSQEGRDPGRPFESSGEVSALLGMAEEPPRWLEGDLGSLSFNTKGSQGPPWDPQAEATLSCHEGDPKAEPLSTASQESVNRRALRQERRKMIETDILQKVTRDACGPTSSDKGGVKEAPCHAAESAPRSKMPLVEPPEGPPVLSLQQLEAWDLDDILQSLAGQEDNQGNRAPGTVWWAADHRQVQDRMVPSAHNRLMEQLALLCTTQSKASACARKVPADTPQDTKEADSGSRCASRKQGSQAGPGPQLAQGMRLNAESPTIFIDLRQMELPDHLSPESSSHSSSDSEEEEEEEMAALGDAEGASPSSLGLRTCTGKSQLLQQLRAFQKGTAQPELPASKGPAGGRAQAPEDTAGSRTGRKQHMKLCAKGQSAQARLPRGRPRALGDVPEPGAAREALMPPLEQL
Protein: Phospholipase A2 acanmyotoxin-2 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (P85060)
Organism: Acanthophis sp. (strain Seram) (Seram death adder)
Function: Snake venom phospholipase A2 (PLA2) that has myotoxic activity but no significant neurotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:16242671}.
Interaction partners:
Sequence:
NLYQFGGMIGCANKGTRSWLSYVNYGCYCG
Protein: Ribosome hibernation promoting factor (HPF) (Hibernation factor HPF) (P0AFX0)
Organism: Escherichia coli (strain K12)
Function: During stationary phase, promotes and stabilizes dimerization of 70S ribosomes by the ribosome modulation factor (RMF), leading to the formation of inactive 100S ribosomes. Converts immature 90S particles formed by RMF into 100S ribosomes. Crystallization with T.thermophilus 70S ribosomes shows it binds in the channel between the head and body of the 30S subunit, where mRNA, tRNAs, initiation factors IF1 and IF3 and elongation factor G would bind; however RMF is still able to bind. In this crystal binding of HPF induces movement of the 30S head domain away from the rest of the ribosome, presumably so they would more easily form dimers. May also function as a potential translational inhibitor.
Interaction partners:
- Ribosome modulation factor
- Small ribosomal subunit protein bS21
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein bS20
- Small ribosomal subunit protein bS18
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS17
Sequence:
MQLNITGNNVEITEALREFVTAKFAKLEQYFDRINQVYVVLKVEKVTHTSDATLHVNGGEIHASAEGQDMYAAIDGLIDKLARQLTKHKDKLKQH
Protein: Rothein 3.4 (P86514)
Organism: Litoria rothii (Roth's tree frog) (Hyla rothii)
Function: Lacks antimicrobial activity. Does not inhibit the formation of NO by neuronal nitric oxide.
Subcellular location: Secreted {ECO:0000269|PubMed:16124032}.
Interaction partners:
Sequence:
ASAAGAVREDDDETLLNPVLNSLDNLVSGL
Protein: Amyloid-beta A4 protein (Q08E54)
Organism: Bos taurus (Bovine)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU367156}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU367156}. Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004600}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLPALALVLLAAWTARALEVPTDGNAGLLAEPQVAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHAHMVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVIEVAEEEEVADVEEEEADDEEDDEDGEELEEEAEEPYEEATERTTSIATTTTTTTESVEEVVRVPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANIISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHPFGVDSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN
Protein: Transmembrane protein (Q57XK7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTTSNGFESPRESVAAAAACSSQLREAAERARKDPSKDIGLTTEELQERKRCAAEPHRFVSKSTSRPFEVKSSSRAQQIMTKGVVERQVTARQKEVLRKVSSLRKLQVGLFFVGVGFAYWVGVEFLLPHYAAVQERNRILRLRYEMAQRKREEHLRVQGSSQ
Protein: Adenylate cyclase type 1 (EC 4.6.1.1) (ATP pyrophosphate-lyase 1) (Adenylate cyclase type I) (Adenylyl cyclase 1) (AC1) (Ca(2+)/calmodulin-activated adenylyl cyclase) (P19754)
Organism: Bos taurus (Bovine)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates responses to increased cellular Ca(2+)/calmodulin levels. May be involved in regulatory processes in the central nervous system. May play a role in memory and learning. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:2022671, ECO:0000269|PubMed:2472670}; Multi-pass membrane protein {ECO:0000305|PubMed:2022671, ECO:0000305|PubMed:2472670}. Cell membrane {ECO:0000269|PubMed:19029295, ECO:0000269|PubMed:2022671}; Multi-pass membrane protein {ECO:0000305|PubMed:2022671}. Cytoplasm {ECO:0000250|UniProtKB:O88444}. Membrane raft {ECO:0000269|PubMed:19029295}. Note=Expressed in the cytoplasm of supporting cells and hair cells of the cochlea vestibule, as well as to the cochlear hair cell nuclei and stereocilia. {ECO:0000250|UniProtKB:O88444}.
Interaction partners:
- Calmodulin-like protein 4
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- CALML5 protein
- Calmodulin
- EF-hand calcium-binding domain-containing protein 11
- Rap guanine nucleotide exchange factor 4
- Rap guanine nucleotide exchange factor 3
- Guanine nucleotide-binding protein G
- Adenylate cyclase type 3
Sequence:
MAGAPRGRGGGGGGGGAGESGGAERAAGPGGRRGLRACDEEFACPELEALFRGYTLRLEQAATLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQQVGQLALLFSLTFALLCCPFALGGPAGAHAGAAAVPATADQGVWQLLLVTFVSYALLPVRSLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFLGVNVYGIFVRILAERAQRKAFLQARNCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGHGHERNSFLKTHNIETFFIVPSHRRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALRTASEKLRNRSSFSTNVVQTTPGTRVNRYIGRLLEARQMELEMADLNFFTLKYKQAERERKYHQLQDEYFTSAVVLALILAALFGLVYLLIIPQSVAVLLLLVFCICFLVACVLYLHITRVQCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWSWSSSPNGSLVVLSSGGRDPVLPVPPCESAPHALLCGLVGTLPLAIFLRVSSLPKMILLAVLTTSYILVLELSGYTKAMGAGAISGRSFEPIMAILLFSCTLALHARQVDVKLRLDYLWAAQAEEERDDMEKVKLDNKRILFNLLPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEIIADFDELMDKDFYKDLEKIKTIGSTYMAAVGLAPTAGTKAKKCISSHLSTLADFAIEMFDVLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQVTEEVHRLLRRGSYRFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQTRSLNSERKMYPFGRAGLQTRLAAGHPPVPPAAGLPVGAGPGALQGSGLAPGPPGQHLPPGASGKEA
Protein: Suppressor of fused homolog (A0A8I6A606)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR011844}. Nucleus {ECO:0000256|PIRNR:PIRNR011844}.
Interaction partners:
Sequence:
MAELRPSVAPGPAAPPASGPSAPPAFASLFPPGLHAIYGECRRLYPDQPNPLQVTAIVKLGGPDPLDYVSMYRNMGSPSANIPEHWHYISFGLSDLYGDNRVHEFTGTDGPSGFGFELTFRLKRETGESAPPTWPAELMQGLARYVFQSENTFCSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVQTPFGVVTFLQIVGVCTEELHSAQQWNGQGILELLRTVPIAGGPWLITDMRRGETIFEIDPHLQERVDKGIETDGSNLSGVSAKCAWDDLSRPPEDDEDSRSICLGTQPRRLSGKDTEQIRETLRRGLEINSKPVLPPINSQRQNGLTYDRAPSRKDSLGSDISTAVIPHELIRTRQLESVHLKFNQESGALIPLCLRGRLLHGRHFTYKSITGDMAITFVSTGVEGAFATEEHPYAAHGPWLQILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH
Protein: Membrane frizzled-related protein (Membrane-type frizzled-related protein) (Q8K480)
Organism: Mus musculus (Mouse)
Function: May play a role in eye development.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:17122143}; Single-pass type II membrane protein {ECO:0000269|PubMed:17122143}.
Interaction partners:
- Complement C1q tumor necrosis factor-related protein 5
- Serine protease 56
- Transmembrane protein 98
- Protein RD3
Sequence:
MKDYDDVILRPEASELSKTEFCNPAFDPEAGPSCPPPALQRDVGSRLQAPWHAQRLRGLQPDCHFSWFCILLLSGLLLLLLGLLVAVILAQLQATSLPRTTKNPLLTRGLTPMGVIPSTTPNTTTTTTTTTPARTGQQEAAMSPTHQTTCGGLLPGPSGFFSSPNYPDLYPPLSHCVWHIQVAAGQTIQLKIQALSIESMLTCLFDRLEIISEPTGPLLRVCGKTPPATLNTNTSHLRVSFVSDNDVEGSGFQAWYQAVAPGHWSCAHNEFHCDLLLCLKRDSVCDGITECADGSDEANCSAKTLGCGGNLTGLYGVFSTPNYPQHYPHQQLCTWYIEVPVGYGIRLEFHNFSLEAQAECKFDYVEVYEASNLGTFSFLGRFCGAEPPLNVVSSMHQLAVIFKTDLGISSGGFLATYQAINTTESGCPWAEFCQSGGYRDLQWMCDLWKDCANDSNDNCSSHLSPQPDLTCEPVQVEMCLGLSYNTTAFPNIWVGLATQTEVTDILRGYKSLTSLPCYQTFQRFLCGLLVPRCTSLGTILPPCRSVCQAAEQQCQSSLALLGTPWPFNCNRLPVAASLEACSQP