wanglab/gogpt-training-data huggingface dataset:
Protein: Endoglucanase (EC 3.2.1.4) (Q9L3J5)
Organism: Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum)
Interaction partners:
Sequence:
MKKMGLGRFSNKFVLTVLLFFLTAVLLPSSSFESKVQAASSPRYGGAYYNYGEALQKAILFYKANRLGDLPDDYILPYRADAAMTDGQDVGLDLTGGWADAGDGIKFTHPMSYAAGQLGWAVYEYRQAFEKAGLLDDILDEIKWATDFFIKAHPEPNVLYYMCGYNDSDHSVWVPHELLDYVTDRKSFVLNPSTPGSDVAGQTAACLAIALIIFEPTDPEYAETCLTHAKQIFEFGDKYRAKKSSGCFYTPSGGYLDDLAWGAVWLYIKTGDSTYLEKAKSFLPVTSLGGGHTHCWDDVSYGAALKIAQLTHDEGYAAMVEKNLDFWLPGGGITYTPGGLAWLSPWGSLRYASTAAFLAFVWADDPTVGTPSKKETYRAFAEKQINYILGDNPRKGSYVVGFGENSPKHPHHRTAHGSWVSMLEVPSFHRHILYGALVGGPTDDDSWEDDISDYTRNEVATDYNAGFVGALAKMYDMYGGEPLENWPQPEDFRAPGDDIVEYFCRGWIIYEGYGTLNLLLQVNNSSGWPPTMKDKLSVRYFMDLTEVFESGGTVDDVQISLGQNEGAKLIGLKHYRDNIYYFTVDFTGTMIMPAEWEMCEKDAHVTIKYRDGITGSNENDWSYQNLRKDPDYDATSFAGLTPYIPVYDNGVLLWGEEPPAVDDPGSSPPPTPTEPVIVYGDLNGDGNINSTDFTMLKRAILGNPAPGTNLAAGDLNRDGNTNSTDLMILRRYLLKLIGSLPI
Protein: Olfactory receptor 7A40 (Odorant receptor M12) (Olfactory receptor 140-1) (Olfactory receptor 19) (Q9JHB2)
Organism: Mus musculus (Mouse)
Function: Odorant receptor.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MELKNDTQISKFILLGISEDPLWQPFLFGLFLFMYLVTLLGNLLIIIATITDSHLHTPMYFFLSNLSFADICFTSASIPKMLVNIQTKNKVITYEGCISQVFFFILFGVLDNFLLAVMAYDRYVAICHPLHYMVIMNCRLCGFLVLGSWVTTALNSLLQSSMALRLSFCTDLKIPHFVCELNQLVLLACNDTFPNDMVMYFAAILLGGGPLAGILYSYSKIVSSIRAISSSQGKYKAFSTCASHLSVVSLFYSTLLGVYLSSSFTQNSHSTARASVMYSVVTPMLNPFIYSLRNKDLMGALRRLLRRKS
Protein: Serine-threonine kinase receptor-associated protein (UNR-interacting protein) (Q9Z1Z2)
Organism: Mus musculus (Mouse)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localized predominantly in the cytoplasm but also found in the nucleus. {ECO:0000250}.
Interaction partners:
- Gem-associated protein 2
- Probable ATP-dependent RNA helicase DDX20
- Gem-associated protein 7
- Survival motor neuron protein
- Gem-associated protein 8
- Gem-associated protein 5
- Gem
- Small nuclear ribonucleoprotein Sm D1
- Gem-associated protein 6
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MAMRQTPLTCSGHTRPVVDLAFSGITPYGYFLISACKDGKPMLRQGDTGDWIGTFLGHKGAVWGATLNKDATKAATAAADFTAKVWDAVSGDELMTLAHKHIVKTVDFTQDSNYLLTGGQDKLLRIYDLNKPEAEPKEISGHTSGIKKALWCSDDKQILSADDKTVRLWDHATMTEVKSLNFNMSVSSMEYIPEGEILVITYGRSIAFHSAVSLEPIKSFEAPATINSASLHPEKEFLVAGGEDFKLYKYDYNSGEELESYKGHFGPIHCVRFSPDGELYASGSEDGTLRLWQTVVGKTYGLWKCVLPEEDSGELAKPKIGFPETAEEELEEIASENSDSIYSSTPEVKA
Protein: Calcium uniporter protein C-terminal domain-containing protein (Q38CK8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- EF-hand domain-containing protein
- EF-hand domain-containing protein
Sequence:
MEHVVARVAGVQKPVDMPLRLLKKQQWVRCALDCSHKRVLRKEAFIELCTSNPYTPLCERMSKSEGIKFLQALHNARQVIVVQDYVYINPADVVDAVHVRLELPNVARRAPVTSRNCSSGQPKDSEVTLRSDMERRRFFWAIVSLLSSAQMSILAYLTFSVYGWSVMEPICYFVTTSTSLCAYAYGLCYKRNCSYEAIDSQLASSDTLVEGKSPSTVCTQPFFMEAVELLRTVQAESDNSGLAEASSSDTKDKA
Protein: Sirtuin 1 (cDNA FLJ90324 fis, clone NT2RP2001817, highly similar to NAD-dependent deacetylase sirtuin-1) (B0QZ35)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCLCSGRKTILEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELAYLSELPPTPLHVSEDSSSPERTSPPDSSVIVTLLDQAAKSNDDLDVSESKGCMEEKPQEVQTSRNVESIAEQMENPDLKNVGSSTGEKNERTSVAGTVRKCWPNRVAKEQISRRLDGNQYLFLPPNRYIFHGAEVYSDSEDDVLSSSSCGSNSDSGTCQSPSLEEPMEDESEIEEFYNGLEDEPDVPERAGGAGFGTDGDDQEAINEAISVKQEVTDMNYPSNKS
Protein: Endophilin-B1 (SH3 domain-containing GRB2-like protein B1) (Q9JK48)
Organism: Mus musculus (Mouse)
Function: May be required for normal outer mitochondrial membrane dynamics. Required for coatomer-mediated retrograde transport in certain cells. May recruit other proteins to membranes with high curvature. May promote membrane fusion (By similarity). Involved in activation of caspase-dependent apoptosis by promoting BAX/BAK1 activation. Isoform 1 acts proapoptotic in fibroblasts. Involved in caspase-independent apoptosis during nutrition starvation and involved in the regulation of autophagy. Activates lipid kinase activity of PIK3C3 during autophagy probably by associating with the PI3K complex II (PI3KC3-C2). Associated with PI3KC3-C2 during autophagy may regulate the trafficking of ATG9A from the Golgi complex to the peripheral cytoplasm for the formation of autophagosomes by inducing Golgi membrane tubulation and fragmentation. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Isoform 2 acts antiapoptotic in neuronal cells; involved in maintenance of mitochondrial morphology and promotes neuronal viability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17381077}. Golgi apparatus membrane {ECO:0000269|PubMed:17086176}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6AYE2}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9Y371}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y371}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9Y371}. Midbody {ECO:0000250|UniProtKB:Q9Y371}. Note=Association with the Golgi apparatus depends on the cell type. Following starvation colocalizes with ATG5 and LC3 autophagy-related protein(s)on autophagosomal membranes. {ECO:0000250|UniProtKB:Q9Y371}.
Interaction partners:
- UV radiation resistance-associated protein
- Beclin-1
- Activating molecule in BECN1-regulated autophagy protein 1
- Beclin 1-associated autophagy-related key regulator
- Phosphoinositide 3-kinase regulatory subunit 4
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Endophilin-B2
- Immunity-related GTPase family M protein 1
Sequence:
MNIMDFNVKKLAADAGTFLSRAVQFTEEKLGQAEKTELDAHLENLLSKAECTKIWTEKIMKQTEVLLQPNPNARIEEFVYEKLDRKAPSRINNPELLGQYMIDAGTEFGPGTAYGNALIKCGETQKRIGTADRELIQTSALNFLTPLRNFIEGDYKTIAKERKLLQNKRLDLDAAKTRLKKAKAAETKSSSEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDFVEAQMTYYAQCYQYMLDLQKQLGSFPSNYLSNNNQTSGTPVPYALSNAIGPSAQASTGSLVITCPSNLNDLKESSNNRKARVLYDYDAANSTELSLLADEVITVFSVVGMDSDWLMGERGNQKGKVPITYLELLN
Protein: Rod outer segment membrane protein 1 (ROSP1) (P32958)
Organism: Mus musculus (Mouse)
Function: Plays a role in rod outer segment (ROS) morphogenesis. May play a role with PRPH2 in the maintenance of the structure of ROS curved disks (By similarity). Plays a role in the organization of the ROS and maintenance of ROS disk diameter. Involved in the maintenance of the retina outer nuclear layer.
Subcellular location: Photoreceptor inner segment membrane {ECO:0000305|PubMed:26406599}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor outer segment membrane {ECO:0000305|PubMed:26406599, ECO:0000305|PubMed:29961824}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peripherin-2
- Cone-rod homeobox protein
- Rhodopsin
- Aryl-hydrocarbon-interacting protein-like 1
- Regulator of G-protein signaling 9-binding protein
- Cyclic nucleotide-gated channel beta-1
- Sodium/potassium/calcium exchanger 1
- S-arrestin
- Guanine nucleotide-binding protein G
Sequence:
MAPVLPVVLPLQPRIRLAQGIWLLSWLLALVGGLTLLCSGHLLVQLGHLGTFLAPSCSFPALPQTALAAGTVALGTGLGGAGASRASLDAAQYPPWRGVLTPLLAVGTAAGGGLLTLALGLALALPVSLNQGLEEGLEAALAHYKDTEVPGRCQAKRLMDELQLRYHCCGRHGYKDWFGVQWVSNRYLDPSDQDVVDRIQSNVEGLYLIDGVPFSCCNPHSPRPCLQSQLSDPYAHPLFDPRQPNLNLWAQGCHEVLLEHLQGLSGTLGSILAVTLLLQILVLLGLRYLQTALEGLGGVIDGEGEAQGYLFPGGLKDILKTAWLQGGLAHKPAPEEAPPDEEPPKEVLAEA
Protein: cDNA FLJ75629, highly similar to Homo sapiens transmembrane protease, serine 4 (TMPRSS4), transcript variant 2, mRNA (A8K2U6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPDSDQPLNSLDVKPLRKPRIPMETFRKVGIPIIIALLSLASIIIVVVLIKVILDKYYFLCGQPLHFIPRKQLCDGELDCPLGEDEEHCVKSFPEGPAVAVRLSKDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSSKPTFRAVEIGPDQDLDVVEITENSQELRMRNSSGPCLSGSLVSLHCLACGKSLKTPRVVGGEEASVDSWPWQVSIQYDKQHVCGGSILDPHWVLTAAHCFRKHTDVFNWKVRAGSDKLGSFPSLAVAKIIIIEFNPMYPKDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGG
Protein: Peroxisomal membrane protein 4, putative (Q38FX7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Peroxin 19
Sequence:
MRPFPTPRPAAICDLWHLSATGYCFPVTPSCNVHIRYSAWTPFFGLSILFFVSVTVSCVSALVGTGSISTSHSVAKGRPQLRVVMAAEPADRGCGPISAAKKVTLLIDDMIRSGKYKILFDALKSFRNGFVYGARIRAPHALVLNLVWSSAPYSVIARRVFDATRQHALRLGATAFTFSLLRSLMALVEGRQRPWHSVVAGFIIGCLYWGEQGAVTVQMSMYILSRILSALFFILMERLAVTTSVHPPPWAFRLYSGVLWMFVMPLFLYHREALQPTMRTSMQYIYEDCTRYSNWYNLLCFNSDTSF
Protein: Hepatitis A virus cellular receptor 1 isoform X4 (TIM-4 like protein) (A0A1C6ZYS3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTDLHSWFLSSWILCCLTICRCSDIIVQSFEGDNVTLPCKYDSRYHGKCEICWMRGDIPSRGCGEEIIASDGDKVSTRNSDRYDLAGPIQHGDVSLTIFNIDKTDSGKYGCRVHVPGWFNDEKYYVHLIVDDAIIPTTLETTSMSSSTSEHETTGVYTTAMTEDNKTRKEISSTISPSYAPRSSTAGMWLSNTTSVEPSVSVVYHESSSAESKDNVTVSAVLVPVLLLLLALIAIAAAFMWKQKKKTRASLEVRQNSEISVIYSNSGSSVGLYNREMAVENVYQIQAESEYEQWH
Protein: CDK5 regulatory subunit-associated protein 2 (B1AMJ5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
DSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQVEHFSQEELKKKVSDLIQLVKELYTDNQHLKKTIFDLSCMGFQGNGFPDRLASTEQTEIMKDLSKGGCKNGYLRHTESKISDCDGAHAPGCLEEGAFINLLAPLFNEKATLLLESRPDLLKVVRELLLGQLFLTEQEVSGEHLDGKTEKTPKQKGELVHFVQTNSFSKPHDELKLSCEAQLVKAGEVPKVGLKDASVQTVATEGDLLRFKHEATREAWEEKPINTALSAEHRPENLHGVPGWQAALLSLPGITNREAKKSRLPILIKPSRSLGNMYRLPATQEVVTQLQSQILELQGELKEFKTCNKQLHQKLILAEAVMEGRPTPDKTLLNAQPPVGAAYQDSPGEQKGIKTTSSVWRDKEMDSDQQRSYEIDSEICPPDDLASLPSCKENPEDVLSPTSVATYLSSKSQPSAKVSVMGTDQSESINTSNETEYLKQKIHDLETELEGYQNFIFQLQKHSQCSEAIITVLCGTEGAQDGLSKPKNGSDGEEMTFSSLHQVRYVKHVKILGPLAPEMIDSRVLENLKQQLEEQEYKLQKEQNLNMQLFSEIHNLQNKFRDLSPPRYDSLVQSQARELSLQRQQIKDGHGICVISRQHMNTMIKAFEELLQASDVDYCVAEGFQEQLNQCAELLEKLEKLFLNGKSVGVEMNTQNELMERIEEDNLTYQHLLPESPEPSASHALSDYETSEKSFFSRDQKQDNETEKTSVMVNSFSQDLLMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELHSSLTSEIHFLRKQNQALNAMLIKGSRDKQKENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEEVKLRQQLLSQNDKLLQSLRVELKAYEKLDEEHRRLREASGEGWKGQDPFRDLHSLLMEIQALRLQLERSIETSSTLQSRLKEQLARGAEKAQEGALTLAVQAVSIPEVPLQPDKHDGDKYPMESDNSFDLFDSSQAVTPKSVSETPPLSGNDTDSLSCDSGSSATSTPCVSRLVTGHHLWASKNGRHVLGLIEDYEALLKQISQGQRLLAEMDIQTQEAPSSTSQELGTKGPHPAPLSKFVSSVSTAKLTLEEAYRRLKLLWRVSLPEDGQCPLHCEQIGEMKAEVTKLHKKLFEQEKKLQNTMKLLQLSKRQEKVIFDQLVVTHKILRKARGNLELRPGGAHPGTCSPSRPGS
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (P9WQ09)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Adenine glycosylase active on G:A and C:A mispairs, as well as processing 7,8-dihydro-8-oxoguanine:A (8-oxoG) mismatches. Minor activity against 8-oxoG:G and 8-oxo:T mismatches is also seen. Bind dsDNA oligonucleotides containing the above mismatches.
Interaction partners:
- Formamidopyrimidine-DNA glycosylase 1
- Endonuclease III lyase)
- Probable exodeoxyribonuclease III protein XthA
- Endonuclease 8 2 lyase Nei 2)
- Carbonic anhydrase 2
- Endonuclease 8 1 lyase Nei 1)
- UvrABC system protein B
- Type-5 uracil-DNA glycosylase
- ATP-dependent DNA helicase UvrD1
- Probable bifunctional transcriptional activator/DNA repair enzyme AlkA
Sequence:
MPHILPEPSVTGPRHISDTNLLAWYQRSHRDLPWREPGVSPWQILVSEFMLQQTPAARVLAIWPDWVRRWPTPSATATASTADVLRAWGKLGYPRRAKRLHECATVIARDHNDVVPDDIEILVTLPGVGSYTARAVACFAYRQRVPVVDTNVRRVVARAVHGRADAGAPSVPRDHADVLALLPHRETAPEFSVALMELGATVCTARTPRCGLCPLDWCAWRHAGYPPSDGPPRRGQAYTGTDRQVRGRLLDVLRAAEFPVTRAELDVAWLTDTAQRDRALESLLADALVTRTVDGRFALPGEGF
Protein: Isobutyryl-CoA dehydrogenase, mitochondrial (IBDH) (EC 1.3.8.5) (Activator-recruited cofactor 42 kDa component) (ARC42) (Acyl-CoA dehydrogenase family member 8) (ACAD-8) (Q9UKU7)
Organism: Homo sapiens (Human)
Function: Isobutyryl-CoA dehydrogenase which catalyzes one of the steps of the valine catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of (2S)-2-methylbutanoyl-CoA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11013134, ECO:0000269|PubMed:12359132}.
Interaction partners:
- Enoyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Peroxisomal bifunctional enzyme
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Enoyl-CoA delta isomerase 2
- Electron transfer flavoprotein subunit beta
- 3-ketoacyl-CoA thiolase, mitochondrial
Sequence:
MLWSGCRRFGARLGCLPGGLRVLVQTGHRSLTSCIDPSMGLNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDIYVVMCRTGGPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVALCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE
Protein: Probable replication restart primosome protein PriA (Probable primosomal protein n') (Putative ATP-dependent DNA helicase PriA) (P9WMQ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA.
Interaction partners:
- Single-stranded DNA-binding protein
- Single-stranded DNA-binding protein
- Lysoplasmalogenase
- Methionyl-tRNA formyltransferase
- Replicative DNA helicase DnaB
- Coenzyme A biosynthesis bifunctional protein CoaBC
Sequence:
MLSVPHLDRDFDYLVPAEHSDDAQPGVRVRVRFHGRLVDGFVLERRSDSDHHGKLGWLDRVVSPEPVLTTEIRRLVDAVAARYAGTRQDVLRLAVPARHARVEREITTAPGRPVVAPVDPSGWAAYGRGRQFLAALADSRAARAVWQALPGELWADRFAEAAAQTVRAGRTVLAIVPDQRDLDTLWQAATALVDEHSVVALSAGLGPEARYRRWLAALRGSARLVIGTRSAVFAPLSELGLVMVWADADDSLAEPRAPYPHAREVAMLRAHQARCAALIGGYARTAEAHALVRSGWAHDVVAPRPEVRARSPRVVALDDSGYDDARDPAARTARLPSIALRAARSALQSGAPVLVQVPRRGYIPSLACGRCRAIARCRSCTGPLSLQGAGSPGAVCRWCGRVDPTLRCVRCGSDVVRAVVVGARRTAEELGRAFPGTAVITSAGDTLVPQLDAGPALVVATPGAEPRAPGGYGAALLLDSWALLGRQDLRAAEDALWRWMTAAALVRPRGAGGVVTVVAESSIPTVQSLIRWDPVGHAEAELAARTEVGLPPSVHIAALDGPAGTVTALLEAARLPDPDRLQADLLGPVDLPPGVRRPAGIPADAPVIRMLLRVCREQGLELAASLRRGIGVLSARQTRQTRSLVRVQIDPLHIG
Protein: Serine protease inhibitor 42Dd (Serpin 42Dd) (Q7YTY6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine protease inhibitor with activity toward trypsin. Involved in innate immunity to fungal infection by negatively regulating the Toll signaling pathway and suppressing the expression of the antifungal peptide drosomycin. Acts upstream of SPE and grass, and downstream of the fungal cell wall pattern recognition receptor GNBP3. May function specifically in the GNBP3-dependent beta-1,3-glucan branch of the Toll pathway.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- GH10112p
- FI01422p
Sequence:
MYYLCIFLWVTSVACQTSKEIYQLLSKSHTNQNLVVSPVSIETILSMVFMGAEGSTAKELQSALGLPSEDKEAVAARYGALLNDLQGQEEGPILKLANRIYVNDQYSLNQNYNLAVREPFKSEAESISLTNGPVAAERINQWVLDQTSGKIKGMIDPGSMTSDVKALLVNAIYFKGQWESKFDPAKTRASTFQVTANKSVPVQMMAQMGTFRANYFRDLDAQVIELPYLNSNLSMTIFLPREVEGLSALEEKIVGFARPLVAKEVYLKLPKFKIEFRDELKETLEKLGIRELFTDKSDLSGLFADKSGGKVSQVSHKAFLEVNEEGAEAAGATSVAVTNRAGFSTFLMADHPFAFVIRDANTIYFQGRVVSP
Protein: Protein FEV (Fifth Ewing variant protein) (PC12 ETS domain-containing transcription factor 1) (PC12 ETS factor 1) (Pet-1) (Q99581)
Organism: Homo sapiens (Human)
Function: Functions as a transcriptional regulator. According to PubMed:12761502, it functions as a transcriptional repressor. Functions in the differentiation and the maintenance of the central serotonergic neurons. May play a role in cell growth.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:12761502}.
Interaction partners:
Sequence:
MRQSGASQPLLINMYLPDPVGDGLFKDGKNPSWGPLSPAVQKGSGQIQLWQFLLELLADRANAGCIAWEGGHGEFKLTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMSKVHGKRYAYRFDFQGLAQACQPPPAHAHAAAAAAAAAAAAQDGALYKLPAGLAPLPFPGLSKLNLMAASAGVAPAGFSYWPGPGPAATAAAATAALYPSPSLQPPPGPFGAVAAASHLGGHYH
Protein: Securin-like protein (Interactor of Fizzy protein) (Q18235)
Organism: Caenorhabditis elegans
Function: Acts as a chaperone and as an inhibitor for separase sep-1. Plays an essential role in maintaining chromosome cohesion prior to meiotic and mitotic anaphase, in cytokinesis and in organizing the spindle and the centrosome. Ubiquitination-dependent degradation at the onset of anaphase is likely to activate sep-1 resulting in the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. Also required for cortical granule exocytosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23578927}. Chromosome {ECO:0000269|PubMed:23578927}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23578927}. Note=Localizes to cytoplasm in germ cells. After oocyte nuclear envelope breakdown, localizes to chromosomes and spindle microtubules until meiotic anaphase I where the chromosome localization disappears. Maintained at low levels in the cytoplasm during meiosis II and in subsequent mitotic divisions during early embryogenesis. Localizes to chromosomes during mitotic metaphase at the 4E embryonic stage. {ECO:0000269|PubMed:23578927}.
Interaction partners:
- Separin homolog sep-1
- WD repeat-containing protein fzy-1
- G2/mitotic-specific cyclin-B1
- OOcyte Partner of Spe-11
- Cyclin N-terminal domain-containing protein
- G2/mitotic-specific cyclin-B
- MEiotic SPindle
- Histone H3-like centromeric protein hcp-3
- separase
- MAD related
Sequence:
MEDLNFEERGSTQIPASLQQHFSAKLGRQNELEKTPSRGGLGLVVNSSKTPGGKSLQSLASACKVPPSTKKNTIPIAFECYEDETDDQIADVATIKKTEKHPCSPIDTANRCETFDSLAADIEDDMLNLEDQDVVLSEDRPYGDVIDPAESEAEALAELGVEEWDSYPPIDPASRIGDDFNYVLRTEDFAEEGDVKLEETRHRTVIADIDEVKMSKAERNELFSMLADDLDSYDLLAEEANLPL
Protein: Guanine nucleotide-binding protein subunit gamma (Q4WJQ0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- G protein complex beta subunit SfaD
- G-protein complex alpha subunit GpaA/FadA
- Guanine nucleotide-binding protein alpha-2 subunit
- G protein complex alpha subunit GpaB
- Serine/threonine-protein kinase ste20
- non-specific serine/threonine protein kinase
- Mating-type alpha-pheromone receptor PreB
Sequence:
MPAYELRSGGDVRNKKQSVADLKYRRLTELNARLKEDLDRPRVKVSEAAMSLINYCNNTRDFMVPSVWGQVDKREDPYAPQQQGGCCTVM
Protein: Cutinase (EC 3.1.1.74) (A0A024SC78)
Organism: Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Subcellular location: Secreted {ECO:0000255|RuleBase:RU361263}.
Interaction partners:
Sequence:
MRSLAILTTLLAGHAFAYPKPAPQSVNRRDWPSINEFLSELAKVMPIGDTITAACDLISDGEDAAASLFGISETENDPCGDVTVLFARGTCDPGNVGVLVGPWFFDSLQTALGSRTLGVKGVPYPASVQDFLSGSVQNGINMANQIKSVLQSCPNTKLVLGGYSQGSMVVHNAASNLDAATMSKISAVVLFGDPYYGKPVANFDAAKTLVVCHDGDNICQGGDIILLPHLTYAEDADTAAAFVVPLVS
Protein: Kinesin associated protein 3, isoform H (A8JUR4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQTNDDAKFIKKRWKGGSIEPHPTDKALIVNYQLEATVFGEPNNPMIEEKKHCQKIIRLRSLNAKTDPAALAREVVEKCDLIHKSQLNDVEQIIFYLKNRKDNASNDIPDNNTHSRRSAALHTSHTRSSARSHSSVAAMTSSTGSGGGSTGASNGVSNALSAATPTADVSINNIDEYVELLYEELGERIRGSAMILQMARNPDNLEELEKNEACLSALSRVLREDWRKSLDLSTNIIYIFFCFSTYTKFHPLIVQYKIGSLCMDVIDYELRRYETMRNELDVRKQPNGSSTPHSAKASKEKLNRSTDDFLDIMNEEKPKEMEPPRRRIPELKQRPKSGNWSSFHGSMSSSLIKSQILNSSYHESLCAGGSPGGDTPAVPAEQKAQSNESLDRNDPKVKKEEIDRLNKQLKIFAKKQEQLLRVAFYLLLNMAENVKLEEKMRRKHIVKMLVKALDRQNIDLLMLVSTFLKKLSIVGDNKDEMGALNIVAKLPRLFQSTHTDLVQVTLKLVFNLSFDGGLRRKMIAAGYLPMLVMFINDEKHHGIAVKILYHMSLDDKVKGMFTQTECVQMATDAIILNLNVKVDLDLIALCINLSLNRRNAQIMVEGQRLHSLMDRAFKYQDALLMKLLRNLSQHESLQLQFIDYVGDLARILTICDDEAFIVECLGILGNLALTDLDYSQILQNFQLIPWIRQILLPCARMDDLVLDTIVYLGTCACDELCALLFCRAKVVISLIELLKAKQEDDEIVLQIIFVFQQILRHESTREYMIKETESAAYLIDLMHDKNEEIRKVCDYCLDIIAISDSEWAKRIKLEKFRNHNSQWLCMVESQQDQDNEQDYADQEDECDNDLDTYLRSEYLDNCDLYNDNADNDSNSNSNHSNNNPASPAMSTYSRPLSTYRRSQDLDDLYNMTSSSKSQGSSDNNYIFKSNKSLDADGLHEELLMA
Protein: Neurocan core protein (Chondroitin sulfate proteoglycan 3) (O14594)
Organism: Homo sapiens (Human)
Function: May modulate neuronal adhesion and neurite growth during development by binding to neural cell adhesion molecules (NG-CAM and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic acid.
Subcellular location: Secreted {ECO:0000269|PubMed:25326458}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase zeta
- Aggrecan core protein
- Neural cell adhesion molecule 1
- Versican core protein
- Neural cell adhesion molecule L1
- Brevican core protein
- Glypican-1
- Syndecan-3
- Contactin-2
- Myocyte-specific enhancer factor 2B
Sequence:
MGAPFVWALGLLMLQMLLFVAGEQGTQDITDASERGLHMQKLGSGSVQAALAELVALPCLFTLQPRPSAARDAPRIKWTKVRTASGQRQDLPILVAKDNVVRVAKSWQGRVSLPSYPRRRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVFHYRSARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRSSLPGVRSYGRRNPQELYDVYCFARELGGEVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFANRTGFPSPAERFDAYCFRAHHPTSQHGDLETPSSGDEGEILSAEGPPVRELEPTLEEEEVVTPDFQEPLVSSGEEETLILEEKQESQQTLSPTPGDPMLASWPTGEVWLSTVAPSPSDMGAGTAASSHTEVAPTDPMPRRRGRFKGLNGRYFQQQEPEPGLQGGMEASAQPPTSEAAVNQMEPPLAMAVTEMLGSGQSRSPWADLTNEVDMPGAGSAGGKSSPEPWLWPPTMVPPSISGHSRAPVLELEKAEGPSARPATPDLFWSPLEATVSAPSPAPWEAFPVATSPDLPMMAMLRGPKEWMLPHPTPISTEANRVEAHGEATATAPPSPAAETKVYSLPLSLTPTGQGGEAMPTTPESPRADFRETGETSPAQVNKAEHSSSSPWPSVNRNVAVGFVPTETATEPTGLRGIPGSESGVFDTAESPTSGLQATVDEVQDPWPSVYSKGLDASSPSAPLGSPGVFLVPKVTPNLEPWVATDEGPTVNPMDSTVTPAPSDASGIWEPGSQVFEEAESTTLSPQVALDTSIVTPLTTLEQGDKVGVPAMSTLGSSSSQPHPEPEDQVETQGTSGASVPPHQSSPLGKPAVPPGTPTAASVGESASVSSGEPTVPWDPSSTLLPVTLGIEDFELEVLAGSPGVESFWEEVASGEEPALPGTPMNAGAEEVHSDPCENNPCLHGGTCNANGTMYGCSCDQGFAGENCEIDIDDCLCSPCENGGTCIDEVNGFVCLCLPSYGGSFCEKDTEGCDRGWHKFQGHCYRYFAHRRAWEDAEKDCRRRSGHLTSVHSPEEHSFINSFGHENTWIGLNDRIVERDFQWTDNTGLQFENWRENQPDNFFAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKKGTVLCGPPPAVENASLIGARKAKYNVHATVRYQCNEGFAQHHVATIRCRSNGKWDRPQIVCTKPRRSHRMRRHHHHHQHHHQHHHHKSRKERRKHKKHPTEDWEKDEGNFC